SSB1

Ribosome-associated molecular chaperone SSB1

614 amino acids

Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.

Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily.

67.03 kDa

MAEEVYDGAIGIDLGTTYSCVAVYEGTNVEIIANEQGNFTTPSFVSFTENERLIGEAAKNQAAMNPANTIFDVKRLIGRRFDDPTVKKDMESWPFKVVDDNGNPKVEVQYLGQTHTFSPQEISAMVLTKMKEIAETKLGKKVEKAVITVPAYFNDNQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLGSGKSDKERNVLIYDLGGGTFDVSLLNIQGGVFTVKATAGDTHLGGQDFDTNLLEYCKKEFTRKTKKDLSGDARALRRLRTACERAKRTLSSGAQTTIEIDSLFDGEDFNIQITRARFEDLNAKAFAGTLEPVAQVLKDAGIEKHQVDEIVLVGGSTRIPRIQKLLSEFFDGKKLEKSINPDEAVAYGAAVQAGILSGKATSADTSDLLLLDVVPLSLGVAMEGNIFAPVVPRGQTVPTIKKRTFTTVADNQQTVQFPVYQGERVNCEDNTLLGEFTLAPIPPMKAGEPVLEVVFEVDVNGILKVTATEKTSGRSANITIANSVGKLSTDEIEKMISDAEKFKSKDEAFSKRFEAKQQLESYISRVEEIISDPTLSLKLKRGQKDKIEQALSEAMAQLEIEDSTADELKKKELALKRLVTKAMASR

SSB1

Heat shock protein SSB1

614 amino acids

Chaperone that interacts with the histone acetyltransferase HAT1 and mediates its translocation from the nucleus to the cytoplasm during germination and starvation conditions. Within the cytoplasm, HAT1 regulates autophagy via acetylation of the autophagy-related proteins ATG3 and ATG9.

Belongs to the heat shock protein 70 family.

66.666 kDa

MSTEVYDGAIGIDLGTTYSCVATYEGSNVEIIANEQGSFTTPSFVSFTADERLIGEAAKNQAAMNPANTVFDVKRLIGRRFDDPTVKKDMESWPFKVVDEDGNPKVEVEYLGTTHKFSPQEISAMVLVKMKEIAEAKIGKKVEKAVITVPAYFNDNQRQSTKDAGAISGLNVLRIINEPTAAAIAYGLGSGKSEKERNVLIYDLGGGTFDVSLLNIQGGVFTVKATAGDTHLGGQDFDTNLLDHCKKDFQRKTKKDLSGDARALRRLRTACERAKRTLSNGTQTTLEIDSLFDGEDFSLQITRAKFEELNQTAFKGTLDPVTQVLKDAGVDKAAVDEIVLVGGSTRIPKIQKLLSDYFGGKKLEKSINPDEAVAYGAAVQAGILSGKATSAETADLLLLDVVPLSLGVAMEGNIFAPVVPRGTTVPTLKKRSFTTVADQQQTVQFPVYQGERTNCSENVSLGEFTLAPIPPMRAGEPVLEVVFEVDVNGILKVTATEKTSGRSANITIANSVGKLSTSEIENMISEAEKYKTNDEEFTKKHEAKQQLESYIARVEDIISDPTLALKLKRGQKEKIENTMSEAMAQLELGESTADDLKKKELALKRAVTKAMSSR

SSB1

Ribosome-associated molecular chaperone SSB1

613 amino acids

Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.

Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily.

66.479 kDa

MADGVFQGAIGIDLGTTYSCVATYDSAVEIIANEQGNRVTPSFVAFTSEERLIGDAAKNQAALNPKNTVFDAKRLIGRAFDDESVQKDIKSWPFKVVESNGQPLIEVEYLDETKTFSPQEISSMVLTKMKEIAEAKIGKKVEKAVVTVPAYFNDAQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLGAGKSEKERHVLIFDLGGGTFDVSLLNITGGVFTVKATAGDTHLGGQDFDTNLLEHFKKEFQKKTGNDISSDARALRRLRTACERAKRSLSSGTQTTVEIDSLFDGEDFSANITRARFEDINSALFKSTLEPVEQVLKDAKISKSQVDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAILTGQSTNDDTKDLLLLDVIPLSLGVAMQGNVFAPVVPRNTTVPTIKRRTFTTVADHQTTVQFPVYQGERVNCTENTLLGEFDLKNIPPMQAGEPVLEAIFEVDANGILKVTAVEKSTGRSANITISNSIGRLSTEEIEKMISDAEKFKSSDDAFAKRHEQKQKLEAYVASVESTVTDPVLSAKLKKSAKDKIEAALSDALQTLEIEESSADDYRKAELALKRAVTKGMATR

SSB1

Ribosome-associated molecular chaperone SSB

613 amino acids

Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.

Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily.

66.396 kDa

MADGVFQGAIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPKNTVFDAKRLIGRRFDEESVQNDMKTWPFKVVDVDGAPVIEVEYLGENKQFSPQEISSMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISGLNVLRIINEPTAAAIAYGLGAGKSDKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKGEFKKKTGLDISNDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFEGEDFEASLTRARFEDLNAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDYFDGKQLEKSINPDEAVAYGAAVQGAILTGQSTSDETKDLLLLDVAPLSLGVGMQGDIFGVVVPRNTTVPTIKRRTFTTVGDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPPMPAGEPVLEAIFEVDANGILKVTAVEKSTGKSANITISNAVGRLSSEDIEKMVNQAEEFKAADEAFAKRHEAKQRLESYVASIEQTVTDPVLSSKLKRGSKTKIEAALADALSALQIEDGSAEEYRKAEVGLKRVVTKAMSSR

SSB1

Ribosome-associated molecular chaperone SSB1

613 amino acids

Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.

Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily.

66.428 kDa

MADGVFQGAIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPKNTVFDAKRLIGRRFDEESVQNDMKTWPFKVVDVEGAPVIEVEYLGETKQFSPQEISSMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISGLNVLRIINEPTAAAIAYGLGAGKSDKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKSDFKKKTGLDISNDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFEASLTRARFEDLNAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAILTGQSTSDETKDLLLLDVAPLSLGVGMQGDIFGVVVPRNTTVPTIKRRTFTTVGDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPPMQAGEPVLEAIFEVDANGILKVTAVEKSTGKSANITISNAVGRLSSEDIEKMVNQAEEFKAADEAFAKRHEAKQRLESYVASIEQTVTDPVLSSKLKRGSKTKIEAALADALAALQIEDGSTEEYRKAEVGLKRVVTKAMSSR

SSB1

Ribosome-associated molecular chaperone SSB1

613 amino acids

Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.

Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily.

66.244 kDa

MAEGVFPGAIGIDLGTTYSCVATYENSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPKNTVFDAKRLIGRRFDEESVQSDMKTWPFKVIDSNDAPLIEVEYLGETKTFSPQEISSMVLTKMKEIAEAKIGKKVEKAVVTVPAYFNDAQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLGAGKSDKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKTEFKKKTGLDISGDARALRRLRTAAERAKRTLSSVAQTTVEVDSLFDGEDFEATITRARFEDINAALFKSTLEPVEQVLKDAKIAKSQIDEVVLVGGSTRIPKVQKLLSDFFEGKQLEKSINPDEAVAYGAAVQGAILTGQSTSDETKDLLLLDVAPLSLGVGMAGDVFGVVVPRNTTVPTIKRRTFTTVADHQTTVTFPVYQGERVNCKENTLLGEFDLKGVPPMPAGEPVLEAIFEVDANGILKVTAVEKSTGKSANITISNAIGRLSSEEIEQMVNQAEEFKAADEAFAKKHEARQRLESYISSVEQTVTDPVLSAKIKRNAKAKVEAALAEAFSTLQIEDASTDDLRKAEVGLKRAVTKAMSTR

SSB1

Ribosome-associated molecular chaperone SSB1

613 amino acids

Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.

Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily.

66.087 kDa

MAEGVFPGAIGIDLGTTYSCVATYENSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPKNTVFDAKRLIGRRFDEESVQSDMKTWPFKVIDSNGAPLIEVEYLGETKTFSPQEISSMVLTKMKEIAEAKIGKKVEKAVVTVPAYFNDAQRQATKDAGAIAGLNVLRIINEPTAAAIAYGVGAGNSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKTEFKKKTGADISGDARALRRLRTAAERAKRTLSSVAQTTVEVDSLFDGEDFEATITRARFEDINAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAILTGQSTSDETKDLLLLDVAPLSLGVGMAGDVFGVVVPRNTTVPTIKRRTFTTVADHQTTVTFPVYQGERVNCKENTLLGEFDLKGVPPMPAGEPVLEAIFEVDANGILKVTAVEKSTGKSANITISNAIGRLSSEEIEQMVNQAEEFKAADEAFAKKHEARQRLESYISSVQQTVTDPVLSAKIKRNAKAKVEAALADAFSTLQIEDASADDLRKAEVGLKRAVTKAMSTR

SSB1

Ribosome-associated molecular chaperone SSB1

613 amino acids

Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.

Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily.

66.253 kDa

MAEGVFSGAIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQSDMKTWPFKVIDANGSPMIEVEYLGETKSFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLGAGKSEKERHVLIFDLGGGTFDVSLLNIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEFKKKTGLDISGDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFEGEDFETSITRARFEDINAALFKSTLEPVEQVLKDAQISKSQIDEVVLVGGSTRIPKVQKLLSDFFEGKQLEKSINPDEAVAYGAAVQAAILTGSNLSDDTKDLLLLDVAPLSLGVAMQGDVFACVIPRNTTVPTIKRRTFTTVHDGQTTVTFPVYQGERVNCKDNTLLGEFDLKGIPPLPAGEPVLEAIFEVDANGILKVTAVEKSTGKTANITISNAIGRLSSEDIEKMVSQAEEFKAADEAFAKRHEARQRLESYVSSIEQTVSDPVLSAKMKKGAKSKVEAALADAFSALQIEESSAEDYRKAEIGLKRVVTKAMATR

SSB1

Ribosome-associated molecular chaperone SSB1

613 amino acids

Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.

Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily.

66.602 kDa

MAEGVFQGAIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKDMKTWPFKVIDVDGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISGLNVLRIINEPTAAAIAYGLGAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAILTGQSTSDETKDLLLLDVAPLSLGVGMQGDMFGIVVPRNTTVPTIKRRTFTTCADNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIFEVDANGILKVTAVEKSTGKSSNITISNAVGRLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTVTDPVLSSKLKRGSKSKIEAALSDALAALQIEDPSADELRKAEVGLKRVVTKAMSSR

SSB1

Ribosome-associated molecular chaperone SSB1

613 amino acids

Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.

Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily.

66.73 kDa

MAEGVFQGAIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPENTVFDAKRLIGRRFDDESVQKDRKTWPFKLIDVEGNPVVEVQYLGETKTFSPQEISSMVLTKMKEIAEAKIGQKVEKAVITVPAYFNDAQRQATKDAGSISGLNVLRIINEPTAAAIAYGLGAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNMLEHFKNEFKKKTGNDISGDARALRRLRTACERAKRTLSSVTQTTIEVDSLYNGDDFETSITRARFEDLNSSLFKSTLEPVEQVLKDAKVPKTEIDEVVLVGGSTRIPKVQKMLSDFFEGKQLEKSINPDEAVAYGAAVQGAILTGQSTSEDTKDLLLLDVAPLSLGVGMQGDIFGIVVPRNTTVPTIKRRTFTTVADHQSTVQFPVYQGERVNCKENTLLGEFDLKNIPPMQAGEPVLEAIFEVDANGILKVTAVEKSTGKSANITISNAVGRLSSDEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQQVTDPVLSSKLKRGSKTKIESALSDALASLEIQDASTDDLRKAEVGLKRVVTKAMSSR

ssb1

Replication factor A protein 1

609 amino acids

As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism.

Belongs to the replication factor A protein 1 family.

68.197 kDa

MAERLSVGALRIINTSDASSFPPNPILQVLTVKELNSNPTSGAPKRYRVVLSDSINYAQSMLSTQLNHLVAENKLQKGAFVQLTQFTVNVMKERKILIVLGLNVLTELGVMDKIGNPAGLETVDALRQQQNEQNNASAPRTGISTSTNSFYGNNAAATAPAPPPMMKKPAAPNSLSTIIYPIEGLSPYQNKWTIRARVTNKSEVKHWHNQRGEGKLFSVNLLDESGEIRATGFNDQVDAFYDILQEGSVYYISRCRVNIAKKQYTNVQNEYELMFERDTEIRKAEDQTAVPVAKFSFVSLQEVGDVAKDAVIDVIGVLQNVGPVQQITSRATSRGFDKRDITIVDQTGYEMRVTLWGKTAIEFSVSEESILAFKGVKVNDFQGRSLSMLTSSTMSVDPDIQESHLLKGWYDGQGRGQEFAKHSVISSTLSTTGRSAERKNIAEVQAEHLGMSETPDYFSLKGTIVYIRKKNVSYPACPAADCNKKVFDQGGSWRCEKCNKEYDAPQYRYIITIAVGDHTGQLWLNVFDDVGKLIMHKTADELNDLQENDENAFMNCMAEACYMPYIFQCRAKQDNFKGEMRVRYTVMSINQMDWKEESKRLINFIESAQ

ssb1

Single-stranded DNA-binding protein 1

202 amino acids

20.244 kDa

MAGETVITVVGNLVDDPELRFTPSGAAVAKFRVASTPRTFDRQTNEWKDGESLFLTCSVWRQAAENVAESLQRGMRVIVQGRLKQRSYEDREGVKRTVYELDVEEVGASLKNATAKVTKTTGRSGQGGQGGYGGGGGGQQGGGWGGGSGGAPQGGGAPADDPWATGTPAGGNQGGGGGGGWGGSSGGSSGGSGGGYSDEPPF

ssb1

Single-stranded DNA-binding protein 1

186 amino acids

20.313 kDa

MDATVTVVGNLTADPELRYTATGAAVVNMTIASTPRMYDRQSGEWKDGEPLFLRGILWREYAINAAASLAKGMRVVAVGKLKQRNYETREGDRRTSVELEIDEIGPTLRYATAKCSRATQAGHGVSPDPWADSQTGQGIDSHTTRSEEITENAKNGEGAGKNELNKKVLVGDNVSYEDFDSDEVPF

ssb1

Single-stranded DNA-binding protein 1

186 amino acids

20.299 kDa

MDATVTVVGNLTADPELRYTATGAAVVNMTIASTPRMYDRQSGEWKDGEPLFLRGILWREYAINAAASLAKGMRVVAVGKLKQRNYETREGDRRTSVELEIDEIGPTLRYATAKCSRATQAGHGVSPDPWADSQGSQGIDSHTTRSEEITENAKNGEGAGKNELNKKVLVGDNVSYEDFDSDEVPF

ssb1

Single-stranded DNA-binding protein 1

179 amino acids

Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.

19.604 kDa

MMNRVVLVGRLTKDPELRYTPAGVAVATFTLAVNRTFTNQQGEREADFINCVVWRKPAENVANFLKKGSMAGVDGRVQTRNYEGNDGKRVYVTEIVAESVQFLEPRNSNGGGGNNNYQGGNNNNNYNNGGNNFGQAPTNNGGFGQDQQQSQNQNYQSTNNDPFASDGKPIDISDDDLPF

ssb1

Single-stranded DNA-binding protein 1

178 amino acids

Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.

19.493 kDa

MMNRVVLVGRLTKDPELRYTPAGVAVATFTLAVNRTFTNQQGEREADFINCVVWRKPAENVANFLKKGSMAGVDGRVQTRNYEGNDGKRVYVTEIVAESVQFLEPRNSNGGGGNNYQSGNNNNNYNSGGNNFGQAPTNNGGFGQDQQQSQNQNYQSTNNDPFASDGKPIDISDDDLPF

ssb1

Single-stranded DNA-binding protein 1

163 amino acids

Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.

18.166 kDa

MINNVVLVGRMTRDAELRYTPSNQAVATFSLAVNRNFKNQSGEREADFINCVIWRQQAENLANWAKKGALVGITGRIQTRNYENQQGQRVYVTEVVAESFQLLESRATREGGSPNSYNNGGYNNAPSNNSYSASSQQTPNFSRDESPFGNSNPMDISDDDLPF

ssb1

Single-stranded DNA-binding protein 1

163 amino acids

Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.

18.166 kDa

MINNVVLVGRMTRDAELRYTPSNQAVATFSLAVNRNFKNQSGEREADFINCVIWRQQAENLANWAKKGALVGITGRIQTRNYENQQGQRVYVTEVVAESFQLLESRATREGGSPNSYNNGGYNNAPSNNSYSASSQQTPNFSRDESPFGNSNPMDISDDDLPF

ssb1

Single-stranded DNA-binding protein 1

162 amino acids

17.805 kDa

MARGLNKVMLIGHLGNDPERRETASGQSVVNFTLATSEGFKDSSGNLQERTEWHRIVAWGKLADICSQYLKKGRQVYIEGRLQTRSWDDNKTGDKKYATEIVCTDMQMLGAKDSGGGTSDASYSQNRPSYSRPSRPEPSSGNYGASPSSGGAQEFEKDDLPF

ssb1

Single-stranded DNA-binding protein 1

156 amino acids

17.674 kDa

MLNRTILVGRLTRDPELRTTQSGVNVASFTLAVNRTFTNAQGEREADFINIIVFKKQAENVNKYLSKGSLAGVDGRLQTRNYENKEGQRVYVTEVVADSIQFLEPKNTDDNQQDLYQQQAQQTRGQSQYSNNKPVKDNPFANANCPIEIDDNDLPF

ssb1

Single-stranded DNA-binding protein 1

156 amino acids

16.833 kDa

MNETMICAVGNVATTPVFRDLANGPSVRFRLAVTARYWDREKNAWTDGHTNFFTVWANRQLATNASGSLAVGDPVVVQGRLKVRTDVREGQSRTSADIDAVAIGHDLARGTAAFRRTARTEASTSPPRPEPNWEVPAGGTPGEPVPEQRPDPVPVG

ssb1

Single-stranded DNA-binding protein 1

150 amino acids

Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.

16.644 kDa

MINNVVLVGRLTRDPELRHTPQNQAVGTFGLAVNRQFKNANGEREADFINCVIWRQQAENLAKFAKKGALIGITGRIQTRNYENQQGQKVYVTEVVADTFQMLESNKTQGQQTSKPQAQNKKPQAPDPFKAPAADPFAGGTEISDDDLPF

ssb1

Single-stranded DNA-binding protein 1

136 amino acids

15.384 kDa

MASLNKMQLIGNLGADPDIRYMQDGTPTVTVSVATTDTWKDKDTGNKEEKTEWHRVVFFGGLAEIVGEFLKKGSQIYVEGALRSRNWTDKEGNKRYTTEIMAKEMQMLGKKQDNNKVGNARHGDALPADEDDYYDF

ssb1

Single-stranded DNA-binding protein 1

131 amino acids

14.788 kDa

MYNKVIAIGRLVAKPELVKTATDKHVARLSLAVNRRFKNASGEREADFISVVVWGKLAETLVSYASKGSLMSIDGELRTRKYDKDGQVHYVTEVLCQSFQLLESRAQRAMRENNVTNDLVDLVLEEDTLPF

ssb1

Single-stranded DNA-binding protein 1

130 amino acids

14.756 kDa

MINNVVLIGRLTKDVELRYTPSQVACAQFTLAVNRNFKNQDGQKEADFINCVIWRKSAENLSNWAKKGQLIAITGRIQTRNYENQQGQRVYVTEVVAESFQILEKRDNTANTSSLADSMPDYGPEPDLPF

ssb1

Single-stranded DNA-binding protein 1

119 amino acids

13.254 kDa

MSINIVTLVGRVGTDPDIKYFESGSVKCRLTLAVNRRSKNDKPDWFTLELWDKTAEVAGNYVRKGSLIGVKGSLKFDSWSDRQTGVNRSTPVIRVDQLELLGSKQDRDGGSSDFAPENF

ssb1

Single-stranded DNA-binding protein

119 amino acids

13.254 kDa

MSINIVTLVGRVGTDPDIKYFESGSVKCRLTLAVNRRSKNDKPDWFTLELWDKTAEVAGNYVRKGSLIGVKGSLKFDSWSDRQTGVNRSTPVIRVDQLELLGSKQDRDGGSSDFAPENF

ssb1

Single-stranded DNA-binding protein 1

110 amino acids

12.524 kDa

MNKILLIGRMTKNPSIKQIETTGNNRCNFTIAVNRRVRNTNGENEADFIPVTVWGKTAENVARYMKKGYLVGVSGRLQVRTYQDVDGNRKYITEVVGEEVQFLETKKEAV