POLD1

DNA polymerase delta catalytic subunit

1107 amino acids

As the catalytic component of the trimeric (Pol-delta3 complex) and tetrameric DNA polymerase delta complexes (Pol-delta4 complex), plays a crucial role in high fidelity genome replication, including in lagging strand synthesis, and repair. Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities (PubMed:16510448, PubMed:19074196, PubMed:20334433, PubMed:24035200, PubMed:24022480). Requires the presence of accessory proteins POLD2, POLD3 and POLD4 for full activity. Depending upon the absence (Pol-delta3) or the presence of POLD4 (Pol-delta4), displays differences in catalytic activity. Most notably, expresses higher proofreading activity in the context of Pol-delta3 compared with that of Pol-delta4 (PubMed:19074196, PubMed:20334433). Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated (PubMed:24035200). Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation (PubMed:20227374). Under conditions of DNA replication stress, in the presence of POLD3 and POLD4, may catalyze the repair of broken replication forks through break-induced replication (BIR) (PubMed:24310611). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites (PubMed:19074196).

Belongs to the DNA polymerase type-B family.

123.631 kDa

MDGKRRPGPGPGVPPKRARGGLWDDDDAPRPSQFEEDLALMEEMEAEHRLQEQEEEELQSVLEGVADGQVPPSAIDPRWLRPTPPALDPQTEPLIFQQLEIDHYVGPAQPVPGGPPPSRGSVPVLRAFGVTDEGFSVCCHIHGFAPYFYTPAPPGFGPEHMGDLQRELNLAISRDSRGGRELTGPAVLAVELCSRESMFGYHGHGPSPFLRITVALPRLVAPARRLLEQGIRVAGLGTPSFAPYEANVDFEIRFMVDTDIVGCNWLELPAGKYALRLKEKATQCQLEADVLWSDVVSHPPEGPWQRIAPLRVLSFDIECAGRKGIFPEPERDPVIQICSLGLRWGEPEPFLRLALTLRPCAPILGAKVQSYEKEEDLLQAWSTFIRIMDPDVITGYNIQNFDLPYLISRAQTLKVQTFPFLGRVAGLCSNIRDSSFQSKQTGRRDTKVVSMVGRVQMDMLQVLLREYKLRSYTLNAVSFHFLGEQKEDVQHSIITDLQNGNDQTRRRLAVYCLKDAYLPLRLLERLMVLVNAVEMARVTGVPLSYLLSRGQQVKVVSQLLRQAMHEGLLMPVVKSEGGEDYTGATVIEPLKGYYDVPIATLDFSSLYPSIMMAHNLCYTTLLRPGTAQKLGLTEDQFIRTPTGDEFVKTSVRKGLLPQILENLLSARKRAKAELAKETDPLRRQVLDGRQLALKVSANSVYGFTGAQVGKLPCLEISQSVTGFGRQMIEKTKQLVESKYTVENGYSTSAKVVYGDTDSVMCRFGVSSVAEAMALGREAADWVSGHFPSPIRLEFEKVYFPYLLISKKRYAGLLFSSRPDAHDRMDCKGLEAVRRDNCPLVANLVTASLRRLLIDRDPEGAVAHAQDVISDLLCNRIDISQLVITKELTRAASDYAGKQAHVELAERMRKRDPGSAPSLGDRVPYVIISAAKGVAAYMKSEDPLFVLEHSLPIDTQYYLEQQLAKPLLRIFEPILGEGRAEAVLLRGDHTRCKTVLTGKVGGLLAFAKRRNCCIGCRTVLSHQGAVCEFCQPRESELYQKEVSHLNALEERFSRLWTQCQRCQGSLHEDVICTSRDCPIFYMRKKVRKDLEDQEQLLRRFGPPGPEAW

Pold1

DNA polymerase delta catalytic subunit

1105 amino acids

As the catalytic component of the trimeric (Pol-delta3 complex) and tetrameric DNA polymerase delta complexes (Pol-delta4 complex), plays a crucial role in high fidelity genome replication, including in lagging strand synthesis, and repair. Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities. Requires the presence of accessory proteins POLD2, POLD3 and POLD4 for full activity. Depending upon the absence (Pol-delta3) or the presence of POLD4 (Pol-delta4), displays differences in catalytic activity. Most notably, expresses higher proofreading activity in the context of Pol-delta3 compared with that of Pol-delta4. Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated. Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation. Under conditions of DNA replication stress, in the presence of POLD3 and POLD4, may catalyze the repair of broken replication forks through break-induced replication (BIR). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites.

Belongs to the DNA polymerase type-B family.

123.79 kDa

MDCKRRQGPGPGVPPKRARGHLWDEDEPSPSQFEANLALLEEIEAENRLQEAEEELQLPPEGTVGGQFSTADIDPRWRRPTLRALDPSTEPLIFQQLEIDHYVGSAPPLPEGPLPSRNSVPILRAFGVTDEGFSVCCHIQGFAPYFYTPAPPGFGAEHLSELQQELNAAISRDQRGGKELSGPAVLAIELCSRESMFGYHGHGPSPFLRITLALPRLMAPARRLLEQGVRVPGLGTPSFAPYEANVDFEIRFMVDADIVGCNWLELPAGKYVRRAEKKATLCQLEVDVLWSDVISHPPEGQWQRIAPLRVLSFDIECAGRKGIFPEPERDPVIQICSLGLRWGEPEPFLRLALTLRPCAPILGAKVQSYEREEDLLQAWADFILAMDPDVITGYNIQNFDLPYLISRAQALKVDRFPFLGRVTGLRSNIRDSSFQSRQVGRRDSKVISMVGRVQMDMLQVLLREHKLRSYTLNAVSFHFLGEQKEDVQHSIITDLQNGNEQTRRRLAVYCLKDAFLPLRLLERLMVLVNNVEMARVTGVPLGYLLTRGQQVKVVSQLLRQAMRQGLLMPVVKTEGSEDYTGATVIEPLKGYYDVPIATLDFSSLYPSIMMAHNLCYTTLLRPGAAQKLGLKPDEFIKTPTGDEFVKSSVRKGLLPQILENLLSARKRAKAELAQETDPLRRQVLDGRQLALKVSANSVYGFTGAQVGKLPCLEISQSVTGFGRQMIEKTKQLVESKYTVENGYDANAKVVYGDTDSVMCRFGVSSVAEAMSLGREAANWVSSHFPSPIRLEFEKVYFPYLLISKKRYAGLLFSSRSDAHDKMDCKGLEAVRRDNCPLVANLVTSSLRRILVDRDPDGAVAHAKDVISDLLCNRIDISQLVITKELTRAAADYAGKQAHVELAERMRKRDPGSAPSLGDRVPYVIIGAAKGVAAYMKSEDPLFVLEHSLPIDTQYYLEQQLAKPLLRIFEPILGEGRAESVLLRGDHTRCKTVLTSKVGGLLAFTKRRNCCIGCRSVIDHQGAVCKFCQPRESELYQKEVSHLNALEERFSRLWTQCQRCQGSLHEDVICTSRDCPIFYMRKKVRKDLEDQERLLQRFGPPGPEAW

POLD1

DNA polymerase delta catalytic subunit

1105 amino acids

This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction.

Belongs to the DNA polymerase type-B family.

123.757 kDa

MSSGGRGGKRRGAPPPGPSGAAAKRAHPGGTPQPPPPAATAAAPVAEEEDMMDEDVFLDETILAEDEEALLLLDRDEALASRLSRWRRPALPADLASGCSRNVAFQQLEIDYVIGESHKVLLPNSSGPAAILRIFGVTREGHSVCCQVHGFEPYFYISCPMGMGPDDISRFHQTLEGRMKDSNRNSNVPRFVKRIELVQKQTIMHYQPQQSQPFLKIVVALPTMVASCRGILERGITIEGLGSKSFLTYESNILFALRFMIDCNIVGGNWIEVPAGKYMKAARIMSYCQLELDCLYSDLVSHAAEGEHSKMAPFRILSFDIECAGRKGHFPEPTHDPVIQIANLVTLQGEGQPFVRNVMTLKSCSPIVGVDVMSFDTERDVLLAWRDFIREVDPDIIIGYNICKFDLPYLIERAEVLKIVEFPILGRIRNSRVRVRDTTFSSRQYGMRESKDVAVEGRVQFDLLQAMQRDYKLSSYSLNSVSAHFLGEQKEDVHHSIISDLQNGNSETRRRLAVYCLKDAYLPQRLLDKLMYIYNYVEMARVTGVPISFLLSRGQSIKVLSQLLRKAKQKNLVIPNIKGQASGQDTFEGATVLEARAGFYEKPIATLDFASLYPSIMMAYNLCYCTLVPPEDARKLNLPPESVNKTPSGETFVKPDVQKGILPEILEELLAARKRAKADLKEAKDPFERAVLDGRQLALKISANSVYGFTGATVGQLPCLEISSSVTSYGRQMIEHTKKLVEDKFTTLGGYEHNAEVIYGDTDSVMVQFGVSTVEDAMKLGREAADYISGTFIKPIKLEFEKIYFPYLLISKKRYAGLYWTNPEKFDKMDTKGIETVRRDNCLLVKNLVTECLHKILVDRDVPGAVQYVKNTISDLLMNRVDLSLLVITKGLTKTGEDYAVKAAHVELAERMRKRDAATAPTVGDRVPYVIIKAAKGAKAYERSEDPIYVLDNNIPIDPQYYLENQISKPLLRIFEPILKNASRELLHGSHTRAVSISTPSNSGIMKFAKKQLTCLGCKAVISGSNQTLCFHCKGREAELYCKTVGNVSELEMLFGRLWTQCQECQGSLHQDVLCTSRDCPIFYRRRKAQKDMAEARVQLQRWDF

pold1

DNA polymerase delta catalytic subunit

1104 amino acids

Possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction.

Belongs to the DNA polymerase type-B family.

125.346 kDa

MKRSIVTGGGNNDKKFKAQPPPKNNYRGGGDDEEDDEFEEDDDEDEGDEFGEEEDEDDIDVENIIASDSMDIDIQDDGSQQLFLWSRKPVQDLVPHKKPLIFQQLEVDYTEIKEPVPGMPGPKVGPLPAIRLFGVTKEGNSVLCKVHGFLPYFFISCPPGFTEADCKSLKHDLNESMKMSSNQSNEKDIENIVVSIDIEKKKSIMGYNPNPLSDFIRITLILPKFVTRCREIFESGRHHFTIPGQPFRQYQTYESNILFALRFLIDKGITGCSWIELPANTYKLSETPVSTCQIEVDTSLETIISLSDDDSPAPYRILSFDIECAGRKGVFPEPEKDPVIQISNIVKNNGDAEPFIKNIFTLKGCSSIVGAHVIPHKREEDLLREWRKFVIKVDPDVIIGYNIVNFDIPYLISRARQLKIPEFALLGRIKTTISKIKSTRFSSSNLGTRESKEISMPGRTQFDLMQAIQRDHKLTSYSLNNVSAHFLKEQKEDVHFSIISDLQNGTDDDRRRLAVYCIKDAVLPMRLLDKLMILINYTEMARVTGVPLSYLLGRGEGIKVLSQLYRKAMVENFLIPTYKVTGKGEKFQGAIVIEPTPGFYDTPIATLDFTSLYPSIMMAHNLCYSTLLSAEEAKKLPPEIYTTTPFGDHFIKSDTKKGLLPRILEELLSARKKAKDELKNEKDPFKRAVLDGRQLALKISANSVYGFTGARVGKLPCLEISRSVTSFGREMLDKTKKIVEERYTIANGYKHDAVIIYGDTDSVMVKFGVKTVAEAMEMGRDAAKFVTTTFIRPINLDFEKVYYPYLLMAKKKYAGLYWTKPDIHDRMDVKGLEMVRRDTCLLVRNVVSTILKKILIEKDLKSAEEYTKSVISDLLQNRLDLSMLVITKALSKTQYKGKVIHNELARKMRARDPATAPNLGDRVPYVVIQGSKGAPIYEKAEDPLYALEHNILLDCQYYLDKQLKAPLIRIFKPIMSNPDLIFHGEHTRTIAQSTLSDNNKGFFGTLKKKKVCMNCPKELTDTESTTCINCQHKEASLYQTSLEKVTSLETKFSEAWTQCQRCSGSLHQPVLCSNRDCPIFYMRTKVQLDLIEAKKTLNRFNVEW

POLD1

DNA polymerase delta catalytic subunit

1103 amino acids

As the catalytic component of the trimeric (Pol-delta3 complex) and tetrameric DNA polymerase delta complexes (Pol-delta4 complex), plays a crucial role in high fidelity genome replication, including in lagging strand synthesis, and repair. Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities. Requires the presence of accessory proteins POLD2, POLD3 and POLD4 for full activity. Depending upon the absence (Pol-delta3) or the presence of POLD4 (Pol-delta4), displays differences in catalytic activity. Most notably, expresses higher proofreading activity in the context of Pol-delta3 compared with that of Pol-delta4. Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated. Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation. Under conditions of DNA replication stress, in the presence of POLD3 and POLD4, may catalyze the repair of broken replication forks through break-induced replication (BIR). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites.

Belongs to the DNA polymerase type-B family.

123.466 kDa

MDFKRRQGPGPGVPPKRARGGLWDEDEPSQFEENLALLEEIEAENRLQEAEEELQLPPQGPAGGQFSTADIDPRWKRPALCALDPNTEPLIFQQLEIDHYVGSAVPLPGGPPTSCNSVPILRAFGVTDEGFSVCCHIHGFAPYFYTPAPPGFGAEHLSDLQRELSTAISRDQRGGKELSGPAVLAIELCSRESMFGYHGHGPSPFLRITLALPRLVAPARRLLEQGIRVPGLGTPSFAPYEANVDFEIRFMVDADIVGCNWLELPAGKYVWRTEKKATQCQLEVDVLWSDVISHPPEGQWQRIAPLRVLSFDIECAGRKGIFPEPERDPVIQICSLGLRWGEPEPFLRLALTLRPCAPILGAKVQSYEREEDLLQAWPNFILAMDPDVITGYNIQNFDLPYLISRAQTLKVDRFPFLGRVTGLRSNIRDSSFQSRQVGRRDSKVVSMVGRVQMDMLQVLLREHKLRSYTLNAVSFHFLGEQKEDVQHSIITDLQNGNEQTRRRLAVYCLRDAFLPLRLLERLMVLVNNVEMARVTGVPLGYLLSRGQQVKVVSQLLRQAMRQGLLMPVVKTEGGEDYTGATVIEPLKGYYDVPIATLDFSSLYPSIMMAHNLCYTTLLRPGAAQKLGLKPDEFIKTPTGDEFVKSSVRKGLLPQILENLLSARKRAKAELAQETDPLRRQVLDGRQLALKVSANSVYGFTGAEVGKLPCLEISQSVTGFGRQMIEKTKQLVESKYTLENGYNANAKVVYGDTDSVMCRFGVSSVAEAMSLGREAANWVSSHFPSPIRLEFEKVYFPYLLISKKRYAGLLFSSQPDTHDRMDCKGLEAVRRDNCPLVANLVTSSLRRILVDRDPDGAVAHAKDVISDLLCNRIDISQLVITKELTRAAADYAGKQAHVELAERMRKRDPGSAPSLGDRVPYVIIGAAKGVAAYMKSEDPLFVLEHSLPIDTQYYLGQQLAKPLLRIFEPILGEGRAESVLLRGDHTRCKTVLTSKVGGLLAFTKRRNCCIGCRSVINHQGAVCEFCQPRESELYQKEVSHLNALEERFSRLWTQCQRCQGSLHEDVICTSRDCPIFYMRKKVRKDLEDQERLLQRFGPPGPEAW

Pold1

DNA polymerase delta catalytic subunit

1103 amino acids

As the catalytic component of the trimeric (Pol-delta3 complex) and tetrameric DNA polymerase delta complexes (Pol-delta4 complex), plays a crucial role in high fidelity genome replication, including in lagging strand synthesis, and repair. Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities. Requires the presence of accessory proteins POLD2, POLD3 and POLD4 for full activity. Depending upon the absence (Pol-delta3) or the presence of POLD4 (Pol-delta4), displays differences in catalytic activity. Most notably, expresses higher proofreading activity in the context of Pol-delta3 compared with that of Pol-delta4. Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated. Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation. Under conditions of DNA replication stress, in the presence of POLD3 and POLD4, may catalyze the repair of broken replication forks through break-induced replication (BIR). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites.

Belongs to the DNA polymerase type-B family.

123.601 kDa

MDGKRRQAPSSGVPPKRACKGLWDEDEPSQFEENLALLEEIEAENRLQEAEEELQLPPEGIVGGQFSTADIDPRWLRPTPLALDPSTEPLIFQQLEIDHYVGTSPPLPEGPPASRNSVPILRAFGVTDEGFSVCCHIHGFAPYFYTPAPPGFGAEHLSELQRELNAAISRDQRGGKELSGPAVLAIELCSRESMFGYHGHGPSPFLRITLALPRLMAPARRLLEQGIRVPGLGTPSFAPYEANVDFEIRFMVDADIVGCNWLELPAGKYVRRAEKKATLCQLEVDVLWSDVISHPPEGQWQRIAPLRVLSFDIECAGRKGIFPEPERDPVIQICSLGLRWGEPEPFLRLALTLRPCAPILGAKVQSYEREEDLLQAWATFILAMDPDVITGYNIQNFDLPYLISRAQTLKVDRFPFLGRVTGLRSNIRDSSFQSRQVGRRDSKVVSMVGRVQMDMLQVLLREYKLRSYTLNAVSFHFLGEQKEDVQHSIITDLQNGNEQTRRRLAVYCLKDAFLPLRLLERLMVLVNNVEMARVTGVPLGYLLSRGQQVKVVSQLLRQAMREGLLMPVVKTEGGEDYTGATVIEPLKGYYDVPIATLDFSSLYPSIMMAHNLCYTTLLRPGAAQKLGLKPDEFIKTPTGDEFVKASVRKGLLPQILENLLSARKRAKAELAQETDPLRRQVLDGRQLALKVSPNSVYGFTGAQVGKLPCLEISQSVTGFGRQMIEKTKQLVETKYTLENGYDANAKVVYGDTDSVMCRFGVSSVAEAMSLGREAANWVSSHFPSPIRLEFEKVYFPYLLISKKRYAGLLFSSRSDAHDRMDCKGLEAVRRDNCPLVANLVTSSLRRILVDRDPDGAVAHAKDVISDLLCNRIDISQLVITKELTRAAADYAGKQAHVELAERMRKRDPGSAPNLGDRVPYVIIGAAKGVAAYMKSEDPLFVLEHSLPIDTQYYLEQQLAKPLLRIFEPILGEGRAESVLLRGDHTRCKTVLTSKVGGLLAFTKRRNSCIGCRSVIDHQGAVCKFCQPRESELYQKEVSHLNALEERFSRLWTQCQRCQGSLHEDVICTSRDCPIFYMRKKVRKDLEDQERLLQRFGPPGPEAW

POLD1

DNA polymerase delta catalytic subunit

1094 amino acids

This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction.

Belongs to the DNA polymerase type-B family.

126.884 kDa

MEELKTCPFTNVIPYGLLYDKLKKEKNNDVPENYVIEEFDKLLKNYERPNVYDEIGNATFKNDEDLITFQIDLDYTVENIFKNMIYNESGSNNSILNDIYMPYRILLSKDKNYVSVPIIRIYSLRKDGCSVLINVHNFFPYFYVEKPDDFDNEDLIKLEMLMNENLNLNSQYKIYEKKILKIEIVKTESLMYFKKNGKKDFLKITVLLPKMVPSLKKYFEGIVHVNNKSIGGIVYEANLPFILRYIIDHKITGSSWINCKKGHYYIRNKNKKISNCTFEIDISYEHVEPITLENEYQQIPKLRILSFDIECIKLDGKGFPEAKNDPIIQISSILYFQGEPIDNCTKFIFTLLECASIPGSNVIWFNDEKTLLEAWNEFIIRIDPDFLTGYNIINFDLPYILNRGTALNLKKLKFLGRIKNVASTVKDSSFSSKQFGTHETKEINIFGRIQFDVYDLIKRDYKLKSYTLNYVSFEFLKEQKEDVHYSIMNDLQNESPESRKRIATYCIKDGVLPLRLIDKLLFIYNYVEMARVTGTPFVYLLTRGQQIKVTSQLYRKCKELNYVIPSTYMKVNTNEKYEGATVLEPIKGYYIEPISTLDFASLYPSIMIAHNLCYSTLIKSNHEVSDLQNDDITTIQGKNNLKFVKKNVKKGILPLIVEELIEARKKVKLLIKNEKNNITKMVLNGRQLALKISANSVYGYTGASSGGQLPCLEVAVSITTLGRSMIEKTKERVESFYCKSNGYEHNSTVIYGDTDSVMVKFGTNNIEEAMTLGKDAAERISKEFLSPIKLEFEKVYCPYLLLNKKRYAGLLYTNPNKHDKMDCKGIETVRRDFCILIQQMMETVLNKLLIEKNLNSAIEYTKSKIKELLTNNIDMSLLVVTKSLGKTDYETRLPHVELAKKLKQRDSATAPNVGDRVSYIIVKGVKGQAQYERAEDPLYVLDNNLAIDYNHYLDAIKSPLSRIFEVIMQNSDSLFSGDHTRHKTILTSSQTALSKFLKKSVRCIGCNSSIKKPPLCNHCKENKEFSIYMQKIKDFKNKQNEFFQLWTECQRCQGNLHVDVICMNRDCPIFYRRAKIKKDIANLQEQVTSLRMDW

POLD1

DNA polymerase delta catalytic subunit

1088 amino acids

This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction.

Belongs to the DNA polymerase type-B family.

123.188 kDa

MTQEEEFMDEDVFINETLVSEDEESLILRDIEQRQALANRLSKWTRPPLSAGYVAQSRSVLFQQLEIDYVIAESHGELLPNSSGPVAIIRIFGVTKEGHSVCCNVHGFEPYFYICCPPGMGPDDISHFHQTLEGRMREANRNSNVGKFVRRIEMVQRRSIMYYQQSNSQPFLKIVVALPTMVASCRGILDRGIQLDGLGMKSFLTYESNVLFALRFMIDCNIVGGNWIGIPAGKYKKTAKSLSYCQLEFDCLYSELISHAPEGEYSKMAPFRILSFDIECAGRKGHFPEPTHDPVIQIANLVTLQGEDQPFIRNVMTLKSCSPIVGVDVMPFETEREVLLAWRDFIREVDPDIIIGYNICKFDLPYLIERALNLKIAEFPILGRIRNSRVRVKDTTFSSRQYGTRESKEVAVEGRVTFDLLQVMQRDYKLSSYSLNSVSSHFLSEQKEDVHHSIISDLQNGNAETRRRLAVYCLKDAYLPQRLLDKLMFIYNYVEMARVTGVPISFLLSRGQSIKVLSQLLRRARQKNLVIPNAKQAGSEQGTFEGATVLEARAGFYEKPIATLDFASLYPSIMMAYNLCYCTLVIPEDARKLNIPPESVNRTPSGETFVKSNLQKGILPEILEELLTARKRAKADLKEAKDPLEKAVLDGRQLALKISANSVYGFTGATIGQLPCLEISSSVTSYGRQMIEHTKKLVEDKFTTLNGYEHNAEVIYGDTDSVMVQFGVSAVEEAMNLGREAAEHISGTFTKPIKLEFEKVYYPYLLISKKRYAGLFWTKPDNFDKMDTKGIETVRRDNCLLVKNLVNDCLHKILIDRDIPGAVQYVKNAISDLLMNRMDLSLLVITKGLTKTGDDYEVKAAHVELAERMRKRDAATAPNVGDRVPYVIIKAAKGAKAYERSEDPIYVLENNIPIDPHYYLENQISKPILRIFEPILKNASKELLHGSHTRSISISTPSNSGILRFAKKQLPALVVKLYLARVITLSVHIAKEGRLSCTVKQYLKCLSWRCFLGGCGHSVRSAKVHFIRMFSAPVGIVQFSIDEKRHRKIWVKQSCNWTDGTSKFCQEFDLADLFEPMDTNTIWCLPQS