TCEA2

Tuliposide A-converting enzyme 2, chloroplastic

382 amino acids

Lactone-forming carboxylesterases, specifically catalyzing intramolecular transesterification, but not hydrolysis. Involved in the biosynthesis of tulipalins, defensive chemicals that show antimicrobial activities against a broad range of strains of bacteria and fungi. Substrates are 6-tuliposide A > 6-tuliposide B.

Belongs to the AB hydrolase superfamily.

41.14 kDa

MSVASFFSSLPARPFGYKDGRGRTGMVSTTDIGRRMVKPPVLACRPIESNTYHGSVFLTKSSRSPSPSLSPTPTALDDEIVLDLKPFLIIYKSGRIERFLGTTVIPACPEVATKDVVIDPATGVSVRLYLPNVVDLPSKKLPVLVYFHGGGFVIENTGSPNYHNYLTLLAAKAGVLIVSINYRLAPEYPLPASYDDCMAGFNWVVSHSAGPALEPWLAQHGDFSQILLSGDSAGGNVTHYVAMRADAGVIEGVAIVHPYFLGSEPVGNEINDPANIEFHDKLWRLAAPDTEGLDDPLINPVAPGAPILAGLKCKRAVVFVAGNDFLVERGRMYYEALVKSGWGGEAELVQHEGVGHVFHLSDYSGDISVAMMTKLIAFLKGE

TCEA2

Transcription elongation factor A protein 2

300 amino acids

Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus (By similarity).

Belongs to the TFS-II family.

33.642 kDa

MMGKEEEIARIARRLDKMVTKKSAEGAMDLLRELKAMPVTLHLLQSTRVGMSVNALRKQSSDEEVVTLAKSLIKSWKKLLDASDAKARERRRGGSLPTSSSKEASEAQDPSRKRPELPRMPSTPRITTFPPVPVTCDAVRTKCREMLTAALQTDHDHVAIGADCECLAGQIEECIFRDVGNTDMKYKNRVRSRLSNLKDAKNPGLRRKVLCGAITPQQIAVMTSEEMASDELKEIRKAMTKEAIREHQMARTGGTQTDLFTCGKCRKKNCTYTQVQTRSSDEPMTTFVVCNECGNRWKFC

TCEA2

Transcription elongation factor A protein 2

299 amino acids

Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.

Belongs to the TFS-II family.

33.601 kDa

MMGKEEEIARIARRLDKMVTKKSAEGAMDLLRELKAMPITLHLLQSTRVGMSVNALRKQSSDEEVIALAKSLIKSWKKLLDASDAKARERGRGMPLPTSSRDASEAPDPSRKRPELPRAPSTPRITTFPPVPVTCDAVRNKCREMLTAALQTDHDHVAIGADCERLSAQIEECIFRDVGNTDMKYKNRVRSRISNLKDAKNPDLRRNVLCGAITPQQIAVMTSEEMASDELKEIRKAMTKEAIREHQMARTGGTQTDLFTCGKCRKKNCTYTQVQTRSSDEPMTTFVVCNECGNRWKFC

Tcea2

Transcription elongation factor A protein 2

299 amino acids

Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.

Belongs to the TFS-II family.

33.663 kDa

MGKEEEIARIARRLDKMVTRKNAEGAMDLLRELKNMPITLHLLQSTRVGMSVNALRKQSSDEELIALAKSLIKSWKKLLDVSDGKSRNQGRGTPLPTSSSKDASRTTDLSCKKPDPPRTPSTPRITTFPQVPITCDAVRNKCREMLTLALQTDHDHVAVGVNCEHLSSQIEECIFLDVGNTDMKYKNRVRSRISNLKDAKNPGLRRNVLCGAITPQQIAVMTSEEMASDELKEIRKAMTKEAIREHQMARTGGTQTDLFTCNKCRKKNCTYTQVQTRSSDEPMTTYVVCNECGNRWKFC

Tcea2

Transcription elongation factor A protein 2

299 amino acids

Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.

Belongs to the TFS-II family.

33.528 kDa

MGKEEEIARIARRLDKMVTRKNAEGAMDLLRELKNMPITLHLLQSTRVGMSVNALRKQSSDEELIALAKSLIKSWKKLLDVSDGKSRDQGRGTPLPTSSSKDASGTTDLSCKKPDPPRTSSTPRITTFPQVPITCDAVRNKCREMLTLALQTDHDHVAVGVSCEHLSSQIEECIFLDVGNTDMKYKNRVRSRISNLKDAKNPGLRRNVLCGAITPQQIAVMTSEEMASDELKEIRKAMTKEAIREHQMARTGGTQTDLFTCNKCRKKNCTYTQVQTRSSDEPMTTYVVCNECGNRWKFC