| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Transcription-repair-coupling factor |
Protein Synonyms/Alias | TRCF |
Gene Name | mfd |
Gene Synonyms/Alias | SPD_0006 |
Created Date | 3-June-2014 |
Organism | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
NCBI Taxa ID | 373153 |
Phosphorylation | Position | Peptide | Code | Type | References | | 1119 | YFKALSVTNLKAGIA | T | HTP | [1] | | 786 | MLGIRDLSVIETPPT | S | HTP | [1] | | 767 | QVDVLTLTATPIPRT | T | HTP | [1] | | 765 | KKQVDVLTLTATPIP | T | HTP | [1] | |
Reference | [1]Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae. Sun X,Ge F,Xiao CL,Yin XF,Ge R,Zhang LH,He QY J. Proteome Res. 2010, Jan;9(1):275-82. [ PMID:19894762] |
Functional Description From UniProt | FUNCTION: Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site (By similarity) |
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| ATP-binding; Completeproteome; Cytoplasm; DNAdamage; DNArepair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding |
Protein Sequence | MVTLLDLFSE NDQIKKWHQN LTDKKRQLIL GLSTSTKALA IASSLEKEDR IVLLTSTYGE 60
AEGLVSDLIS ILGEELVYPF LVDDAPMVEF LMSSQEKIIS RVEALRFLTD SSKKGILVCN 120
IAASRLILPS PNAFKDSIVK ISVGEEYDQH AFIHQLKENG YRKVTQVQTQ GEFSLRGDIL 180
DIFEISQLEP CRIEFFGDEI DGIRSFEVET QLSKENKTEL TIFPASDMLL REKDYQRGQS 240
ALEKQISKTL SPILKSYLEE ILSSFHQKQS HADSRKFLSL CYDKTWTVFD YIEKDTPIFF 300
DDYQKLMNQY EVFERELAQY FTEELQNSKA FSDMQYFSDI EQIYKKQSPV TFFSNLQKGL 360
GNLKFDKIYQ FNQYPMQEFF NQFSFLKEEI ERYKKMDYTI ILQSSNSMGS KTLEDMLEEY 420
QIKLDSRDKT SICKESVNLI EGNLRHGFHF VDEKILLITE HEIFQKKLKR RFRRQHVSNA 480
ERLKDYNELE KGDYVVHHIH GIGQYLGIET IEIKEIHRDY VSVQYQNGDQ ISIPVEQIHL 540
LSKYISSDGK APKLNKLNDG HFKKAKQKVK NQVEDIADDL IKLYSERSQL KGFAFSADDD 600
DQDAFDDAFP YVETDDQLRS IEEIKRDMQA SQPMDRLLVG DVGFGKTEVA MRAAFKAVND 660
HKQVVILVPT TVLAQQHYTN FKERFQNFAV NVDVLSRFRS KKEQTATLEK LKNGQVDILI 720
GTHRVLSKDV VFADLGLMII DEEQRFGVKH KETLKELKKQ VDVLTLTATP IPRTLHMSML 780
GIRDLSVIET PPTNRYPVQT YVLEKNDSVI RDAVLREMER GGQGYYLYNK VDTIVQKVSE 840
LQELIPEASI GYVHGRMSEV QLENTLLDFI EGQYDILVTT TIIETGVDIP NANTLFIENA 900
DHMGLSTLYQ LRGRVGRSNR IAYAYLMYRP EKSISEVSEK RLEAIKGFTE LGSGFKIAMR 960
DLSIRGAGNL LGKSQSGFID SVGFELYSQL LEEAIAKRNG NANANTRTKG NAELILQIDA 1020
YLPDTYISDQ RHKIEIYKKI RQIDNRVNYE ELQEELIDRF GEYPDVVAYL LEIGLVKSYL 1080
DKVFVQRVER KDNKITIQFE KVTQRLFLAQ DYFKALSVTN LKAGIAENKG LMELVFDVQN 1140
KKDYEILEGL LIFGESLLEI KESKEKNSI 1169 |
| GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell GO:0005524 F:ATP binding IEA:UniProtKB-HAMAP GO:0008026 F:ATP-dependent helicase activity IEA:InterPro GO:0003684 F:damaged DNA binding IEA:InterPro GO:0006355 P:regulation of transcription, DNA-templated IEA:UniProtKB-HAMAP GO:0000716 P:transcription-coupled nucleotide-excision repair, DNA damage recognition IEA:UniProtKB-HAMAP |
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