MFD_SYNY3
ID MFD_SYNY3 Reviewed; 1199 AA.
AC Q55750;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Transcription-repair-coupling factor {ECO:0000255|HAMAP-Rule:MF_00969};
DE Short=TRCF {ECO:0000255|HAMAP-Rule:MF_00969};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_00969};
GN Name=mfd {ECO:0000255|HAMAP-Rule:MF_00969}; OrderedLocusNames=sll0377;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA
CC polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent
CC release of RNAP and its truncated transcript from the DNA, and
CC recruitment of nucleotide excision repair machinery to the damaged
CC site. {ECO:0000255|HAMAP-Rule:MF_00969}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC {ECO:0000255|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC RecG subfamily. {ECO:0000255|HAMAP-Rule:MF_00969}.
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DR EMBL; BA000022; BAA10395.1; -; Genomic_DNA.
DR PIR; S76549; S76549.
DR AlphaFoldDB; Q55750; -.
DR SMR; Q55750; -.
DR IntAct; Q55750; 4.
DR STRING; 1148.1001661; -.
DR PaxDb; Q55750; -.
DR EnsemblBacteria; BAA10395; BAA10395; BAA10395.
DR KEGG; syn:sll0377; -.
DR eggNOG; COG1197; Bacteria.
DR InParanoid; Q55750; -.
DR OMA; WAPPCRE; -.
DR PhylomeDB; Q55750; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0043175; F:RNA polymerase core enzyme binding; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.1150.50; -; 1.
DR HAMAP; MF_00969; TRCF; 1.
DR InterPro; IPR036101; CarD-like/TRCF_dom_sf.
DR InterPro; IPR003711; CarD-like/TRCF_domain.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR004576; Mfd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR037235; TRCF-like_C_D7.
DR InterPro; IPR005118; TRCF_C.
DR InterPro; IPR041471; UvrB_inter.
DR Pfam; PF02559; CarD_CdnL_TRCF; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF03461; TRCF; 1.
DR Pfam; PF17757; UvrB_inter; 1.
DR SMART; SM01058; CarD_TRCF; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00982; TRCF; 1.
DR SUPFAM; SSF141259; SSF141259; 1.
DR SUPFAM; SSF143517; SSF143517; 1.
DR SUPFAM; SSF52540; SSF52540; 3.
DR TIGRFAMs; TIGR00580; mfd; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1199
FT /note="Transcription-repair-coupling factor"
FT /id="PRO_0000102174"
FT DOMAIN 660..822
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT DOMAIN 847..997
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT MOTIF 775..778
FT /note="DEEQ box"
FT BINDING 673..680
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
SQ SEQUENCE 1199 AA; 134536 MW; 4D4C32AF60BAC1C9 CRC64;
MAEPRAVLKQ GNRNRDKDSV GLGNRLRFVS ISSALNPMTF SSILRHLQTL PLSKDLREKL
QKRGHVQLSG LPRLPKGLIV SSLAQSLEKN LLVITATLEE AGRWTAQLEL MGWQTVNFYP
TSEASPYDPG RLESEMVWGQ MQVLAELIQG HQVKGKAIVA TEKALQPHLP PVATLREYCL
ALRRGQEMDS KSLELTLARL GYERGSTVET EGQWSRRGDI VDIFPVSAEL PVRLEWFGDE
LEKIREFDPA SQRSLDDLTG LVLTPTSFDQ VIEPALNAQA IDLSAWGEDA ETEQLFGKEG
LQRFLGLAFT EPACLLDYLP TETVCVLDEP EQCAAHSERW FEAVAQDWSA LQLPNLPQLH
RNFSALGDRL KTDFQYITLS EIHEANGDSL DISARPIPTM PHQFAKLAEI LRGKREIYSG
LTLGQYSTWL ISAQPSRTVS LLQEHDCAVQ FIANPRDYPA IEKSQIQRTA VTLKYSGLAE
LEGFILPTFR LVLVTDRELF GQHALATPEY VRKRRRATSK QVDINKLSPG DYVVHKSHGI
GKFLKLDALA NREYLMIQYA DGILRVPADS LDSLSRFRHT GTRPPELHKM GGKVWEATKN
KVRKAVKKLA VDLLNLYAKR AKQVGYAYPP DSPWQQELED SFPYQPTPDQ LKAVQDVKRD
LEGDRPMDRL VCGDVGFGKT EVAVRAIFKA VTSGNKQVAL LAPTTVLTQQ HYHTLKERFA
PYPITIGLLN RFRTASEKKE ILAKLKSGEL DIVVGTQQVL GTSVKFKDLG LLVIDEEQRF
GVNQKEKIKT LKTEVDVLTL TATPIPRTLY MSLSGIREMS LITTPPPSRR PIKTHLSPYN
PEVIRTAIRN ELDRGGQVFY VVPRIEGIEE LGGQLRQMVP SARIAIGHGQ MEESELESTM
LAFNDGEADI LVCTTIIEAG LDIPRVNTII VEDAQKFGLA QLYQLRGRVG RSGIQAHAWL
LYPNQKQLTE KARLRLRALQ EFSQLGSGYQ LATRDMEIRG VGNLLGAEQS GQMEAIGYEF
YMEMLQDAIK EIQGQEIPKV EDTQIDLPLT AFIPSDYIPD LEEKMAAYRR ITSIESTDEL
PKIALDWGDR YGMLPSPVEE LFKVVKLKHL AKSLGFSRIK VEGKQNLVLE TPMEEPAWKL
LAENLPNHLQ SRFVYSAKKV VVRGLGVLAP AKQMDNLIDW FGKMQGALPE TKMETLVGK
