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Database: UniProt
Entry: A0A0C5WYL2_9GAMM
LinkDB: A0A0C5WYL2_9GAMM
Original site: A0A0C5WYL2_9GAMM 
ID   A0A0C5WYL2_9GAMM        Unreviewed;      1151 AA.
AC   A0A0C5WYL2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969};
DE            Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969};
DE            EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969};
GN   Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969};
GN   ORFNames=H744_2c1467 {ECO:0000313|EMBL:AJR08145.1};
OS   Photobacterium gaetbulicola Gung47.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR08145.1, ECO:0000313|Proteomes:UP000032303};
RN   [1] {ECO:0000313|EMBL:AJR08145.1, ECO:0000313|Proteomes:UP000032303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gung47 {ECO:0000313|EMBL:AJR08145.1,
RC   ECO:0000313|Proteomes:UP000032303};
RA   Kim Y.-O.;
RT   "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT   gaetbulicola Gung47.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00969}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC       RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC       {ECO:0000256|HAMAP-Rule:MF_00969}.
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DR   EMBL; CP005974; AJR08145.1; -; Genomic_DNA.
DR   RefSeq; WP_044622944.1; NZ_CP005974.1.
DR   AlphaFoldDB; A0A0C5WYL2; -.
DR   STRING; 658445.H744_2c1467; -.
DR   KEGG; pgb:H744_2c1467; -.
DR   PATRIC; fig|658445.3.peg.3379; -.
DR   HOGENOM; CLU_005122_1_3_6; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000032303; Chromosome 2.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR   CDD; cd17991; DEXHc_TRCF; 1.
DR   Gene3D; 2.40.10.170; -; 1.
DR   Gene3D; 3.40.50.11140; -; 1.
DR   Gene3D; 3.40.50.11180; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR   Gene3D; 3.90.1150.50; Transcription-repair-coupling factor, D7 domain; 1.
DR   HAMAP; MF_00969; TRCF; 1.
DR   InterPro; IPR003711; CarD-like/TRCF_RID.
DR   InterPro; IPR036101; CarD-like/TRCF_RID_sf.
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; IPR048635; MFD_D3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047112; RecG/Mfd.
DR   InterPro; IPR037235; TRCF-like_C_D7.
DR   InterPro; IPR005118; TRCF_C.
DR   InterPro; IPR041471; UvrB_inter.
DR   NCBIfam; TIGR00580; mfd; 1.
DR   PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR   Pfam; PF02559; CarD_TRCF_RID; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF21132; MFD_D3; 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; CarD-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR   SUPFAM; SSF143517; TRCF domain-like; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00969}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00969};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00969};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00969}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00969};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00969}; Reference proteome {ECO:0000313|Proteomes:UP000032303}.
FT   DOMAIN          619..780
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          802..955
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1151 AA;  129569 MW;  CC188CB7C3024305 CRC64;
     MKDQSILSLP LPSKTGDSRF IGNVSGAALA LSVAELAHDH QGPILAVVPD TQTALRLQPE
     ISQFSAQEVS VFPDWETLPY DNFSPHQDII SDRLTRLYSL PQQANGVVLV PISTLLQRLT
     PRAFIHQHAL MVRNGDKLSL EKLRLQLEAS GYRHVDQVIE HGEYASRGSL IDLFPMGSNQ
     PYRIDFFDDE VDSIRQFDPE NQRSTGEIEH IRLLPAHEFP TDEIAIENFR MRWRERFEAR
     REPESIYQQV SKRTWPAGIE YWQPLFFEQT ETLFDYLPDN SLLITIGTLE PAVDQFLADA
     EYRFEQRRVD PLRPLLEPKE LWLTKDEMFS HFKTLPQVRI RPDNEPEKAG RYNLPLQAIP
     KLTINHQLKE PLAELRRFAE SYPGKIVFSV ASEGRREALL DLLARIKLRP VVAPTLTEAL
     ATPGKFSLVI GAAEQGFVLE KPEVALICES DLLGERVVQR RRRDEKKSVN ADTIIRNLAE
     LKVGQPVVHI DHGIGRYQGL QTLEAGGMKT EYVTLEYQGG AKLYVPVASL HLISRYSGGA
     EDTAPIHKLG GEAWVKARKK AAEKVRDVAA ELLDVYAKRE LKPGHKFKLD REAYADFCTG
     FPFEETHDQA LAINAVLSDM CQAKAMDRLV CGDVGFGKTE VAMRAAFVAV DNSKQVTVLV
     PTTLLAQQHF ENFRDRFANT PVRVEVLSRF KTAKEQKQIL ADMAEGKIDI LIGTHKLLNA
     SVDYHDLGLL IVDEEHRFGV RQKEKLKAIR ADVDILTLTA TPIPRTLNMA MSGMRDLSII
     ATPPARRLAI KTFVRESDDA LVREAVLREI MRGGQVYFLH NDVDSIEKTA EDLAKLIPEA
     RITFAHGQMR ERELEKIMSD FYHQRFNLLV CTTIIETGID VPTANTIVIN RADHLGLAQL
     HQLRGRVGRS HHQAYAYLLT PHPKRMTKDA VKRLEAISSL EDLGAGFTLA THDLEIRGAG
     ELLGDEQSGQ IQSVGFTLYM EMLEQAVEAL KEGKEPSLDD LLRQQTEVEL RLPALLPEDF
     IPDINTRLSL YKRIASANSE KALDELKVEL IDRFGLLPDP TTNLLVLNKI KLKAAGIGVR
     KIEAGEKGGF IEFTPNANID PGLLVGLLQS QPQHFRMEGP TKLKVMAPMS DRKDRIKYVD
     GLLTKLAENA L
//
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