ID A0A2N0WN72_9GAMM Unreviewed; 1155 AA.
AC A0A2N0WN72;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=CW748_12950 {ECO:0000313|EMBL:PKF55406.1};
OS Alteromonadales bacterium alter-6D02.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX NCBI_TaxID=2058087 {ECO:0000313|EMBL:PKF55406.1, ECO:0000313|Proteomes:UP000233605};
RN [1] {ECO:0000313|EMBL:PKF55406.1, ECO:0000313|Proteomes:UP000233605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alter-6D02 {ECO:0000313|Proteomes:UP000233605};
RX PubMed=27311813; DOI=.1038/ncomms11965;
RA Datta M.S., Sliwerska E., Gore J., Polz M.F., Cordero O.X.;
RT "Microbial interactions lead to rapid micro-scale successions on model
RT marine particles.";
RL Nat. Commun. 7:11965-11965(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKF55406.1}.
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DR EMBL; PIZK01000023; PKF55406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0WN72; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000233605; Unassembled WGS sequence.
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 CDD; cd18810; SF2_C_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:UP000233605}.
FT DOMAIN 621..782
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 795..957
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1155 AA; 129974 MW; 108EFB053625E00A CRC64;
MPLSTQLLNT IPSLSDNNIT LANLRGSALP LAMIEAAQQH DGLNVLICSD TSTALKLETE
LSFLGQEHGL PVLLFPDWET LPYDNFSPHQ DIISQRLETL YRLPSMTNGI LIVPIATTMA
KLAPKQYLQG NTILLSVDQQ HDAAQFKSQL EMAGYQNVHQ VLAHGEYSQR GSILDIYPMG
SNQPYRIDYI DDEIDSIAFF DPETQRSKDK VSQIRILPAH EFPTTKLAIE QFRSNWRDKF
SASNEAESIY QQVSKRVLPA GIEYYLPLFF AACDSLFDYL PQNTQLLSVG DIHQSANEYW
NDVAARYEER RYDRQRPILA PEDLFNRVEQ TFSQLKTFHR IDFTQQPVEE KAGKFNINAH
DITGIAVNHQ LDHPTADLLQ YLTQHQDHQI IFCVESLGRS QALLELLAKD KIKPIVCDSF
IHAIKQKLAI VVSPLENSVK LPTLALSLIC ESELFGIQVS QRRRREKAQT ISSEAIVRSL
AELSIGQPVV HYDHGVGRYQ GLTYIENGGI NVEYVTLEYA SEAKLYVPVS SLNLISRYSG
ASEDSAPLHH LGSDKWTKAK RKAAEKVRDV AAELLDIYAQ RAAKKGYKFN LNHDEYNQFS
AGFPFEETVD QQNAILHVVN DMQKPTAMDR LVCGDVGFGK TEVAMRAAFV AVNDAKQVAI
LVPTTLLAQQ HFENFRDRFA NTAIKVEQLS RFRSAKQQQQ TIDELADGKI DIIIGTHKLI
QGDIKFADLG LLIVDEEHRF GVRQKEKIKA LRADIDILTM TATPIPRTLN MAMSGMRDLS
IIATPPSRRL SVNTFVREYD EAIVKEAVRR EIMRGGQVYF LHNDVDKIED MAQDLEQLLP
EARIGIAHGQ MRERELEKVM SDFYHQRYNV LLCSTIIETG IDIPSANTII INRADKFGLA
QLHQLRGRVG RSHHQAYAYL LTPNQKNLSK DAIKRLEAIE SLTDLGAGFV LATHDLEIRG
AGELLGDDQS GQIQTIGFSL YMEMLDGATN ALKNGETPAL DNLLPQGGDV DLKIAALLPD
DYIFDVNTRL SLYKRVANCR NQKQLDALQV ELIDRFGLLP DAAKNLFVIT RIKQRICALG
IDRLEAGING GQIVFSNRSK VDLGYLLTLL QQQPSIYKLD GSNKLKFLIK TDTPADRLSL
VNAMLDEFEK HQTEN
//
