ID D3UID2_HELM1 Unreviewed; 991 AA.
AC D3UID2;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 87.
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 ECO:0000313|EMBL:CBG40255.1};
GN OrderedLocusNames=HMU09980 {ECO:0000313|EMBL:CBG40255.1};
OS Helicobacter mustelae (strain ATCC 43772 / LMG 18044 / NCTC 12198 / 12198)
OS (Campylobacter mustelae).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=679897 {ECO:0000313|EMBL:CBG40255.1, ECO:0000313|Proteomes:UP000001522};
RN [1] {ECO:0000313|EMBL:CBG40255.1, ECO:0000313|Proteomes:UP000001522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43772 / LMG 18044 / NCTC 12198 / 12198
RC {ECO:0000313|Proteomes:UP000001522};
RX PubMed=20219135; DOI=10.1186/1471-2164-11-164;
RA O'Toole P.W., Snelling W.J., Canchaya C., Forde B.M., Hardie K.R.,
RA Josenhans C., Graham R.L.J., McMullan G., Parkhill J., Belda E.,
RA Bentley S.D.;
RT "Comparative genomics and proteomics of Helicobacter mustelae, an
RT ulcerogenic and carcinogenic gastric pathogen.";
RL BMC Genomics 11:164-164(2010).
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; FN555004; CBG40255.1; -; Genomic_DNA.
DR AlphaFoldDB; D3UID2; -.
DR STRING; 679897.HMU09980; -.
DR KEGG; hms:HMU09980; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_2_7; -.
DR Proteomes; UP000001522; 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: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; 3.40.50.11180; -; 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; 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; 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; 3.
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:UP000001522}.
FT DOMAIN 496..653
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 674..828
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 991 AA; 112215 MW; 356BE5A122E3201D CRC64;
MQANLYAHLT KKQPPQILVV EDDKEAQSAF HLAEYCYEKG ILTKKPLVLP DFRAKKGEDL
RSFQEEFLDL LVGLREFYAQ DCFLIAPLSS VLYPLPKKEL LEPFVISKEE PLDVRDLKEK
LVHFGYEVVE IVEMDGEVSF RGDILDIAIP QDKSYRLSFF DIECESIREF DVQSQKSKTL
ELESLSIPPA VFHLSKEQYE RMIEEIAGLD TDSFYKDIFS LGFWCLGDLG WEPLRQMHTI
LSPNAKNSLT EVFDFVSDSP YGKEFFLQLP SLQEQKDYAD IRIEAKNLEY FLDLNADKPI
TILVPTQMLK EQFEARQIHA EISSLVVNIS TPDCFIISLN QIQKSRKKQK PRIAINELNV
GEYVVHIQYG IGVFGGIEQA KILGAVRDFI RIDYQGGDSL LLPVENLNLI DRYVAGSSGV
PMMDRLGKGS FAKLKEKIKK KLFEIADSII SLAARRKLIE GKKIDTTLPE ILFFKEQAGF
VLTEDQERCI QEIFADMSSG QVMDRLLSGD VGFGKTEVAM NAIYAACQNG FQALMIVPTT
LLALQHYHTL KERLKGLRVA RLDRFVSARS KKGILQGLLE GKIDVVVGTH SLLGVGFKNL
GLIVIDEEHK FGVKQKEAIK SLSKDVHLLS MSATPIPRTL NMALSQIKGM SSLLTPPSER
QSTKTFVKEK SASLIKEVIL RELRRNGQVF YIHNNIANIP MIERELKALL PQLEIALLHS
QIDSKTTEEI LLSFAEKKTH LLLCTSIVES GIHLPNANTI IVDGADHFGL ADLHQLRGRV
GRGDREGFCY YLIDDRESIT QEATKRLLAL EKNSFLGSGA MIAYQDLEIR GGGNLLGEAQ
SGHIKNIGYN LYLKMLEDAI YQLSSNKEQI EERDVELKLQ VSAYLDSHLI SSDTLRLELY
RRLSLCKDKE CVYAIEGEIA DRFGELDFYT KQFLKLILIK ILARGLGITQ ISNFKKSITL
FFGDGNKKFL QADEEEQILD EILKFLHKSR A
//
