ID A0A2W6MTZ2_9HELI Unreviewed; 1004 AA.
AC A0A2W6MTZ2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=B6S12_05940 {ECO:0000313|EMBL:PZT48005.1};
OS Helicobacter valdiviensis.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1458358 {ECO:0000313|EMBL:PZT48005.1, ECO:0000313|Proteomes:UP000249746};
RN [1] {ECO:0000313|EMBL:PZT48005.1, ECO:0000313|Proteomes:UP000249746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WBE14 {ECO:0000313|EMBL:PZT48005.1,
RC ECO:0000313|Proteomes:UP000249746};
RA Fresia P., Jara R., Sierra R., Ferres I., Greif G., Iraola G., Collado L.;
RT "Genomic and clinical evidence uncovers the enterohepatic species
RT Helicobacter valdiviensis as a potential human intestinal pathogen.";
RL Submitted (MAR-2017) 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}.
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:PZT48005.1}.
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DR EMBL; NBIU01000015; PZT48005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W6MTZ2; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000249746; 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 Gene3D; 2.40.10.170; -; 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:UP000249746}.
FT DOMAIN 507..666
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 687..841
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1004 AA; 115163 MW; 2A3896CBA92628F7 CRC64;
MQASFYEFLK TKEKELLLNK EGFVVLTQDK EQAQSLSDVA KYLGYETFIM PDFRAIFGDD
LRSYQEELKE LLGELLRFYQ SKNLKKILLS PLQTLLHKLP KREKLEGIRL EYGQTIQLEE
LKNTLLYFGY EFVDLVEVGG EVSFRGDIID IFLPHCEEPY RISLFGDEIE SIREFDRESQ
LSKKEEIEFL EIAPALFNLD SQEYEEILEN IQENQEELEV GNFNLNAYGF WYLKDSCFLP
KIYKSFLAPK VSEEIKELLE FKEIDAEILQ TCLELEEIKE AKEYEDFEFS FKNILSFLEF
HRDKKIILIS KSEAQIRQAG INLVEHREYE VLLDKDYAIF IIGKNELILS LNTKLKQNRK
RNTKILLDEL QVGDYVVHID YGVALFSGII QANIFGAKRD FIELKYLGED KLLLPVENLD
RIDRYIADGG IPLLDRLGKG SFVKLKEKVK EKLFIIASEI VAMAAKRELI EGVKINVEKE
EIAIFQAQSG FAYTEDQQRS VEEIFKDISQ GRVMDRLLSG DVGFGKTEVA MNALFAIYLS
GYQGALIAPT TLLVYQHYNT LKERLEAFGV KTARLDRYIS AKEKRAILEG LKSGKIDVVV
GTHAIFNVEF QKLALIVVDE EHKFGVKQKE KIKELSENIH LLSMSATPIP RTLNMALSHI
KGMSELKTPP KERLAVRTFV KVASEALVKE VILRELRRGG QIFYIHNNIS SIERKKEELL
EILPALKIAI LHSKIQAQMS EDILLEFAKG NFNLLLCTSI VESGIHLPNA NTILVDRSDC
FGIADLHQLR GRVGRGSKEG FCYFLIEDKE KITQEATKRL LALEKNSYLG SGGALAYHDL
EIRGGGNLLG EAQSGHIKNV GYSLYLRMLE EAIYKLSGNL KEEQKNVDVK LSVTAFLSPE
LISSERLRLE LYRRLSRACE INEVYGIEHE IEERFGRLDI YTKQFLELIC IKIKAKMAKI
SSISNYGQNI SFVDEEGKRS VINAVSKDEE DILKAVNEEL ERRK
//
