ID G5H6U0_9BACT Unreviewed; 1155 AA.
AC G5H6U0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=HMPREF9450_00650 {ECO:0000313|EMBL:EHB92937.1};
OS Alistipes indistinctus YIT 12060.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=742725 {ECO:0000313|EMBL:EHB92937.1, ECO:0000313|Proteomes:UP000006008};
RN [1] {ECO:0000313|EMBL:EHB92937.1, ECO:0000313|Proteomes:UP000006008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12060 {ECO:0000313|EMBL:EHB92937.1,
RC ECO:0000313|Proteomes:UP000006008};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Alistipes indistinctus YIT 12060.";
RL Submitted (AUG-2011) 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:EHB92937.1}.
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DR EMBL; ADLD01000008; EHB92937.1; -; Genomic_DNA.
DR RefSeq; WP_009133456.1; NZ_JH370371.1.
DR AlphaFoldDB; G5H6U0; -.
DR STRING; 742725.HMPREF9450_00650; -.
DR PATRIC; fig|742725.3.peg.705; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_10; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000006008; 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; 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:UP000006008}.
FT DOMAIN 565..726
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 747..901
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1155 AA; 128917 MW; 60B00E975B482A14 CRC64;
MTAQQLQELF LSQPSYRELL RQLENRGTTV GLDSLVGSSY SLVAAGAVRE RGGVHVFVME
DRDAAGYLYN DLSPFLDEER LLFFPTAYKR SIQFGQEDPS GIVQRTAALN AVKNFTDGYL
AICTYPEALV EKVVGMQRLR ESILTIRVGD TLSTSTIEEI LADNGFERVE FVYEPGQYSV
RGGIVDIFSF SDNKPYRIDL FGDEVDSIRH FDLSSQLSVD RLQQIEVVPN LKDAVSGRER
VSFPAFAAGA TYWLDDGEYT LKRFQDIRTK LLGELDDPAQ IDTLVTGRKG FLADTAGATM
VLLKDNCQER AADATISFHT SPQPQFNKKF ELLADDIRDN REKGYTTCLL TENKAQIERL
RNIFNSMGER DVPFEAVGVT LHAGFIDHAS RYCFYTDHQL FDRYHRYQIR GGIDRSESLT
IQELNELKVG DYVVHIDHGV GRFGGLTRTV ENGKVHEAIK LVYRDNDVLL VNVHALHRIS
KYKDKDSEPP KIYKLGSGAW QRMKQNTKKA VKDIARELIA LYARRKASDG FAFSPDSFLQ
YELEASFIYE DTPDQQAATQ AVKADMEART PMDRLVCGDV GFGKTEVAIR AAFKAVTDSK
QVAVLVPTTI LALQHYRTFS ERLKEFPVRI EHLSRAKSTA EVNQILKDVA DGRIDILIGT
HKILGKNVGF KDLGLLIIDE EQKFGVAAKE KLRQLRADVD TLTMTATPIP RTLQFSLMGS
RDLSVISTPP PNRQPVSTES HLFDEELIRE AVDYELQRGG QVYFVHNKVE TIDNVRRMVG
QLCPKARVAV GHGQMPAQQL EKLMMDFIYG EFDVLVATTI VESGVDVPNA NTIIINNAQN
FGLSDLHQLR GRVGRSNRKA FCYLLTPPEE MLSSDARRRL RAIEEFSDLG AGFNIAMQDL
DIRGAGNLLG GEQSGFIADI GFETYQKILS EAMAELREEE FAKAAEAGRT IASGDVALQG
GSVHSVPGGS IAGQADMNGS AFPGVTSPQD GGGTVAYISD CQIETDREAV IPDSYVSSAG
EKLRLYRELD SITDEERLAR FESQLTDRFG DIPTATHELF DIVRLRWICI RLGFEKAIVK
NGIMILQFVH NQKSAYYKSE LFGRILRVST RPGSKFIFRQ NNNKLSVVVR SIKDIAAAAA
TLRELETEAA KQPTA
//
