ID J6HH27_9FIRM Unreviewed; 1127 AA.
AC J6HH27;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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:EJU21998.1};
GN ORFNames=HMPREF1143_0898 {ECO:0000313|EMBL:EJU21998.1};
OS Peptoanaerobacter stomatis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoanaerobacter.
OX NCBI_TaxID=796937 {ECO:0000313|EMBL:EJU21998.1, ECO:0000313|Proteomes:UP000005244};
RN [1] {ECO:0000313|EMBL:EJU21998.1, ECO:0000313|Proteomes:UP000005244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OBRC8 {ECO:0000313|EMBL:EJU21998.1,
RC ECO:0000313|Proteomes:UP000005244};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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:EJU21998.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ALNK01000025; EJU21998.1; -; Genomic_DNA.
DR RefSeq; WP_009531214.1; NZ_ALNK01000025.1.
DR AlphaFoldDB; J6HH27; -.
DR PATRIC; fig|796941.3.peg.1457; -.
DR Proteomes; UP000005244; 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; 3.40.50.11180; -; 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; 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:UP000005244}.
FT DOMAIN 629..790
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 815..965
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1127 AA; 131519 MW; A8649386630A083E CRC64;
MDKFLNYLSE TDEFMQMDRA ISERNTPILL NGISTESIPF FLDYIYSAHK QKVIFITPSD
IAAQDIYREL LRYNSSKIII LQSDELKFYQ IDAINRDNEF QRISCLKKIY DNDYDILILS
IASLLRKYMP KKYYEKNIID IKLSSNIDIY ELTKKLVIVG YDRVRKIESK GQFSLRGSII
DIFPPDFSNP VRIEFFDDEV DSIRIFDLYS QVSIDKEEKV IIIPAREYIY PENIDKSLKN
IENLLKDNTS EDIRIDIEKI QSKTYFKGLE KYIGFLYEEK DLSILQFIDK NCNIVLSEPN
RVFEKIDNIY YEFFENYKSS LERGFALKGQ DNIFIDKDSI MQKIYDYKLI LTSEVTGNIK
KIKTKAIFNF DVQSAPKYRG DINQLIVDIN TYKDRKYKIV ILLQEEKVIK NIISELESSD
ISAKYINSDK FDIESSDVFI LKDNKTQGLI LKKANFVFIT NNDIFFRLSK LSTPRKRKNI
KSERLKGFAD LKKGDIVVHE VYGIGKFIGI EQKENDGIKK DYIKVSYKGG DFIYVPISQM
DRVQRYIGNA SDRISLTQLG SNQWKKQKQK AKKAVDEIAK YLIELYAERE NQKGYAFSKD
TVWQREFEAL FPFEETQDQL KSIKDIKRDM ENIRPMDRLI CGDVGYGKTE VALRGIFKAC
MDQKQVAFLV PTTILAQQHY KTLSDRFENY PINVDVLSRF KTKKEQEKTV EKIKNGEVDV
VIGTHRLLSK DVEFKNIGML VIDEEQRFGV KHKEKIKQMK SNIDVLTLTA TPIPRTLNMS
LSGIRDMSVL EEPPNDRYPV ITYVTEAREG IILDAIEREM ARNGQVFFVY NSIENIDKMY
NFIQKLVPSA RIAIAHGQMS AIALEDIMMD YLEKKYDVLL CTTIIETGMD ISNANTIIVY
NADKMGLSQL YQLRGRVGRS SRQAYAYLMY EKDKVLTEIA QKRLKAIREF TEFGSGFRVA
MMDLEIRGSG NILGEVQHGH IEEVGYDLYI KMLNDSFNRL KGKTVEEKVS TEVYLNVNAY
IPDDYIEDEI QKMEIYKKIA SINSKEDYFD IQAEIEDRFS DIPQEVENLL KISSIRSLGE
KIRVVKISQK NRNIVYETKT QKFIQTLKTV KEDQMLKEII EFMRKFL
//
