ID A0A1I4ZEI8_9FLAO Unreviewed; 1116 AA.
AC A0A1I4ZEI8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN05421741_10648 {ECO:0000313|EMBL:SFN48694.1};
OS Paenimyroides ummariense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Paenimyroides.
OX NCBI_TaxID=913024 {ECO:0000313|EMBL:SFN48694.1, ECO:0000313|Proteomes:UP000199036};
RN [1] {ECO:0000313|Proteomes:UP000199036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-12 {ECO:0000313|Proteomes:UP000199036};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOVI01000006; SFN48694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4ZEI8; -.
DR STRING; 913024.SAMN05421741_10648; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000199036; 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:SFN48694.1};
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}.
FT DOMAIN 570..731
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 752..906
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1116 AA; 127805 MW; B28B0530A01BB279 CRC64;
MSIKKVFEQA TKTQQLQQQL NKLGNKIHAK GFIGSALSFQ IQALFKESDQ HFLLIFNDKE
EAAYYLNDLE NLISKDYVLF YPGSYRRPYQ IEETDNANVL LRAEVLNRLN ARKKPVVIVS
YADALFEKVV TRKQLDKNTL KIAVNDKMTI DFVNEVLFEY NFKRVDFVSE PGEFSVRGGI
IDVFSFSNEN PYRIEFFGNE IDSIRAFDVE TQLSIETNKK ITIIPNVENK FLQENRESFL
NYISPNTVVF IQNTVLIKEQ LTKMFQKATE AFDKLSKDVQ HLAPDQMFLP SAEFLQKADD
FTVFELAQQN FFTPNFSVDF HFNPQPSFNK QFDLLIENLN QNTENGYTNY LYCSSESQSK
RFEEIFSSLK DQNKSIQQYK TVVMPLFQGF IDKENQIACY TDHQIFERYH KFSIKNGYTK
KQTITLKELT TLSVGDYVTH IDHGIGKFGG LQKIDVEGKK QEAIKLVYAD NDIVYVSIHS
LHKISKYNGK EGAPPKIYKI GSGAWKALKQ KTKARVKHIA FNLIKLYAKR RLEKGFACAP
DSYLQAELES SFIYEDTPDQ LKSTIEVKAD MENERPMDRL VCGDVGFGKT EVAIRAAFKM
VDNGKQVAVL VPTTILAFQH YKTFTERLKD MPVKVAYLNR FKTAKQKAET LKELSEGKVD
ILIGTHQLVN KNVVFKDLGL LVIDEEQKFG VAVKDKLKTI GENIDTLTLT ATPIPRTLQF
SLMAARDLSV ITTPPPNRYP IETNVVGFNE EVIRDAIAYE IERGGQVYFI NNRIENIKEV
AGMIQRLVPH AKVGIGHGQM EGKKLEDLLL SFMEGEFDVL VATTIIESGL DVPNANTIFI
NNANNFGLSD LHQMRGRVGR SNKKAFCYFI TPPYSVMTEE ARKRISALEQ FSDLGSGFNI
AMKDLEIRGA GDILGGEQSG FINEIGFETY QKIINEAIDE LKENEFKDLY EEEQNIDTKE
YVKDIVIESD FEILFPDEYI NNVSERLTLY NELATLKTED ELIAFQNKLI DRFGALPRQV
VNLLDSVRIK WIASKAGIEK LVLKQGKMIG YFVSDQQSMY YQSAQFRKVL QFIQLYPKLA
TLKEKQTKNG LRLLLTFDHI KSISKALENL QKLQQL
//
