ID A0A1S2VEI3_9BACT Unreviewed; 1121 AA.
AC A0A1S2VEI3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=BLX24_20655 {ECO:0000313|EMBL:OIN57177.1};
OS Arsenicibacter rosenii.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Arsenicibacter.
OX NCBI_TaxID=1750698 {ECO:0000313|EMBL:OIN57177.1, ECO:0000313|Proteomes:UP000181790};
RN [1] {ECO:0000313|EMBL:OIN57177.1, ECO:0000313|Proteomes:UP000181790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:OIN57177.1,
RC ECO:0000313|Proteomes:UP000181790};
RA Huang K.;
RT "Arsenicibacter rosenii gen. nov., sp. nov., an efficient arsenic-
RT methylating bacterium isolated from an arsenic-contaminated paddy soil.";
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}.
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:OIN57177.1}.
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DR EMBL; MORL01000014; OIN57177.1; -; Genomic_DNA.
DR RefSeq; WP_071505110.1; NZ_MORL01000014.1.
DR AlphaFoldDB; A0A1S2VEI3; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000181790; 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; 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:UP000181790}.
FT DOMAIN 576..737
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 758..912
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1121 AA; 127642 MW; CD684DBE7845628B CRC64;
MKPEELIGLY ADDSFIQLLA EPLIHPPGEP MRLQIKGLVG SIDAVLASAI ARLTTGNQLF
ILNDRDEASY FYNDLQNLTG KDVLLFPMSY KKPYQYEEVE NANVLMRAEV LNKLNATAKQ
NLLIVTYPEA LSEKVINKRS LQANTLTIRV GDRLDTNFVS ELLQDYEFEK TDFVYEAGQF
SLRGGIIDVF SFATEFPVRI DLFDDEVESI RFFNPETQLS TTSVDFINII PNIQTKLIQE
SREPFFDFLP ENTYVWLRDV DFALDIVDKC FEKAEQSFEA VLAGSGGIKV VSDPNQLFET
RRSLLNQLKQ FTTVEFGRKF YFKTDTRQLY QAKAQPSFNK DFKRLVENLA ENQSKGFTNI
IAAESFKQLE RLRTIFDELD PFVKFQPLNI GLREGFIDES LKIACFTDHQ IFDRYFKYRV
QDKFSKSKAL TLRELKTLQP GDYVTHIDHG IGRFAGLEKV DVGGKMQEAI RLIYRDNDVL
LVSIHSLHKI AKYSGKEGGP PTMSKLGSQE WELKKSRVKK QVKDIAKELI SLYAKRRQAP
GYAFSRDSFL QAELESSFIY EDTPDQAKAT ADVKVDMEQP HPMDRLVCGD VGFGKTEVAI
RAAFKAVSDN KQVAVLVPTT ILAMQHYRTF SERLSDFPVK IEYINRFRTA GQIKDILKET
ANGQIGILIG THRIVNKDIK FKDLGLLIID EEQKFGVKTK DRLKEMRVEV DVLTLTATPI
PRTLHFSLMG ARDLSVIATP PPNRQPVTTE VHTFSETVVR DAISYELRRG GQVFFVHNRV
GDIESIGNLI LRLVPDARVC VAHGQMEGEK LEKVMTRFIE GDYDVLVSTN IIESGLDIPN
ANTILINTAH MFGMSDLHQM RGRVGRSNRK AFCYLLTPPQ SSLTSDARKR LQTLEDFSDL
GEGFKIAMRD LDIRGAGNLL GAEQSGFIND LGYEMYHKIL DEAVQELREN EFKDLFLPDS
NPFKAAVPDT VIETDLQVVI PEKYVSNISE RLSLYTRLDN IRNQEELAAF RKEVEDRFGP
LPEEVENLIK MVNIRWKAES LYLEKLTLKN NILKGYFVSS ENGSGTAERF FQSEQFGKVI
DYIKLNPLKC SLKDVKNRLI FTHSNVSSVV QMDEVLTALT D
//
