ID V4Q8R8_9CAUL Unreviewed; 1163 AA.
AC V4Q8R8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=ABENE_01760 {ECO:0000313|EMBL:ESQ94260.1};
OS Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ94260.1, ECO:0000313|Proteomes:UP000017837};
RN [1] {ECO:0000313|EMBL:ESQ94260.1, ECO:0000313|Proteomes:UP000017837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ94260.1,
RC ECO:0000313|Proteomes:UP000017837};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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:ESQ94260.1}.
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DR EMBL; AWGB01000004; ESQ94260.1; -; Genomic_DNA.
DR RefSeq; WP_018080146.1; NZ_AWGB01000004.1.
DR AlphaFoldDB; V4Q8R8; -.
DR STRING; 1121022.GCA_000376105_00474; -.
DR PATRIC; fig|1121022.4.peg.350; -.
DR eggNOG; COG1197; Bacteria.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000017837; 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; 3.40.50.11140; -; 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:UP000017837}.
FT DOMAIN 628..789
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 810..964
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1163 AA; 128390 MW; 9548E511E0CD3F42 CRC64;
MSDLSQIARS SQPLTLSGCP EGFESLMAAD LARSEGLSVF VARDFARMNA VAEALKFFAP
ELEILSFPAW DCLPYDRMSP TAGIVAQRMF ALSRLAALKT QKPSTPLLLL TTAAAMMQKV
PPLSVINEDR LSLKPGQTID IRVLEGYFLK HGYTRVSTVA EKGEFAVRGG LLDVFSPSFD
EPVRLDFFGD SLESIRSFDT ETQRSLKQIT SLDFTAVAEI RMDEASIKRF RQHYLESFGA
AGDDPLYTAL SAGIRRQGIE HLLPLFYDGL DGVFDYLPRN SLLMLDALAD NAFAERAATV
QDAYELRAEA AKEKGGSAYR ALPPPQLYLD DAHWNTALSA HRLRRFEPFE REGGDIIDLG
GRLGRNFSQE RLLDSTNLFA AVTDHAKALA KQGKRVLFAS WTDGSSDRLG VMLADHGLTS
LRLAPSWSEA LSFGVAGTKV KPIQRAVLPL DHGFETESLA VISETDILGD RLARPRKRRR
AQNFLAEASA LSPGDLVVHI EHGIGRYDGL KTLDVAGAPH DCLDLQYAND AKLYLPVENI
DLLTRYGADS DSAQLDRLGS ASWQARKAKA KERLRDMADG LIQLAAARAM KQGQTIDPPA
GLYDEFCAQF PYEETDDQLN AIADVLEDLA KGQPMDRLIC GDVGFGKTEV ALRAAFVVAM
SGQQVAIICP TTLLARQHFK TFTQRFQGWP IRVRQLSRLV TKKEADETRD GLKKGEIEVV
IGTHALLSEQ VSFRDLGIVI VDEEQHFGVK HKEKLKTFRA DVHMLALSAT PIPRTLQMAL
SGIRDMSIIA TPPVDRIAVR TYVLPYDPVA LREALLREKY RGGQAYYVVP RLSDIADVAD
FLRVQVPEIK FVVGHGQLTP TALEDVMNAF YEGQYDVLLS TTIVESGLDV PTANTLIVHR
ADMFGLAQLY QIRGRVGRSK TRAYAYLTTP QHKTLSVASE KRLKVLQSLD NLGAGFQLAS
HDLDIRGGGN LLGNEQSGHI REIGVELYQQ MLEDAVAELR QKGDQSLADA RSWSPQINAG
AAVMIPESYI PDLNIRLSLY RRVSEAEKLA DREALASELI DRFGPIPEEA EQLLKVVGIK
GLCRESNVAK LDIGPKGAVI TFRNDSFNNP MGLIKLIQGR PNDWKLRPDQ KLLVKGEWPD
AAQRLAAAER IMKELAKLAA ETA
//
