ID B9XRJ1_PEDPL Unreviewed; 1212 AA.
AC B9XRJ1;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=Cflav_PD0612 {ECO:0000313|EMBL:EEF57562.1};
OS Pedosphaera parvula (strain Ellin514).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF57562.1, ECO:0000313|Proteomes:UP000003688};
RN [1] {ECO:0000313|EMBL:EEF57562.1, ECO:0000313|Proteomes:UP000003688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin514 {ECO:0000313|EMBL:EEF57562.1,
RC ECO:0000313|Proteomes:UP000003688};
RX PubMed=21460084; DOI=10.1128/JB.00299-11;
RA Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A.,
RA Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Larimer F.W., Land M.L., Hauser L., Brettin T.S.,
RA Detter J.C., Han S., de Vos W.M., Janssen P.H., Smidt H.;
RT "Genome sequence of 'Pedosphaera parvula' Ellin514, an aerobic
RT Verrucomicrobial isolate from pasture soil.";
RL J. Bacteriol. 193:2900-2901(2011).
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:EEF57562.1}.
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DR EMBL; ABOX02000064; EEF57562.1; -; Genomic_DNA.
DR RefSeq; WP_007418424.1; NZ_ABOX02000064.1.
DR AlphaFoldDB; B9XRJ1; -.
DR STRING; 320771.Cflav_PD0612; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000003688; 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:UP000003688}.
FT DOMAIN 651..812
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 821..987
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1212 AA; 135701 MW; 858CE7D77949E7C4 CRC64;
MATSKLFAKI SETPAVQSLL RRLENGGVLS LNGISASAQP FLAALLRQLL PELPIVLVSD
SLKTQESFQQ DVETWLNFEG SQQKSKGKAP ASQPSTISDR PLFYPAWEVM PHESKLPHAD
VISERLETLV ALARQSPGKR GAAPHIIANV TALLQKTFPA SVLKERTRML NRGDRVEPLD
LIEWLEEQGY EPEAQVTQKG EIALRGGILD VYPMTSPWPV RLEFFGDELE SLRYFDPITQ
ISREQIATVT LPPGGEFGIL KQLAARDQQA SLATLLDYLP TGTLFILSEP ERIEEHTEQY
STQVPNEDPF HIPWSDFQEL LSEKGMKSLQ LSEIVMDGES EGMDVLSESE AVAEDERPFG
ESTENSLPFS SLEAFRPLGA RAPEPQIAEA QRREFFAQLH RWSRQGYDVH LFCNNDGERQ
RFQEVWKDYG FGEDFGLKMH LGALGRGFLN EEAKVVVVTD AEIFGRYKVQ RPRRLKSPHA
QATRSALDID FTELEEGDYV VHLQHGIGRY QGLKVLPVTL GRKGVDPNAT PADSGQECLV
IEYAASDPQQ PAPKLYVPVT EAHLVSKYVG AGKARPQLNT IGGTRWAKAK AQAERAVRDV
ASELLAIQAA RESQPGYSFK ADTPWQREFE SAFLYEETRD QMRAINETKG DMERPKPMDR
LICGDVGFGK TEVAIRAAFK AVMEGKQVAI LVPTTVLAQQ HYNTFKERVA DYPMRVELLS
RFRSPKNRKR VISELPAGAV DIVIGTHRLI QSDINFKDLG LVIIDEEQRF GVLHKEKFKQ
IRKLVDVLTL SATPIPRTLY LALTGARDMS TIETPPQDRL PVETIVAQYD ERLIREAIQR
ELNRGGQVYF LHNRVGTIDA MAQKLRTLVP HARIVVGHGQ MKPDDLEEVM TAFINGEADV
LLSTTIIESG LDIPNANTMI IDRADRFGLS DLYQLRGRVG RYKHQAYAYL LLPRHAGLLA
DARKRISALK QYSTLGSGFK IAMRDLEIRG AGNMLGPEQS GQITAVGFDL YCQLLKQSVA
ALKGEKVKPR VEVQVRFDFL ALNPGEESAA PERGAKAEAP KRRKAEPEII IPREVLTYVE
YDEVAEQKTE QPMQVEKGSA FIPLSYVSEA KQRIDIYRKL AQATDKAALE NLAKELRDRF
GTLPPAMELL LQVGELKILA GEKNITIIEV KDDKLMLTRN NDYIMLGGKF PRLTKGDAKG
RLKEIKKLLL AL
//
