ID S2XCG2_9BACL Unreviewed; 1180 AA.
AC S2XCG2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=HMPREF1210_03493 {ECO:0000313|EMBL:EPD49381.1};
OS Paenisporosarcina sp. HGH0030.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae;
OC Paenisporosarcina.
OX NCBI_TaxID=1078085 {ECO:0000313|EMBL:EPD49381.1, ECO:0000313|Proteomes:UP000014412};
RN [1] {ECO:0000313|EMBL:EPD49381.1, ECO:0000313|Proteomes:UP000014412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGH0030 {ECO:0000313|EMBL:EPD49381.1,
RC ECO:0000313|Proteomes:UP000014412};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Paenisporosarcina sp. HGH0030.";
RL Submitted (MAY-2013) 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:EPD49381.1}.
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DR EMBL; AGEQ01000020; EPD49381.1; -; Genomic_DNA.
DR RefSeq; WP_016429951.1; NZ_KE150425.1.
DR AlphaFoldDB; S2XCG2; -.
DR STRING; 1078085.HMPREF1210_03493; -.
DR PATRIC; fig|1078085.3.peg.3450; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_9; -.
DR Proteomes; UP000014412; 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:UP000014412}.
FT DOMAIN 638..799
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 813..974
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1180 AA; 134979 MW; 3B0FABC0009FE35F CRC64;
MEPLHQLFTK DHHIKTLLTD LQTGVDQQLV TGLTGGARPL FIHSMAKETE RPILVVSPNL
LQAQRLFEDM VKLLGEDEVR LYPADELIAA DMSVSSPELR AERIETLDFM LSQKRGVVIT
PIAGLRRHMP NLAQWRASRL ETAIGQEVKM DEWLDQLVAM GYSRQAMVTT PGEFALRGGI
LDIYPIYLQH PVRLEFFDTE VDSIRMFSAE DQRSIEKLKE VCILPATEFV WTRQQLMILA
EKLEESLAGS LKKLKKPETK ELLLQHINHD IELLRQGDTP EQMTKYVSIL EDHPTFLGDY
FAQDGLVLFD ELGRIQETTD SLEREEKDWY VSLLEEGKTV HDVKLSFSFK EILGMLDQKK
IYFSLFARTF SGISLKKSIA FSCKPMQHFH GQMSVLKNEM ERFEAGKFFI FVLAEGNERQ
KKVKDVLEDY GMDSHVLTKQ EAPDQPGIYI IDGEISSGFE LPLQRIALMT DEELFKQRPK
KKSRPQKMTN AERIKSYSEI KPGDHIVHIH HGIGKYIGIE TLEINGIHKD YLHIRYRAED
KLFVPVDQID QIQKYVASEE REPKLHKLGG ADWKKTKTKV SAAVQDIADD LIKLYAKRES
EKGHAFEPDQ DMQQAFETAF PYEETDDQLR SIEEVKRDME KERPMDRLIC GDVGYGKTEV
AIRAAFKAVQ DSKQVAFLVP TTILAQQHYE TMKERFADFP VEVGLLSRFR SKKQQTETTK
GLKAGTIDVV VGTHRLLSKD IVYYDLGLLI VDEEQRFGVT HKEKIKQLKT NVDVLTLTAT
PIPRTLHMSM IGVRDLSVIE TPPANRFPVQ TYVMEQNGAL VREAIEREMA RGGQAFYLYN
RVEDMARKVE EIQMLVPEAR VGFAHGQMTE RELESVILAF LEGDYDVLVT TTIIETGIDI
PNVNTLIVQN ADRMGLSQLY QLRGRVGRSN RVAYAYFMYQ RDKVLTDVAE KRLQAIKEFT
ELGSGFKIAM RDLSIRGAGN LLGSQQHGFI DSVGFDLYAQ MLQEAIEEKQ TGVKQEEVLD
VEISLPFDAY LPDAYIPDGF QKIQMYKRIK AVDSEKDYED LVDELIDRFG NMPIEAERLM
RIARIKVWAK ISGVESIKEQ QKQLVIKLSK KGTQNTNGAM LVESSMDYGR AVGFQMNNQQ
QLLVTIDEKK TAKHHPFDVL EAMMKHLPEA RKEVNSFVGE
//
