ID A0A1N6FEP3_9LACT Unreviewed; 1180 AA.
AC A0A1N6FEP3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=SAMN05878443_0564 {ECO:0000313|EMBL:SIN93676.1};
OS Carnobacterium alterfunditum.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=28230 {ECO:0000313|EMBL:SIN93676.1, ECO:0000313|Proteomes:UP000184758};
RN [1] {ECO:0000313|EMBL:SIN93676.1, ECO:0000313|Proteomes:UP000184758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=313 {ECO:0000313|EMBL:SIN93676.1,
RC ECO:0000313|Proteomes:UP000184758};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FSRN01000001; SIN93676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6FEP3; -.
DR STRING; 28230.SAMN05878443_0564; -.
DR eggNOG; COG1197; Bacteria.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000184758; 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}.
FT DOMAIN 636..797
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 811..972
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1180 AA; 134720 MW; 9BF987756EC75F0E CRC64;
MGDIKKILAN APDVGTLLSQ LEQHQSQLIT GLSGSARTLV LSTLVAEKKK PFIIVTHNLF
HANQLMEDFA DWMPEDRLHL FPVDEMIYAE MSVASPEARA ERVATLDFLL SEKYGVVIIP
LAGVRKLLPP KELWKSAQFT IKQGGELDLT NLAQRLVDMG YTRQQLVNSP GEFSIRGGII
DIYSLTEEFP IRIDLFDTEV DSLRYFDATT QRSIQTINKV TILPATDTFY TKEQLMAAAP
RFSKAVERNL GLIQDASDRQ TFTKQVTPIS DAFQRGEPID ELTMFTDFIY PEKNSVLDYV
SKKGIVVMDE YPRVMDTDRR LNEEEAEFIT SKLSERRILQ EQVFSNNFRD QLKTLSNSIL
YFAVFQKGMG NTRFNNIQAF QYRNMQQFFG QMPLFKTEID RWIKQKNTVI IMVPNADRAK
KVQQIFKDFE ITSKVVKPAR IELEKVQVTV GYVQAGFEMP TEKLVVITER ELFNKVTKKT
ARRQTLSNAE RLKSYSELNP GDYVVHVNHG IGKYTGMETL EINGIYQDYM SIIYKDEAKL
FIPVTQLNLL QKYVSSEAKT PKVNKLGGTE WAKTKKKVAT KIEDIADELI ELYASREQEV
GYAFSPDDAY QEEFENAFPY TETDDQLRST AEIKHDMEQK KPMDRLLVGD VGYGKTEVAM
RAVFKAIQEG KQAAFLVPTT ILAQQHYETM LQRFADFPIE IGLLSRFRTK KQQSETIASI
KKGQVDIVIG THRILSKDIE FQDLGLLVVD EEQRFGVKHK EKLKQLKAQV DVLTLTATPI
PRTLHMSMLG VRDLSVIETP PANRYPVQTY VMEQNLGAIR EAVEREMARG GQVFYLYNRV
ATIEKKVDEL QQLIPDARIA YAHGQMTEGQ LENTLLQFIE GEYDMLVTTT IIETGVDIPN
VNTLFVENAD HMGLSQLYQL RGRVGRSNRV AYAYFLYQPN KVLNEVSEKR LQAIKDFTEL
GSGFKIAMRD LSIRGAGNLL GAQQHGFIDS VGFDLYSEML SEAVARKRGL DTKEEKTQVE
IDLGINAYLP STYIEDERQK IEIYKRIREL KSHEQYVELQ DDLIDRFGEY ADEVADLLTI
GLIKMYGEHA LIETVKRPGD EIVVTFSVSG TQSLPAEEVF RALSEIPLRA NVAIKSDRLM
VTLQLKKEPT YQWLGHIQKF AQKIVDYRSK DADRSTIAKK
//
