ID A0A0D0N5K8_KITGR Unreviewed; 1202 AA.
AC A0A0D0N5K8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=TR51_32595 {ECO:0000313|EMBL:KIQ63405.1};
OS Kitasatospora griseola (Streptomyces griseolosporeus).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=2064 {ECO:0000313|EMBL:KIQ63405.1, ECO:0000313|Proteomes:UP000032066};
RN [1] {ECO:0000313|EMBL:KIQ63405.1, ECO:0000313|Proteomes:UP000032066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MF730-N6 {ECO:0000313|EMBL:KIQ63405.1,
RC ECO:0000313|Proteomes:UP000032066};
RA Arens J.C., Haltli B., Kerr R.G.;
RT "Draft genome sequence of Kitasatospora griseola MF730-N6, a bafilomycin,
RT terpentecin and satosporin producer.";
RL Submitted (FEB-2015) 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:KIQ63405.1}.
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DR EMBL; JXZB01000004; KIQ63405.1; -; Genomic_DNA.
DR RefSeq; WP_043915767.1; NZ_JXZB01000004.1.
DR AlphaFoldDB; A0A0D0N5K8; -.
DR STRING; 2064.TR51_32595; -.
DR PATRIC; fig|2064.6.peg.6898; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000032066; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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:UP000032066}.
FT DOMAIN 661..822
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 840..997
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1202 AA; 131488 MW; 3B13BF886569FFC7 CRC64;
MSLSGLLDVV VRDAALAEAI EAAATGRRQH LDLVGPPAAR PFAIAALARS LAARAGEGGR
PVLAVTATGR EAEDLAASLR SLLPPDAVAE FPAWETLPHE RLSPRSDTVG RRLAVLRRIV
HPRADDPAAG PVQVVVAPVR SVLQPQVKGL AELEPVALQR GEQHDLGEIA RKLSAAAYAR
VELVEKRGEF AVRGGILDVF PPTEEHPLRV EFWGDDVEEI RYFKIADQRS LEIAEHGLWA
PPCRELLLTD EVRGRAAELA AQHPELGEIL DKIAQGVAVE GMESLAPVLV DDMELLLDVL
PAGSIAVVCD PERVRTRAAD LVATSQEFLA ASWVAAAAGA DRPIDLEAID VSAASLWSLA
DVREHAAEIG LPWWSVSPFA TSDSTVSEIL EFDADTLTLG MHAVEAYRGD TARAIADAKE
RLAADWRVVL VTEGHGPAAR LAEVLGNEGI PARLVADLGE APTRDVVYVS CGSIEHGFVD
EALKLTVITE TDLSGQKSST KDMRRMPSRR RNAIDPLALA AGDYVVHEQH GVGRYVEMVQ
RTVQGATREY LVLEYAPAKR GHPGDRLFVP TDQLDQVTKY VGGEAPTLHR LGGADWAKTK
QRAKKAVKEI AADLIKLYSA RMAAPGHAFG QDTPWQRELE DAFPYAETPD QLTTIGEVKS
DMEKSVPMDR LICGDVGYGK TEIAVRAAFK AVQDGKQVAV LVPTTLLVQQ HFSTFAERYA
NFPVNVKALS RFQTDTEAKA VLEGLFEGSV DVVIGTHRLF SSETRFKDLG LVIVDEEQRF
GVEHKEQLKK LRANVDVLTM SATPIPRTLE MAVTGIREMS TITTPPEERH PVLTFVGPYD
EKQIAAAIRR ELLREGQVFY IHNRVESIDK AAARLKDLVP EARVATAHGQ MGETQLEKVV
VDFWEKEFDV LVSTTIVESG IDISNANTLI VERGDTFGLS QLHQLRGRVG RGRERGYAYM
LYPPEKPLTE TAHERLATIA QHTEMGAGMY VAMKDLEIRG AGNLLGGEQS GHIAGVGFDL
YMRMVGEAVA DFRQSLEAGG GEPEEEPLEV KIELPVDAHV PHDYAPGERL RLQAYRSIAA
VNSEDDITQV REELTDRYGK LPEPVENLLL VAGLRLFARR CGIGDITLQG AFVRFGPVDL
RESQQLRLNR LYPRTQIKSA AQQLLVPRPS SGGRIGGKPL VGRELLSWCT EFLSTMFDDL
KR
//
