ID A0A285IX31_9RHOB Unreviewed; 1156 AA.
AC A0A285IX31;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN06297129_2354 {ECO:0000313|EMBL:SNY52610.1};
OS Pseudooceanicola antarcticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1247613 {ECO:0000313|EMBL:SNY52610.1, ECO:0000313|Proteomes:UP000231655};
RN [1] {ECO:0000313|EMBL:SNY52610.1, ECO:0000313|Proteomes:UP000231655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12662 {ECO:0000313|EMBL:SNY52610.1,
RC ECO:0000313|Proteomes:UP000231655};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; OBEA01000004; SNY52610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285IX31; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000231655; 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 615..776
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 797..951
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1156 AA; 127691 MW; 6D6145BD39FEB9D6 CRC64;
MAEQRHFTLG GAPEGFDAAL LVKEVEGRGA PVIHVARDDK RMAAMADALR FFAPQMPVVT
FPGWDCLPYD RVSPHADISA TRMATLAGLV HGMPEQFILL TTLNAATQRI PAREVLKDAA
FQARVGDRID EAALRQFLVR MGFSQTQSVA EPGDYAVRGG IIDIFPPGPS GPVRLDLFGD
VLDGARRFDA GSQRTTDKLE LVELAPVSEV ILDEAAITRF RQNYRIEFGA AGTDDPLYEA
VSAGRKQQGM EHWLPFFHER LETLFDYLPG ATISLDDQAT PARLSRWDTI ADQYESRRIA
MGERGRMDSV YKPVPPGLLY LDDAAWEKQI AARRVLQLSP LAQSPGPGVL DAGGRQGRNF
SPERQLENVS LFNVLSKHIQ ARLQEGPVVV ASYSEGARER LEGLIADEGL AEAIHVRDAA
RIGRTGLHLA VWPLEHGFTG RWHDRPLTVI SEQDVLGDRL IRSARKKRKA ENFLTEAQSL
SPGDLVVHVD HGIGRYHGME VITAAGAAHE CLLLEYAENA RLYLPVENIE LLSRYGHEEG
LLDKLGGGAW QAKKAKLKER IREMADKLIR VAAERALRRA PILEPPEAEW NAFLSRFPYQ
ETDDQLSTIE DVLGDMSSGH SMDRLVCGDV GFGKTEVALR AAFVAAMSGV QVAVIAPTTL
LARQHYQGFA ERFRGFPIQV SPLSRFVNAS DATRTRHGIT DGTVDIAVGT HALLAKNIRF
KNLGLLIVDE EQRFGVAHKE RLKQLRTDVH VLTLTATPIP RTLQLSLSGV RDLSIIGTPP
IDRLAIRTYV SEFDAVTIRE ALLREHYRGG QSFYVVPRVS DLAEIEDFLK TQVPEVSFVT
AHGGMAAGDL DQRMNAFYDG KFDVLLATTI VESGLDIPRA NTMVVHRADM FGLAQLYQIR
GRVGRAKTRA YAYLTTKPRA KLTDTAQKRL RVLGSLDTLG AGFTLASQDL DIRGAGNLLG
EEQSGNMRDV GYELYQSMLE EAIAKIKSGE AEGLTDSDDQ WAPQINLGVP VLIPEHYVPD
LDLRLGLYRR LSGLSTKVEL EGFAAELIDR FGKLPKEVNT LMLVVRIKAM CKRAGIAKLD
GGPKGATVQF HNDKFASPEG LVEFIRDERG LAKVKDNKIV LRRDWKSEAD RIKGAFSIAR
DLAEKVIAAE KARAKR
//
