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Database: UniProt
Entry: A0A1G8N7J3_9RHOB
LinkDB: A0A1G8N7J3_9RHOB
Original site: A0A1G8N7J3_9RHOB 
ID   A0A1G8N7J3_9RHOB        Unreviewed;      1157 AA.
AC   A0A1G8N7J3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=SAMN04487993_1009205 {ECO:0000313|EMBL:SDI76269.1};
OS   Salipiger marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=555512 {ECO:0000313|EMBL:SDI76269.1, ECO:0000313|Proteomes:UP000199093};
RN   [1] {ECO:0000313|EMBL:SDI76269.1, ECO:0000313|Proteomes:UP000199093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26424 {ECO:0000313|EMBL:SDI76269.1,
RC   ECO:0000313|Proteomes:UP000199093};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNEJ01000009; SDI76269.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8N7J3; -.
DR   STRING; 555512.SAMN04487993_1009205; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000199093; 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:UP000199093}.
FT   DOMAIN          618..779
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          800..954
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1157 AA;  127462 MW;  DA265CFF0B2F8C1E CRC64;
     MVQSRILMGG APEGFDAKLI LSEVAKAAGP VLHVARDDKR LAALREALAF YAPAMPVVTF
     PGWDCLPYDR VSPNPEICAT RMATLAGLVH GMPERFILLT TLSAVTQRLP ARAVLREAAF
     SARVGSRIDE KALRNFLVRM GFVMAPTVTE PGDYAIRGGI IDIYPPGPGG PVRLDLFGDV
     LDGARRFDAA SQRTTEKLDL VELAPVSEVI LDEPAITRFR QNYRIEFGAG GTDDPLYEAV
     SAGRKAQGME HWLPFFHERL ETLFDYLPDA PVLLDDQLTP SRIARWDSIE DQYQTRRHAM
     AQKGRMDTVY KPVPPGLLYL DDAAWEAAVA DRRVVQFHPL PQAPGPQVAD AGGRIGRSFA
     PERQQESLSL FGALATHVKA KMQAGPVLIA SWSEGARERL TGLIEDEGLA EAIPVADATR
     IGKRGLHLAV WGLEQGFEAP WGDPKDKLRI TVISEQDVLG DRLIRAPKKR RKAENFLTEA
     QALTPGDLVV HVDHGIGRYQ GMEVITAAGA AHECLLLEYA EQARLYLPVE NIELLSRYGH
     EDGLLDKLGG GAWQAKKARL KERIREMADK LIRVAAERAL RRAPVIDPPP GAWESFCARF
     PYTETDDQLR AIEDVLADMT SGNPMDRLIC GDVGFGKTEV AMRAAFVAAM SGVQVAVIAP
     TTLLARQHYK SFAERFRGFP LNVAPLSRFV SAGDAAKTRD GITKGTVDIA VGTHALLAKG
     IRFKDLGLLI IDEEQHFGVG HKERLKELRT DIHVLTLTAT PIPRTLQLSL SGVRDLSIIG
     TPPVDRLSIR TYVSEFDGIT IREALLREHY RGGQSFFVVP RLTDLPEIEA FLKEQVPEVS
     YVVAHGQMAA GELDDRMNAF YDGRYDVLLA TTIVESGLDI PTANTMIVHR ADMFGLAQLY
     QIRGRVGRSK TRAYAYLTTK PRAKLTDTAE KRLRVLGSLD TLGAGFTLAS QDLDIRGAGN
     LLGEEQSGQM RDVGYELYQQ MLEEAIAKIR SGEGEGLLEE SGQWAPQINL GVPVLIPEEY
     VPDLDVRLGL YRRLSELSTK VELEGFAAEL IDRFGKLPRE VNTLLLVVRI KDMCKKAGIA
     RLDGGPKGAT IQFHNDRFAR PEALVTFLQD QKGDAKIKDN KVVIRRDWAS EGDKIKGAYA
     IARDLAEKAG AIRLRKA
//
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