ID A0A1G5ALB2_9CLOT Unreviewed; 1172 AA.
AC A0A1G5ALB2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN03080606_00185 {ECO:0000313|EMBL:SCX78600.1};
OS Alkaliphilus peptidifermentans DSM 18978.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=1120976 {ECO:0000313|EMBL:SCX78600.1, ECO:0000313|Proteomes:UP000198636};
RN [1] {ECO:0000313|EMBL:SCX78600.1, ECO:0000313|Proteomes:UP000198636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18978 {ECO:0000313|EMBL:SCX78600.1,
RC ECO:0000313|Proteomes:UP000198636};
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; FMUS01000001; SCX78600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5ALB2; -.
DR STRING; 1120976.SAMN03080606_00185; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000198636; 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:UP000198636}.
FT DOMAIN 640..801
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 810..976
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1172 AA; 134575 MW; D5AEBEC2F0405A48 CRC64;
MLSKVLLSPI KKTIEYNQII GAIKGRKTPV VIHGLSESQK PHIAFGIFEE LDGQVCIITY
NELEARQIYE DLKFYMGERI LFFPTKEVVF YQIEATGEAI QAERAKTLEK LAEGGNYIVI
TSIDALLLKL TKPQYYIYHH ITFRVGETIE LQQMLNTLLI QGFERVDRVE RSGEFSIRGG
IIDIFPASEE APYRIELFDD EVDSIRRFQV DTQISINKLE EIKIYPTIET IIEPEDNKFI
NEKLSKELKK TLEKLDEDPG KRLKEKFDEI LEKLNELADT KTAQLLLPYL EGREASLLEY
LDRNATLILD EPRRLREKGE GVLKEFNDNF ETLLERGEVL PSQCKLQFSY DEILGKMVRH
PVVTLNLLPK YNPDFQPKEI INFASRSVQT FNGKMDFMVE ELKLLQYKGY KVVLLPGTKE
RALRLLELLN ERGLNVSFVV TPQEDLMSGQ VIIMQGSVHR GFEYVGAKYM LITDNEIYGV
HKRKKQITKR KDAAPIKSFI DLKVGDYVVH EGHGIGKYVG IQQLRVDGLK KDYLKIRYSG
EDNLYVPTDQ MDLIQKYVGS EDHPPKVNKL GGSEWIKTKA KVKKAIEDMA QDLLKLYAER
QKSRGHIFSA DTEWQKQFED LFPYEETPDQ LKCIEEVKLD MENHLPMDRL LCGDVGYGKT
EVAIRAAFKA VMDGKQVALL VPTTILAQQH YNTFAQRFSG FPVKIDMLSR FKTPQQQKNI
LENVRTGNVD VIIGTHRILS KDIQFKDLGI LIIDEEQRFG VKHKEALKHL KKNIDVLTLT
ATPIPRTLHM AMIGIRDMSV IEDPPEERFP VQTYVMAHNE SIIADAITRE IARGGQVYYV
YNRVKGIHQM AARLTNLIPH ARIGVGHGQM SERQLENLML EYYEGEYDVL VCTTIIETGL
DIPNVNTIII HDADRLGLSQ LYQLRGRVGR SNRQAYAYLM YEKDKVLSEV AEKRLKAIKE
FTEFGSGFKI AMRDLEIRGA GNLLGGEQHG HMSAIGYDLY VKLLEEAIGE LKGESVERFE
ETTIELSIDA YISDKYIINQ SQKIEIYKKI ASIRNKEDLY SVEEEIEDRF GDIPNSVRNL
LLISYIKAMA KNLRITSITQ KSKEITISFK DSIMLMPENI GEALHTYNRR LSFHGTKVPY
FVYKVIETDQ NKILSELKDI IEKISGLQKT AN
//
