ID A0A239XM99_9FLAO Unreviewed; 1122 AA.
AC A0A239XM99;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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 ECO:0000313|EMBL:SNV47797.1};
GN ORFNames=SAMEA4412677_01803 {ECO:0000313|EMBL:SNV47797.1};
OS Chryseobacterium taklimakanense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=536441 {ECO:0000313|EMBL:SNV47797.1, ECO:0000313|Proteomes:UP000215196};
RN [1] {ECO:0000313|EMBL:SNV47797.1, ECO:0000313|Proteomes:UP000215196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13490 {ECO:0000313|EMBL:SNV47797.1,
RC ECO:0000313|Proteomes:UP000215196};
RG Pathogen Informatics;
RL Submitted (JUN-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; LT906465; SNV47797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239XM99; -.
DR KEGG; ctak:4412677_01803; -.
DR Proteomes; UP000215196; Chromosome 1.
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:UP000215196}.
FT DOMAIN 572..733
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 742..908
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1122 AA; 128375 MW; 24116297F224CE2C CRC64;
MQLKNISETL LPELLKRNFG YEIFNELENS QSISVKGFAG SAPSVFAAEL FLIQKKPVLF
LLNDKEEGLY ATSELEELLG KENVLYFPPS HLEPYQIEKV QNANLVLRTE VLNRLNSETQ
PKVIVAPFAA LSEKVLKKED FKAISHHIKV GDTLDFDFVD ELLTHYQFHQ TDFVSEPGEF
SVRGGIVDVF SYSNEEPYRI TFFGSEVESI KTFDIETQLS KQKIDEFQLV SNMNFTVSGS
KVPFFDLMNN DSIIVARNAF LGEKKIRDFY EKAEENFLKL SRELKHQTPQ ELFISEEILH
QNLQKFKFVD FTAQALSGLN LKTVQLSQTA QPSFHKNFEL LAEDLNNKKK EGYETWISFS
SEKQKERLES ILEEISTETD FRSFKSELHE GFVDAQLKIS VYTDHQIFDR YQRFQAKNAF
AKSEQLTLKD LMSLKIGDYI THIDHGIGKF MGLVKVNNDG KVQECFKLVY KNQDLLYVSI
HSLHKISKYN GPEGREIVLS KLGSPAWKSL KQKTKAKVKQ IAFDLIKLYS QRKSAKGFAF
TPDSYLQNEL EASFIYEDTP DQEKATIDVK KDMEAPTVMD RLVCGDVGFG KTEVAIRAAF
KAATDGKQVA VLVPTTILAF QHYRSFKERL KDFPVNISYL NRFRTAKQKS ETKEGLKNGI
IDIVIGTHQL VGKDIEFKDL GLLIIDEEHK FGVNVKDKLK TLKNNIDTLT LTATPIPRTL
QFSLMAARDL SVIKTPPPNR QPVDTQVIGF NEEIIRDAVA YELHRDGQVY FINNRIENLK
DIAGLIQRLV PDARVITGHG QMEGKQLEQN VLDFMEGKYD VLVSTTIVES GVDVPNANTI
FINDAQKFGM ADLHQMRGRV GRSNRKAFCY LITPPYDLMT SDARKRLEAI EQFSDLGSGF
QIAMKDLEIR GAGDLLGAEQ SGFINEMGFE TYQKIMQEAL EELQNDEEFE NLFDNEEERK
KLITTTKDVN IDTDMELMLP DSYVQSTEER LTLYQKLAEI PNENELQRFE NQLTDRFGEL
PKEAKNLLKS VELKWLAAEI GFEKIVVKNG IFLGYFPANP QDKFYSGDKF KQIISYLNQN
PTEATLKEKN NQLLMRKEKV QNVDEVNGVL VRILDFERNV SK
//
