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Database: UniProt
Entry: A0A3T1CXU3_9BACL
LinkDB: A0A3T1CXU3_9BACL
Original site: A0A3T1CXU3_9BACL 
ID   A0A3T1CXU3_9BACL        Unreviewed;      1173 AA.
AC   A0A3T1CXU3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, 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   ECO:0000313|EMBL:BBI30653.1};
GN   ORFNames=KCTCHS21_00520 {ECO:0000313|EMBL:BBI30653.1};
OS   Cohnella abietis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=2507935 {ECO:0000313|EMBL:BBI30653.1, ECO:0000313|Proteomes:UP000289856};
RN   [1] {ECO:0000313|EMBL:BBI30653.1, ECO:0000313|Proteomes:UP000289856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS21 {ECO:0000313|EMBL:BBI30653.1,
RC   ECO:0000313|Proteomes:UP000289856};
RA   Jiang L., Kang S.W., Kim S., Jung J., Kim C.Y., Kim D.H., Kim S.W., Lee J.;
RT   "Complete genome sequence of Cohnella hallensis HS21 isolated from Korean
RT   fir (Abies koreana) rhizospheric soil.";
RL   Submitted (JAN-2019) 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; AP019400; BBI30653.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3T1CXU3; -.
DR   KEGG; cohn:KCTCHS21_00520; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000289856; Chromosome.
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:UP000289856}.
FT   DOMAIN          626..787
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          808..962
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1173 AA;  133327 MW;  3663C1C0FC1DB243 CRC64;
     MKPLIQSLVT DPDLISIIQG LKGGMREQLV AGLSGSARQV TLAGMYRELQ RPILVITHNM
     FSAQKMTDDL QECLSTDEVL LYPANELIAA ETAISSPETS ARRLEVLLKL AEGFRGIIVV
     PFAGVRKFQP DLLTMSEAHI DLKVGDTLPM EQFLRGMIEL GYERVDRVEQ KSHLSVRGGI
     VDFFPLASSS AYRVEWFDDE IDSIRTFDPA DQRSIDKLES YTVQPCREWI AGERRFQNAA
     KHAQDLLEKQ LEKMADRQAK ERLSSEISRE IELLRQNVYF TEIYKYISLL YPERQTLLDY
     IPKDTVLLMD EPNRLGETAR QLERDESEWT THLLQQGKSL PGFVLAVPAE QALYPKGFQT
     VYMSLFVRQI PHTQPQNIIN FVCRSMQNFH GQMNVLKAEM ERWRKGGIKI VMLAGNSERA
     DRMRRVLEDY QIEAPEILQG NLQSGFELPS IKLVVITEGE MFTQKQRKAR RVDRHLDNAE
     RIKSYTELKV GDYVVHQNHG VGKYLGIGTL EVGGIHKDYL HIVYAAGDRL SVPVEQFDLI
     QKYVGNEDKE PKVSKLGGSD WNRAKSKVRS SVQDIADDLI KLYAARQSTV GFGFGEDTPY
     QQEFEEMFPY EETVDQLRAI REIKEDMQTA RPMDRLLCGD VGYGKTEVAI RAAFKAAIEG
     KQVAVLVPTT ILAQQHYETF RERFSGYPFN IKVLSRFRTR KEQTDTMKGL KAGTVDVVIG
     THRLLSQDII FKELGLLIVD EEQRFGVTHK EKLKRIKTNV DVLTLTATPI PRTLHMSMLG
     VRDLSVIETP PENRFPVQTY VVEYSPTLIR EAVERELARD GQVYYLFNRV QGIYQMAEQI
     SALVPDARVA VAHGQMSEQE LERTILDFLD GEYDVLVSTS IIETGVDIPN VNTLLVHDAD
     RMGLSQLYQL RGRVGRSNRI AYAYFTYQRD KVLTEVAEKR LQSIKEFTEL GSGFKIAMRD
     LTIRGAGNLL GAEQHGFIAS VGFDLYSQML AEEIQSRKSE MGGVVLPPQP VNTQLDLGVD
     AYLPPEYIYD SIQKIEIYKK VAAATSLEDV ADLFEELMDR FGEPPKAVLN LMTVVRLKVY
     GRQYGIESIV RRGDEVTLKL EERRREDVDS SKLKALEAKF QGRMVQAITA QQLLIRLKVR
     GLDENALLAL VEDFLVQYKE ATKSKGELQD VAP
//
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