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Database: UniProt
Entry: A0A139SI68_9BACT
LinkDB: A0A139SI68_9BACT
Original site: A0A139SI68_9BACT 
ID   A0A139SI68_9BACT        Unreviewed;      1210 AA.
AC   A0A139SI68;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=AXK12_07880 {ECO:0000313|EMBL:KXU34184.1};
OS   Cephaloticoccus capnophilus.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC   Cephaloticoccus.
OX   NCBI_TaxID=1548208 {ECO:0000313|EMBL:KXU34184.1, ECO:0000313|Proteomes:UP000071392};
RN   [1] {ECO:0000313|EMBL:KXU34184.1, ECO:0000313|Proteomes:UP000071392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CV41 {ECO:0000313|EMBL:KXU34184.1,
RC   ECO:0000313|Proteomes:UP000071392};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXU34184.1}.
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DR   EMBL; LSZP01000060; KXU34184.1; -; Genomic_DNA.
DR   RefSeq; WP_068713162.1; NZ_LSZP01000060.1.
DR   AlphaFoldDB; A0A139SI68; -.
DR   STRING; 1548208.AXK12_07880; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000071392; 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; 3.40.50.300; 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; 3.
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:UP000071392}.
FT   DOMAIN          626..787
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          809..962
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1148..1177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1210 AA;  133785 MW;  452174A27BE81826 CRC64;
     MSKARAQVVS GVCPPARGLA LAELIAAHPE QTLWLVVAPD AKTAEHLAED IPFFQNLGEA
     RSTKTRASAC DREHAPKKKR AAPPRPIIEA ATFPEAMPDT RDMRDAFAAS SQRLAVLSKL
     RELRATVAGD STRRRSAPLD ARAGAPLVVL CTLPALLQPV PALEALSSRE ITLRTGQAQP
     FAGLLEQLQA LDYDCEALCE APGHYAVRGG IIDLYPITAT QPYRVDFFGD EIESIRLLDP
     VTQRSGSPVE SITLSATPRV KLDPARSGLA DYLPADHTAL VFIEAAELDE VFRRETTSEG
     EGQADPLETL STIRAKAALS ISLCEIEQES ELFPTPPHDA EGPARPSLDK RVCDPLALHR
     RYPTEALLAH ERVAAEADAR RDFLEQLVQW QRDGYALHFV ASRDGEAQRM TEILEEEGLA
     KTLRVQTHIG SLNEGFLYRS GADSSPRRLA FVTEVEIFGR QRARRPRATT QQVAQRAQID
     QLLDFSELVE GDYVVHLQHG IAHFRGLATL DTAQGPREVI SLEFDEQVTL HVPLQESHLI
     SRYVGLTKVR PQLGKIGSGR WEKTRKAAER ATIDLAAELL RIHAAREAQP GFACPADTDW
     QKEFEASFPY TETRDQLRAI EDTKADMERT RPMDRLICGD VGFGKTEVAI RAAFKAVQGG
     RQVALLVPTT VLAQQHLNTF RERMAGYPIV VEMLSRFRSR KDQQAILAAT AAGQVDILIG
     THRLLQSDVA FKSLGLLIVD EEQRFGVKHK ERFKALRATL DVLSMSATPI PRTLYMALTG
     ARDLSVIETP PADRHPIHTI VKTYDEKLVA EAIHQELRRG GQVFYLHNRV QTIDLIAARL
     RELVPGARVG VGHGQMEPTE LERVMTDFVA GTYQVLVCTT IIESGLDIPN CNTIIIESAD
     RFGLSQLYQL RGRVGRFKHQ AYAYLLLHRH SRLLDIARQR LGAMRQHNQL GAGFRIAMRD
     LELRGAGNLL GSQQSGHIVG VGFELYCQLL RQSVARLKGE AQAAAIRATV KLDFVVVGDD
     RETAETKAGD DLRPTRRTQN KGQFVSGYTA LRDAEHAAAP PLAPIRACLP ANYIPETRLR
     IDFYRRLALA GSSAQLKEIA AELRDRFGKF GEPVNALLTL TEIRIRAEQK GILSVETEGA
     KLKCLRAKPL NTPSAPPGRA SNGSPPNNPA KQPWVQHGTR FPRLTAPKPL LRLREILIFL
     NNLPDSPPNS
//
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