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Database: UniProt
Entry: E4UDC1_LIBSC
LinkDB: E4UDC1_LIBSC
Original site: E4UDC1_LIBSC 
ID   E4UDC1_LIBSC            Unreviewed;      1185 AA.
AC   E4UDC1;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 75.
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   OrderedLocusNames=CKC_03060 {ECO:0000313|EMBL:ADR52361.1};
OS   Liberibacter solanacearum (strain CLso-ZC1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=658172 {ECO:0000313|EMBL:ADR52361.1, ECO:0000313|Proteomes:UP000007038};
RN   [1] {ECO:0000313|Proteomes:UP000007038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLso-ZC1 {ECO:0000313|Proteomes:UP000007038};
RA   Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y., Zhou L.,
RA   Glynn J.;
RT   "Complete genome sequence of Candidatus Liberibacter solanacearum CLso-
RT   ZC1.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CLso-ZC1;
RA   Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y., Zhou L.,
RA   Glynn J.;
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ADR52361.1, ECO:0000313|Proteomes:UP000007038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLso-ZC1 {ECO:0000313|EMBL:ADR52361.1,
RC   ECO:0000313|Proteomes:UP000007038};
RX   PubMed=21552483; DOI=10.1371/journal.pone.0019135;
RA   Lin H., Lou B., Glynn J.M., Doddapaneni H., Civerolo E.L., Chen C.,
RA   Duan Y., Zhou L., Vahling C.M.;
RT   "The Complete Genome Sequence of 'Candidatus Liberibacter solanacearum',
RT   the Bacterium Associated with Potato Zebra Chip Disease.";
RL   PLoS ONE 6:E19135-E19135(2011).
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; CP002371; ADR52361.1; -; Genomic_DNA.
DR   RefSeq; WP_013462017.1; NC_014774.1.
DR   AlphaFoldDB; E4UDC1; -.
DR   STRING; 658172.CKC_03060; -.
DR   KEGG; lso:CKC_03060; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_3_1_5; -.
DR   Proteomes; UP000007038; 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; 3.40.50.11140; -; 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}.
FT   DOMAIN          639..800
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          821..975
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1185 AA;  134226 MW;  6303EEDCF9A28E4E CRC64;
     MIFGDYINKI NEKPCKKITL SQVFPGTEPF VLAEIARSGL SLVYIGSDER ALVNIKKTLA
     FIVPDIDVII FPAWDCLPYD RISASPRVVT DRLACFSHLI SCNPSKKTSI ILTTVSAVMC
     RSVNFMSIKD CKFSIQSKDQ ISMAKVIEKL EKNGFQRVNT VYKVGEYAVR GGILDVYGPS
     EKYPVRLDFF GDTIESLRLF DYASQRTIRE ISTFTINTLS EVVLTSENIS LFRKNYLLNF
     GAATQKDLLY VTVSQGNRYP GMEHWLPFFY QKMETIFSYL ADFCIVTDSA VKDTAHKRSQ
     LIQDYYEARC QHSSDKKNYS IYKPILPEKL YLTYQQFEAM LESSNKLIQM TPFSQQETSH
     SCVVCLNVRP GKSWVPSAVQ KIESQENWES MNRFDRFLSY VAQQFQKGKK AFIAASSKGA
     LQHLIHLMES DGLNKIKKID CFNEIHSLAK EEIAAAVLPI DQGFETGNMI LVTEKDLLGK
     RIIRRTVRKS SLANSFFESS NIEEGSIIVH AEHGIGRFIR LSSIEVSGTS HDCLELHYAD
     NAKLFVPVEN IDLISQYSTE NETIMLDKLG GSSWQSRKSN LKKRLEDLAQ KLVDIAAKRL
     IHNVPALTVS QDLYSQFVKK FPHVETEDQE KAVDAVIQDF TSGHLMDRLI CGDVGFGKTE
     IALRAAFIAV MNGLQVAVIA PTTLLVRQHF RLFSERFQDF PVRIVSVSRF VKPKEVALHK
     KAIAEGQVDI VIGTHALLDP KITFSNLGLI IVDEEQHFGV KHKEALKETH TGVHVLTLSA
     TPIPRTLQLA ITGVRELSLI SMPPINRIAC RTSISIFDPL LIRETLMREY YRGGQSFYVC
     PRLLDLDKCY DFLQSEVPEL KVAMAHGQMS PKNLEETMNG FYERKYDILL STSIVESGLD
     LPNANTIIIQ RADMFGLAQL YQLRGRVGRS KISSFALFLL PENKPLTSSA QKRLRILQSL
     NTLGAGFQLA SHDLDIRGTG NLLGEEQSGH IKEVGFELYQ KMLGETVASI KGKRELVDSD
     WSPQIMIEAS VMIPDSYVSD VNLRLSLYRR LGNITDHTDI NRFKEEMVDR FGSLPIEVVH
     LLKVLFLKLL CRIANIEKMD IGPKGIIVQF RNKKFHNPEK LLQYIMQQKG KIIIRPDQSL
     FFDCLLPTIN KRFIEAKHIL SQLIKLIDVD IQKCDKNDSA SLKVK
//
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