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Database: UniProt
Entry: A0A0Q6KJW4_9SPHN
LinkDB: A0A0Q6KJW4_9SPHN
Original site: A0A0Q6KJW4_9SPHN 
ID   A0A0Q6KJW4_9SPHN        Unreviewed;      1157 AA.
AC   A0A0Q6KJW4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-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=ASG67_06610 {ECO:0000313|EMBL:KQU55785.1};
OS   Sphingomonas sp. Leaf339.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736343 {ECO:0000313|EMBL:KQU55785.1, ECO:0000313|Proteomes:UP000051371};
RN   [1] {ECO:0000313|EMBL:KQU55785.1, ECO:0000313|Proteomes:UP000051371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf339 {ECO:0000313|EMBL:KQU55785.1,
RC   ECO:0000313|Proteomes:UP000051371};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQU55785.1, ECO:0000313|Proteomes:UP000051371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf339 {ECO:0000313|EMBL:KQU55785.1,
RC   ECO:0000313|Proteomes:UP000051371};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQU55785.1}.
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DR   EMBL; LMRS01000012; KQU55785.1; -; Genomic_DNA.
DR   RefSeq; WP_056528148.1; NZ_LMRS01000012.1.
DR   AlphaFoldDB; A0A0Q6KJW4; -.
DR   STRING; 1736343.ASG67_06610; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000051371; 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:UP000051371}.
FT   DOMAIN          627..788
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          809..963
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1157 AA;  126048 MW;  DC421BE72238ADA2 CRC64;
     MPDLKTILSA KTPLTLAGVP TGFQPSLLAD LARAAGRVVF ITADDAAMRA IASTAPFFAP
     ELEVVTFPAW DCLPYDRASP TLRVMAERVA ALYRLQGKAP KSGGVPQLVL TTANAATQRV
     LTPFRIRQLV ASLAPGERIG RDDLATLLQA NGYVRTETVH DHGEYSVRGG IVDLFPSGEE
     QALRLDFFGD EIESVRTFDP ADQRTTGRVD GFTLLPASEA LLDADSIKRF RTRYRETFGA
     TATGDPLYQA VSDGRRQAGM EHWLALFEDK LATLFDHLGD AVVVRDGAVA AAAESRIEAI
     ADYYDNRKRA EAAQPGSYRP LPAKALYLDA EAWATGLAEA TAHVTTAFHE PESTRVLDFG
     VDGPRDFGAE RAAQANVYEA VVAHVEKLRR EGRKPVLASY SVGARDRLGS LLKDYGLKGG
     KNAETWQEAL GVADTSKSFG VALVMLPLDH GFAAPGVAVL TEQDMLGDRL IRRNKRKKSA
     DAFLAELATL SPGDLVVHSD HGIGRYEGLT SIPVGKSPHD CVALSYAGGD KLYVPVENLE
     VLTRYGSGED GAALDRLGGE AWQRRKSKMK ERIREIAGEL IAVAAERALR PGEVAEPDAS
     GYPSFVDRFP YDPTDDQDRA IDDVLGDLAA GKPMDRLIVG DVGFGKTEVA LRAAFVAAMG
     GMQVAIVCPT TLLARQHFNN FSARFEGFPI KIGRMSRLVG TAETKATKEG TASGDLDVVI
     GTHALLAKNV SFKRLGLVIV DEEQRFGVTH KERLKALKAD VHMLTLTATP IPRTLQMAMS
     GLRELSVIQT PPVDRLAVRT YIMPWDPVVL REALLREHYR GGQSFMVTPR VADLPDIEEF
     LRNEVPEIRY VIAHGQMSAS EVEERMSAFY EKRFEVLVST TIIESGLDIP SANTMIVNRA
     DRFGLAQLYQ LRGRVGRSKT RAYAYMVTPP ERQMTETADK RLKVLSDLDT LGAGFQLASH
     DLDIRGAGNL LGDEQSGHIK EVGYELYQSM LEEAIMDAKA GGFASRPRDF SPQITVDAPI
     LIPEDYVPDL DLRMGLYRRL NDVEDAGEVE AFAAEMIDRF GALPDATENL IRVIEIKLNA
     KKACIAKMDV GAKGVLVSFH DDKPPNVAGL IAYVDRLGGV AKLRPDSKLV LQRVWPDAKA
     RLHGALQLSK GLAKVAG
//
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