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Database: UniProt
Entry: I0USW9_9MICC
LinkDB: I0USW9_9MICC
Original site: I0USW9_9MICC 
ID   I0USW9_9MICC            Unreviewed;      1249 AA.
AC   I0USW9;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
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:EID50972.1};
GN   ORFNames=HMPREF1324_0515 {ECO:0000313|EMBL:EID50972.1};
OS   Rothia aeria F0474.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Rothia.
OX   NCBI_TaxID=1125724 {ECO:0000313|EMBL:EID50972.1, ECO:0000313|Proteomes:UP000004863};
RN   [1] {ECO:0000313|EMBL:EID50972.1, ECO:0000313|Proteomes:UP000004863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0474 {ECO:0000313|EMBL:EID50972.1,
RC   ECO:0000313|Proteomes:UP000004863};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (MAR-2012) 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:EID50972.1}.
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DR   EMBL; AJJQ01000032; EID50972.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0USW9; -.
DR   PATRIC; fig|1125724.3.peg.1080; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000004863; 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}.
FT   DOMAIN          704..865
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          890..1040
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1249 AA;  136421 MW;  F80839E2F7302A3C CRC64;
     MKLTGLSRTL LGYPSYRNVV AAAQLPATER SAQTLIGAVP GLHAPLIADI AAAIRNSTRR
     EGVGKEPLTL VITPTERQAE DTAHALGAYL PDNDIALLPA WETLPHERLS PRSDTVGRRL
     GVLRAITQAG ERTPLVLVAP VRAVIQPIVA GIEKLVPVTL TRGEEYSFKE VIKGLTNAAY
     SRVDLVAKRG EYAVRGGIID VFSPTATNPV RLEFFGDELD EIRYFSAADQ RTLTGEGSQP
     DRITLPPCRE LLITPEVMSR AARLVGDYPA ASAMLEKIAG GIYVEGMESL TPLLVERMNT
     LISLLPSGSL ALSVEPERIA ARAEDLVATN EEFLTAAWDT AAEENSAAPI DLGQLRMSEA
     GFRTITATRT EALDAGIGWW EITELIANAE LAASVPDDPA ETDTATEKTS AHCALADAVA
     DGVDTLVVRA SAAASFTGSV QRMLEEVGAL VKDGWRVLAL TNGRGSTDRL IELFNDSEVP
     ASRRDTLDKG IEPGIIEVCE APASAGFLLP QEQLAVFTEG EILGRRGTYA PRGVTGSKLK
     ARRRRNAVDP LSLTPGDYVV HERHGIGRFI EMTSRSVAGV KPAAGQNVPM REYLVLEYAP
     SKRGGAPDRL FVPSEQLDMI SHYVGSEKPT LSKMGGSDWA KTKSRARKAV KEIAADLIKL
     YSARQASRGH AFTEDTPWQR ELEESFPYNE TPDQLNAIYE VKADMEKELP MDRLISGDVG
     FGKTEVAVRA AFKAVQDGKQ VAVLVPTTLL AQQHYETFTE RFSGFPIKIK VLSRFQKPKE
     SRQITEEIAS GAVDVVIGTH RILSESISFK DLGLVIIDEE QRFGVEHKEK LKQMRTNVDV
     LAMSATPIPR TLEMSLTGIR ETSTLATAPE ERHPVLTFVG ARTDAQITAA IRRELMREGQ
     VFFVHNRVAN IDNVAAELAK LVPEARIATA HGRMSEARLE QIIVDFWERR FDVLVCTTIV
     ETGLDISNAN TLIVDNAQNY GLSQLHQLRG RVGRGRERAY AYFLYPPGKP LGEVALERLK
     AVATHNELGA GLQLAMKDLE IRGAGNLLGG EQSGHIAGVG FDLYLRLVGE AVADFRGEKD
     ERDVEVKVDL PVNAHIPHSY IDAERLRLQA YRQIAAADTE QKMAEAREEL TDRYGELPEP
     VQNLLAVTAL RQRARAAGIR EIVVMGPKVR VVTDEQLPDS RQMRLGRVYP GSSHTQPKGL
     QTWLTLLPRP KSSPVGGIEL VDAAMLEWCQ QLIDTIFADV PGASRSAPE
//
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