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Database: UniProt
Entry: Q21JS3_SACD2
LinkDB: Q21JS3_SACD2
Original site: Q21JS3_SACD2 
ID   Q21JS3_SACD2            Unreviewed;      1153 AA.
AC   Q21JS3;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   24-JAN-2024, entry version 118.
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=Sde_1796 {ECO:0000313|EMBL:ABD81056.1};
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD81056.1, ECO:0000313|Proteomes:UP000001947};
RN   [1] {ECO:0000313|EMBL:ABD81056.1, ECO:0000313|Proteomes:UP000001947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024
RC   {ECO:0000313|Proteomes:UP000001947};
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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; CP000282; ABD81056.1; -; Genomic_DNA.
DR   RefSeq; WP_011468276.1; NC_007912.1.
DR   AlphaFoldDB; Q21JS3; -.
DR   STRING; 203122.Sde_1796; -.
DR   KEGG; sde:Sde_1796; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_0_3_6; -.
DR   OMA; WAPPCRE; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000001947; 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   CDD; cd18810; SF2_C_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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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:UP000001947}.
FT   DOMAIN          622..783
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          804..960
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1153 AA;  130334 MW;  D3030B6B1A8A01CC CRC64;
     MTSNMPLPLP SKLGDKKTWG GVSGLARVFA CAEAAAQHNG TTVIIVQSMT EADRFARDLM
     LLTKGKKNTP EVLQFADWET LPYDNFSPHQ DIISDRMRCL YQLSNQAQAI VVVAASTLMQ
     RLAPANYIIA NSLVVEKNET INRDNLLTSL INAGYQRVDT VFNHGEFAIR GALLDIFPMG
     SSAAYRIELF DDEVDSIRTF DPETQRTVDQ VSKIELLPGK ECQLDAEGIS RFKLNWYENF
     NVDHRECPVF QDVSSGISPA GIEYYLPLFF EQTASLFDYL HENTLVMVTK GFETAVEDFW
     RDASSRFESH NIDMRRPLLP PAKVFHSVSE IYSQLKRFQR VVLEPTQVEE RSGSANIKTL
     STPNLNIDAK AQNPLYKLEE FIYSYDGRIL FCAESNGRRE TLKEHFKKID LQPEDVASTD
     AFLQGKSSIA ICVADFQEGL HLKTPNICII AESQLFGQRV QQYRRRKESN TDFNENIVKN
     LTELKIGAPV VHIEHGVGRY LGLQTIEFDG QKDEFLVLEY ANEAKLYVPV ANLHFISRYS
     GAEDSSAPLN RLGSDQWQKA KRKAAEKLRD VAAELLEIYA KRQAREGFQY TYPKDAYEIF
     AESFPFEETV DQQQAIDAVR QDMISAQPMD RLVCGDVGFG KTEVAMRAAF IAVQNSKQVA
     VLVPTTLLAQ QHYENFKDRF ADWPVNVEVI SRFKSSKDIS EIQKKLEAGK VDILIGTHKL
     IQGELIFPNL GLLIIDEEHR FGVRQKEALK ALRTEVDILT LTATPIPRTL NMAMSGIRDL
     SIIATPPAKR LSVKTFVRQS DNAVIKEAIL REIMRGGQLY YLHNEVSTIE KTAADLQELV
     PEARIRVAHG QMRERELEAA MSDFYHKRHN ILVCTTIIET GIDIPSANTI IIDRADKFGL
     AQLHQLRGRV GRSHHQAYAY LLTPHKKAMT ADAVKRLEAI AEAQDLGAGF TLASHDLEIR
     GAGELLGDEQ SGQMQAIGFS LYMEMLDKAV EALKSGKELD FESNFNNNVE FNLRIPALIP
     DDYLPDVHTR VILYKRMASV KNENELNDLQ VEMIDRFGLL PDPIKNLVRQ TRLRLTAEQL
     GVCKVEANNT GGRIEFTTKP NIDPLTIVKM VQTTPQHYRM EGASHLKFFF DMESADERLL
     TIHNIFETLM KSS
//
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