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Database: UniProt
Entry: D0LU01_HALO1
LinkDB: D0LU01_HALO1
Original site: D0LU01_HALO1 
ID   D0LU01_HALO1            Unreviewed;      1257 AA.
AC   D0LU01;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 86.
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=Hoch_4876 {ECO:0000313|EMBL:ACY17365.1};
OS   Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC   Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX   NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY17365.1, ECO:0000313|Proteomes:UP000001880};
RN   [1] {ECO:0000313|EMBL:ACY17365.1, ECO:0000313|Proteomes:UP000001880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC   {ECO:0000313|Proteomes:UP000001880};
RX   PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA   Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA   Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA   Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA   Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL   Stand. Genomic Sci. 2:96-106(2010).
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; CP001804; ACY17365.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0LU01; -.
DR   STRING; 502025.Hoch_4876; -.
DR   KEGG; hoh:Hoch_4876; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_0_3_7; -.
DR   OMA; NKKAFCY; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000001880; 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; 3.40.50.11180; -; 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   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:UP000001880}.
FT   DOMAIN          701..862
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          908..1066
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          390..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          910..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..929
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1257 AA;  137235 MW;  B69DA0AB6E3916AD CRC64;
     MSMASLDEAI RAVLSETDAP VIAHGLTRAS LALVAARLAE RADERAGPVV VVAPDESSAR
     DLAQDVAFFL PHAQHAAAGT EPLAPPPALH LPALDTSPYA ELSPDRLALA QRMAGLVRLA
     RGGALLGPVV VLSAPALLRR VMPREALLAR TAVLARDDEF DRDATAERLL RAGYTRAPVV
     EDAGTFAVRG GVIDVFTPLY RYPARIELFG DMVESIRLFD PESQRTLRDL DQVYVHPVRE
     TVVSEGAEVR RRILDAADAA HHPSAETRRV LERIDSGEEF VGIETLTPAF HTHLAPLASY
     LVAGDAPPAC WVIVDPDAIG QAAEDEHDVA EDRYRERLDD GRLAFPPSDH YVSPDELRAT
     LAEHAYRLEA RGLEMYQAAA DPLLSASDEM AAAPEAKSKP KAKSKPKPKP EQDGAQLMRF
     GVDDNRLLRA SLERTRRQAA DELMKPLVEA ITAWRGDAYC IAVAAGTMAR ARQLAGLLSD
     YECTAHVIEE RSVDVDALSP GAPPVIYPGE LSAGFALRTD KLVMLTADEI FGPRRRTSVR
     QRAAARRARK ALAGGISDFS QLAPGDHVVH AMHGIGLYRG LAKLPVSATG PAVDFLHIEY
     RGGQFYLPVY RLGEVSRYVG AEGHAPRLDK LGGVTWQKAR KKASAQVKAL AEELLKLYAQ
     RAAQPGHAYP SSDHMFREFE ATFAFEETPD QQRAIDEVLA DMESERPMDR LVCGDVGYGK
     TEVALRACFK AVAGGKQAAL LAPTTVLVEQ HYATVCERFA GWPVSVGRLS RFQSRAEQLD
     TIKGLAAGTV DLVVGTHRVL SKDVRFKDLG LLVIDEEQRF GVTHKERLKR VRTQLDVLTL
     TATPIPRTLH LAMSGLRDLS IIATPPADRR AVRTFVAQVD DGVLREGIRR ELGRGGQVFF
     VCPRIGADPA PSKGKVKGKG KSQGETARRV RRGDISLDEW AEHLRALVPE ARVAVAHGQM
     SAEALEKVMI DFVSGNLEIL VSTTIVESGL DIARANTMFV DRADSFGLAQ LYQLRGRIGR
     SKQRAFCYLL VPPPEKLSSD ARRRLETLQR FSELGAGFQI ASHDLEIRGG GELLGAKQSG
     AIAAVGFEAY AAMLEEAVAE LRSGDAGLVR PRDPELNVDV PGYIPDEYIP DTGQRLDLYK
     RLSDAEDEDE LKILVEEITD RYGELPDEVE LLADLMVLKI HARTLRAQSL ELTQSRMSLA
     LAEDTPLAPQ TLASLARKKA FRLTPDMRLV RNFTAEEGER PSASARACLL ELIACVT
//
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