位置:首页 > 蛋白库 > MPH1_CANGA
MPH1_CANGA
ID   MPH1_CANGA              Reviewed;        1052 AA.
AC   Q6FPQ3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=ATP-dependent DNA helicase MPH1 {ECO:0000250|UniProtKB:P40562};
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:P40562, ECO:0000250|UniProtKB:Q9UT23};
DE   AltName: Full=FANCM-like protein 1 {ECO:0000250|UniProtKB:Q9UT23};
GN   Name=MPH1 {ECO:0000250|UniProtKB:P40562}; OrderedLocusNames=CAGL0J01980g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: ATP-dependent DNA helicase involved in DNA damage repair by
CC       homologous recombination and in genome maintenance. Capable of
CC       unwinding D-loops. Plays a role in limiting crossover recombinants
CC       during mitotic DNA double-strand break (DSB) repair. Component of a
CC       FANCM-MHF complex which promotes gene conversion at blocked replication
CC       forks, probably by reversal of the stalled fork.
CC       {ECO:0000250|UniProtKB:Q9UT23}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000250|UniProtKB:Q9UT23};
CC   -!- SUBUNIT: Interacts with the MHF histone-fold complex to form the FANCM-
CC       MHF complex. {ECO:0000250|UniProtKB:Q9UT23}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40562}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       FANCM sub-subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR380956; CAG60740.1; -; Genomic_DNA.
DR   RefSeq; XP_447791.1; XM_447791.1.
DR   AlphaFoldDB; Q6FPQ3; -.
DR   SMR; Q6FPQ3; -.
DR   STRING; 5478.XP_447791.1; -.
DR   PRIDE; Q6FPQ3; -.
DR   EnsemblFungi; CAG60740; CAG60740; CAGL0J01980g.
DR   GeneID; 2889816; -.
DR   KEGG; cgr:CAGL0J01980g; -.
DR   CGD; CAL0133376; CAGL0J01980g.
DR   VEuPathDB; FungiDB:CAGL0J01980g; -.
DR   eggNOG; KOG0354; Eukaryota.
DR   HOGENOM; CLU_002513_1_0_1; -.
DR   InParanoid; Q6FPQ3; -.
DR   OMA; IRPHIFI; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0033677; F:DNA/RNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0070336; F:flap-structured DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:EnsemblFungi.
DR   GO; GO:0007535; P:donor selection; IEA:EnsemblFungi.
DR   GO; GO:0036297; P:interstrand cross-link repair; IEA:EnsemblFungi.
DR   GO; GO:0060543; P:negative regulation of strand invasion; IEA:EnsemblFungi.
DR   GO; GO:0000725; P:recombinational repair; IEA:EnsemblFungi.
DR   CDD; cd18033; DEXDc_FANCM; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR039686; FANCM/Mph1-like.
DR   InterPro; IPR044749; FANCM_DEXDc.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR14025:SF20; PTHR14025:SF20; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..1052
FT                   /note="ATP-dependent DNA helicase MPH1"
FT                   /id="PRO_0000333371"
FT   DOMAIN          89..256
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          432..649
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          495..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          798..832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1002..1052
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           204..207
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   COMPBIAS        503..536
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1002..1029
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1030..1044
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         102..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1052 AA;  120576 MW;  9A3496875A22095A CRC64;
     MEDSDFDDAE LDELYEKAIN RRVNETLIRR SLPVQRDLQN GVVPGQDTYY EEIRTEVTFG
     PTHHQLNEEL LHSYIYPTNF EVRDYQFDIV RKGLLQNILC AIPTGMGKTF IASTVMLNFF
     RWTKTAKIIF TAPTRPLVAQ QIKACLGITG IPHDQTAILL DKTRKNREEI WANKRVFFTT
     PQVVENDLKR GVLNPKDIVC LVIDEAHRAT GSYAYANLVK FINRFNSSYR LLALTATPAT
     DIEGVQEVVN NLNISKIEIR TEESMDIVKY MKKKIKDRVN IQTTVEIENI VEQLGIAILP
     VLNQAVELGI YESCPPSAIN AFKAMQKSQA IIMNPSIPEG IKWRNYFILQ LLNHVGQMLK
     RIKIYGIRTF FSYFQNKVKE FTTKYDLGKS TNKIAAGFYY HPMIQAITKE CEEKIKDPNF
     LGHGKLEHLR DELTQFFYEN PFESRVIIFT ELRESALEIV KCIDSMENSE IRPHIFIGQA
     KGKEGFDEVK FVRKHGPKGR KKSDREKRLE EERRMDEEKK QAALQEKLER TSRRTGSSEE
     AQLSGMNQKQ QKEVIKKFKS GLYNVLVCTS IGEEGLDIGE VDLIICYDTT SSPIKNIQRM
     GRTGRKRDGR IVLMFSSNEA SKFDQSMNDY YNLQKLISQH LVQYRKSDRI LPPENQEPEC
     EKKFIEVSEE DQELNNMEDT DDVIRFATQC MLGKIPKTKK GRDKGKAKKG KTFFMPDNVI
     TGIITANNLV RKRKSAQNGS GAALLDSIVN DDIDLEDEDG QVEILDVDQE VNRRLASNAV
     QKTNDMALQI RNEETPEIGD TRNKAKASSS MKVKKEPTMA VDHSDDEEDL PLSRHVERAS
     RETAKEVPNA TNVAEKPFPP LEFGVQRPSK RQRLQPEVQP EVQPEVQPEV QPEVQPEVQP
     EVTVKPEVKI KTEEGSKLYK NIFFSDEGFL QPHEKELFLS KYNPEDATVT IEPVPRFVRA
     HGRVKHSKRT EQLITLFEDM NHNRVARTIE MNKLRGIARR LHTVSQSQGQ SNSQSQAHST
     SQKSQQASQK DRSSQDKDLT NSELEDLLDS DF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024