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MPH1_ASPCL
ID   MPH1_ASPCL              Reviewed;        1119 AA.
AC   A1CS00;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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}; ORFNames=ACLA_031540;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR   EMBL; DS027059; EAW08421.1; -; Genomic_DNA.
DR   RefSeq; XP_001269847.1; XM_001269846.1.
DR   AlphaFoldDB; A1CS00; -.
DR   SMR; A1CS00; -.
DR   STRING; 5057.CADACLAP00003025; -.
DR   PRIDE; A1CS00; -.
DR   EnsemblFungi; EAW08421; EAW08421; ACLA_031540.
DR   GeneID; 4701240; -.
DR   KEGG; act:ACLA_031540; -.
DR   VEuPathDB; FungiDB:ACLA_031540; -.
DR   eggNOG; KOG0354; Eukaryota.
DR   HOGENOM; CLU_002513_0_0_1; -.
DR   OMA; FMMRAIF; -.
DR   OrthoDB; 989616at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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..1119
FT                   /note="ATP-dependent DNA helicase mph1"
FT                   /id="PRO_0000333363"
FT   DOMAIN          313..481
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          651..825
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          112..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          823..905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1002..1042
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           429..432
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   COMPBIAS        180..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        881..895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1011..1042
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         326..333
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1119 AA;  125004 MW;  9E3A3707C1EE3382 CRC64;
     MSDSDNGSAD SFDDEIDDFV VTTPRQSAGA WMLATRKASY DKNIVTRRLE SDSVNALGSD
     SFIDRDEEDE LPSPDHALFE GIDFENVEKT SRYKVFVPKH SNYQENIFVT QLTQPPSPPE
     MIRGPRWKKP DPEPPTPKPP ATMTIPASRA DQYRDDEKEI EAAIAASLRS FEEENCGPTS
     AMVDKSSATR TAAVPSNAQK QHVADVPFDV DDIPDDAFDS DLSLSPPRSN SQAALRGPVQ
     SQFSTNRPLG LRQSTLFGMT ARASEASIPR GEQVFSPPDK NEAPTHHKLD EEALNTWIYP
     TNLGKTRDYQ FNITQRGLFH NLLVALPTGL GKTFIAATIM LNWYRWTKSS QIIFVAPTKP
     LVSQQISACF GIAGIPRSQT TMLTGEAAPG IRAEEWKAKR VFFMTPQTLI NDLKSGIADP
     KRIVLLVVDE AHRATGGYAY VEVVKFIKRY NKSFRVLALT ATPGSTVESV QAVIDGLDIA
     KVEIRTEQSL DIREYVHARN TDVQTFQNSD EMVLCMDLFS RTLQPLVDQL CSLNAYWGKD
     PMALTPFGLT KARQQWMLSD AGRNANYGLK GKVNAIFTVL ASLAHAIDLL KYHGITPFYR
     HLVHFRSNTD GQKGGKYQRQ IVQDESFKKL MNHLQPWTKN PEFIGHPKLE YLKQVVLNHF
     MDAGEGSGAD GNHTRSATRI MVFAHFRDSA EEIVRVLKRY EPLIRPHVFV GQSSAKGSEG
     MDQKTQLSIV QKFKKGDYNT IVATSIGEEG LDIGEVDLIV CYDSSASPIR MLQRMGRTGR
     KRAGNIVLLL MQGKEEESYI RAKDNYEKMQ EMIASGTRFA FHDDTSPRIL PPGIRPTADK
     KQIDIPVENT QADLPEPKRR ARPPKRPPKK FHMPDDVETG FSKASSLTGN KGAKKTDKQT
     TIRKPTPEPV AIPALEEVLL TPSQQNDLER RYCHIGGTSP QFIRNPRVDA YPRLQSVPRP
     TRAVKHGALT SRMIGTLQKM HQVGADCESR YKDILALESS KRPEDSVLVQ ESARPRQNKK
     LSVGVSRPSK AQPPQTQSTL APIREGLVDD GILEPTVPNE LASLLGHQNP KPFYSSQISQ
     DDLESDFDLP DFDTLINRNA ERTTPRKRNR FVLGDDSDE
 
 
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