GenomeNet

Database: UniProt
Entry: A3GH78
LinkDB: A3GH78
Original site: A3GH78 
ID   MPH1_PICST              Reviewed;        1050 AA.
AC   A3GH78;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 3.
DT   18-SEP-2019, entry version 72.
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=PICST_53391;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 /
OS   NRRL Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-
RT   fermenting yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- FUNCTION: ATP-dependent DNA helicase involved in DNA damage repair
CC       by 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
CC       a FANCM-MHF complex which promotes gene conversion at blocked
CC       replication 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
CC       FANCM-MHF complex. {ECO:0000250|UniProtKB:Q9UT23}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40562}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. FANCM sub-subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAZ63005.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AAVQ01000002; EAZ63005.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001387028.2; XM_001386991.1.
DR   SMR; A3GH78; -.
DR   STRING; 4924.XP_001387028.2; -.
DR   EnsemblFungi; EAZ63005; EAZ63005; PICST_53391.
DR   GeneID; 4851627; -.
DR   KEGG; pic:PICST_53391; -.
DR   eggNOG; KOG0354; Eukaryota.
DR   eggNOG; COG1111; LUCA.
DR   HOGENOM; HOG000066122; -.
DR   InParanoid; A3GH78; -.
DR   KO; K14635; -.
DR   OrthoDB; 331426at2759; -.
DR   Proteomes; UP000002258; Chromosome 1.
DR   Proteomes; UP000002258; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   InterPro; IPR039686; FANCM/Mph1-like.
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; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1   1050       ATP-dependent DNA helicase MPH1.
FT                                /FTId=PRO_0000333379.
FT   DOMAIN       95    262       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      431    631       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     108    115       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       210    213       DEAH box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
SQ   SEQUENCE   1050 AA;  120120 MW;  74FCD9B067318AAF CRC64;
     MPIDSDDNVF DDDDDFIELL QDSSNQTSNV TNEIATDSTN STNTRLVVPN NRLLEEIPVP
     KRILLGPTHH KIDYGNLDKY VYPSNFEVRD YQFNIVQRAF YHNLLVALPT GLGKTFIAST
     VMLNFLRWFP ESKMIFVAPT KPLVAQQIKA CCSITGIPSS KVAILLDKTR KNRGEIWDEK
     QVFFTTPQVV ENDLASGLVD PKTIALLVID EAHRAKGNYA YNNIVKFMDR FTNSYRILAL
     TATPASDVDG VQEIIDNLNI SKVEVRSEES IDIIKYMKRK RIIRRNIYQS DEIKECIDLL
     CTAIAPVLKV ANGKGILEIT DPSRINFFQC MDASRKIVAN PTIPEGTKWS NFFTLQLLGV
     VGQCFRRLNV YGLRSFFSYF NEKYTEFMAK HSKKKSSNKL NADFYFSEPI KQLMKRIRTM
     IDDPKVFSHP KIEAMMEELD EFFTINNATD SKVIIFTEFR ESALEIVRFI EKVGKNLKPH
     IFIGQAKERD KFDESNFGKK SKGKRVGKKQ QDDSKSSSEN AQINGMNQKL QKEIIKNFKQ
     GTYNILVATS IGEEGLDIGE VDLIICYDST SSPIKNIQRM GRTGRKRDGK VVLLFSSNEE
     SKFDKAMNGY EYIQQHIMKG QLIDLKEQNR MIPKDWEPKV EMRFIEIPEE NHELQVVDDE
     DEIIRIATQY MMGGKSKKKK AAASKKGKTK EKRAKQFFMP DNVEIGFRSV TSMVRAVGSS
     KSLEEEKKEE KVRDVLDRIV DSDSDEEIPL GSIPIPRSEV IAHKQSTTDE QLLERDCQSG
     SNISDRTLDQ HHSASEERGI NSNFSHESNL PTPPENSPPK RKSIVLEEAR IAKKKHKKSL
     GIRKPTIRPP SIIDQLKKQK SKIIRPDSAN ETICLDEDDI LLPEYTNITE KEVTVQEDRR
     EIEHDDDSEI FDDGLDEQLA MIDDMNTTKS FVEPTRIDFK DEVFKNDFDE HEGFLNNDEL
     MELHTSYFTA IDPMDKVFYY DPSSSVHVDG ANREYAFYGK IGHSKRSQVL IGLQKRAHEM
     AAKSKQSKTA TPSEPETFQN YLDSDFIALQ
//
DBGET integrated database retrieval system