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Database: UniProt
Entry: A0A1Y2VAH5_9PEZI
LinkDB: A0A1Y2VAH5_9PEZI
Original site: A0A1Y2VAH5_9PEZI 
ID   A0A1Y2VAH5_9PEZI        Unreviewed;       898 AA.
AC   A0A1Y2VAH5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   08-NOV-2023, entry version 28.
DE   RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN   ORFNames=M434DRAFT_30693 {ECO:0000313|EMBL:OTA93698.1};
OS   Hypoxylon sp. CO27-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA93698.1, ECO:0000313|Proteomes:UP000194361};
RN   [1] {ECO:0000313|EMBL:OTA93698.1, ECO:0000313|Proteomes:UP000194361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO27-5 {ECO:0000313|EMBL:OTA93698.1,
RC   ECO:0000313|Proteomes:UP000194361};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC   -!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which
CC       is the replicative helicase essential for 'once per cell cycle' DNA
CC       replication initiation and elongation in eukaryotic cells. The active
CC       ATPase sites in the MCM2-7 ring are formed through the interaction
CC       surfaces of two neighboring subunits such that a critical structure of
CC       a conserved arginine finger motif is provided in trans relative to the
CC       ATP-binding site of the Walker A box of the adjacent subunit. The six
CC       ATPase active sites, however, are likely to contribute differentially
CC       to the complex helicase activity. {ECO:0000256|RuleBase:RU368061}.
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:0000256|RuleBase:RU368061};
CC   -!- SUBUNIT: Component of the MCM2-7 complex.
CC       {ECO:0000256|RuleBase:RU368061}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU368061}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR   EMBL; KZ112466; OTA93698.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2VAH5; -.
DR   STRING; 1001938.A0A1Y2VAH5; -.
DR   Proteomes; UP000194361; Unassembled WGS sequence.
DR   GO; GO:0031261; C:DNA replication preinitiation complex; IEA:UniProt.
DR   GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005656; C:nuclear pre-replicative complex; IEA:UniProt.
DR   GO; GO:0043596; C:nuclear replication fork; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0033260; P:nuclear DNA replication; IEA:UniProt.
DR   GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:UniProt.
DR   CDD; cd17754; MCM3; 1.
DR   Gene3D; 2.20.28.10; -; 1.
DR   Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR031327; MCM.
DR   InterPro; IPR008046; Mcm3.
DR   InterPro; IPR018525; MCM_CS.
DR   InterPro; IPR001208; MCM_dom.
DR   InterPro; IPR041562; MCM_lid.
DR   InterPro; IPR027925; MCM_N.
DR   InterPro; IPR033762; MCM_OB.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR   PANTHER; PTHR11630:SF46; DNA REPLICATION LICENSING FACTOR MCM3; 1.
DR   Pfam; PF00493; MCM; 1.
DR   Pfam; PF17855; MCM_lid; 1.
DR   Pfam; PF14551; MCM_N; 1.
DR   Pfam; PF17207; MCM_OB; 1.
DR   PRINTS; PR01657; MCMFAMILY.
DR   PRINTS; PR01659; MCMPROTEIN3.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00350; MCM; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00847; MCM_1; 1.
DR   PROSITE; PS50051; MCM_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU368061};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368061};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368061};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368061};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194361}.
FT   DOMAIN          301..507
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          672..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..689
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..742
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..799
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   898 AA;  99606 MW;  0B10D5AE2A88C0BC CRC64;
     MDSFMLRDEA AKERIRLAEE FLDPHDQHAR SYRSDIILML QKNQRRLVVN IDHVRDHNTE
     LADGLLFDPF DYTLAFNHAL KEIVKTIPQA RPDQTDPDVL YYCAWAGSFG LNACNPRTLS
     SNHLNHMVSI EGIVTRCSLI RPKVVKSVHY NEKKNIFHFR EYRDQTMTNG VTTSSVYPQE
     DEEGNPLLTE YGFCTYRDHQ TISIQEMPER APAGQLPRGV DVILDDDLVD KVKPGDRVQL
     VGIFRTLGNR NTNHNSALFK TIILANNIVL LSSKGSGGVA TATITDTDIR NINKVAKKKN
     VFELLSQSLA PSIFGHDYIK KAILLMLLGG MEKNLENGTH LRGDINILMV GDPSTAKSQL
     LRFVLNTAPL AIATTGRGSS GVGLTAAVTS DKETGERRLE AGAMVMADRG VVCIDEFDKM
     SDIDRVAIHE VMEQQTVTIA KAGIHTSLNA RCSVIAAANP IFGQYDTHKD PHKNIALPDS
     LLSRFDLLFV VTDDIEDTRD RQVSEHVLRM HRYRQPGTDE GAPVRENTQQ ALGVALQSQD
     ATQRPTDVYE KYDAMLHAGV TITSGRGANR RREVLSIPFM KKYIQYAKTR VKPVLTEEAS
     ERIAEIYVGL RNDEMEGNQR RTSPLTVRTL ETLIRLATAH AKSRLSNRVE ERDALAAESI
     LRFALFKEVV EDESKRKRRR TQRLESDSSS EGSDDDDEDR GDTAYRGSTA RGRTAPSTRT
     TARGQPSSNG SRRANGTNGV NGRKAAASPE LGNDDGDEDN IYNATPRRSN RSGATSSSNA
     PGTSQVSFAS SVPASQLETQ EEETQEDAEL AAGAADLNID TPITPERLAV FRTALGQLLN
     TDLFDDDSAN VSDVIEAVNR RIEGRESAFS REEAIKALKK MDDANQIMYT DGNLVYKI
//
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