ID A0A2T3BBZ0_AMORE Unreviewed; 894 AA.
AC A0A2T3BBZ0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN ORFNames=M430DRAFT_96270 {ECO:0000313|EMBL:PSS25845.1};
OS Amorphotheca resinae ATCC 22711.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Amorphothecaceae; Amorphotheca.
OX NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS25845.1, ECO:0000313|Proteomes:UP000241818};
RN [1] {ECO:0000313|EMBL:PSS25845.1, ECO:0000313|Proteomes:UP000241818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS25845.1,
RC ECO:0000313|Proteomes:UP000241818};
RX PubMed=29315638; DOI=10.1111/nph.14974;
RA Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT as versatile saprotrophs and plant mutualists.";
RL New Phytol. 217:1213-1229(2018).
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; KZ679007; PSS25845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3BBZ0; -.
DR STRING; 857342.A0A2T3BBZ0; -.
DR InParanoid; A0A2T3BBZ0; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000241818; 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:0006279; P:premeiotic DNA replication; 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:UP000241818}.
FT DOMAIN 303..509
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 674..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 894 AA; 98124 MW; F5BE384F8D8EB3AF CRC64;
MDGLQLRDEA VRDRVRAAQE FLDPVDRSTA RGYRSDIILM LQKFQRRLVV SIDEVRAHNA
ELAEGLLQQP FDYAQAFDRA LHEVIQTLPN TTPKQTSEDV MYYCAFSGSF GQYACNPRTL
SSSHLNHMVS LEGIVTRCSL VRPKVVKSVH YNEKKKVFHF REYKDQTMTA SGASTSSVYP
QEDEEGNPLI TEYGYSTYRD HQTISIQEMP ERAPAGQLPR GVDVILDDDL VDKVKPGDRV
QLVGIYRSLG NRNAGHNSAL FKTVVIANNV VLLSSKSGGG IAAATITDTD IRNINKVSKK
KNLFDLLSQS LAPSIYGHEH IKKAILLMLL GGQEKNLENG THLRGDINIL MVGDPSTAKS
QLLRFVLNTA PLAIATTGRG SSGVGLTAAV TSDKETGERR LEAGAMVLAD RGVVCIDEFD
KMSDIDRVAI HEVMEQQTVT IAKAGIHTSL NSRCSVIAAA NPIFGQYDTH KDPHKNIALP
DSLLSRFDLL FVVTDDIDDS RDRQISEHVL RMHRYRQPGT EEGAPVREQS QQTLGVGVEQ
ESEANRPTEV YEKFDPMLHA GVTLTTGRGS NKKVEVLSIP FMKKYIQYAK SRIKPVLTQE
ASDRISDIYV ALRNDDMQGN QRKTSPMTVR TLETIIRLAT AHAKARLSNR VEERDALAAE
SILRFALFKE VVEDEKRSKR RKTRPLEDES SGNESSDSDS DSPPPTTRAG SSRTPGGTSR
TRLLASRRGG TNGSSSRTNG DTGGGAISED EEDDIYTSSP RKTTQRSGPR MSGALPTQTQ
TSFASSLPAS QIPSQSQSQE ESELASGTAA LSIAPAAITP ARLQLFRTTL GQLLNTPLFE
NDSAYVNDIM TAVNERIGGA GGGAFDRAEV EAALLKMDEA NNIMYTDGEL VYKI
//
