ID R4XIC0_TAPDE Unreviewed; 854 AA.
AC R4XIC0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN ORFNames=TAPDE_004683 {ECO:0000313|EMBL:CCG84249.1};
OS Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC Taphrinales; Taphrinaceae; Taphrina.
OX NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG84249.1, ECO:0000313|Proteomes:UP000013776};
RN [1] {ECO:0000313|EMBL:CCG84249.1, ECO:0000313|Proteomes:UP000013776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA Overmyer K., Hauser P.M., Pagni M.;
RT "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT agent of peach leaf curl.";
RL MBio 4:e00055-e00013(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCG84249.1}.
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DR EMBL; CAHR02000216; CCG84249.1; -; Genomic_DNA.
DR AlphaFoldDB; R4XIC0; -.
DR STRING; 1097556.R4XIC0; -.
DR VEuPathDB; FungiDB:TAPDE_004683; -.
DR eggNOG; KOG0479; Eukaryota.
DR Proteomes; UP000013776; 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:UP000013776}.
FT DOMAIN 306..512
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 674..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 94620 MW; DB971E1663F303F2 CRC64;
MADLPVFQDA IFLDRVRVFE EYLDHSVSAT VSASQTNYKD AITRMLNTQA RRLTVNLDEI
RDFNRELASG ILMTPGDYLP AFDKALKNVV LTLRDPLRHK IDDLPFYIAF SGSFGENHVN
PRTLRAMHLS RLISIEGIVT RCSLVRPKVV KSVHYCEKTG EFLSREYRDA TMGDGIPGSS
AYPQTDKDGN PLMTEYGHST YRDHQTISIQ EMPERAPAGQ LPRSIDVIMD DDLVDRCKPG
DRIQLVGAYR TQGGGGLNNT TGKFTTHIMG NNVVLLSSKA GGGIAQAQMF DTDIRNINKV
AKKKNIFELL SQSLAPSIFG HDHIKKAILL MLLSGMEKNL DNGTHIRGDI NILMVGDPST
AKSQMLRFVL NTAPLAIATT GRGSSGVGLT AAVTTDKETG ERRLEAGAMV LADRGVVCID
EFDKMSDVDR VAIHEVMEQQ TVTIAKAGIH TSLNARCSVI AAANPIYGQY DTHKDPHKNI
ALPDSLLSRF DLLFVVTDEI DDTHDRMISE HVLRMHRYLA PGAEEGQPVR DNPGQSLSIG
TDEAEVARES PVFEKFNQML HAGVTYTNKK SKQKEVLSIA FVKKYIQYAK NRIKPVLSKG
AADHIVMTYG NLRNDELGAN QRKTSPMTAR TLETLIRLST AHAKARLSNR VDPKDAEAAE
AILRFALFKE VVKEDRRKRR RTTAEPEAES DEEESDDDDT PAQAAPVRPA RRTQRINGSQ
SNGHTTNGHT NGHTAEDDEE MQDTNTAATQ LSWASDRNES QLESQTQTET QVPTPAPTTV
LTSERYGLFE SRLSSLINTP VFSDDSCTTE NLLPEVNKTL SPEELFSPRE MSQALEKMTE
ENKIFVSGGI CYKV
//
