ID A0A2T9YRM4_9FUNG Unreviewed; 912 AA.
AC A0A2T9YRM4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN ORFNames=BB561_002120 {ECO:0000313|EMBL:PVU94995.1};
OS Smittium simulii.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133385 {ECO:0000313|EMBL:PVU94995.1, ECO:0000313|Proteomes:UP000245383};
RN [1] {ECO:0000313|EMBL:PVU94995.1, ECO:0000313|Proteomes:UP000245383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWE-8-4 {ECO:0000313|EMBL:PVU94995.1,
RC ECO:0000313|Proteomes:UP000245383};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(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}.
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:PVU94995.1}.
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DR EMBL; MBFR01000068; PVU94995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9YRM4; -.
DR STRING; 133385.A0A2T9YRM4; -.
DR Proteomes; UP000245383; 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 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:UP000245383}.
FT DOMAIN 361..539
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 687..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..754
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..780
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 99833 MW; 240011ED065C3614 CRC64;
MATSVQKPYV PLNIENIGIL SEDLYKERVN FFKEFLNQDY SENIYIPELK RLAQAGGGRF
VVDIDQLREY DNDACEAILK QPSEYIPAFE AASTEIARGY LNKDKVPAAI GSSGADGFYI
PMGFVGSFGE QHISPRKLGS DLLGKLVCIE GIVTRTSLVR PKVVRSVHYS EKKNAFYSKL
YNDQTSSNNG FGTLNLENPV MNSSGYPKED EEGNPLTTEY GLSYYANHQT INIQEMPERA
PPGQLPRGVD VILDNDLVDS TKPGDRILVV GIYRALAGKN SASTSGVFRS LVLANSVRGF
GASSLIWSGI SEGSGGNSSS NKSSNGAAPV IPITDGDIKN IRSLSKRDDI VNILSNSLAP
SGCEQNLDNG SHIRGDINML MVGDPSTAKS QLLRYVLRIA PLAIATTGRG SSGVGLTAAV
TTDKDTGERR LEAGAMVLAD RGIVCIDEFD KMTDGDRVAI HEAMEQQTVT IAKAGIHATL
NARCSVVAAA NPIYGRYDPS RPPHQNIALP DSLLSRFDLL YIVTDVAEEE KDRELSLHVL
NMHRYIPNGL DPGQPIDDLL DASSLTASAN EDTDKSKDQI LSTQFLRRYI YYAKSLFKPK
LLKSSAEIIA NAYANLRTHA AMASSGRRMG TPTTSPITPR TLETLIRLAS AHAKARLSSE
IEEIDANEAK ALLSFALFRE NIENAKQTNA AKQKSKKNDH KSKKLRTDYD NDDSDSSDIV
DNQKNKSSEP SSSKVATKPK SKQLSKRSKK IKKSAAQKYK DLLHDDDDDA DFDLYDSGED
SEELSAPSSP ELLPARSKSN NNVYVEVQKG NVSDEDINSD VEMQSTEIVI KQLEPHRFEK
FKTCFHAAIS NGSLVTSDEG VGWSISNEIV VSVNKNLSSS DEEFTLEEVI LALKSLQDEN
RVFISDDSVY MI
//