ID A0A420HQ48_9PEZI Unreviewed; 904 AA.
AC A0A420HQ48;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN ORFNames=OnM2_059045 {ECO:0000313|EMBL:RKF59565.1};
OS Erysiphe neolycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF59565.1, ECO:0000313|Proteomes:UP000286134};
RN [1] {ECO:0000313|EMBL:RKF59565.1, ECO:0000313|Proteomes:UP000286134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG2 {ECO:0000313|EMBL:RKF59565.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(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:RKF59565.1}.
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DR EMBL; MCFK01005932; RKF59565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420HQ48; -.
DR STRING; 212602.A0A420HQ48; -.
DR Proteomes; UP000286134; 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:UP000286134}.
FT DOMAIN 302..508
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 676..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 100396 MW; 2B8DC68938384ADE CRC64;
MESIQLRDEA VRDRVRDAQE FLDPSDQSLR SYRSEIIMML QKNERRLVVS IDDIRSRNPQ
LAEGLFNHPF DFSQAFDRAL KEVVQTLPNT TASQTSEETM YYCAYSGSFG QYACNPRTLS
SSFLNRMVSL EGIVTRCSLI RPKVIKSVHY NENKKVFHFR EFKDQTMTMN GATTSSVYPQ
EDESGNPLIT EYGYCTFRDH QTISLQEMPE RAPAGQLPRG VDVILDDDLV DKCKPGDRVQ
LVGIFRSLGN VNSGSSSALF KTLILANNVV LLSSKSGGGI AAATITDIDI RNINKISKKK
NLFDLLSQSL APSIFGHEYI KKAILLMLLG GQEKNLENGT HLRGDINILM VGDPSTAKSQ
LLRFVLNTAP LAIATTGRGS SGVGLTAAVT SDKETGERRL EAGAMVLADR GVVCIDEFDK
MSDIDRVAIH EVMEQQTVTI AKAGIHTSLN ARCSVIAAAN PIFGQYDTHK DPHKNIALPD
SLLSRFDLLF VVTDDIEDAR DRQISEHVLR MHQYRRPGTE EGAPVREQSQ QSIGVGVDVQ
ADNSRNTDVY EKYNQMLHAG VTVTSGRGSN KRVEVLSIPF VKKYIQYAKS RIKPTLTSYA
AERISEIYVA LRNDDMQGGQ RKTSPMTVRT LETIIRLSTA HAKARLSNRV EEVDALAAET
ILRFALFKEV YEDEKKQSKR RKIRPLEGIE NSSESDSDSD SSMPVVRSIS TRSRSTPHSR
RGRAGSINNS RQGANRSNGI SHTSKRIQEE DEDEENIYRS SPRINVNTQS SQSNGLITSN
DSQPSFASSI PISQIESQIK TSNTQAEDEI LANGTASLSL QTPSITSNRL KTFRSTLGQL
LNTDLFQDDC AAVNSIVDAI NQRLSLNFSS LEDPFDKLEA LAALTEMKAQ NQIFVDDDEI
VYKV
//
