ID H2AV09_KAZAF Unreviewed; 979 AA.
AC H2AV09;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN Name=KAFR0E00550 {ECO:0000313|EMBL:CCF58209.1};
GN ORFNames=KAFR_0E00550 {ECO:0000313|EMBL:CCF58209.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF58209.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF58209.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE650825; CCF58209.1; -; Genomic_DNA.
DR RefSeq; XP_003957344.1; XM_003957295.1.
DR AlphaFoldDB; H2AV09; -.
DR STRING; 1071382.H2AV09; -.
DR GeneID; 13884066; -.
DR KEGG; kaf:KAFR_0E00550; -.
DR eggNOG; KOG0479; Eukaryota.
DR HOGENOM; CLU_000995_6_1_1; -.
DR InParanoid; H2AV09; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000005220; Chromosome 5.
DR GO; GO:0071162; C:CMG complex; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; 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:0031298; C:replication fork protection complex; 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:0003688; F:DNA replication origin binding; IEA:UniProt.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProt.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:UniProt.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IEA:UniProt.
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:UP000005220}.
FT DOMAIN 355..561
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 744..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..824
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..846
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 109842 MW; 77E420C9C4D1AD3A CRC64;
MDQSTTINEF EIDQANAFAP DAVFGDRVRR FQEFLDTFSS YKEQIRNIQI YNGNIHTADK
SLDDEYDDFN DDDYKKKNSN ANSVNILPQR ITISLDELRE FDRSFWTGIL AEPSYFIPPA
EKALTDMAST LDDIPNNDYN SSLSSKRPWR LSFKGSFGSH ALSPRTLNSQ FLNKLISIEG
IVTRTSLVRP KLIRSVHFAE KTGRFHYRDY TDSTTTLTTQ IPTPAIYPTE DTEGNKLTTE
YGYSTYIDHQ RITVQEMPEM APAGQLPRSI DIILDDDLVD KTKPGDRVNV IGVFKSLGAG
GLTQSNSKTQ HGFRTLIIGN SVYPLHARST GVSAKEVLTD YDIRNINKLA RRDDIFDLLS
QSLAPSIYGH ENIKRAILLM LLGGVEKNLE NGSHLRGDIN ILMVGDPSTA KSQLLRFVLN
TASLAIATTG RGSSGVGLTA AVTTDRETGE RRLEAGAMVL ADRGVVCIDE FDKMTDVDRV
AIHEVMEQQT VTIAKAGIHT TLNARCSVIA AANPVFGQYD VNRDPHQNIA LPDSLLSRFD
LLFVVTDDIN EIRDRSISEH VLRTHRYLPP GYLEGEPIRE RLNLSLAVGV EGENEEDERE
RIGALNNDEE DDNVFEKFNP LLQAGAILAR NKGDHNGTKV PSLVTIPFLR KYIQYAKERV
IPQLTQEAVD VIVKNYAALR NDENTKKSPI TARTLETLIR LSTAHAKVRL SKTVNQHDAL
VAAHLLRFAL LGEDVDMDEF FNGDDEEESL RKRSPKKSPK KRQRVRATPR SQSGRSTPHG
KPRSTESSVL TPRRRLSFDE NAEDSEDAEY NDDRDDEDYT PIATEEEETL MRRLERGLRV
SPRRKEKNAS SLGPAGPLKE VDTPSLANVA SAAHTEGAGQ EQQYHRHQEQ EGRTVVTFDT
HEPGSISTSR LSIISGIIAR LMQTELFEDE SYPVSSLFER INEELPEEDK FSPSEYLAGL
ELMADRNNLM VADDKVWRV
//
