ID A0A0L1KQH9_9EUGL Unreviewed; 792 AA.
AC A0A0L1KQH9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=DNA replication licensing factor MCM4 {ECO:0000256|RuleBase:RU368062};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368062};
GN ORFNames=XU18_2933 {ECO:0000313|EMBL:KNH06177.1};
OS Perkinsela sp. CCAP 1560/4.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Prokinetoplastina;
OC Ichthyobodonidae; Perkinsela.
OX NCBI_TaxID=1314962 {ECO:0000313|EMBL:KNH06177.1, ECO:0000313|Proteomes:UP000036983};
RN [1] {ECO:0000313|EMBL:KNH06177.1, ECO:0000313|Proteomes:UP000036983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1560/4 {ECO:0000313|EMBL:KNH06177.1};
RA Tanifuji G., David V., Flegontov P., Gerasimov E., Hashimi H.,
RA Logacheva M., Maruyama S., Onodera N., Gray M., Archibald J., Curtis B.,
RA Cenci U., Lukes J.;
RT "Draft genomes of Paramoeba pemaquidensis and its kinetoplastid
RT endosymbiont Perkinsela sp. CCAP 1560/4.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:RU368062}.
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:RU368062};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368062}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC 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:KNH06177.1}.
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DR EMBL; LFNC01000177; KNH06177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L1KQH9; -.
DR EnsemblProtists; KNH06177; KNH06177; XU18_2933.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000036983; Unassembled WGS sequence.
DR GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR Gene3D; 2.20.28.10; -; 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; IPR031327; MCM.
DR InterPro; IPR008047; MCM_4.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
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:SF66; DNA REPLICATION LICENSING FACTOR MCM4; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01660; MCMPROTEIN4.
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|RuleBase:RU368062};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368062};
KW Hydrolase {ECO:0000256|RuleBase:RU368062};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|RuleBase:RU368062};
KW Reference proteome {ECO:0000313|Proteomes:UP000036983}.
FT DOMAIN 370..575
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 88262 MW; 01135BCF008E6AE1 CRC64;
MSQESSHEPN QEVSNIHDPF AHAPVPPLEF FEDSIVQPSP DADNYVRSMN LNPSDSTSDE
NTVIWGTSIY INFFGDLSRE YLEKHEMQTI LSLTCEGSRL HLDLEKVESF SSYLHMAIIK
HPVSCLSVFE MALGDIWNMQ HGRTSAQDSR TINQRPITVC PFNAKEYRIS QLSKELTEML
VAVRGIVIRT SMVIPEMNEA EFRCEECHSI STATVDRARI SEPNRCPGCD GKLTFRLMHH
LCKYEDKQIV KLQETPEEMK AGEIPTALSL VIFNAMVDSV VPGDVVVATG ILRVAPSRVN
SNGQQCFSVM RSYLDGMYLK KLKKRNAHDR MSQNTEAFLS VLANDGSELH TEEFEQEVAR
LHKISLREDI HSVLRRSMAP SIYGMEQAKD GLLSLLFGGT AKEFTSSTCR GEINICLCGD
PGLAKSQLLA HVHRISHRGV YVSGRSSSSV GLTAYVSRDY DTGERVLESG ALVLSDGGVC
CIDEFDKMDQ QQRNVLKEVM EQHTLSIAKA GIVCQLNART SILAAANPKE SKWNRNLTVV
ENLNLDSGLL SRFDLIYLML DEHPEDFHRL LAAHLIDMFG CQKEGKAVDL QTSDTTNEES
SGEFTLSSTD LTKYIAYARA KIKPKLNAAA QQELIQSYCS LRGARSSGSM SPTLRTLESL
IRLAESRAKM RWSEVVTAAD VRDAQNMVYA AWGSTGIDMA KIEEGGVDVS VVFGGKAVQG
ATGILENRLQ VYIEKHKPNR SSLRMAEILQ NFSTFSPEQV HEALRILETK SVISGYDANS
IYWKRENETL GV
//
