ID A0A023B9G8_GRENI Unreviewed; 823 AA.
AC A0A023B9G8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=DNA replication licensing factor MCM4 {ECO:0000256|RuleBase:RU368062};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368062};
GN ORFNames=GNI_049510 {ECO:0000313|EMBL:EZG72974.1};
OS Gregarina niphandrodes (Septate eugregarine).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Gregarinasina;
OC Eugregarinorida; Gregarinidae; Gregarina.
OX NCBI_TaxID=110365 {ECO:0000313|EMBL:EZG72974.1, ECO:0000313|Proteomes:UP000019763};
RN [1] {ECO:0000313|EMBL:EZG72974.1, ECO:0000313|Proteomes:UP000019763}
RP NUCLEOTIDE SEQUENCE.
RA Omoto C.K., Sibley D., Venepally P., Hadjithomas M., Karamycheva S.,
RA Brunk B., Roos D., Caler E., Lorenzi H.;
RL Submitted (DEC-2013) 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:EZG72974.1}.
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DR EMBL; AFNH02000384; EZG72974.1; -; Genomic_DNA.
DR RefSeq; XP_011129669.1; XM_011131367.1.
DR AlphaFoldDB; A0A023B9G8; -.
DR EnsemblProtists; EZG72974; EZG72974; GNI_049510.
DR GeneID; 22911791; -.
DR VEuPathDB; CryptoDB:GNI_049510; -.
DR eggNOG; KOG0478; Eukaryota.
DR OMA; TEIGDGW; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000019763; 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:UP000019763}.
FT DOMAIN 360..569
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 584..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 90632 MW; 34CA99B8FA73F5E8 CRC64;
MAAAAAIIPA QERGGIAGGG RSWSQLQDVE GELRREFAAW VRTARFEDVA EDELEMAEQE
CGASGQGGYY YRVLECLCRG SRKVRACKRS PRSGFVSVIF SFNHLSQGAA AVKKWVLEYP
VDTSLLIDDE LKRLVSEELL PATQIALPPF IGLRSSFCHH PKPTAIRQLC ASKDVETLVC
ITGVCLRLSS VIPEMQVAVF RCTGKASRNF QYVLCNHEVS VPVIAGTVAE PQVCEACQGR
KTLTLAHDKC VFASRQVCKL QELPDQVPEG EPPQMLFVYL YDNYVECCRP GDVIAVTGVY
RTVETRVNPR TRNLKKVHKI SIDAFSVSTE GTNVFDVDVN RPFAPSFVGD AHRLAADPGC
YERLVCSFAP DIWGMADVKK GLLCQLFGGL TEHVDGEGSR MQSRGELHVL LCGDPAVAKS
QLLRYVNKLA TRSVYVVGRG TTSAGLTASV TRDPETKEFV MESGAVVLSD RGVCCIDEFD
KMNDHTRAIL HEVMEQQTVS FAKAGIVCSL NARTAILASA NPIGSRYDTK KSVVENINLP
ASLMSRFDLI FLCLDLRTDE NDERLSRHIC RLFRETPNAQ PEVVHLGMNE PSGRNGRDHR
MEAEPRSAPE SSSGGVLSPA FFAQYVTYAR STCRPEMSGE AETALVEAYV GLRGVGGRNP
VGTPRQLDSL VRLATALAKM ELAREVRARH VREAARLIRA ATYEALTDAA TGKLDFDQLT
TGKSHSQRLR EKVLCNKVLD LLDAVKPDGL SREDLGLRVD EYLARCLRGE ETSLVDTRNR
VDGVDPQVVF APVRMREVAD IVALLERTRK IGPISGQRYT IIN
//
