ID   A0A6G0UUT3_9BILA        Unreviewed;       904 AA.
AC   A0A6G0UUT3;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   10-FEB-2021, entry version 4.
DE   RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=FO519_003957 {ECO:0000313|EMBL:KAE9552844.1};
OS   Halicephalobus sp. NKZ332.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Panagrolaimoidea; Panagrolaimidae;
OC   Halicephalobus; unclassified Halicephalobus.
OX   NCBI_TaxID=2598192 {ECO:0000313|EMBL:KAE9552844.1, ECO:0000313|Proteomes:UP000488831};
RN   [1] {ECO:0000313|EMBL:KAE9552844.1, ECO:0000313|Proteomes:UP000488831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NKZ332 {ECO:0000313|EMBL:KAE9552844.1};
RC   TISSUE=Whole-body {ECO:0000313|EMBL:KAE9552844.1};
RX   PubMed=31814372;
RA   Ragsdale E.J., Koutsovoulos G., Biddle J.F.;
RT   "A draft genome for a species of Halicephalobus (Panagrolaimidae).";
RL   J. Nematol. 51:1-4(2019).
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|ARBA:ARBA00001665};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KAE9552844.1}.
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DR   EMBL; VOSG01000113; KAE9552844.1; -; Genomic_DNA.
DR   Proteomes; UP000488831; Unassembled WGS sequence.
DR   GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:1905775; P:negative regulation of DNA helicase activity; IEA:InterPro.
DR   InterPro; IPR031327; MCM.
DR   InterPro; IPR008045; MCM2.
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; PTHR11630; 1.
DR   Pfam; PF00493; MCM; 1.
DR   Pfam; PF12619; MCM2_N; 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; PR01658; MCMPROTEIN2.
DR   SMART; SM00350; MCM; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52540; SSF52540; 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   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000488831}.
FT   DOMAIN          473..679
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..74
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   904 AA;  102475 MW;  0AD8DEB6F773B835 CRC64;
     MSQGSRGGRR TRRIFADDDD QSQFQSQASS VANPRDVDAL LGDDGHADDV VNELFGDERD
     EMDPEEEDGE DLFGDNMEAD YRPQPELDIL SQSGIDDDDV SEMSYSDRRA AELEMEERDR
     QLTGHEDRLF YEEGDVSQSQ TDSTRRARER MRRIRIVEDE DQMEEDIPID ILENLRGRTV
     RDHVNDKAIA REIIRRFKHF LRHFKGKGND QLKYVQRIQQ MASENKESLV VDYDDLADDE
     GQPSLSMFLP EAPLEVLELF DMATTDVVTS MYPHYKRICA NINTRVAGLP TYEDIRMLRH
     IHLNMLITTS GVVTVTSGIL PRLALVKYNC VACGYVIGPI TQGSEDEVKP SSCASCQSRG
     PFELNVEETV YQNYQRITIQ ESPNLVEAGR LPRSKDIILT GDLCDSCKPG DEIEVTGTYT
     NNYDSSLNSR QGFPVFAAVV IANYIRTKDQ IESDALTDED VAQIRKLSKD PDIAQRVFAS
     IAPTIYGHHD VKQAIALALF RGEQKNPNQK HALRGDINIL LCGDPGTAKS QFLRYVVHMA
     PRAVLTTGQG ASAVGLTAYV QRHPVTREWT LEAGAMVLAD KGVCLIDEFD KMTDQDRTSI
     HEAMEQQSIS ISKAGIVTSL RARCTVIAAA NPIGGRYDSS RTFAENVDLT EPILSRFDVL
     CVIRDQVDPI EDEHLAKFVI GNHIRMHPSR KNENQGSEES QIETESEYKL IPQNLLRKYI
     IFARNNIHPK LEEKAMDRLN GVYADLRKEA QSTGSVAITV RHIESMIRMS EAHAKLHLRS
     YVNDDDVNAA IRIMLESFIQ TQKASVMRQM RKHFIRQLTY KKDSNELLLY ILKQLIRDQL
     AYEQSRSHGD SASIEAITIS ETDLKTKARQ YNIDNLVPFY RSRLFTSNNF THDPSKKVIT
     QSLY
//