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Database: UniProt
Entry: A0A162RSJ2_9CRUS
LinkDB: A0A162RSJ2_9CRUS
Original site: A0A162RSJ2_9CRUS 
ID   A0A162RSJ2_9CRUS        Unreviewed;       863 AA.
AC   A0A162RSJ2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=APZ42_012388 {ECO:0000313|EMBL:KZS20747.1};
OS   Daphnia magna.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS20747.1, ECO:0000313|Proteomes:UP000076858};
RN   [1] {ECO:0000313|EMBL:KZS20747.1, ECO:0000313|Proteomes:UP000076858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xinb3 {ECO:0000313|EMBL:KZS20747.1,
RC   ECO:0000313|Proteomes:UP000076858};
RC   TISSUE=Complete organism {ECO:0000313|EMBL:KZS20747.1};
RA   Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT   "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZS20747.1}.
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DR   EMBL; LRGB01000115; KZS20747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162RSJ2; -.
DR   STRING; 35525.A0A162RSJ2; -.
DR   Proteomes; UP000076858; Unassembled WGS sequence.
DR   GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
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; 2.
DR   InterPro; IPR031327; MCM.
DR   InterPro; IPR008045; MCM2.
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:SF44; DNA REPLICATION LICENSING FACTOR MCM2; 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; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50051; MCM_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000313|EMBL:KZS20747.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076858}.
FT   DOMAIN          488..608
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          1..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..91
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  97456 MW;  E09FF20AE8EC9096 CRC64;
     MSDYNAASPP PMSVSSLEPA TPSSRRAGRR VRSQSRASAT SVETGITTGG AAGSVADDEL
     PEFDDEQDLG GDDDDNAVLQ EDEDEGEELF GDNMEADYRA IPALDRYDGE ELDESDYDAI
     SESGRREAER AMRKRDQEMG VGDMRRGLFY DESDEDDDSR PARKRRLAER AAEGMEVENE
     QAVESIENLE DMQGYSVSEW VSLLAPRIEI LNRFKNFLRT YTDSKGNAIF KEKIRHMCEE
     NKSSFELDYN KLASEEHVLA YFLPEAPLEM LAIFDEATKD IVLAMFPQYE RIAKEIHVRI
     TDLPLVEDIR SLRQLHLNQL VRTHGVVTAQ TGVLPQLSVV KYDCNKCSYV LGPFSQTQNN
     EVKPTSCPEC QSTGPFQINM EQTVYQNYQR VTLQEAPGKV VAGRLPRAKD AILLGDLCDM
     CKPGDEIELT GVYTNNYDGS LNTAQGFPVF ATVLLANHIA KKDGDASTRS LTDEDVKAIM
     ALSKDERIAE RIVASIGPSI YGHNDIKRAL ALALFGGESK NPGQKHQVRG DINVLICGDP
     GTAKSQFLKY VEKIAPRAVF TTGQGASAVG LTAYVQRSPV TREWTLEAGA LVLADKGFCL
     IDEFDKVDLT EPILSRFDIL CVVRDTVDAV QDEYLARFVV NSHIRHHPNV TASEQVENDP
     VDMNDTNLSG VEKIPQDLLR KYITYAREKI HPKLHQIDQD KIARMYSDLR RESMATGSIP
     ITVRHIESMI RMAEAHAKLH LREHVIDDDV NMAIRVMLES FIDTQKYSVM RTMRKTFARY
     LAYKRDNNEL IFFLLRQLVH EQTVYLRNRF DSEPDTVEIL ESDLIDRARQ INILNLKPFY
     ESEIFQANRF THDAKKKMII QTL
//
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