ID A0A1S3CNN0_CUCME Unreviewed; 944 AA.
AC A0A1S3CNN0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=LOC103502828 {ECO:0000313|RefSeq:XP_008465160.1};
GN Synonyms=103502828 {ECO:0000313|EnsemblPlants:MELO3C026749.2.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008465160.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|EnsemblPlants:MELO3C026749.2.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2023) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_008465160.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_008465160.1; XM_008466938.2.
DR EnsemblPlants; MELO3C026749.2.1; MELO3C026749.2.1; MELO3C026749.2.
DR GeneID; 103502828; -.
DR Gramene; MELO3C026749.2.1; MELO3C026749.2.1; MELO3C026749.2.
DR KEGG; cmo:103502828; -.
DR eggNOG; KOG0477; Eukaryota.
DR InParanoid; A0A1S3CNN0; -.
DR OrthoDB; 147095at2759; -.
DR Proteomes; UP000089565; Unplaced.
DR Proteomes; UP000596662; Unplaced.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR GO; GO:0000347; C:THO complex; IEA:UniProt.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:EnsemblPlants.
DR CDD; cd17753; MCM2; 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; 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; 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; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000089565};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 507..713
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..71
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 107522 MW; 36870FA08A7EDDD9 CRC64;
MAGDTPDGHS SNPPSTPDSP TTSAGFETDQ LPHLSQTSDN YPDEDEAAVD PHILPDEPDP
DEEEEGEDLY HDNFLDDYRR MDEHDQYESL GLDDSLEDER DFDQIIRDRR AAEIELENRD
AQFNRRKLPE LLHDHDSEDD NYRPSKRSRA DFRPPAGARG YDDIDGMQSS PGRSQRENSR
DDVPMTDQSV DDQYEDEDDD ENENEMYRVQ GPLREHVTMD AVRRFIGKKF KKFLETYVNP
KSGNGELEYM RLINEMVLAN RCSLEIDYKQ FIFVHPNIAI WLADAPQPVL EVMEDVAKKV
VFDIHPNYKN IHQKIYVRIN NLPVYDQIRN IRQIHLNTMI RIGGVVTRRS GVFPQLQQVK
YDCNKCGTIL GPFFQNSYSE VKVGSCPECQ SKGPFTVNVE QTVYRNYQKL TLQESPGIVP
AGRLPRYKEV ILLNDLIDCA RPGEEIEVTG IYTNNFDLSL NTKNGFPVFS TVVEANYITK
KQDLFSAYKI TQEDKEEIEK LAKDPRIGER IIKSIAPSIY GHEDIKTAIA LAMFGGQEKN
VEGKHRLRGD INVLLLGDPG TAKSQFLKYV EKTGHRAVYT TGKGASAVGL TAAVHKDPVT
REWTLEGGAL VLADRGICLI DEFDKMNDQD RVSIHEAMEQ QSISISKAGI VTSLQARCSV
ISAANPIGGR YDSSKTFSQN VELTDPIISR FDILCVVKDV VDSVADEMLA TFVVDSHFKS
QPKGGILDDK SINESQEDSQ DTARPLDPEV LPQDLLRKYI TYSKLNVFPR LHDADLDKLT
HVYAELRRES SHGQGVPIAV RHIESMIRMS EAHARMHLRQ HVTQEDVDMA IRVLLDSFIS
TQKFGVQKAL QKSFRKYMTF KKDYNELLLY LLRELVKNAL HFEEIVRGST SELTQINVKL
EDLQSKAQEH EIYDLKPFFN STHFSNANFV LDEEHGLIRH NLAR
//
