ID A0A1I8ERR0_WUCBA Unreviewed; 933 AA.
AC A0A1I8ERR0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
OS Wuchereria bancrofti.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX NCBI_TaxID=6293 {ECO:0000313|WBParaSite:maker-PairedContig_4389-snap-gene-1.17-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-PairedContig_4389-snap-gene-1.17-mRNA-1}
RP IDENTIFICATION.
RC STRAIN=pt0022
RC {ECO:0000313|WBParaSite:maker-PairedContig_4389-snap-gene-1.17-mRNA-1};
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A1I8ERR0; -.
DR STRING; 6293.A0A1I8ERR0; -.
DR WBParaSite; maker-PairedContig_4389-snap-gene-1.17-mRNA-1; maker-PairedContig_4389-snap-gene-1.17-mRNA-1; maker-PairedContig_4389-snap-gene-1.17.
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: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:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 459..665
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..64
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 933 AA; 106198 MW; 922EC272EFD3C003 CRC64;
MSQHSDSRRA HSQGEDDYQS EDTAADVFEE NADLAGDGDD NALAELFGAE EEEVQDEEGE
NLFGDDMERD YRPQPELDVY SQSGMDDASE YTELTEGARR AAEREMDERD NLLDEDALLY
EQDDVDVGRH VRRYFRKNRA DDNEMELEEE EEIPIDILEN FRGRSTREHV SDEAVGREIV
RRFKSFVRGY KDAKTKKLKY LDAIKLMVAE NRESLEIDYE DLASENGEQN ICYFLPEAPV
QVLSYLDRAV TEVTLSLFPF FPRIAPEVKI RIRGLPVEED IRMLRQLHLN MLIRTSGVVT
VTTGMLPRLS VVKFDCGACG YLLGPFVQHQ DEEVKPTMCP SCQSRGPFEL NMENTIYHNY
QRITIQESPN SVAAGRLPRS KDVVLTADLC DACKPGDEVE LTGIYTNNYD GSMNSKQGFP
VFNTVIYANY ISRKDKIASD SLTDEDIQIV RQLSKDPQIA ERIFASIAPS IYGHDDIKRA
IALALFRGEQ KNPGEKHSIR GDINVLLCGD PGTAKSQFLR YAAHAAPRAV LTTGQGASAV
GLTAYVQRHP ITREWTLEAG AMVLADKGVC LIDEFDKMND QDRTSIHEAM EQQSISISKA
GIVTSLHARC TVIAAANPIG GRYDPSRTFA ENVDLTEPIL SRFDVLCVVR DTVDLVEDER
LANFVVDSHR KHHPNAKELQ EKEARPRNSQ QTSASCFSFS IIIYFLKHSA ILSNTEPNSH
FAKLANFLLQ QSEKDPATGL ELIPQTMLRK YLMYARENIH PKLEQLPQDK ISKFFAEMRK
ESLATGSVAV TVRHVESLIR LAEAHAKMHL RSYVCDEDVD VAVRVILESF INTQKASVMR
QMRKNFDRYI FVNRDHNELL LYLLKQLVRD QLHYERARHK ETTLSAIGIP ESDFIEKAQQ
VHIENVRNFY RSQHFLTNNF IYDSKRKLIV HNL
//
