UniProt: A0A1L8G8R9

Database: UniProt
Entry: A0A1L8G8R9_XENLA

LinkDB:  A0A1L8G8R9_XENLA 
Original site:  A0A1L8G8R9_XENLA

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   NCBI-Gene (1)   
   XENBASE (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
Protein domain (13)   
   InterPro (7)   
   Pfam (3)   
   PROSITE (1)   
   SMART (2)   
All databases (27)   

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ID   A0A1L8G8R9_XENLA        Unreviewed;      1143 AA.
AC   A0A1L8G8R9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA helicase MCM9 {ECO:0000256|ARBA:ARBA00041085};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE   AltName: Full=Minichromosome maintenance 9 {ECO:0000256|ARBA:ARBA00042301};
GN   Name=mcm9.L {ECO:0000313|RefSeq:XP_018117303.1,
GN   ECO:0000313|RefSeq:XP_018117304.1,
GN   ECO:0000313|Xenbase:XB-GENE-949289};
GN   Synonyms=mcm9 {ECO:0000313|RefSeq:XP_018117303.1,
GN   ECO:0000313|RefSeq:XP_018117304.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|RefSeq:XP_018117303.1};
RN   [1] {ECO:0000313|RefSeq:XP_018117303.1, ECO:0000313|RefSeq:XP_018117304.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018117303.1,
RC   ECO:0000313|RefSeq:XP_018117304.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018117303.1,
RC   ECO:0000313|RefSeq:XP_018117304.1};
RG   RefSeq;
RL   Submitted (APR-2022) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC       ECO:0000256|RuleBase:RU004070}.
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DR   RefSeq; XP_018117303.1; XM_018261814.2.
DR   RefSeq; XP_018117304.1; XM_018261815.2.
DR   STRING; 8355.A0A1L8G8R9; -.
DR   PaxDb; 8355-A0A1L8G8R9; -.
DR   GeneID; 431809; -.
DR   AGR; Xenbase:XB-GENE-949289; -.
DR   CTD; 431809; -.
DR   Xenbase; XB-GENE-949289; mcm9.L.
DR   OMA; ECVMEET; -.
DR   OrthoDB; 1342948at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 431809; Expressed in egg cell and 14 other cell types or tissues.
DR   GO; GO:0042555; C:MCM complex; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:UniProt.
DR   CDD; cd17760; MCM9; 1.
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; IPR003593; AAA+_ATPase.
DR   InterPro; IPR031327; MCM.
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:SF48; DNA HELICASE MCM9; 1.
DR   PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR   Pfam; PF00493; MCM; 1.
DR   Pfam; PF17855; MCM_lid; 1.
DR   Pfam; PF17207; MCM_OB; 1.
DR   PRINTS; PR01657; MCMFAMILY.
DR   SMART; SM00382; AAA; 1.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW   Helicase {ECO:0000313|RefSeq:XP_018117303.1,
KW   ECO:0000313|RefSeq:XP_018117304.1};
KW   Hydrolase {ECO:0000313|RefSeq:XP_018117303.1,
KW   ECO:0000313|RefSeq:XP_018117304.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT   DOMAIN          303..506
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          721..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          838..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..921
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          999..1022
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          636..663
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        729..767
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..862
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..917
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1143 AA;  126643 MW;  BA746E8FA7189249 CRC64;
     MYLGSEQVAL VGQVFESFVL EHHKNEIAQI LTEKEEHAHY SLVVNAMTLF EANMEIGEYF
     NAFPNEVLPV FDNALRRAAM SFLQSCSEKY TFLMKQNLHA RITGLPVCPE LTREHIPRTR
     DVGHFLSVTG TVIRTSLVKV LEYEQDFMCN KCKHVVTVKA DFEQHYTFKP PIACSNEEGC
     NSTKFTCLSD SSSPASCRDY QEIKIQEQVQ RLSVGSIPRS MIVVLEDDLV DSCKSGDDIT
     VYGVVMQRWK PLYIDMRCDL EIVLKANYIS VNNEQPCGVV INEEVRKEYE DFWVKYRNNP
     LEGRNEILAS LCPQVFGMFV VKLAVAMVLA GGVQRIDSAG TRVRGESHLL LVGDPGTGKS
     QFLKYAVKIT PRSVLTAGIG STSAGLTVTA VKDSGEWNLE AGALVLADGG LCCIDEFNSI
     KEHDRTSIHE AMEQQTISVA KAGLVCKLNT RTTILAATNP KGQYDPDESI SVNVALASPL
     LSRFDLVLVL LDTKNEDWDR IISSFILESK GCPRKSDKLW SMEKMKTYFC LIKNLQPKMS
     QDANVILVRY YQLQRQSSCR NAARTTIRLL ESLIRLAEAH ARLMYRDVVT TEDAITVVSI
     MESSMQGGAL LGGVNALHTS FPENPREQYR LQCELLLDKL GLQKLLEEEL QRLERQQSED
     SSESDLGESA TNLVGHKVVH SECVMEETFS TFEASSLPDE THLGVTGSAA FIQTPKKTIS
     DMTKSDDTIR KGTITPAEQN RGISTDAESS LKQGNAQPLA GGHLSENNLT RCTDNSLGWF
     DTLQSIQMSP ITKQREGCTA EKLQQEVLPV STESSCHPAD KKVVNLGGRN KLEVLQASGS
     SPGGNGRDLS NHTVTCGSSP ERNKRDLSNH IVTEHVSKKW RRINKDSLCG KNVPSFQPQS
     ENTDSAPVCS SVPLHSTPDV PQRRKRIIAQ VEKQSKAEVE DPDTKARLAQ LAKFSFKRHS
     KLVHSPAGDT DTASNAQKHD HPVQKITLSE KLNNLGRTVN NVDKSSNSVN GSKQQKHVEN
     TSKQTVITQK SNFESNTLNA PVHETKLNEG CDSRKVSSST LAKLARFSFS PPPENQAAET
     SKETLILPRA VAPGSKRKCF ELNPSTDKTT MSSKSLFSTT DLDDEELDVD WEAEIKGNQR
     IAT
//

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