MCM10_XENLA
ID MCM10_XENLA Reviewed; 860 AA.
AC Q5EAW4; Q9DEX0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Protein MCM10 homolog;
GN Name=mcm10;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11864598; DOI=10.1016/s1097-2765(02)00456-2;
RA Wohlschlegel J.A., Dhar S.K., Prokhorova T.A., Dutta A., Walter J.C.;
RT "Xenopus Mcm10 binds to origins of DNA replication after Mcm2-7 and
RT stimulates origin binding of Cdc45.";
RL Mol. Cell 9:233-240(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RA Utsumi H.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg, and Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DOMAIN ARCHITECTURE, AND DNA-BINDING.
RX PubMed=18065420; DOI=10.1074/jbc.m706267200;
RA Robertson P.D., Warren E.M., Zhang H., Friedman D.B., Lary J.W., Cole J.L.,
RA Tutter A.V., Walter J.C., Fanning E., Eichman B.F.;
RT "Domain architecture and biochemical characterization of vertebrate
RT Mcm10.";
RL J. Biol. Chem. 283:3338-3348(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 230-427, DNA-BINDING, SUBUNIT, AND
RP MUTAGENESIS OF LYS-385 AND LYS-386.
RX PubMed=19081065; DOI=10.1016/j.str.2008.10.005;
RA Warren E.M., Vaithiyalingam S., Haworth J., Greer B., Bielinsky A.K.,
RA Chazin W.J., Eichman B.F.;
RT "Structural basis for DNA binding by replication initiator Mcm10.";
RL Structure 16:1892-1901(2008).
RN [6]
RP STRUCTURE BY NMR OF 755-842, ZINC-FINGER-LIKE DOMAINS, AND ZINC-BINDING.
RX PubMed=20489205; DOI=10.1074/jbc.m110.131276;
RA Robertson P.D., Chagot B., Chazin W.J., Eichman B.F.;
RT "Solution NMR structure of the C-terminal DNA binding domain of Mcm10
RT reveals a conserved MCM motif.";
RL J. Biol. Chem. 285:22942-22949(2010).
CC -!- FUNCTION: Acts as a replication initiation factor that brings together
CC the MCM2-7 helicase and the DNA polymerase alpha/primase complex in
CC order to initiate DNA replication. Additionally, plays a role in
CC preventing DNA damage during replication (By similarity).
CC {ECO:0000250|UniProtKB:Q7L590, ECO:0000269|PubMed:11864598}.
CC -!- SUBUNIT: Self-associates. {ECO:0000269|PubMed:19081065}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11864598}.
CC -!- DOMAIN: Each zinc finger-like domain binds a zinc ion and is involved
CC in both ssDNA and dsDNA binding, as is the OB-fold domain.
CC {ECO:0000269|PubMed:18065420}.
CC -!- DOMAIN: The N-terminal domain mediates homodimerization.
CC {ECO:0000269|PubMed:18065420}.
CC -!- SIMILARITY: Belongs to the MCM10 family. {ECO:0000305}.
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DR EMBL; AF314535; AAG33858.1; -; mRNA.
DR EMBL; BC070548; AAH70548.1; -; mRNA.
DR EMBL; BC090220; AAH90220.1; -; mRNA.
DR RefSeq; NP_001082047.1; NM_001088578.1.
DR PDB; 2KWQ; NMR; -; A=755-842.
DR PDB; 3EBE; X-ray; 2.30 A; A/B/C=230-427.
DR PDB; 3H15; X-ray; 2.72 A; A=230-427.
DR PDB; 4JBZ; X-ray; 2.40 A; A/B/C=95-124.
DR PDBsum; 2KWQ; -.
DR PDBsum; 3EBE; -.
DR PDBsum; 3H15; -.
DR PDBsum; 4JBZ; -.
DR AlphaFoldDB; Q5EAW4; -.
DR BMRB; Q5EAW4; -.
DR SMR; Q5EAW4; -.
DR MaxQB; Q5EAW4; -.
DR DNASU; 398196; -.
DR GeneID; 398196; -.
DR KEGG; xla:398196; -.
DR CTD; 398196; -.
DR Xenbase; XB-GENE-1015396; mcm10.L.
DR EvolutionaryTrace; Q5EAW4; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 398196; Expressed in egg cell and 15 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR040184; Mcm10.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR015411; Rep_factor_Mcm10_C.
DR InterPro; IPR015408; Znf_Mcm10/DnaG.
DR PANTHER; PTHR13454; PTHR13454; 1.
DR Pfam; PF09332; Mcm10; 1.
DR Pfam; PF09329; zf-primase; 1.
DR SMART; SM01280; Mcm10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; DNA damage; DNA replication; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..860
FT /note="Protein MCM10 homolog"
FT /id="PRO_0000278323"
FT REGION 1..145
FT /note="N-terminal domain"
FT REGION 18..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..380
FT /note="OB-fold domain"
FT REGION 381..406
FT /note="Zinc finger-like 1"
FT REGION 553..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..860
FT /note="C-terminal domain"
FT REGION 657..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..787
FT /note="Zinc finger-like 2"
FT REGION 801..821
FT /note="Zinc finger-like 3"
FT COILED 93..131
FT /evidence="ECO:0000255"
FT COMPBIAS 72..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 385
FT /note="K->E: 10-fold reduction in ssDNA binding affinity;
FT when associated with E-386."
FT /evidence="ECO:0000269|PubMed:19081065"
FT MUTAGEN 386
FT /note="K->E: 10-fold reduction in ssDNA binding affinity;
FT when associated with E-385."
FT /evidence="ECO:0000269|PubMed:19081065"
FT CONFLICT 189
FT /note="Q -> P (in Ref. 3; AAH90220)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="H -> R (in Ref. 3; AAH90220)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="D -> Y (in Ref. 3; AAH90220)"
FT /evidence="ECO:0000305"
FT HELIX 98..120
FT /evidence="ECO:0007829|PDB:4JBZ"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3EBE"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:3EBE"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:3EBE"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3EBE"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:3EBE"
FT STRAND 285..295
FT /evidence="ECO:0007829|PDB:3EBE"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:3H15"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:3EBE"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:3EBE"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:3EBE"
FT HELIX 327..333
FT /evidence="ECO:0007829|PDB:3EBE"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:3EBE"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:3EBE"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:3EBE"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:3EBE"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:3EBE"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:3EBE"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:3H15"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:3EBE"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:3EBE"
FT HELIX 404..411
FT /evidence="ECO:0007829|PDB:3EBE"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:3EBE"
FT STRAND 762..768
FT /evidence="ECO:0007829|PDB:2KWQ"
FT TURN 769..771
FT /evidence="ECO:0007829|PDB:2KWQ"
FT STRAND 774..777
FT /evidence="ECO:0007829|PDB:2KWQ"
FT HELIX 780..784
FT /evidence="ECO:0007829|PDB:2KWQ"
FT STRAND 789..795
FT /evidence="ECO:0007829|PDB:2KWQ"
FT STRAND 797..800
FT /evidence="ECO:0007829|PDB:2KWQ"
FT STRAND 806..813
FT /evidence="ECO:0007829|PDB:2KWQ"
FT TURN 819..821
FT /evidence="ECO:0007829|PDB:2KWQ"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:2KWQ"
FT STRAND 833..835
FT /evidence="ECO:0007829|PDB:2KWQ"
SQ SEQUENCE 860 AA; 95417 MW; 9D64E75D24E9C1FD CRC64;
MEVDADLELL TSLLEENEAA ERNGVVSHEA SSELDEFDEL FDGDEDGSYH GSDNGTEEQT
IGGVEEDFTT LFGDIDDIKE EEAAASDTKK QSSSVCQEKS KDELEDELRK MQAQMKKLQE
QLQKTALAKT SSPGNPKKSP ENKMVQSGKT SRTSPLIERK KTDSNTVAPQ LTSPTVPKAK
LPDAPKRKQN LSDKSPVQKK MASFLSPPEK SSARPGQSTA TQPITNTLKS PVGQQYHVEK
FSGLRIRKPR VSSSEMERKM NGRKLIRLAQ LQNKIATEKL EEEDWVTFGV IVKKITPQSS
NNGKTFSIWR LNDLKDLDKY ISLFLFGDVH KEHWKTDQGT VIGLLNANPM KPKEGTDEVC
LSVDNPQKVL LMGDAVDLGT CKARKKNGDP CTQMVNLNDC EYCQYHVQAQ YKKVSSKRAD
LQSSYSGHVP KKMARGANGL RERLCQGGFH YGGVSSMAYA ATLGSTTAPK KTVQSTLSNM
VVRGAEAIAL EARQKIAAAK NVVQTDEFKE LMTLPTPGAL NLKKHLSGVS PQANCGKEGQ
PIQSISASTL LKQQKQQMLN ARKKRAEESQ KRFLESTEKS EKSSTLTSSA CSVFQSPKQG
AEFPNAQKMA TPKLGRGFAE GDDVLFFDIS PPPAPKLSTS AEAKKLLAIQ KLQAKGQTLA
KTDPNSIKRK RGSSSEELVA QRVASHASTS PKSPDENEPA IKKHRDQLAY LESEEFQKIL
NAKSKHTGIL KEAEVEIQEH YFDPLVKKEQ LEEKMQSIRE QSCRVVTCKT CKYTHFKPKE
TCVSENHDFH WHNGVKRFFK CPCGNRTISL DRLPKKHCST CGLFKWERVG MLKEKTGPKL
GGETLLPRGE EHGKFLNSLK
