MCM10_XENTR
ID MCM10_XENTR Reviewed; 845 AA.
AC Q28E45;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Protein MCM10 homolog;
GN Name=mcm10; ORFNames=TEgg053h10.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SUBUNIT: Self-associates. {ECO:0000250|UniProtKB:Q5EAW4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5EAW4}.
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:0000250|UniProtKB:Q5EAW4}.
CC -!- DOMAIN: The N-terminal domain mediates homodimerization.
CC {ECO:0000250|UniProtKB:Q5EAW4}.
CC -!- SIMILARITY: Belongs to the MCM10 family. {ECO:0000305}.
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DR EMBL; CR848457; CAJ82204.1; -; mRNA.
DR RefSeq; NP_001016909.1; NM_001016909.2.
DR RefSeq; XP_012814512.1; XM_012959058.2.
DR AlphaFoldDB; Q28E45; -.
DR SMR; Q28E45; -.
DR STRING; 8364.ENSXETP00000019989; -.
DR PaxDb; Q28E45; -.
DR PRIDE; Q28E45; -.
DR Ensembl; ENSXETT00000019989; ENSXETP00000019989; ENSXETG00000009113.
DR GeneID; 549663; -.
DR KEGG; xtr:549663; -.
DR CTD; 55388; -.
DR Xenbase; XB-GENE-1015391; mcm10.
DR eggNOG; KOG3056; Eukaryota.
DR HOGENOM; CLU_014680_0_0_1; -.
DR InParanoid; Q28E45; -.
DR OMA; VFGLRMI; -.
DR OrthoDB; 758449at2759; -.
DR PhylomeDB; Q28E45; -.
DR TreeFam; TF313330; -.
DR Reactome; R-XTR-176187; Activation of ATR in response to replication stress.
DR Reactome; R-XTR-68962; Activation of the pre-replicative complex.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000009113; Expressed in ovary and 9 other tissues.
DR ExpressionAtlas; Q28E45; baseline.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031298; C:replication fork protection complex; IBA:GO_Central.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Coiled coil; DNA damage; DNA replication; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..845
FT /note="Protein MCM10 homolog"
FT /id="PRO_0000278324"
FT REGION 1..145
FT /note="N-terminal domain"
FT /evidence="ECO:0000250"
FT REGION 15..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..367
FT /note="OB-fold domain"
FT /evidence="ECO:0000250"
FT REGION 368..393
FT /note="Zinc finger-like 1"
FT REGION 564..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..773
FT /note="Zinc finger-like 2"
FT /evidence="ECO:0000250"
FT REGION 787..807
FT /note="Zinc finger-like 3"
FT /evidence="ECO:0000250"
FT COILED 93..131
FT /evidence="ECO:0000255"
FT COMPBIAS 33..47
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 845 AA; 94491 MW; D264D9DD947C2D00 CRC64;
MEAVDADLEL LTSLLEENEA AESNSVESHE ASSELDEYDE LFDGDEDGSY HESDNGTEEQ
TVDGVEENFD TLFGDIDDIN EEETVAPDTK KQSSVCQDKS KHELEDELRK MQEQMRKLQK
QLQQTALAKT SSPGNPMKSP DNKLLLSGKT FQSGPLLERS LTVPKANLQD TPKRKQNLQD
KSPLQKQMTS FLSPPDKSST RPVSSTATQP VLNPVRSPVG QQYPVEKFSG LRLRKPRVSS
SEMERKMNGR KLIRLAQLQN KIVTEKLEDE DWVTFGVIVK KITPQSSNNG KTFSIWRLND
LKNLDKYVSL FLFGDVHKEH WKTDQGTVIG LLNANPMKPK EGTDEVCLSV DNPQKVLLMG
DAVDLGTCKA RKKNGDPCTQ MVNLNDCEYC QYHVQAQYKK VSSKRADLQS SYSGHVPKKM
ARGGNGLRER LCQDGFHYGG VSSMAYATTL ASTTAPKKTV QSTLSNMVVR GAEAIALEAR
QQIAAARKNM VQSDEFKELM TLPTPGALNL KKHFSGVPTQ ANEKGGQPFQ SISASALLKQ
QKQQMLGARK KRAEEIQKRF LESTEKSEKS STLVSSERSV FQSPKQGAEF PNAQKMATPK
LGRGFAEGED VLFFDISPPA AKSNTSAQAT KLAAIQKLQA KGQTLTKADP NSIKRKRSSS
AEELVAQRVA SHAPASTKSP DENEPAMKKH REQLAYLESK EFQKILNAKS KHTGILKEAE
AEIQERYFDP LVKKEQLEEK MRSIREQECR VVTCKTCKYT HFKPKETCVS ENHDFHWHNG
VKRFFKCACG NRTISLDRLP KKHCSTCGLF KWERDGMLKE KTGPKIAGET LLPRGEEHGK
FLNSH
