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Protein

Protein MCM10 homolog

Gene

mcm10

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Additionally, plays a role in preventing DNA damage during replication (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA replication

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein MCM10 homolog
Gene namesi
Name:mcm10
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-1015396. mcm10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi385 – 3851K → E: 10-fold reduction in ssDNA binding affinity; when associated with E-386. 1 Publication
Mutagenesisi386 – 3861K → E: 10-fold reduction in ssDNA binding affinity; when associated with E-385. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 860860Protein MCM10 homologPRO_0000278323Add
BLAST

Proteomic databases

PRIDEiQ5EAW4.

Interactioni

Subunit structurei

Self-associates.1 Publication

Structurei

Secondary structure

1
860
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi98 – 12023Combined sources
Turni240 – 2423Combined sources
Beta strandi245 – 2484Combined sources
Helixi253 – 2608Combined sources
Helixi268 – 2703Combined sources
Helixi271 – 2766Combined sources
Beta strandi285 – 29511Combined sources
Beta strandi301 – 3033Combined sources
Beta strandi307 – 3126Combined sources
Beta strandi314 – 3163Combined sources
Beta strandi321 – 3255Combined sources
Helixi327 – 3337Combined sources
Beta strandi340 – 3467Combined sources
Beta strandi359 – 3624Combined sources
Helixi366 – 3683Combined sources
Beta strandi369 – 3757Combined sources
Beta strandi378 – 3803Combined sources
Beta strandi382 – 3843Combined sources
Beta strandi388 – 3903Combined sources
Beta strandi394 – 3963Combined sources
Turni397 – 3993Combined sources
Helixi404 – 4118Combined sources
Helixi414 – 4174Combined sources
Beta strandi762 – 7687Combined sources
Turni769 – 7713Combined sources
Beta strandi774 – 7774Combined sources
Helixi780 – 7845Combined sources
Beta strandi789 – 7957Combined sources
Beta strandi797 – 8004Combined sources
Beta strandi806 – 8138Combined sources
Turni819 – 8213Combined sources
Beta strandi827 – 8293Combined sources
Beta strandi833 – 8353Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KWQNMR-A755-842[»]
3EBEX-ray2.30A/B/C230-427[»]
3H15X-ray2.72A230-427[»]
4JBZX-ray2.40A/B/C95-124[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5EAW4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 145145N-terminal domainAdd
BLAST
Regioni230 – 380151OB-fold domainAdd
BLAST
Regioni381 – 40626Zinc finger-like 1Add
BLAST
Regioni596 – 860265C-terminal domainAdd
BLAST
Regioni768 – 78720Zinc finger-like 2Add
BLAST
Regioni801 – 82121Zinc finger-like 3Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili93 – 13139Sequence analysisAdd
BLAST

Domaini

Each zinc finger-like domain binds a zinc ion and is involved in both ssDNA and dsDNA binding, as is the OB-fold domain.1 Publication
The N-terminal domain mediates homodimerization.1 Publication

Sequence similaritiesi

Belongs to the MCM10 family.Curated

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

HOVERGENiHBG055312.
KOiK10736.

Family and domain databases

InterProiIPR015411. Rep_factor_Mcm10_C.
IPR015408. Znf_Mcm10/DnaG.
[Graphical view]
PfamiPF09332. Mcm10. 1 hit.
PF09329. zf-primase. 1 hit.
[Graphical view]
SMARTiSM01280. Mcm10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5EAW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVDADLELL TSLLEENEAA ERNGVVSHEA SSELDEFDEL FDGDEDGSYH
60 70 80 90 100
GSDNGTEEQT IGGVEEDFTT LFGDIDDIKE EEAAASDTKK QSSSVCQEKS
110 120 130 140 150
KDELEDELRK MQAQMKKLQE QLQKTALAKT SSPGNPKKSP ENKMVQSGKT
160 170 180 190 200
SRTSPLIERK KTDSNTVAPQ LTSPTVPKAK LPDAPKRKQN LSDKSPVQKK
210 220 230 240 250
MASFLSPPEK SSARPGQSTA TQPITNTLKS PVGQQYHVEK FSGLRIRKPR
260 270 280 290 300
VSSSEMERKM NGRKLIRLAQ LQNKIATEKL EEEDWVTFGV IVKKITPQSS
310 320 330 340 350
NNGKTFSIWR LNDLKDLDKY ISLFLFGDVH KEHWKTDQGT VIGLLNANPM
360 370 380 390 400
KPKEGTDEVC LSVDNPQKVL LMGDAVDLGT CKARKKNGDP CTQMVNLNDC
410 420 430 440 450
EYCQYHVQAQ YKKVSSKRAD LQSSYSGHVP KKMARGANGL RERLCQGGFH
460 470 480 490 500
YGGVSSMAYA ATLGSTTAPK KTVQSTLSNM VVRGAEAIAL EARQKIAAAK
510 520 530 540 550
NVVQTDEFKE LMTLPTPGAL NLKKHLSGVS PQANCGKEGQ PIQSISASTL
560 570 580 590 600
LKQQKQQMLN ARKKRAEESQ KRFLESTEKS EKSSTLTSSA CSVFQSPKQG
610 620 630 640 650
AEFPNAQKMA TPKLGRGFAE GDDVLFFDIS PPPAPKLSTS AEAKKLLAIQ
660 670 680 690 700
KLQAKGQTLA KTDPNSIKRK RGSSSEELVA QRVASHASTS PKSPDENEPA
710 720 730 740 750
IKKHRDQLAY LESEEFQKIL NAKSKHTGIL KEAEVEIQEH YFDPLVKKEQ
760 770 780 790 800
LEEKMQSIRE QSCRVVTCKT CKYTHFKPKE TCVSENHDFH WHNGVKRFFK
810 820 830 840 850
CPCGNRTISL DRLPKKHCST CGLFKWERVG MLKEKTGPKL GGETLLPRGE
860
EHGKFLNSLK
Length:860
Mass (Da):95,417
Last modified:February 20, 2007 - v2
Checksum:i9D64E75D24E9C1FD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti189 – 1891Q → P in AAH90220 (Ref. 3) Curated
Sequence conflicti740 – 7401H → R in AAH90220 (Ref. 3) Curated
Sequence conflicti788 – 7881D → Y in AAH90220 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF314535 mRNA. Translation: AAG33858.1.
BC070548 mRNA. Translation: AAH70548.1.
BC090220 mRNA. Translation: AAH90220.1.
RefSeqiNP_001082047.1. NM_001088578.1.
UniGeneiXl.712.

Genome annotation databases

GeneIDi398196.
KEGGixla:398196.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF314535 mRNA. Translation: AAG33858.1.
BC070548 mRNA. Translation: AAH70548.1.
BC090220 mRNA. Translation: AAH90220.1.
RefSeqiNP_001082047.1. NM_001088578.1.
UniGeneiXl.712.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KWQNMR-A755-842[»]
3EBEX-ray2.30A/B/C230-427[»]
3H15X-ray2.72A230-427[»]
4JBZX-ray2.40A/B/C95-124[»]
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ5EAW4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi398196.
KEGGixla:398196.

Organism-specific databases

CTDi55388.
XenbaseiXB-GENE-1015396. mcm10.

Phylogenomic databases

HOVERGENiHBG055312.
KOiK10736.

Miscellaneous databases

EvolutionaryTraceiQ5EAW4.

Family and domain databases

InterProiIPR015411. Rep_factor_Mcm10_C.
IPR015408. Znf_Mcm10/DnaG.
[Graphical view]
PfamiPF09332. Mcm10. 1 hit.
PF09329. zf-primase. 1 hit.
[Graphical view]
SMARTiSM01280. Mcm10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMCM10_XENLA
AccessioniPrimary (citable) accession number: Q5EAW4
Secondary accession number(s): Q9DEX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: February 20, 2007
Last modified: May 11, 2016
This is version 51 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.