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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)DescriptionActionsGraphical viewLength
Mutagenesisi385K → E: 10-fold reduction in ssDNA binding affinity; when associated with E-386. 1 Publication1
Mutagenesisi386K → E: 10-fold reduction in ssDNA binding affinity; when associated with E-385. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002783231 – 860Protein MCM10 homologAdd BLAST860

Interactioni

Subunit structurei

Self-associates.1 Publication

Structurei

Secondary structure

1860
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi98 – 120Combined sources23
Turni240 – 242Combined sources3
Beta strandi245 – 248Combined sources4
Helixi253 – 260Combined sources8
Helixi268 – 270Combined sources3
Helixi271 – 276Combined sources6
Beta strandi285 – 295Combined sources11
Beta strandi301 – 303Combined sources3
Beta strandi307 – 312Combined sources6
Beta strandi314 – 316Combined sources3
Beta strandi321 – 325Combined sources5
Helixi327 – 333Combined sources7
Beta strandi340 – 346Combined sources7
Beta strandi359 – 362Combined sources4
Helixi366 – 368Combined sources3
Beta strandi369 – 375Combined sources7
Beta strandi378 – 380Combined sources3
Beta strandi382 – 384Combined sources3
Beta strandi388 – 390Combined sources3
Beta strandi394 – 396Combined sources3
Turni397 – 399Combined sources3
Helixi404 – 411Combined sources8
Helixi414 – 417Combined sources4
Beta strandi762 – 768Combined sources7
Turni769 – 771Combined sources3
Beta strandi774 – 777Combined sources4
Helixi780 – 784Combined sources5
Beta strandi789 – 795Combined sources7
Beta strandi797 – 800Combined sources4
Beta strandi806 – 813Combined sources8
Turni819 – 821Combined sources3
Beta strandi827 – 829Combined sources3
Beta strandi833 – 835Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KWQNMR-A755-842[»]
3EBEX-ray2.30A/B/C230-427[»]
3H15X-ray2.72A230-427[»]
4JBZX-ray2.40A/B/C95-124[»]
SMRiQ5EAW4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5EAW4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 145N-terminal domainAdd BLAST145
Regioni230 – 380OB-fold domainAdd BLAST151
Regioni381 – 406Zinc finger-like 1Add BLAST26
Regioni596 – 860C-terminal domainAdd BLAST265
Regioni768 – 787Zinc finger-like 2Add BLAST20
Regioni801 – 821Zinc finger-like 3Add BLAST21

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili93 – 131Sequence analysisAdd BLAST39

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)DescriptionActionsGraphical viewLength
Sequence conflicti189Q → P in AAH90220 (Ref. 3) Curated1
Sequence conflicti740H → R in AAH90220 (Ref. 3) Curated1
Sequence conflicti788D → Y in AAH90220 (Ref. 3) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KWQNMR-A755-842[»]
3EBEX-ray2.30A/B/C230-427[»]
3H15X-ray2.72A230-427[»]
4JBZX-ray2.40A/B/C95-124[»]
SMRiQ5EAW4.
ModBaseiSearch...
MobiDBiSearch...

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: November 2, 2016
This is version 53 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.