ID A0A0V1PL70_9BILA Unreviewed; 2006 AA.
AC A0A0V1PL70;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Protein MCM10 homolog {ECO:0000256|ARBA:ARBA00017770};
DE Flags: Fragment;
GN ORFNames=T08_3346 {ECO:0000313|EMBL:KRZ96946.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ96946.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ96946.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ96946.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM10 family.
CC {ECO:0000256|ARBA:ARBA00009679}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ96946.1}.
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DR EMBL; JYDM01000005; KRZ96946.1; -; Genomic_DNA.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 6.
DR Gene3D; 2.40.155.10; Green fluorescent protein; 1.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR009017; GFP.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR040184; Mcm10.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR015411; Rep_factor_Mcm10_C.
DR InterPro; IPR015408; Znf_Mcm10/DnaG.
DR PANTHER; PTHR13454; PROTEIN MCM10 HOMOLOG; 1.
DR PANTHER; PTHR13454:SF11; PROTEIN MCM10 HOMOLOG; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 5.
DR Pfam; PF09332; Mcm10; 1.
DR Pfam; PF06119; NIDO; 2.
DR Pfam; PF09329; zf-primase; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 6.
DR SMART; SM01280; Mcm10; 1.
DR SMART; SM00539; NIDO; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 7.
DR PROSITE; PS01187; EGF_CA; 4.
DR PROSITE; PS51220; NIDO; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 1924..1946
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 921..1063
FT /note="NIDO"
FT /evidence="ECO:0000259|PROSITE:PS51220"
FT DOMAIN 1128..1170
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1307..1346
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1347..1388
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1393..1435
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1436..1474
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1712..1752
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1753..1795
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 136..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1811..1830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1839..1914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 613..640
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 396..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1847..1914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1139..1156
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1358..1375
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ96946.1"
SQ SEQUENCE 2006 AA; 223622 MW; 2EEB58FB0BF7368B CRC64;
LDILVDLLNT NIDEEFDDSR CPLPDVLLTE DAERNENDID LDKFLSQLEN ELESDPFDIS
SELQGGNCDG NENSLSTLSE DDLNAKARDI FRELQRRKLR RLNYSVGSGV QREKAVHSVL
CKNFDFTKPT SMKVKNSSVV HSGDTSSSED EAKRDPEACG HNWLSDEGRL IKYQLAEMES
YQMNRPKSKD NYKYQPSSSA SRISSKSSVL DPFFGIKIKN AKMSLATFTH IIGSRPKFQL
IAINNSKRID WSNWVTMAVI VDKTDQRRSS QGNLYMIWKL CDLIDCQRIV SAFLFGSCLK
DHWKLPVGTV VALLNASLFN SDTSVQAKGI TLKLETAGKV LELGYSEDFG ICKSKQNKTG
NPCSNVINKS KSEYCDFHVL NVSRQFTSKR SEFYTPSGHP RLKKDSKLLP PKDCSNLKKS
KPSSSERKLI VDELSAAKLC QELKMQNALN SLKSLPSTVK GKSSSYKKME KDDEFALLNL
LKKHEIVDQT VSMIHDENKL PLKAANASEK NKSKLSCKEF LKAYEPTTVK NPVPLPKIGK
GTTSSGCINL EDAKMKLTKQ KAIEIVRSAG GIKKQDPNRP TSGYCILEKR SAETTANIKD
NATVSKRSRL GEKNFTIDEM RQLLKQKSRF ENELRNDEAE KEAKYFEIME LKEKFDRHAE
QVFELKNCQV VSCKTCNYTW HSQSDLCKSQ RHEILRHTAT KRFFRCLNCK KRTISYSLYP
SRPCHQCRSR NFERVAMKQE RRGPKLPAEE LKIRGEELPF SADKRIFFTF RNRCFHFTEQ
GVAQHTSTAN FMNSANFIWL LALLILLCQI IFCSGDVDGI RLRRRRHDQS PNLGAPMHID
LNITVPFIFK PRLYPYGEGT GDNELSLWTS VQGYVLQNEI SYWGESFASV YISKDGVIGF
SPNFAESKPT AFPSGEKVLA IFWTPSSLGD IGKVYFRETT DPQILSLAAS EVQLQYNYDS
NFTPSSVFIV TWENLAPPMA SNDLPDSHRN LFQAALIMSE NGSFAHVIYS KLKWHGNAIV
GFNNGDGIEH LTLPWSGSSD VLKVGAESDI GIPGEWMFKL DESSGVHLCG KGYKGIDCTR
TCSKNEFSYD CHRKCHCENG ILCNEITGIC PTARCEKGWT NAPTCDEDID ECTMQTKLCN
TQAQPDCVNT PGSYNCTCLV GYDAVTNTCS GLFHNSASTG LSHVPEQTNS DQSQLTNAML
SAFKPMVQAD VILKPQKTSE FVLNPFMPAP LRGFFEETKI LTAQREDLSG TGPNFWSLTS
SNRPQGKPVQ VTCRLSCTEN SKCQFVNDTE KCVCNKGWTG DGVYCVDVNE CLTENLCPSN
SKCLNTIGSY DCICEKGFRF NGQDCIDIDE CAEGTAICQG GAASTCINTN GSYECHCKTG
FNGNPNSPAG CIDINECLIP KFYCGPNAEC ENSVGSYMCR CLPGYLPKQD GIGCEDIDEC
ENHPCSAKAT CINSPGSFIC KCDATYYGDG FHCEKSRLFP YSRAQSDSIF NYNQGSVFIN
LKRLVRILGY NYDKMRVFTT GMIAFGNPPS VNNIDRMYAS SIMPFHYDLG FDKNGTVYVE
QVVSGPLLKE LADFVRESYN LKVNPANYAI VVTYERIDDT LTYQAVLASF DYQTFAIFIY
DSVIPVAAQI GAKNNGNDKI GTMLPFRGDD IFNLVNKSNI GIPGKWMFRI EDMEVDPCRQ
GYEEPPFCSK GDIGFNHKII CINHRNHSTS SDVDECKAEQ PPCHKDAICV NTPGSYLCKC
KHGFTGNGAN CFEINPCYAS TGSVCGQNAE CYVPSFKGGK PECVCKEGFV GDGFSCFPMP
ATNEVTVEVE TESPKIEQTT ASVQTSTSTT EYPMTIRLRS RRPITFGPPT PVTSYNSEQA
STREISRPHT PTSVQIRPLQ KEPRTNTQTE DPNFPPSSAS ISPEEIHSLS SATEKSENNS
ITKLLIVVVP AVLSVIWLGL LVVLMATTTG GFYNEKANSS GSSSVYEIYG SNTGYYQPAF
SPTAHSTLYS TNSAFYSIPG YQHGRY
//
