ID A0A0V1LQ55_9BILA Unreviewed; 1930 AA.
AC A0A0V1LQ55;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Protein MCM10 homolog {ECO:0000256|ARBA:ARBA00017770};
GN ORFNames=T02_10845 {ECO:0000313|EMBL:KRZ61616.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ61616.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ61616.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ61616.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRZ61616.1}.
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DR EMBL; JYDW01000016; KRZ61616.1; -; Genomic_DNA.
DR Proteomes; UP000054721; 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:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; 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; 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; PTHR24039; FIBRILLIN-RELATED; 1.
DR PANTHER; PTHR24039:SF28; FIBULIN-1; 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 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1848..1870
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 871..1013
FT /note="NIDO"
FT /evidence="ECO:0000259|PROSITE:PS51220"
FT DOMAIN 1078..1120
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1252..1291
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1292..1333
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1338..1380
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1381..1419
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1636..1676
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1677..1719
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 143..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1735..1838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 619..646
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 154..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1771..1838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1089..1106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1303..1320
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1930 AA; 215076 MW; C41DA42AAFBBB039 CRC64;
MDDLKDESLD ILVDLLNTNI DEEFDDSRCP LPDVLLTEDA ERNENDIDLD KFLSQLENEL
ESDPFDISFE LQGGNCDGNE NSLSTLSEDD LNAKARDIFR ELQRRKLRRL NYSVGSGVQR
EKAVHSVLCK NFDFTKPTSM KVKNSSVVHS GDTSSSEDEA KRDPEACGHN WLSDEGRLIK
HQLAEMESYQ MNRPKSKADN YKYQPSSSAS RISSKSSVLD PFFGIKIKNA KMSLATFTHI
IGSRPKFQLI AINNSKRIDW SNWVTMAVIV DKTDQRRSSQ GNLYMIWKLC DLIDCQRIVS
AFLFGSCLKD HWKLPVGTVV ALFNASLFNS DTSKGITLKL ETAGKVLELG YSEDFGICKS
KQNKTGNPCN NVINKSKSEY CDFHVLNVSR QFTSKRSEFY TPSGHPRLKK DSKLLPPKDC
SNLKKSKPSS SERKLIVDEL SAAKLCQELK MQNALNSLKS LPSTVKGKSS SYKKMEKDDE
FALLNLLKKH EIVDQTVSVI HDENKLPLKA ANASEKSKSK LSCKEFLKAY EPTTVKNPVP
LPKIGKGTTS SGCINLEDAK MKLTKQKAIE IVRSAGGIKK QDPNRPTSGY CILEKRSAET
TANIKDNATV SKRSRLGEKN FTIDEMRQLL KQKSRFENEL RNDEAEKEAK YFEIMEVKEK
FDRHAEQVFE LKNCQVVSCK TCNYTWHSQS DLCKSQRHEI QRHTATKRFF RCLNCKKRTI
SYSLYPSRPC HQCRSRNFER VAMKQERRGP KLPAEELKIR GEELPFVNRI 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
ECAMQTKLCN TQAQPDCVNT PGSYNCTCLV GYDAVTNTCS GASTGLSHVP EQTNSDQSQL
TNAMLSAFKP TVQADVILKP QKTSEFVLNP FMPAPLRGFF EETKILTAQR EDLSGTGPNF
WSLTSSNRPQ GKPVQVTCRL SCTENSKCQF VNDTEKCVCN KGWTGDGVYC VDVNECLTEN
LCPSNSKCLN TIGSYDCICE KGFRFNGQDC IDIDECAEGT AICQGGAAST CINTNGSYEC
HCKTGFNGNP NSPAGCIDIN ECLIPKFYCG PNAECENSVG SYMCRCLPGY LPKQDGIGCE
DIDECENHPC SAKATCINSP GSFTCKCDAT YYGDGFHCEK SRLFPYSRAQ SDSIFNYNQG
SVFINLKRLV RILGYNYDKM RVFTTGMIAF GNPPSVNNID RMYASSIMPF HYDLGFDKNG
TVYVEQVVSG PLLKELADFV RESYNLKVNP ANYAIVVTYE RIDDTLTYQA VLASFDYQTF
AIFIYDSVIP VAAQIGAKNN GNDKIGTMLP FRGDDIFNLV NKSNIGIPGK WMFRIEDMEV
EPCRQGYEQP PFCSKDVDEC KAEQPPCHKD AICVNTPGSY LCKCKHGFTG NGENCFEINP
CYASTGSVCG QNAECYVPSF KGGKPECVCK EGFVGDGFSC FPMPATNEVT VEVETESPKI
EQTTASVQTS SSTTEYPMTI RLRSRRPITF GPPTPVTSYN SEQASTREIS RPHTPTSVQI
RPLQKEPRTN TQTEDPNFPP SSASISPEEI HSLSSATEKS ENNSITKLLI VVVPAVLSVI
WLGLLVVLMA TTTGGFYNEK ANSSGSSSVY EIYGSNTGYY QPAFSPTAHS TLYSTNSAFY
SIPGYQHGRY
//
