ID A0A183ICZ7_9BILA Unreviewed; 729 AA.
AC A0A183ICZ7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Deleted in malignant brain tumors 1 protein {ECO:0000313|WBParaSite:SBAD_0000156201-mRNA-1};
GN ORFNames=SBAD_LOCUS1491 {ECO:0000313|EMBL:VDO94508.1};
OS Soboliphyme baturini.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Dioctophymatida; Dioctophymatoidea; Soboliphymatidae; Soboliphyme.
OX NCBI_TaxID=241478 {ECO:0000313|Proteomes:UP000050793, ECO:0000313|WBParaSite:SBAD_0000156201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SBAD_0000156201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO94508.1, ECO:0000313|Proteomes:UP000270296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UZAM01006843; VDO94508.1; -; Genomic_DNA.
DR WBParaSite; SBAD_0000156201-mRNA-1; SBAD_0000156201-mRNA-1; SBAD_0000156201.
DR Proteomes; UP000050793; Unplaced.
DR Proteomes; UP000270296; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07974; EGF_2; 1.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 3.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 3.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Reference proteome {ECO:0000313|Proteomes:UP000270296}.
FT DOMAIN 280..319
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 330..451
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 453..568
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 568..604
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 605..641
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 309..318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 453..480
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 594..603
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 631..640
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 729 AA; 79823 MW; FF51FC4BB14AB3F4 CRC64;
MFILDLQAED AWRQVLLTEM FQLFVTPELA EMKPTSIGCP HRRNVLPPQN VVNEFDKRLK
TIRLLCGGGM FATCCIVLLP PGHLKLLKST IKSTCATNKS ISADMFNVKM ADNVSVKLVS
GDASALKNSQ ESSAKKVTSL SPLPYFMLLL EIDFCAHLPC QNGATCVSGM TNGTTVTCGT
GIMVNRLHSA NLKMTTVIDV GPYATVNLMM LLMNFDCHDA AITVHDGADD SFEQLAKYCS
LPSLSYISHA TQRYLTVVYK SFTAISSSKS DVFKLVWSST FVSCNNFTCE HGGHCISSSA
EAHIPHCVCP SGWTGLHCDM PSELIYDISN QNVLKIPNGV LASPNYPNLY PSGQRNLLTL
ITSPTMVFQF KLELLMLEAS FDGACYDSLS IYDGELSDLS SNLLGRFCGS YDKQNLPLFR
RNVTSGPLAT VLFSSDQFVQ DQGFLLCFSS ISCGQTFVSA SSGTISSPHY PKHYPYMSNC
HYTIHANRTG YKVLLTINKF DLETSPDCFA DFLQIQLSEN PATTIRLCGG LAGLTQRNFA
SDSDTIRLYF HSDTYIERTG FSVTYDIVLD TCANMSCPPH SECVLSTTGA KCQCLHGYEG
ESCTEIDYCL HVTCSNHGTC NKMIGGYNCS CNKGWMGKDC ELGGETSIST SGSGQIASPN
YAYHSVGTLT CKWRMMSVLP GKQGIVSGFQ LQFNPLNISS RGNCTEESTD VVMLYDHISQ
TPQVQPVKK
//
