ID A0A0D2WJ46_CAPO3 Unreviewed; 3078 AA.
AC A0A0D2WJ46;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KJE89248.1};
GN ORFNames=CAOG_000758 {ECO:0000313|EMBL:KJE89248.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE89248.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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; KE346360; KJE89248.1; -; Genomic_DNA.
DR STRING; 595528.A0A0D2WJ46; -.
DR EnsemblProtists; KJE89248; KJE89248; CAOG_000758.
DR eggNOG; KOG1388; Eukaryota.
DR InParanoid; A0A0D2WJ46; -.
DR PhylomeDB; A0A0D2WJ46; -.
DR Proteomes; UP000008743; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00055; EGF_Lam; 4.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 4.
DR Gene3D; 2.10.25.10; Laminin; 9.
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; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR46376:SF2; DISTRACTED, ISOFORM B; 1.
DR PANTHER; PTHR46376; LEUCINE-ZIPPER-LIKE TRANSCRIPTIONAL REGULATOR 1; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF12947; EGF_3; 2.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF13418; Kelch_4; 1.
DR Pfam; PF13854; Kelch_5; 1.
DR Pfam; PF00053; Laminin_EGF; 6.
DR Pfam; PF01437; PSI; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00181; EGF; 13.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00180; EGF_Lam; 5.
DR SMART; SM00423; PSI; 9.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF117281; Kelch motif; 2.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 3.
DR PROSITE; PS51820; PA14; 1.
PE 4: Predicted;
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008743};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2697..2719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..185
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 183..215
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 758..920
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT DOMAIN 1171..1211
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1274..1314
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1348..1395
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1447..1646
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1644..1677
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2371..2412
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2445..2490
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2541..2587
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2873..3018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3054..3078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2875..2899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2916..2931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 187..197
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 205..214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1648..1658
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1667..1676
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 3078 AA; 323834 MW; 14BFF7A11AC87491 CRC64;
MSRSLPPCTG ARPSSTTSRN MPAANTAGTS RRQKRLAPPQ HLFRSCSAML ALALLLLLAL
ISPSAAADCS GQRVLIANST SGTFTPSDSG YPAFTTCQWL IEAPALANGG TPLPILLEFL
TFDTECAYDF VDVYDGVNST SPKLGALNGQ IAVAPLVARS GHMLVVLISD INYVTAGFTA
RYSINPCPAN CSDRGICQAN GHCACNPGFA DQGCQTELCP NNCAAALGQG QCDLATVHGC
VCNAGYGGLD CSQPVDDLND GWTLLVGGAS SGNTGTERGF HTTVYSPLNH TIFVYGGYSQ
EDQLLGNVVA YNLVTRARPR ELTFTAHVPS PRYSHSAILT PDNLMVVYGG ITLDQHISDE
VWVLSLNRSV WEQRIPAVGG ISPPPLTGHS ATYIPSSNSM VVIGGKTTFD PFPTSIYEYS
IAANRWYQRT PRGFIAAGVY GHSSVYVEHL HSIFVYGGIR PLSSSYSYRL NTLYVLQVDH
MRWIQLLPSN PIRASAFHGA WLGRSERSMY IQGGYVMSHN ENDNRCFTND LFAFDFDSNR
FRTVEDNSDA PTRYLPGRRM GQGVVTVRDS VSPALAAVDA VLVGGFDGQA LSDAVAYHEE
TNPCLSAMQQ ALASGVSGDV GSGAVMQQCQ SNPSCVACST TLASGFVLPN ITAQDVVLSS
LLNSSQVTTA CIQLTDIARY NCSMALPTTL TQGHASQSFC EALRFCSDCT VFSDCGWCAT
TATCVNASSV LGCPASLSGQ APAPIVVGLA ACVSSSVTNG SVAQERWYNV GGSSVQDMSV
LSTYPDYPDI VTVRSVELAA DMNGDAFTQG TRVRGFLVPP ETGNFTFFIA SSMSSVLGLS
TAADSNDMSL VVNIASVNYF SPFRDYTAQP SQQSAPVFLA ANRRYLFTII NKQSGEWGNH
FSVAWLLPSQ NAFGNATSAE ASVVSAQFLV PYYSSTSNST ATRANMTLAL AGAVSCSTHP
SCKGCIADAS CAWCKSTGRC AERMTGLQMT ASNTTSVCPQ DALEVDDQSC PLCGNYFTCR
GCVSSSTSCQ WAYGSCYPSQ YGIDSSATVT APAFCPTPCR NFTSCATCVG NGNPAACNWC
PATQTCDEIS SFVAVFTAGQ CGTGYATDTS MCVDCSRFGD CRSCLAQDTC GWCSNTTNGL
GGVCMGGTLS GATAECAANP SRQWSWFTCP DINECALGLS NCASNATCQN TPDSFTCTCN
PGFLGDGVSC APDCSAVPSS NSSDPTLRPS CGDMGVCVAP NTCECDPVWT GTDCRTSCSC
NGVLNCTAAL NCVDIDECAQ GLDDCDVHAD CVNVPSTFEC VCKAGYAGNG TFCEPVCPGG
CNGGVCSSPS NCTNCPFGYT GASCQVACQC NGHSDCLPDA PNVCLSCQNR TTGPSCNQCI
PGSYGTPTQP AGCQACACNG HANTVIGECN NVTGVCFCLP PYEGPSCTAC ASGFYYSATN
KLCLAACSGR KTLRFDQGAI GTNGVYPPDS VCSWLIVAEP SAVSNASYFV ASRPERARFD
DGDDDDDDGM DTATASTTLR STNINKQQSQ SVKAFVERAP FLDSDHGREI ARRILGSDSE
AAEIVSEQSL TPLAITLDFY SFGSECLFDY LFVFDGSSTS APLLGSFSGL AVIPPIIVAR
SGTMLVVMYS DINYTVGGFE AKYAISACPN DCSGHGDCTA SVGICTCHPG FAGVACERPL
CPNSCHPELS SMNACDVSRG VCRCAPHLGG TDCSVNVSSA SPALTWSTLS QDQAVIVGPA
TNAAQASIIL PTDFPPRAGH TAQYDASRNS VFVFGGYGQR DTVLNDLWQF DVRSRRWTLV
QPADASAAVP RGRHSHAMVL SPERDSLIVV GGWAYEPFQP VGDIWEFHLG TRTWNLLHAG
SLATDLPVAT LLPAISGHSA TLVDSTIYIL GGRTAQTNFN TRVFAFSFAL GAVRVVNTVG
VNALGMYGHT AVYSPGTDEI IVFGGIQLLD NNLIYTSNSA RLYSFVVGKK AWRSLPDRVS
PDGLNVLPSA NHAAVFVPTG SYMIVVGGSS FIHGWLEMCM TATVSMFAPS CRVWALPNVP
LSSPVTVANS MSNRLGHALV FVPANFDGDA DIAARVLLIG GFDGRVRADV HSLSVPASLC
SLYSMGRCLS DASCTWCATP LSANYSGPLC LPSSSNTASI CNQTTSNNGD CSIDCSSASI
SCEACSSLRS GCSWCTGTRQ CQAANATCTS GQSIPYNGIC PLYPCAAKQS CRECTVSGQC
SWTGSACTTA SPPNAITNIA NCRAPCSSNT NCSTCLLADN TGNIPCLWCE STSTCLDFNA
YTGVFDFGQC FEWSQVPDRC APDCSVFQTC DQCQSNLRCG WCADPGALGT GRCLNGNSEG
PDPGLNCTVP SPAYIGNSTA PPTWNYATCP DVDECLTGQA NCPVNSTVCV NTPDSYECQC
LPGYQPSGST CIAYCAQQCV FGVCVQPNVC KCNRGYIGLN CSMDCGCNGH STCQTYGVCE
RCMDNTAGLR CEVCSDGYYG NPVNGQSCSS CYSHCNQHTT SCNPATGICS GCNNSTTGDL
CQICLPGFTR LGQNPVICGP CICNGHSSTC DAITGVCNCQ DNTRGTQCEQ CARGYMGLPT
NGNQCFLVLG EGELQGPDQV GRGEALYYAI SPKYTNVDIR LTVDVFDGLV TTYLSPRSDK
AVKADTEVQT GLSRRTDLVI SYLDHDFLSS HFYLQVHGTS NATFMVYFAQ RVTQIDLFVF
FSVFFSCFFL LLSVMFLVWR ARMSRARRLA IARRQTELRQ MASRPMSSVR VIMSQAMGNY
RKLALAPIAY QPLVNGQATT MTVLVELPGP GSNAQAGTTS SPVPVAGKPA NPVARNVAAV
AALAPMAASW ERKPPLVIAS NKSIEFELLE TSFGGDEAEP GEPGDVALTE LAGAEGRASS
SSSSSSSSSP LSSTGHDEDA VASGNADAAS SVDQKEPVAP AQQSSAEPDA VENDQASPRP
SAEEGTAAVA GEPGQPSPSD APGAPEQANL SDAIPAGEGV QAATDAAVEP VVNTAAKEAP
SRSAAPATAT AATVARPQSS LPGLRTVAFA TSIIALDRRT YEVLTVPLTQ DDTALKEPRR
PGHFLTSLLR QRRRNQQP
//
