ID A0A0D2WRD9_CAPO3 Unreviewed; 1119 AA.
AC A0A0D2WRD9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KJE94450.1};
GN ORFNames=CAOG_005089 {ECO:0000313|EMBL:KJE94450.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE94450.1, 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE346367; KJE94450.1; -; Genomic_DNA.
DR RefSeq; XP_004346774.2; XM_004346724.2.
DR AlphaFoldDB; A0A0D2WRD9; -.
DR EnsemblProtists; KJE94450; KJE94450; CAOG_005089.
DR GeneID; 14897568; -.
DR eggNOG; KOG4375; Eukaryota.
DR InParanoid; A0A0D2WRD9; -.
DR OrthoDB; 2876516at2759; -.
DR Proteomes; UP000008743; Unassembled WGS sequence.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR12752:SF9; KRAMER, ISOFORM I; 1.
DR PANTHER; PTHR12752; PHOSPHOINOSITOL 3-PHOSPHATE-BINDING PROTEIN; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008743};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 11..74
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 542..616
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 657..753
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 130..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 118117 MW; CB1537DCE5673C6E CRC64;
MSASSKRVAE WTDAEVGQWL EAEGFGEYVA IFADNNVDGE VLVSLQQDHL KDLGVTSLGK
RLKLVKSLRA LVDHQPPPAV AVVPVVVVPA VATPQSARDS TISGHFDDTD DDARVEPKYD
ILRRRRKSED NLASELAGEG VASPTASHTI TADNDATYSV VVRRPSMNSN GDHHNAAAPS
DDNDGDLAAA AAAMMLGSSE QDHDLADAET SHTVDIMRQS HTGTLGRATK VANASLRGAS
AASSRVNIVN VFVKRVSDTT GLPKVSGETA IPEIQTAADI LDDEARAALT TLSELAEQAE
AAELEEERFD PLPETLSFSS ASSVATSRSV ASDAVGAPST AAANAAATST AAHTPATTAV
STAHASSAAS RALKFGRSLF SDSATPTSPP SASEAESTLF HQKLEVLLER SQNALQVCRK
KAAGNPRLTL QLMRMDPALE SALHASSLQV SASSSSTTST LPPSASAGSA SAAPSHRKTD
DDEDDDDDDE PAPSAAHTQA SNGADGLHTR SAASAAAAAL QASERDAAFV AATHLAESVD
LAGGIVVTAL CSYDAQDESE LPFEKGDVLY VLPNFPNEPL RSQQAWWRCR KIPGISSMGP
RDQGFVPACL VNSNQSAVQR IQGLYGQKVY TETAREEVTV NKKGKLQHDV PAASHIHPTF
CGYLSKLGGS GLRKNWRRRW FVLTNCCLFY YKSPEDQFAL GKIAMPGYTV AYAADRRHSF
RAEYGAGRRT YHFQADSREE MQLWMYAMGL ATLLDDLPDQ TKELLSERRK QRAASVAPEN
AEHAETTGRS AASKIAKFVR KPAFGKSSSP ASSFNAEDES RQIMELLGDA VPVSLKEGSL
HVGRAHSGSV LSAHSLDRHG SMTSDAHSDA SIPSSPTAHD EDRSQHWSPL SSSPPDATAG
SARSDDAAPP AKPPRSSHPR PIPQSSLTST SPGSSSPPTG SIASSSSFAR PSGSPRKPPP
PLRGRDEISN LLDSIDSSVE RRDPLGPPAA HQRHSSSASH SSRTPSGSGS FTSTTGGGPP
PVSVARLFLG NLPENRPASP ETSHSPHSST GLRSPRACIS PAPHEDSEHE SDSTTYAEVR
ALQKPSRAAP LNSGPSTRPS LASIASEREV LYAAVDQQF
//
