ID A0A0D2WHR9_CAPO3 Unreviewed; 1613 AA.
AC A0A0D2WHR9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KJE88353.1};
GN ORFNames=CAOG_000016 {ECO:0000313|EMBL:KJE88353.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE88353.1, 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.
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DR EMBL; KE346360; KJE88353.1; -; Genomic_DNA.
DR RefSeq; XP_004364887.2; XM_004364830.2.
DR STRING; 595528.A0A0D2WHR9; -.
DR EnsemblProtists; KJE88353; KJE88353; CAOG_000016.
DR GeneID; 14901695; -.
DR eggNOG; KOG1453; Eukaryota.
DR InParanoid; A0A0D2WHR9; -.
DR OrthoDB; 5395569at2759; -.
DR PhylomeDB; A0A0D2WHR9; -.
DR Proteomes; UP000008743; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20816; C1_GMIP-like; 1.
DR CDD; cd00159; RhoGAP; 1.
DR CDD; cd00174; SH3; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR PANTHER; PTHR15228:SF25; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008743};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 314..580
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 659..705
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 741..924
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 1477..1513
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT DOMAIN 1554..1613
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1053
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1613 AA; 178525 MW; AD7D78821954C5FB CRC64;
MGLFKKDSDA GSAPAAGGPS TPSKKELKEA KEREKANEKK KALISTPNVG SVVHTSSGGG
AAAGGQQQIA GLGAALQRNA SNASASTRPA SGAAAFAASP SPSSAAAAHH VPDNRRSLAL
SARFDSSEDL TGVGLHEHVD VDNHEHLLAL TNKVKEFSEQ ITAFGRLFPS EPNDQAKETV
IVGVTNLHTL IKDISETFSF NLDDVLVHLK TLILATKQWA AGANPTDPQR PHNLNKVLQD
MITVFARIVS EYMQGFATPE AESSAAAQYA AALPLATAGG TIPTTAPPAL QHQASKLHVS
GVLHDVDEEG NFFSSISQDK DLVGMLFMDG VEVLNARCKE WSSYTGELLS YLKSRVALEK
EYSTKLAKLS SDTTATLNEK GWLNRSTMHT NTLAVLASHA GAAARRTEFS HQVVSKVIEP
LHERQTEHDK SRKRIKEQWT KERKRLADTL AATDKAKKHF HDSSRNWEKS LLEKKKEEAT
PMRLKLDKRI KDEEEARAKC GAANDAYKQQ LVVANKAVVD FEAFLRNVIR TLKILSETCE
HKSKNTVGRL HQLEYVLVSP YEDEMISLID HTKHINNVED VARYVARQSA GQELKVESVE
YEDFSLQQET AAYSGHERSG HLGTLPEQRG NHNATGGGLL QVPGLASSAM SGSTSAVNGH
VFRRSDVPGR CAHCQKYAFF NSARCNICNI TCHVGCGDHV VEMPCDRERS SSVSSIHAPA
MRSASGTPSR RKGDKLSFFG SDLVSLARSG QPVPLVVLKC IADIERRGMD LVGIYRIAGQ
KSRIEELCER FEIERENIDV SQQPDEHVVA GVLKLFLRQL ADPLIPFAAY SKFISVSETA
STPAIKALVR SLPDAHYNTL RELMRHLHKV SRNCHVNMMR TDNLGIVFGP TLVRCKEESV
DALLDMPKQV RIVELLITNY EDIFDDVSDE TAARIARETK AAEEEEQERL RNERESEEKR
AQAAKEAEEL RAKQWQLDNE RLEREQKRLQ EERKQRMKEK RRSERESQYL DETADPLQAI
IAATAPIVIE EDEDEAAARQ EEDRATLRRR QEAEAAAAAA EMEAALKLKE EADRRRQKEA
ADRAAAAAAA AAEAEAAAQR QADEQAERER TERAERARRE REAREAQEAL EALEAEETKK
REQAAAAAAA AAEAEAESRR QAEQKAAAER ESQRKADEEA RRRAEQEEED ARPAARQAAA
EEAEREGKRK AKGSARLLPM LPSLRLLRSR RLRQLSFQED DSSPSISRTQ SILDESALPS
LTEAELSNLS EADMQAELER RRVERKRQRE LRAAAAAEAE RQRADEEERE RERQREERRR
KRQSEAEMAA KLEQQEAENR RKKNEEDRRR REQEDAELLA RVAAEKAAEK EAERQAELAA
EEQRRIAAEE RARKRREREE EERRELEALE KAKEERRRKA ASDAESEAKR VADELERSRR
TEAAAAEAAA TAAAAAAASA PAASTPGSAD TDPTSMMCVC GKTAKFRCTM CKSQYYCSRE
CQTSDWKTHK PACKRMSVAP DANAVAAATA KAAEEAEAAK KEAEATPAAA PAATGFKTAK
ALYDYEARSG TEISVKAGAT VTIYSQVNND WYHAGGADGS NGYLPASYLQ MLD
//
