ID A0A0D2D1J7_9EURO Unreviewed; 1375 AA.
AC A0A0D2D1J7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=C2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV06_10801 {ECO:0000313|EMBL:KIW37183.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW37183.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW37183.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW37183.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847346; KIW37183.1; -; Genomic_DNA.
DR RefSeq; XP_016257399.1; XM_016412385.1.
DR STRING; 215243.A0A0D2D1J7; -.
DR GeneID; 27362875; -.
DR VEuPathDB; FungiDB:PV06_10801; -.
DR HOGENOM; CLU_002125_3_0_1; -.
DR OrthoDB; 1465207at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd04041; C2A_fungal; 1.
DR CDD; cd04052; C2B_Tricalbin-like; 1.
DR CDD; cd21676; SMP_Mug190; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037767; C2A_Mug190-like.
DR InterPro; IPR037765; C2B_Tricalbin.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR47348:SF2; MEIOTICALLY UP-REGULATED 190 PROTEIN; 1.
DR PANTHER; PTHR47348; MEIOTICALLY UP-REGULATED GENE 190 PROTEIN; 1.
DR Pfam; PF00168; C2; 2.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS51847; SMP; 1.
PE 4: Predicted;
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053342};
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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 278..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 377..646
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 644..773
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 859..996
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1216
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1375 AA; 154027 MW; E23C23BD9C8653AA CRC64;
MASDDEFEPD SRQRNYRAPY TARHPIPTVQ KYKAERSELK GQQEEAESAQ HDDEDDSKVK
RAYHAAKGVI TGDEPPRSRH DPYRTENRNV QGADTHAEPR ERPEASQGEG EGDEQNEQQQ
QQQQQQQQQQ QQQQQPGQGR SPSQGTSDTQ SKSDGKSDKE AKSATEAVAS EIDPRQKRKA
MKHQKRNDGG REVTDPVTHL PIVIRDSTRK DLKRADENLP AVGEDPETKT GPAGASKSSE
SLDREKDELQ KKHNGMQKLF PPPSFDDLKS ELAKTYQIAL AAGLGSIVLL VSLSMVAVQV
FDLDFSSRRD GRRRSSAVFT TFIPAAAIFL TSVGIGGVVV WIVQGWLGKK VEEVWKDEVW
DAARSEEVEA NDSTDIVPES VSWLNNLLAS VWPLINPDLF TSISDMLEDV MQASLPKVVR
MVSVDDLGQG SEAFRILGVN WLPTGAASQS VGSDGKLESP KDQGNSDRSA PGQGEIQDGD
DGEGEDGNDD KDGGEKNNQG KKQDELEQQA IREGMEAEQG DFVNMELAFA YRARSSGKSL
QAKAKNAHLY LKFYLPGGIA VPVWVELRGI IGTMRLRLQL TPDPPFFSLC TLSFMGQPQA
DLSCVPLSRH ALNLMDVPLI SSFVQSSIDA ALAEYVAPKS LTLDLKDMLV GDDFKKDTIT
RGVVMIFIKS AKGFKEGDGG IGPFEGSSDS YVTVSWGKFG KPVASTRIIV DDQEPVWNEW
SNILVTPEEV NADEKLRLQL WDSDKYTADD DLGRVEVDLK ELMHGTKFKN KMVDREDRFV
GEDPDEKMPG TLQWRVGYFT KIKITEEQLA RQTAEPDIKS QAELRDRVNE TAQRKLREAT
AKDESKEIKQ QTQEDYKDRE DQLMISSPPP DDYLSGIFSI QIHNITGLEV QKLQKQDKKN
NQGDREDEAE HSDDMPSSYA TIILNHQKIY RTRTKPKNAK PFFNAGTERF VPNWKTAEVM
ISVRDDRERE DDALLGMIYL PLRRVFEKRS QIMQTYPLVG GIGYGRARIS MVWRSVDLQL
PKELMGWNYG TLEVKSPVRS KGGRDDSFTQ NRIKLRTNLM RAKMLPSDDE DKGVWKPKHE
KQSLFLAVRK RYSSALVVEF RKSVLGPDKT SQLAVLWLKD IPDEEEVTVP LKVWKGGKDA
MHRATTSYGY DGQENEEPMG EIELTLKMWR GLSGYHKNYA NRASNTDIKD VMEVLDTAND
EGQVSDDDED DGAGEGDSGY SSDSDSTESG GDTESDAKQK QEKQSRRRNN KKLRTHANDD
SSDEDSDAGK TSNSKLDPTQ LASKPLVKVK DVAEKVLNVD GHNDQDDGSR GARAQIRDYK
DHHKQMHRKH KGVMQWRGAR TLDWMAGKVK RGKGKIGEVF EHDDDNKTGG VETEV
//
