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Database: UniProt
Entry: A0A167CUT6_9PEZI
LinkDB: A0A167CUT6_9PEZI
Original site: A0A167CUT6_9PEZI 
ID   A0A167CUT6_9PEZI        Unreviewed;      1491 AA.
AC   A0A167CUT6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=C2 domain-containing protein {ECO:0000313|EMBL:KZL83051.1};
GN   ORFNames=CI238_08081 {ECO:0000313|EMBL:KZL83051.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL83051.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL83051.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL83051.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZL83051.1}.
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DR   EMBL; LFIW01001230; KZL83051.1; -; Genomic_DNA.
DR   STRING; 1573173.A0A167CUT6; -.
DR   Proteomes; UP000076584; 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; cd04044; C2A_Tricalbin-like; 1.
DR   CDD; cd04052; C2B_Tricalbin-like; 1.
DR   CDD; cd04045; C2C_Tricalbin-like; 1.
DR   CDD; cd04040; C2D_Tricalbin-like; 1.
DR   CDD; cd21678; SMP_TCB; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 4.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037761; C2A_Tricalbin.
DR   InterPro; IPR037765; C2B_Tricalbin.
DR   InterPro; IPR037762; C2C_Tricalbin.
DR   InterPro; IPR037756; C2D_Tricalbin.
DR   InterPro; IPR031468; SMP_LBD.
DR   InterPro; IPR017147; Tricalbin.
DR   PANTHER; PTHR46980; TRICALBIN-1-RELATED; 1.
DR   PANTHER; PTHR46980:SF2; TRICALBIN-1-RELATED; 1.
DR   Pfam; PF00168; C2; 5.
DR   PIRSF; PIRSF037232; Tricalbin; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   SMART; SM00239; C2; 5.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 5.
DR   PROSITE; PS50004; C2; 4.
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:UP000076584};
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        184..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          234..439
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000259|PROSITE:PS51847"
FT   DOMAIN          435..553
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          578..698
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          719..836
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          1064..1191
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          47..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1263..1347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1462..1491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1273..1288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1303..1347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1474..1491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1491 AA;  164350 MW;  CF4C500882622DBB CRC64;
     MASALEKNEL KVQGVVESAQ DPETNVTADD AQKKIVEESK KAGITAFTFD PDASPEEKRR
     QAAAAVPAGF HSQRAKGVSI VTDVADSNAP VADLPSPTKE GVIELAKDKD GKPIKTGEDP
     EGNEEEPYTR TGWAPQFGWP ADDVHEGASL LDHSTWLESN LPDKFYGDWY HNAAIIGFAC
     ISSWLVAVLG GGLGWVFILM AACSTYYRTS IRRVRRNFRD DINRELSLKK LETETESLEW
     INSFMLKFWP IYQPVLAQTI VNSVDQVLSS ATPAFLDSLK LKTFTLGSKP PRMEHVKTYP
     KAGDDTVIMD WKFSFTPNDT ADMTYKQIKN KINPKVVLEI RVGKAMISKG LDVIVEDMAF
     SGIMQLKIKL QIPFPHIEKV EMCFLEKPTI DYVCKPLGGE TFGFDINFIP GLETFILEQI
     HGNLAPMMYS PNVFPIEVAK MLAGTPVDQA IGVLAVTLHG AQGLKNPDNF SGSPDPYAAL
     TLNRRQQLAR TKHIKDTGNP RWNETHYIII TSFNDSLDIQ VFDYNDFRKH KELGVASFPL
     DQVEELAVHE NEVLEVIADG KARGQLSCDI RFFPVLEPKK LDDGTLEPPP ESNTGILRFT
     VEQAKDLDGT KSLVGLLNPY ATLHLNGRDV HHTKKLKRTN NPIWDNGSKE MLITDKKNAK
     LGVTIKDDRD LTGDQVIGKY QIKLEDMLEC MEKSQEWFHL AGVATGRVKM MAQWKPVALS
     GVVGGTGGYV TPVGVMRFHF KNARDLRNFE TLGKSDPYVR VLLSGIEKAR TVTHKNTLDP
     DFDEVLYVPV HSARERLTLE VMDSEKMGKD RSLGLVEVFA GDYISQAENG EYNVHDTKKV
     FQGGLQLHGK GIAKGVLTYT VSFFPCLNVA DPEDEEEQEQ AAAAEKAIED APRSAEAGKF
     SSSIEQKKDG AELEISPPKT PVTPVSPSFP RKSKDESGPP KIRLSPQELL KYESGLLIFK
     LMEAEMPEHN THLEVWVDDM AFPSYTSSAA KHKKHTFEEI GDCFIRELDF SRLTLKVREK
     GDKVEGSEKD KDHTIAKLQG NTLDTLKQCL NNPTTLKLKD KENRPSSVKV SLKYIPVKMQ
     LDPSESINNM GTLRVDVLDA QDLPSADSNG KSDPYCKFEL NGEDVYRTKV QKKTLHPAWN
     EFFEVPVPSR TAAKFKVTVW DYDFADKPDF LGAADINLEQ LDPFRPSESR LLLDGKSGTV
     RLRMLFRPSY VTRTRQGTST FSGTFAAPGR IVTGIAGAPI KVGSTVGHGV GRGASFLKRG
     LFSRKDDDSN DASSSFTEIP TIVENGNSPP APTPGLGLKR ATGFSTSDGS ESPDTRPGTS
     NGSTLGHTRT KSNGAASVHS VTPGSPGSGT ASFTVVSATG FPPSTDLYIT INQLTPKPKV
     IGKTKHHKDA TGFFRYNESF KCTCTPDTQF KIEAKGEHTL RSDDDLGEAL YFVDDSGAGG
     EKEIKVGSGT VVIRSTFVPS ASALEPDSPK AIVRRSFMGK RESRSREGTP S
//
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