ID A0A0G4KWZ7_9PEZI Unreviewed; 1347 AA.
AC A0A0G4KWZ7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Tricalbin {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=BN1708_017254 {ECO:0000313|EMBL:CRK14288.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK14288.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK14288.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK14288.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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; CVQH01005502; CRK14288.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4KWZ7; -.
DR OrthoDB; 2787577at2759; -.
DR Proteomes; UP000044602; 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; 4.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 4.
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:UP000044602};
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 111..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 171..376
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 372..490
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 514..635
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 652..770
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1002..1129
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CRK14288.1"
FT NON_TER 1347
FT /evidence="ECO:0000313|EMBL:CRK14288.1"
SQ SEQUENCE 1347 AA; 149391 MW; 461D97FFDD7CEA4C CRC64;
AVPEGFHSKR PHGVSVVTDV AGEDSGPTAD LPPPSKEGII EVTKDADGNV IEDGAGPGGD
TEKPYERTGW APQFGWPNDN AQDAESLLDH STWLEGKVPD KFYGDWYHNA AIIVFACISS
WLVAVLGGGL GWVFMIMAAC STYYRTSLRR VRRNFRDDIN REMQLKKLDN DHESLEWINS
FLLKFWPIYQ PVLAQTIINS VDQVLSSATP AFLDSLKLKT FTLGSKPPRM EHVKTYPKAE
DDIVMMDWKF SFTPNDTADM TSKQIKSKIN PKVVLEIRVG KAMISKGLDV IVEDMAFSGI
MRLKIKLQIP FPHVEKVEMC FLERPTIDYV CKPLGGETFG FDINFIPGLE TFILEQIHGN
LAPMMYAPNV FPIEVAKMLA GTPVDQAIGV LAVTLHGAQG LKNSDRFAGD IDPYAVLSLN
RRQELARTKH ISDTSNPRWN ETHYIIITSF TDSLDIQVFD YNDFRKHKEL GVASFPLDQV
EELNVHENER LDIFADGKNR GQVSIDVRFF PVLESTKLED GSEEPPPESN TGILRFTVEQ
AKDLDGTKSL VGLLNPYATL HLNGRDVHNT KKLKRTNNPI WDNGSKEMLI TDKKHAKLGV
TIKDDRDITG DQVIGKYQIK LEDILECKEK GQEWFHLAGA STGRVKMMAQ WKPVAISGVL
SGTGGYVTPI GVMRFYFRGA RDLRNFETLG KSDPYVRVLL SGIEKARTVT HRNTLDPDWD
EVLYVPVHSN REKLTMEVMD SEKMGKDRSL GQIEVAAGDY IFQDEHGEYL VHDQKTIKEA
GLKLHGKGIA KGVLIYNVSF YPTLNVADPE EEEEEAKETK PETEAGEPEP LARSATAGKF
SSTLDNKSQK ASEGDDSSAL VPLTPTSTRK SKESKGPPKI HLSPEQLLKY ETGLLIFKLM
EAEMPESNTH LEVWVDDMAF PSYISSAAKH KKHKFDEIGD CFIREIDFSR LTLKVREKGQ
AVEGNEKDKE STIAKLQGNT LDTLKQCLNN PTMLKLNDKD GRPSNVKVSL KYIPVKMKLD
PSESINNMGT LRVDVLDAED LPSADRNGKS DPYCKFELNG EEVYKTKVQK KTLHPVWNEF
FEVPVPSRTG ADFKVVIWDY DFADKPDLLG SADINLEHID PFKPSETKLL LDGKSGVVRL
RLLFRPAYVA RTRQGTSTFS GTFAVPGRIV TGVAGAPVKA AGAVGSGVGG LVRNVFSRSK
KDDEDRNTAT AYDTPTITEN GNGLKRSGPV PDGNEPPIST PPGTANGATL GHSRNRSSGA
ASIYSTNGAS PGSGTAVFSI VSTSGYPPAS EVYVVIHQLT PKHKTVGKTE KHKEPSGEIQ
FNESFKWTCT PDTQFKIEVK GDRTFRS
//