ID U7Q579_SPOS1 Unreviewed; 1494 AA.
AC U7Q579;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Tricalbin {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1624_00478 {ECO:0000313|EMBL:ERT02180.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERT02180.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
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DR EMBL; KI440842; ERT02180.1; -; Genomic_DNA.
DR AlphaFoldDB; U7Q579; -.
DR STRING; 1391915.U7Q579; -.
DR eggNOG; KOG1012; Eukaryota.
DR HOGENOM; CLU_001661_0_0_1; -.
DR OrthoDB; 2787577at2759; -.
DR Proteomes; UP000018087; 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; 5.
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; 5.
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:UP000018087};
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 186..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 236..441
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 436..556
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 580..700
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 721..835
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1066..1184
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1333..1447
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1456..1494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1494 AA; 163254 MW; C4E6ABBC9B44FECC CRC64;
MATTQPSAPE AKQSAVIEAA RDPNSAVSSQ DAQAKMVQES KKAGIPAFTF NPDASPEEKK
AQARAAIPDN FHNPKRVKGV AIATDIDDGS AAQYDLPSPT KAGAITAPPA GDEKAAGNGA
AAPGETEMGP ETTGWAPRFG WPVESIRDAP SLLEHSTWLE GRLPANLYGD WYHNTGIIIF
ACLTSWFIAV LGGGLGWVFI IIATCGTYYR TSIRRVRRNF RDDLNRELSM KRLETDSESL
EWMNSFLFKF WPIYQPVLAQ TIINSVDQVL SSATPAFLDS LKLRTFTLGS KPPRMEHVKT
YPKAEDDIVM MDWKFSFSPN DIADMTTQQV KNKINPKVVL EIRVGKAMIS KGLDVIVEDM
AFSGLMRLKI KLQIPFPHVE KIEMCFLEKP TIDYVCKPLG GETFGFDINF IPGLESFILE
QIHGNLAPMM YAPNVFPIEV AKMLSGSPVD QAIGVVAVTL HGAQGLKNPD KFSGTIDPYA
VITLNRRSPL AQTKIIRDTN TPRWNETHYI IVTSFNDSLD LIVNDFNDYR KDKELGVASF
QLENLEEVNE AENETLEVIA DGKAHGQVSC DIRFFPVLTD DKLPDGTVEP APPSNTGILR
FTVEQAKDLD GTKSLVGMLN PYSVLLLNGK EIHTTKKLKR TNNPIWDNGS KEILITDRAK
AKLGVVVKDE RDIAGDQLIG NYQIKLDDML DLMEKGQDWY NLAGAKTGRV KMQAQWKPVA
LSGVIAGTGG YQTPIGVMRV HFIKATALRN FETVGKSDPY ARVLLSGIEK ARTVTFKNNL
NPEWDEVLYV PVHSTRERLQ LEVMDAETMG RDRSLGLLDI FAGDFIAQDE DGAYLVNDKK
TQREEGLKLH GKGMAKGVLS YTISFFPCLN VADPEEEERE KEKEAAKAQN GKEASVSGST
QASQTVPAAA PGSPTTSKPG SDVLSTKADE PKGPPKVHLT PEELLKYESG LIIFKLMEAE
LPRPDTQLEI FVDDMAFPSY VSSSARSRSF TFDEMGDCFI RELDFSRLTI KIRDRGGEKK
EDEKDRPFAR LTGNTLDTLK QCLNNPTTLK LKDEEGRVSS VRISLKYIPV QMELDPRESI
NNMGNLRVDV LDAENLPAAD SNGKSDPYCK FELNGDEVFK TKVQKKTLNP TWNEFFEIPV
PSRIGAAFNL KVYDYDFADK PDFLGGSPIQ LDQLEPFKAS EMRLPLDGKS GTARIRLLFR
PDYVTRQRQG TSTFTAPTRI VTGVAGAPIK GGAAVVGVVG HGVGKGASFL RRGFRGGKKD
EEVVAAQIAA ADTAAPGTAI TTNGDSAVPN TMVKRASGLT DPAVVSQHDE PALDVPPGPA
LAASRSLGHN RTASGAASIY SVAPGSPGAG TAVFTIVSAS GYPPSSDVYV ILNQIGSKSK
TIGKTKHHKP QSGVAKFDES FKTTCTADAQ FQVQVREQHR FGSDDVLGES LYVVDESGSN
AEKEISVGDG SVVVKSTFTP HESNGTTDSP KSFRRSFLSK REARPPSSRE GTPA
//