ID A0A1L9U4F8_ASPBC Unreviewed; 1539 AA.
AC A0A1L9U4F8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Tricalbin {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASPBRDRAFT_34995 {ECO:0000313|EMBL:OJJ66558.1};
OS Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ66558.1, ECO:0000313|Proteomes:UP000184499};
RN [1] {ECO:0000313|Proteomes:UP000184499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC {ECO:0000313|Proteomes:UP000184499};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878698; OJJ66558.1; -; Genomic_DNA.
DR STRING; 767769.A0A1L9U4F8; -.
DR VEuPathDB; FungiDB:ASPBRDRAFT_34995; -.
DR OMA; VLMDDYM; -.
DR OrthoDB; 2787577at2759; -.
DR Proteomes; UP000184499; 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 SMART; SM00239; C2; 4.
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:UP000184499};
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 194..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 244..449
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 445..563
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 592..708
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 728..842
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1118..1238
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1496..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1496..1516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1539 AA; 169619 MW; 10A7426A978F55E1 CRC64;
MASQDVEGSK AELKQQGAIE VAQQASQDPQ SNLQPDVIEE ALVKETRKAG VPAYQFDPDA
SPEDKGAAAL ARLPPGFHHD HKPKGVAVVT DKDDGTPDQY DLPPPRSATD LLQEKADEAS
AAPNGEAQVE EDMRWARDRT GWAPQFEHQP TQEEKEEGTL LDHQTFLEGR LDDKFFGDWY
HNAGVIVFAC LSSWVIAVLG GGLAWIFIVM AACSTYYRTS IRRVRRNFRD DVNREMAKQR
LETDTESLEW INSFLVKFWP IYAPVLCDTI INSVDQVLST STPAMIDNLR LKTFVLGSKP
PRLEHVKTYP KTEVDTVIMD WKFSFTPNDT MDLTARQLKN KINPKVVLEV RLGKGLVSKG
LDVIVEDMAC TGLMRVKVKL QIPFPHIERV DVCFLEPPEI DYVCKPLGGD TLGFDINFIP
GLETFIKDQI HNNLRPMMYA PNVFPVEIAK MLAGNAMDQA IGVVAVTLHG ARQLKNPDAF
AGTPDPYAVV SLNNRVELGR TKTIHDTDSP RWNETIYVII TSFAESLTIT PYDWNEFRKD
KELGAATFPL ERLEQQAEHE GLFLEVMASG RSRGAIHADI RFFPVLEGTP LENGQTQPPP
EMNTGIARFV VEQAKDLDAS KSMVGQLNPY GVLLLNGKEI HITKKLKRTN NPIFQNASKE
FLVTDRKSAR LGLVIKDDRD LGRDPVIGTY QIKMNDMLKM MEKGQQWFHL NGAKSGRAKL
ILDWKPVALA GIAGGSGYVD PIGVMRFHFK SASDLRNLEA FGMSDPYARV LLSGYQKART
VTFRNNLNPE WDEVVYVPVH SPHEKITLEV MDEESINDDR PLGSVDLRVS DYVRENEEGG
YDIDDERQLI SSPLRSGRSQ KGTLNYTVAF YPSIPVVNPE DEEKEDENLN GDAEGAELSR
KSTESKRVGG HSKTASVDSK ATTALNGTST NGVTPEAQSS RVSLDTNGTR PQTAKDSETM
SVKSIKEVPK TYISAEDLTK YGALCFGVLS IRFLHTDLII ESGFIVFNVH EVQLSRPNVQ
VEVLMDDYMF PAYSSPKVRT KTAKIDDVGD AFVRELEFSK ITLRIIDKNN TKDESDDHTV
AKLTGDTLTT LQRILYTPTE LTLRSAQGEV SKVTVSARYI PVTMKLDPTE SINNMGTLVV
HFLDAADLPS ADRNGFSDPY CKFRLNDKEV FKTKVQKKTL HPAWNEMVET DIKSRINSTC
RIDVYDWDFG DKADYLGGTH FDITSLTPFE SKEISLPLDG KSGAIRLKLL FKPSYVVRSR
QGSSTFAGTF ATPGKIVGAP VKGVGFVGGN VIKGASFLKH EGSSFLKNGI MGRFRGDDGA
SLQEAEEETP APLAPAAILV EGETPPASAT SNNLQHSRSR SVASHYGDRL GVAGKGETGT
ATISVVSASG YPPNANVRVF IKAVGPKGAK EVLKSKAIKS GGGPVYYDPS HETCRVHNTT
ADAQYQVRVV DHSTFGSDGQ LGEALFFVDD QGSMAGQDKQ VKIGTGTVTL RSSFAMSESN
LRPGTAHSNN DGASEVMDSP DSKKTGRRSF LSKRSVSGA
//
