ID A0A0F4YWR6_TALEM Unreviewed; 1527 AA.
AC A0A0F4YWR6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Membrane bound C2 domain protein (Vp115) {ECO:0000313|EMBL:KKA22281.1};
GN ORFNames=T310_3716 {ECO:0000313|EMBL:KKA22281.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA22281.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA22281.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA22281.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-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:KKA22281.1}.
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DR EMBL; LASV01000146; KKA22281.1; -; Genomic_DNA.
DR RefSeq; XP_013328893.1; XM_013473439.1.
DR STRING; 1408163.A0A0F4YWR6; -.
DR GeneID; 25316065; -.
DR OrthoDB; 2787577at2759; -.
DR Proteomes; UP000053958; 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; cd00030; C2; 1.
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; 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:UP000053958};
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 179..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 239..444
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 439..558
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 583..703
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 709..837
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1093..1211
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..920
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1527 AA; 168439 MW; EFBEC221821AA1B4 CRC64;
MAPSPEEAPK AEAKQPGAIE TAQAAAQDPQ SHIQAETAEK ELVEQSRKAG VPAFQFDPDA
SPKEKAEAVK SALPPNFSNP KKPTGVAVVS DLDVKGPDKY DLPSPAKPAD IIIHPPAEDG
ANDQLTDDTR WARDRTGWAP QFEQHKEDQE QEETLLDHRT TLEGKLDDKF FGDWYHNAAV
IVFACLSSWL IAVLGGGLGW VLIVMATCGT YYRTSIRRVR RNYRDDIHRE LAKQRLETDT
ESLEWINSFL VKFWPIYAPV LCDTIINSVD QVLSTSTPTF LDSLRLKTFV LGSKPPRLEH
VKTYPKTEPD TVLMDWKFSF TPNDTMDLTA RQLKDKINPK VVLEVRVGKG VVSKGLDVIV
EDFACSGLMR VKVKLQIPFP HIERVDVSFL GRPEIDYVCK PIGGEHLGFD INFIPGLESF
IKEQIHGNLG PMMYEPNVFP IEIAKMLAGN PVDRAIGVVA VTLHGAVNLK NSERLGNTND
PYATVSINSR NELGRTKIIH DTNNPRWNET LYIIITSFTD SLTIHIYDYN DFRKDKELGV
ATFPLDQLEE EHEHENLNLD VLYSGRNRGV LQADVRFFPI LEGRKLENGE VEPPPELNTG
IARFTVEQAK DLDGTKSLVG ALNPYAVLLL NGKEVHITNK LKRTNNPIFQ NPSKELLITD
RKNARLGLVI KDDRDLATDP VIGKYQIKVN DMLKMMEKGQ EWFQLSGAKT GRVKMTLDWK
PVALRGVAGS AGYINPIGVV RLHFKSANDL RNLETMGKSD PYVRVLLSGI PKGRTVTFRN
NLNPEWDEVV YVPVHSPREK LTLEVMDEET MGKDRTLGEA ELPLADYIHE GENGEYEVDD
EKQPITSGLR LHGRGQVKGY LHYTVAFYPT LNVVDPEEEA EEAEEDGSDG RPSTALSRRS
DSKRKSMDST RRKSEDAPRP STDLSKANGR PSLEANSPKP LLNGDAASNA ETTSIASSAK
ETPKIYIGPE DLKNYESGLL VFKLLEGQLS HPNLQLEVVL DDHLFPSYTS QKVKSKDATF
ADIGDAFVRE LDVSQITLRL VQRSKEKDED ESHTVAKMTG PTLQTLQRCL YTPTELVLRS
NDGAVNKIKV SLRFIPVKMK LDPRESINNS GTLRVDVLDA ADLPSADRNG YSDPYCKFKL
AGKEVYKTKV QKKTLHPAWN EFFETPVKSR IGADFRVDVY DWDFGDKADY LGGAPIDLEQ
LEPFQLKEVS FPLDGKSGVI RLKLLFKPSY VTRSRQGSST FSGTFATPGK IVGAPVKGVG
MVGGGVVRGA TFLGRGIVSR FRSHEEEEPA ATTTPPSEAK EQSPPRTPNP KPEGLQRSPA
LLVDGATPPT AAAAAAASTP ESLQRHHSRT RSVVSQFGGD KGGDLGIATF TIISATGFPA
SAHVRVIVKV IGSKGAKDVH KTKAIKSSSG TVQFDASHET FRVPNVAADA QFQLRVVDHS
TFGSDDVFGE TLFFVDDQGS VAGREKTIKV GDGQVTLKSS FIPSDAGSIR PGTAYSANGD
AAEGGETPER KPRRSFLSKR SASTNQG
//
