ID A0A2S7Q328_9HELO Unreviewed; 1512 AA.
AC A0A2S7Q328;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=C2 domain-containing protein {ECO:0000313|EMBL:PQE20944.1};
GN ORFNames=CJF30_00002293 {ECO:0000313|EMBL:PQE20944.1};
OS Rutstroemia sp. NJR-2017a BBW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070414 {ECO:0000313|EMBL:PQE20944.1, ECO:0000313|Proteomes:UP000238072};
RN [1] {ECO:0000313|EMBL:PQE20944.1, ECO:0000313|Proteomes:UP000238072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a BBW {ECO:0000313|EMBL:PQE20944.1,
RC ECO:0000313|Proteomes:UP000238072};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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:PQE20944.1}.
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DR EMBL; NJPT01000031; PQE20944.1; -; Genomic_DNA.
DR STRING; 2070414.A0A2S7Q328; -.
DR Proteomes; UP000238072; 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; 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:UP000238072};
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 173..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 238..443
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 438..557
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 582..702
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 718..837
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1078..1196
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1264..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1470..1512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1322
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1512 AA; 166372 MW; DA28AAE720C2EA97 CRC64;
MSTTNGLEGE LKQQGAVEAA RDPNSSVSAE DAERKIVQES KKAGVEAFTF NPDASPEEKA
AQARARVPEG FHHEHKSKGV AIATDIDDGS PGAYDLPPPT TAGAIPAPAK EKNGAGPGTN
GVLDDDDEDA RWIERAGWAP RFGSGDSGEE AESLLDHQTW VEGKLEDKFY GDWYHNTAVI
VFACLSSWLV ATLGGGLGWV FIIMAICGTY YRTSIRRVRR NFRDDVNREL AKNKLETDTE
SLEWMNSFMV KFWPIFQPVL AETVINSVDQ VLSTSTPAFL DSLRMKTFTL GTKPPRFEHV
KTYPKAEDDI VLMDWKFSFT PNDHADMTSR QIKNKVNPKV VLEIRIGKAM ISKGLDVIVE
DMAFSGMMRV KIKLQIPFPH VDRIEVSFLE RPTIDYVCKP LGGETLGFDI NFIPGLESFI
LEQIHANVGP IMYAPNVFPI EVAKMLSGSP VDQAIGVLAV TLHGAQGLKN PDKFAGTPDP
YTVLSLNNGA PLAQTKIIKE NANPRWNETK YVIVTSFNES LTMQIFDYNE YRKDKELGTA
TFPLERVQEV TEYENEQLEV MANGKARGIL SSDLRFFPVL EGRTLADGTV EPPPESNTGI
ARFCVEQAKD LDGTKSLIGA LNPYAVLLLN NKELHVTRKL KRTNNPIWDN GSKEILITDR
KTATFGLVIK DDRDLGTDPI LGTYQIKLND MLTLMEKGQE WYNLAGANTG RVKLTLQWKP
IALQGIGAGS GGYVTPIGVM RFHFKNARDL RNLETLGKSD PYVRVLLSGI EKGRTVTFQN
NLNPDWDEVI YVPVHSTREK LTLEVMDQET INSDRSLGSV EVLASDYITQ HENGEYLVHD
LKEPQASGLR MHGKGSPRGV LNYNVSFYPC LNIADPEEEK EEEKEEEKEA EQEEAARKSP
IERGRISGVP NGDISEKPAR TSSESAMAAK LAEGEREQEE TPKEKELPKI RLGPEELLKY
ESGLIIFKII DCELTKSNVH VEVVVDDMAF PSYVSSTMRS KKMTLDEIGD CFVRELDFSK
ITIRIREKVS KGEEKKDSTI AKLSGETLAT LKQCLNNPTI LKLRDDEGRT NSIKVSLKYI
PVKMDLDPSE SINNMGKLRV DVLDASDLPS ADRNGYSDPY CKFELNGNSV FKTKVQKKTL
HPAWNEFFEV EIPSRTAANF ICNVLDWDFG DKADHLGKTE INLNLLEPFK PKEMNLALDG
KSGTIRLRLL FRPDYVTRSR QGSSTFSGTF ATPGKIVTGV AGAPIKGVGF AAHGVGKGAS
FIKNSFRGGK KKDADEVNGT PAESEEDVPT TNGFSGPRRA SGHTGVPPPI PEIRPPVTPP
NESAPHHSRT KSFGATSAHS NYLGSPGGSG APIGVANFTI VSAVGFPPSS SVMVYIKSLG
PKPKVIHKTE HIKSPSGTVV FNEKKESFKC TAAADATFQV SVKAHNTFGS DDDLGEGALV
IDETGTMQEK QIRCGAGYII VKSNFVMNST ENGQESPKSG FRRSLLSKKE IGGRTSRDIT
PVGTQGSSSE GR
//
