ID A0A364N669_9PLEO Unreviewed; 1825 AA.
AC A0A364N669;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Meiotically up-regulated 190 protein {ECO:0000313|EMBL:RAR12760.1};
GN ORFNames=DDE83_003908 {ECO:0000313|EMBL:RAR12760.1};
OS Stemphylium lycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Stemphylium.
OX NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR12760.1, ECO:0000313|Proteomes:UP000249619};
RN [1] {ECO:0000313|Proteomes:UP000249619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL Submitted (MAY-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:RAR12760.1}.
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DR EMBL; QGDH01000046; RAR12760.1; -; Genomic_DNA.
DR STRING; 183478.A0A364N669; -.
DR OrthoDB; 1465207at2759; -.
DR Proteomes; UP000249619; 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; cd04041; C2A_fungal; 1.
DR CDD; cd04052; C2B_Tricalbin-like; 1.
DR CDD; cd21676; SMP_Mug190; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037767; C2A_Mug190-like.
DR InterPro; IPR037765; C2B_Tricalbin.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR47348:SF2; MEIOTICALLY UP-REGULATED 190 PROTEIN; 1.
DR PANTHER; PTHR47348; MEIOTICALLY UP-REGULATED GENE 190 PROTEIN; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00239; C2; 2.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS51847; SMP; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 6.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000249619};
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};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT TRANSMEM 820..844
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 137..179
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 180..221
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 223..261
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 271..311
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 394..435
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 436..477
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 478..503
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 908..1146
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 1144..1272
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1358..1494
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1322..1353
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 613..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1719..1734
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1766..1780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1825 AA; 203699 MW; C3C4CA337248C58C CRC64;
MATQYPPPSK RQKRAQAEVA RQQQDIDTTI PDGTVRVRFV DQATGESGSL PVLTVPLSQA
STKNLELLLN NLKDQADDQI PYRFFPDGAT EALADKDDLY NALVKPGKAS AESEIVLQYA
PQAVFRVKAV SRCSAAVSGH GDNILSINFS PTSSSRMASG SGDKTVRVWD CDTGTPVHTM
KGHSRWVLAV SYSPDGSLLA SGGYDNEVRI WDPNTGKQIG GPLKGHTSFI TSLSWEPYHL
QEPGRPRVAS SSKDGTVRVW DAVGGKIDYA LSGHKGSVTC VKWGGTGRIY TASHDKTIKV
WDAAQGTLVN TLSGHAHWVN HLALSTDFVL RTSYHDHTRK VPSTQDEKLA KAKARFEKAA
TINGEIIERL ATASEDCTIM LWTPMTSTKP VTRMTGHQKQ INQVTFSPDG ALLASAAWDN
HVKLWSARDG KFLNTLRAHV GPVYMTCFSA DSRLLASCSK DTTLKVWDMR TGKLKEDLPG
HKDQVFALDW SPDGERVGSG GADKQATSSP CSFQQRLFGA AAADNAALVH SVDLNGRRMT
NVLEIWACTY VNHGRDGGHS SLHLRYLDPD TRHHTRRFEL SPTRRTMSGV EDVDAQRRNY
RRPHNAHNPI PTVQKYREEK QRRQDAYGYA DGESNDPTTR DRLGDAVNVF RHGRDAEQAN
DGNGPYASTN KNLPQDEPIA DDHAGKTVSK DGEQDTSQSQ GVDEGQEDTT EGHLQSADPR
QARKQMKKFS PDGTERIVTD PITHLPLSVH DFTNRELEST AKNTSPPGSD PRTKTGAGAI
NKSDEQLQDE QEESQEAYAS VDVLFPPPSF DRTRSEISTV YMQAVTVGVG ATAVGLMLVN
ALFWPTRHST GWMRQLLKVV ELGTMATVSG AIVLFMRQWS ENKIKNVWDV EVWQAERERG
QELAKTQTAE STQWLNSLFA SVWPLINPDL FTSISDTLED VMQASLPNMV RMVAVEDLGQ
GSEALRILGV RWLPTGAAAR SVNSDGNLKS SNEEKGDRTV QDDSEDQNQQ PHQDTMEAED
GDFVNVEVAF AYRPSTGKGI KSRAKHAHLL LAFYLPGNIK LPVWVDLAGM VGVMRVRLQL
CPDPPFFSLC TMSFMGQPKV TLSCVPLIKK GPNLMDVPLI SKFVQSSMDA ALAEYVAPKS
LTLDLKDMMM GDDFKKDTIT QGVVMVHIKH AFDFKEGDTK IGPFGGSADP YVSVGWAKFG
KPLWSTRVLQ GNMQPHWDEW CFVCVTYDEL NVDERLRIQL WDSDRTTADD DLGRIELDLK
ELMKSDDTNG KMHDREDDFK ALKAGEGMPG KLSWRVGYFS KTRITDDQLA MQDEDPDVKS
IEQLKEKTFA EAENKLREAS EDHRKEVEQQ KMEDFKNRQD QLIIASPPSE EYPSGILSIQ
IHQITGLELE TPSKKEASAN AEATDEEEEG DDLPSSYCTI ILNHKKVFKT RTKPKNAKPF
FNAGCERFIR DVRNTEIHIA VRDARLHEDD ALLGIVYLPL ERVFQKRCQI NSIFPLAGGV
GYGRVRVSMV FRSVQVQLPK ELLGWDYGTV DVKPSVKAID VPQDLEPLRL KVHTPLERAK
LHSRGRNGHV RSEDGHTVWT TRKNRPIRLP VRARYCAPLV FEFRQDAALR DHTHAFCILW
LKDVPDNEEQ TKRLPIWKGD LKRAQDNVLD SYGEKVGEIE VTLTMWSGLS GYHEKLAKGD
KHLTNIMEVL DTCNDTEWSD WDDAGSSDKP GINDSKDTED ETSDSEDSED DEDESTSSKF
VPNFLQKDKK TDSKLSDDGS RGPISQLKEY NASSKQLHRR NRGVMQWKGP RTLAWMKHVG
DRGKRKMGHL FHHHERNGTG VETEA
//
