ID R1ENI7_BOTPV Unreviewed; 922 AA.
AC R1ENI7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative betaine lipid synthase protein {ECO:0000313|EMBL:EOD49122.1};
GN ORFNames=UCRNP2_4121 {ECO:0000313|EMBL:EOD49122.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD49122.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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DR EMBL; KB916107; EOD49122.1; -; Genomic_DNA.
DR RefSeq; XP_007583408.1; XM_007583346.1.
DR AlphaFoldDB; R1ENI7; -.
DR STRING; 1287680.R1ENI7; -.
DR KEGG; npa:UCRNP2_4121; -.
DR eggNOG; ENOG502QQCH; Eukaryota.
DR HOGENOM; CLU_020809_0_0_1; -.
DR OMA; GVCDFYV; -.
DR OrthoDB; 5487564at2759; -.
DR Proteomes; UP000013521; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR021829; DUF3419.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR47473; BTA1P; 1.
DR PANTHER; PTHR47473:SF1; METHYLTRANSFERASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF11899; DUF3419; 2.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 135..200
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
FT REGION 647..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 922 AA; 102860 MW; D26BB0E87F3470C5 CRC64;
MTLDALGVLP GIRLSLNPHI QVALFLVGYV AFLALVLHIG FRWDKPGRKK PESPPNALEA
YVRFIWGCFI KPHSGGNGGN QQDALEGFYR QQASAYDVTR AKLLHGRDDM LGMVAAQLQH
KVNAGLYPRK PVWIDVGGGT GWNIEQMAKF VSVPDFFRSV YLVDLSPSLC EIARARFARL
GWANVKVICQ DARAFRLADH EQPVSDELTL IPIRPDEYVT EGKSTAQEAE LVTMSYALSM
IPEFYPVIDS LSSLLCPTGI IGVVDFYVQS QVDFQSRNYV GGVIDRHCMW LSRVFWRTWF
EIDRVNLEPA RRDYLEYKFG TILNVNARNH FLGVRIPYYV WVGCSKESGS SQSKLAEIDA
VATESPFLSA LDLQARKSGR RDSGVELHSK AYESAVVNLA ASLPLPSSWY QNHHWRIYYD
DQLQKHRQFK DEYIYAFTWE DSRVDARLLQ VKSSDVILAI TSAGDNILSF ALEKPKRIHA
VDLNPAQNHL LELKVAAFTA LGYADVWKLF GEGKHESFRS LLITKLSPHL SSLAFQFWLH
HGDETFSPSG KGLYSTGGSG YALNWVGRLL RFVGLEKEVE KLCAAETLNE QREIWQRSIR
KVLLSRLLAW AVVGNERWLW KALGVPPNQR NMIEEDYAKL NGEEPARAQQ AFQHQQGNST
AATTTSSTSS TSATASSIAT GLRSGHAIWE YAVNTLDPVV NSTLLSTDNH YYLLCLQGRY
SRRCHPEYLT PKAHIKLSKS SPSSPTSPFT SPLTSPFTSP TSSPRPDHLP SLAPSPFPPS
ASASGTGSAF DGLRIHTDEI NEVLARMAPA TLTIAVVMDS MDWFEPRADA SGAATAQIRA
LNRALRLRGR VLLRTAALKP WYVAVFERNG FAARRVAARW PGECIDRVNM YASTWICTKV
ASVEEKAGCV DGLGRPMDRL DI
//
