ID A0A482WQ63_LAOST Unreviewed; 1209 AA.
AC A0A482WQ63;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RZF35160.1};
GN ORFNames=LSTR_LSTR007862 {ECO:0000313|EMBL:RZF35160.1};
OS Laodelphax striatellus (Small brown planthopper) (Delphax striatella).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Fulgoroidea;
OC Delphacidae; Criomorphinae; Laodelphax.
OX NCBI_TaxID=195883 {ECO:0000313|EMBL:RZF35160.1, ECO:0000313|Proteomes:UP000291343};
RN [1] {ECO:0000313|EMBL:RZF35160.1, ECO:0000313|Proteomes:UP000291343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lst14 {ECO:0000313|EMBL:RZF35160.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:RZF35160.1};
RX PubMed=29136191; DOI=.1093/gigascience/gix109;
RA Zhu J., Jiang F., Wang X., Yang P., Bao Y., Zhao W., Wang W., Lu H.,
RA Wang Q., Cui N., Li J., Chen X., Luo L., Yu J., Kang L., Cui F.;
RT "Genome sequence of the small brown planthopper, Laodelphax striatellus.";
RL Gigascience 6:1-12(2017).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000256|ARBA:ARBA00005680}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC {ECO:0000256|ARBA:ARBA00008339}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000256|ARBA:ARBA00007589}.
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:RZF35160.1}.
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DR EMBL; QKKF02029497; RZF35160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482WQ63; -.
DR STRING; 195883.A0A482WQ63; -.
DR InParanoid; A0A482WQ63; -.
DR Proteomes; UP000291343; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00887; MoeA; 1.
DR CDD; cd00886; MogA_MoaB; 1.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 2.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR NCBIfam; TIGR00177; molyb_syn; 1.
DR PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR PANTHER; PTHR11675:SF101; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 3; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00994; MoCF_biosynth; 2.
DR Pfam; PF03453; MoeA_N; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00852; MoCF_biosynth; 2.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 2.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Reference proteome {ECO:0000313|Proteomes:UP000291343};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 7..156
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 432..577
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 1066..1204
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 1209 AA; 135198 MW; 8434D4B1107F1790 CRC64;
MNTITVGILT VSDSCFQGTA VDLSGPNLAS LIRTMESCTL KIESCYNKCV PDDRHKIEDM
IEFWVDELDV DLIITTGGTG FGPRDVTPEA TRTVIEREAH GLTQLMLSES LKITPYASLY
RGICGIRKET LIINTPGSKK ASGEFLQAAI KCIPHALAVI KNINYTVKKD HELIQNEGQH
GSCSHSHSKV DISRVARRHR NHDDLYPMID YEVALKLVLE NSSCKSTESI DLFDKQSRAS
VIGRVLAEDV RSAEPFPGFR ASIKDGYAVK AGLGCGLYRV LEIAKLDQRC SYDGFGDRCS
LWHFSHLETS NRKSNSSLGN SATQHVFSNE CALRLGDSRI GNPIASTIRH AGCRVICASN
CGDTRVVEEL TTAVGRSSSR MLCRAPVGQD ISDIDKGQII AGKGDVISGI EMGLFATLNI
RRVSVFKHPT IGIMSTGDEL VEPWTEASVK PGCIRDSNKV TLMYLLKSKG FDAVDCGTAL
DSPNDVLEKM TNALSKVDVL ITTGSVSMGE KDLLKKILET DFKAKIHFGR VNMKPGKPVT
FATFTFEGVP KTVFALPGNP SSASVTSHVL VLPALNKLAG RQAFKPKKIQ VQMNEMMFRR
SFRRWWPGIT FFGICIFLFW KSYKHSNLQE GNEDGWIPVR LSQNQEEYVD RRGVHVVVGH
YTGDTSSDRH PPNLTEELLN TNMFDPKPLE GKDGTPVLLP PHLNAKVQQL YHINRFNLMA
SDRIPLNRTL PDVRKKRCRL KTIDITGLPK ASVIIVFHNE AWSTLLRTVH SVINRSPSSL
LQEVILVDDA STRKFLGKEL DDYVAKLAVP TRVLRTGKRE GLIRARLKGA KAAQGQILTF
LDAHCECTIG WLENLIERVA ENRKRVVCPV IDIISDDTFA YIRSFELHWG AFNWQLHFRW
YTLDASELAK RRKDITQPFS TPAMAGGLFA MDKNFFFELG AYDDRMEVWG GENLEMSFRV
WQCGGSVEIA PCSHVGHLFR KSSPYTFPGG VSEILFANLA RVALVWMDKW KEFYFKFTPE
AEKVRHRQAI RDRLQLRTQL QCHSFQWYLD NVWPQHFFPT DKRFFGRIKH RIRGECLEKP
TGKGSLNQPM GPARLAHCVT SPGPVLRQMF VMDVSAFDSD VGAPLMTDES VCLDAPPREG
QTAVLKVKVI ACTGHARQAW TYNQQSGALR HVSSGLCLDL PQNGEEALAL AACNTYPSQQ
WTLEPVPWK
//
