ID A0A226E9Z5_FOLCA Unreviewed; 1017 AA.
AC A0A226E9Z5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY {ECO:0000256|ARBA:ARBA00019143};
GN ORFNames=Fcan01_11259 {ECO:0000313|EMBL:OXA53887.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA53887.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA53887.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA53887.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA53887.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000256|ARBA:ARBA00008361}.
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:OXA53887.1}.
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DR EMBL; LNIX01000005; OXA53887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226E9Z5; -.
DR STRING; 158441.A0A226E9Z5; -.
DR Proteomes; UP000198287; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR45036:SF1; METHYLTRANSF_11 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45036; METHYLTRANSFERASE LIKE 7B; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF08238; Sel1; 5.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00671; SEL1; 6.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF81901; HCP-like; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Gibberellin signaling pathway {ECO:0000256|ARBA:ARBA00022941};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:OXA53887.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198287};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OXA53887.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT REPEAT 233..266
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 752..782
FT /note="MYND-type"
FT /evidence="ECO:0000259|Pfam:PF01753"
FT DOMAIN 811..909
FT /note="Methyltransferase type 11"
FT /evidence="ECO:0000259|Pfam:PF08241"
SQ SEQUENCE 1017 AA; 116527 MW; 0DFE45764D953859 CRC64;
MHRLINDKAS EKFRMRFLDL WNASGNPEWE NIPHFGRTFI EDIGSSLYYK SKKIQKQLLE
SGQINTWDLP LLFASIQSIN TYTNTKSSRT DFDELLRIRN KLSHLGSTEL GDDEFAKLWS
AATNILLKYG LSQGEIDDVL TMKLGTTTEF EDKLNQNLDK IKMLREEGNA LFKNGEFKRS
IERYSEAMLV ENISTTELGI LYSNRSAAHL GVKNYSDAKI DARCSVNLRP NWGRGYYRLG
CTYDKLEQYD KALYYYNLSL KYDPSNSRCL DCQQGAIHMI AKRNRQEHLD PLTMPVTDAD
MLAFRERVTG PEMIAVGELL SDKIKKERYL AGDPHYTCTE AHNYLCGLKG YTQNYERAAQ
LFAKAAKEGS AEGMYNLAKL TSEGKGVQRN MVESFQLFLR AADRPRLMEI LPGTGVKTRR
IGVMEAQHAL GLHFETDGIL GRDYHQAYNW YTKALLNGSG PSANNLGLMF SEGKGFTPDL
EKAVGYWQIS ALYGITRAME SLAFHNFYNG RPTRAFKWYT LAVKNKTMNS NLHMIFEKEP
PLEQFVAEEF EQTIEEELMA GPMRKYVDLK DYHENIDGME RRRERRRKML ELVQPNAAGG
KVQTIVNHRI ALNQIKKEKS SESDWTTKQA KLFPTRTPNL LGLKPITLKE LDKSIHDKTY
DGFAIRLTVI EDAILGLPSV QILAEDENGD IEKVYIYNYQ QGPTTQDELG YACAFTVINP
YFRLMADRKW GIRVDDPNLL IKHPLMKGQD RCRYCAKIGS TLKCRKCRRV FYCSKSCLEK
DETELKHGPI RTIGQPFIIC GSAHFIKCFI LEIGVGPGGN FDFYPETVKC HLIGNDPNEY
FYPTLQENVR KFPQIILDRI SSSSAENLID IPNKSVDAVI STMVLCSVPN VDKTLQEVLR
VLKPGGKFFY MEHVIDPEAT WWRSLQQILD FLGIWPFLID DCHSARDTSS KIENAGFGSV
DQKRFYLDPF PVLRLYDSAS LIQYEPRYIH RKFKVALHIQ KCNNNLNEND GLEVSPM
//
