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Database: UniProt
Entry: A0A0K9NTD1_ZOSMR
LinkDB: A0A0K9NTD1_ZOSMR
Original site: A0A0K9NTD1_ZOSMR 
ID   A0A0K9NTD1_ZOSMR        Unreviewed;       398 AA.
AC   A0A0K9NTD1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase {ECO:0000313|EMBL:KMZ60034.1};
GN   ORFNames=ZOSMA_61G00050 {ECO:0000313|EMBL:KMZ60034.1};
OS   Zostera marina (Eelgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX   NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ60034.1, ECO:0000313|Proteomes:UP000036987};
RN   [1] {ECO:0000313|Proteomes:UP000036987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX   PubMed=26814964; DOI=10.1038/nature16548;
RA   Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA   Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA   Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA   Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA   Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA   Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA   Van de Peer Y.;
RT   "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT   the sea.";
RL   Nature 530:331-335(2016).
CC   -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC       family. {ECO:0000256|ARBA:ARBA00009390}.
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:KMZ60034.1}.
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DR   EMBL; LFYR01001661; KMZ60034.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K9NTD1; -.
DR   STRING; 29655.A0A0K9NTD1; -.
DR   OrthoDB; 5051at2759; -.
DR   Proteomes; UP000036987; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.620.30; -; 2.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR12143; PEPTIDE N-GLYCANASE PNGASE -RELATED; 1.
DR   PANTHER; PTHR12143:SF19; PEPTIDE-N(4)-(N-ACETYL-BETA-GLUCOSAMINYL)ASPARAGINE AMIDASE; 1.
DR   Pfam; PF01841; Transglut_core; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          250..305
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
SQ   SEQUENCE   398 AA;  45790 MW;  D9F4A318BB3BC6E3 CRC64;
     MVARQFLLCH HGEEFPIEYD SDDGIEVLKF QIFSLTSVVP DDQKILEEGC EVEVTEESDL
     KTISEKLRLV SFHDDIKGKE TADSKTSERS DEELARMIQA EEDAIAMQMF QDSGASGRRM
     FEQRLRPCIS QVLMYEDSKR KEAARKSVPI DRIEEKALVS LGKEGNLDPS KEEKDHAFLL
     QLLYWFKQSF SWVNSPPCEN CGSETTFIGM GSPLPSETYF SCSSVELFRC QKHCSKNSTR
     FPRYNDPLKL LETRRGRCGE WANCFTLYCR AFNYESRFIL DFTDHVWTEC FSHLHGRWMH
     LDPCEGVYDN PLLYEKGLLP LYFPRDKHEE EVALSKLPAD VGDENGETII DERKIRIKSL
     PIVPMTPTKP STVDVEFPVN RTRLLSQKQN SITGGGFQ
//
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