ID   A0A078AV05_STYLE        Unreviewed;       545 AA.
AC   A0A078AV05;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Peptide-n-(N-acetyl-beta-glucosaminyl)asparagine {ECO:0000313|EMBL:CDW85087.1};
GN   Name=Contig396.g436 {ECO:0000313|EMBL:CDW85087.1};
GN   ORFNames=STYLEM_14157 {ECO:0000313|EMBL:CDW85087.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW85087.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW85087.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW85087.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC       family. {ECO:0000256|ARBA:ARBA00009390}.
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DR   EMBL; CCKQ01013424; CDW85087.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078AV05; -.
DR   EnsemblProtists; CDW85087; CDW85087; STYLEM_14157.
DR   InParanoid; A0A078AV05; -.
DR   OrthoDB; 5051at2759; -.
DR   Proteomes; UP000039865; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 3.10.620.30; -; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR002931; Transglutaminase-like.
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.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          233..288
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   REGION          385..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..446
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..464
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   545 AA;  63544 MW;  DF4ACAF578DB5D01 CRC64;
     MASQSNEEWE IICSDALLKG QKICQIPYYY QGSFLCQACS QLCKSDISGI KKTEHYFFPF
     QCQCQFIDGE CLFKERIQDP VLTQEDIDLR QALVTGMDQA IDKLTTVDVK PNMLQQQRFS
     HSLEDSIEKV YLYEDELLQS ICLSLIPQEV QETQEQVAQL KGLLKWFKSD FFTWCDQPKC
     TKCGSNKNVV GTGNGQPTAE ERSDGHAGNV ELYTCNKCNI PLRFPRYNHP LKLLETRTGR
     CGEWANAFTA VCRALGHEAR FVLDWTDHVW TECYIKSTQR WTHLDSCENA FDTPLIYEGG
     WGKKLSYVIA FSKDEVVDVT KRYVLNKMMN RMRRTLVPES WLQQTIETMR DRMWAMQDNA
     RKMELRLRFS QEQFQLLSGI KEVKEDENVP RQSGSMEWRQ SRGEMGSSDS PAQIQQQQQH
     EQPQQKQQQQ IQPQTQIQPQ QKQTIQSVMK EKHDQQQQKQ VEEQKYQSMV HEMTEQEKYD
     LQQKLKLDVK QLFQQMTLGC PNKNCNNKEF CGNANQSLKA QEATSRLQLV MQKIKSGQYK
     FCNSS
//