ID A0A099P0Z1_PICKU Unreviewed; 370 AA.
AC A0A099P0Z1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Peptide:N-glycanase 1 {ECO:0000256|ARBA:ARBA00032858};
GN ORFNames=JL09_g2934 {ECO:0000313|EMBL:KGK37929.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK37929.1, ECO:0000313|Proteomes:UP000029867};
RN [1] {ECO:0000313|Proteomes:UP000029867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL Microb. Cell Fact. 13:121-121(2014).
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:KGK37929.1}.
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DR EMBL; JQFK01000027; KGK37929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099P0Z1; -.
DR VEuPathDB; FungiDB:C5L36_0D05370; -.
DR eggNOG; KOG0909; Eukaryota.
DR HOGENOM; CLU_031058_0_1_1; -.
DR Proteomes; UP000029867; 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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 186..241
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 337..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 43220 MW; A9A250D574E0D16B CRC64;
MCGSSAYTGN ETGIYIDQAF VCRIKDTLYN GRVDMLHKVI QHLSRNKHLL NEAIKYPFLN
QVIHLSKNFR PLTDDEQNAA IDTVLSSEVY DRVKDEEMKQ DPNYEYVEVL VKQLLRWFKE
EFFTWVNKLD CPNCGNKEQE QIRHLPGLRP YKYEHFQGKA TIIERYQCLK CLSTYEFPRY
NDIRTLLKTR KGRCGEWNNC FIAILKSLDI DTRFIWNAED HVWCEYYNER EGRWIHLDSC
ENSYDQPYLY NEGWGKKMSY TFAIGPNYII DVSDKYLSPN RPENHLPRNK CPEVSLKGIL
AHHNAQSILA SSKDTILRTT SQLIADLMNT RGKVHPVHTE TTSTNEGASL LPRQSGAGAW
TRQRGEDNNE
//
