ID A0A194QX43_PAPMA Unreviewed; 1362 AA.
AC A0A194QX43;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase {ECO:0000256|ARBA:ARBA00018546};
DE EC=3.5.1.52 {ECO:0000256|ARBA:ARBA00012158};
DE AltName: Full=Peptide:N-glycanase {ECO:0000256|ARBA:ARBA00032901};
GN ORFNames=RR48_13164 {ECO:0000313|EMBL:KPJ09530.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ09530.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ09530.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ09530.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ09530.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine
CC residue in which the glucosamine residue may be further glycosylated,
CC to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a
CC peptide containing an aspartate residue.; EC=3.5.1.52;
CC Evidence={ECO:0000256|ARBA:ARBA00001650};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|RuleBase:RU000411}.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC family. {ECO:0000256|PROSITE-ProRule:PRU00731}.
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DR EMBL; KQ461073; KPJ09530.1; -; Genomic_DNA.
DR STRING; 76193.A0A194QX43; -.
DR InParanoid; A0A194QX43; -.
DR Proteomes; UP000053240; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0006516; P:glycoprotein catabolic process; IEA:InterPro.
DR CDD; cd19579; serpin1K-like; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 3.10.620.30; -; 1.
DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 2.
DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 2.
DR Gene3D; 2.60.120.1020; Peptide N glycanase, PAW domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR038680; PAW_sf.
DR InterPro; IPR006588; Peptide_N_glycanase_PAW_dom.
DR InterPro; IPR036339; PUB-like_dom_sf.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR InterPro; IPR002931; Transglutaminase-like.
DR PANTHER; PTHR11461:SF211; ACCESSORY GLAND PROTEIN ACP76A-RELATED; 1.
DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR Pfam; PF04721; PAW; 1.
DR Pfam; PF00079; Serpin; 2.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00093; SERPIN; 2.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF143503; PUG domain-like; 1.
DR SUPFAM; SSF56574; Serpins; 2.
DR PROSITE; PS51398; PAW; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT DOMAIN 419..614
FT /note="PAW"
FT /evidence="ECO:0000259|PROSITE:PS51398"
SQ SEQUENCE 1362 AA; 154898 MW; 3D048984282D111F CRC64;
MEDVARLAVV EQTINDIDKF NKVLNELLQH IDKILENPHE LDHRILKSSY LKKAMEHGVF
CEYLKYVGFK LENDDYIYPK DQSLAKLRFA QVALQRKISI CYGSKQELEI QRPPCYIKNN
EPYLKPVYLD TGVPLFNRIE MLFNNVLLYE RDDVQEKARE LMPLVSLELK AIERVRDHQR
KLKVGEVEGD DLSFELALLL ELMAWFKNEF FEWIDKPECE FCGGETAISS VGQRKLETET
CTVEVFKCKS CERDTLFPRF NDVRSLLRTR RGRCGEWANC FALLCRALGY DTRHVFDTND
HVWVEIYDFE AGGWLHVDPC ECVVDAPLVY SCGWGTRLAY VIAVSRDDIQ DVTWRYTVKH
KQVMFRRTLC AESDLVWYMM SLRGARQAQL SPARREYLAK RTVKELVQLM QEKEPSDYEK
KGRMSGALEW REERGEVSSL SHTFQFVKPG AYSIQYCAAK DEYRVFCDGN KENVIDSFLE
GAYKSEYIFR KVEKDWKQVY LARNEREEKG LISWKLEVEY DDLVLQDLVL LVRATTFEDG
QVRCFVQFDS EPPQDVTLDG PSKFKREFKK VVVSCELSGG SGDNKYQHAQ LFRQPINAKE
SLLKLVTNVD RGEFSCSLDT VNMECLILLF LVAMASTADS FLDHEYSRTP LGDNIDKASV
KLLKEAYLAS ENTNVVTSPL GVLLLLSLYS SGTQGKTRDE ITELLGATGY KEPFRNYFKT
SYITYHPSIQ TLAFIIVASG YDLNDEFLNT ARAYNTEVDS VDFHNVENAA HVINQWANKQ
LRGLIKDPVS KTSLDNDALV ALFNVIYFKG HWHVPFQVES TEMKDFHVNK SLTVKKPMMH
LSKSLFFHAN DQLGAKMIEL PYQEPGFRMV VILPNEVDGL PDVLEKVAQK GLLEDVFALS
PARSKVNLYL PKFDIKSSLD FTQILPKLGV NGIFSGSASG IVNGRSVAIS KIFQEAIVNV
DEEGARAGAF TVSIAFAVEE DEFFFFGHEY KRTELGDAVD KASMRLLKDL YESSEDKNVI
TSPLGVLTLL SLYSTGTTGK IKEEIVNFLG LPDYKKMTES YKSLTEKFTE MNPEFLTMAN
KVYVASRYEL TDEFTAVATR DYHSEVQALN FTNPSEAAKI INEWADQKTR GNIKNPVDEN
TFSPDTAAAL FNIIFFQGHW HVPFEKADTV DKKFQLSATE SVQKPTMHLV QSLFYHEDKE
LGARMVELPY KEPGFRMVVV LPDAVDGLPA VLDKLAQKGV LEDVFAMSPP GQDVDIDMPK
FEVKSKFNLK DVLVKEGVSS IFNQQAEGIV KGQGVEVSEV FQEAFVKVDE EGATAGAFTG
LVLVATSSLS EPPPPLPFKV DRPFLYAILH QDTVLFAGTY TH
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