ID GCP_HALWD Reviewed; 533 AA. AC Q18KI0; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 16-JUN-2009, entry version 26. DE RecName: Full=Putative O-sialoglycoprotein endopeptidase; DE Short=Glycoprotease; DE EC=3.4.24.57; GN Name=gcp; OrderedLocusNames=HQ1341A; OS Haloquadratum walsbyi (strain DSM 16790). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Haloquadratum. OX NCBI_TaxID=362976; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16820047; DOI=10.1186/1471-2164-7-169; RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., RA Pfeiffer F., Oesterhelt D.; RT "The genome of the square archaeon Haloquadratum walsbyi: life at the RT limits of water activity."; RL BMC Genomics 7:169-169(2006). CC -!- CATALYTIC ACTIVITY: Hydrolysis of O-sialoglycoproteins; cleaves CC 31-Arg-|-Asp-32 bond in glycophorin A. Does not cleave CC unglycosylated proteins, desialylated glycoproteins or CC glycoproteins that are only N-glycosylated. CC -!- COFACTOR: Zinc (Probable). CC -!- SIMILARITY: Belongs to the peptidase M22 family. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AM180088; CAJ51469.1; -; Genomic_DNA. DR RefSeq; YP_657116.1; -. DR GeneID; 4194019; -. DR GenomeReviews; AM180088_GR; HQ1341A. DR KEGG; hwa:HQ1341A; -. DR NMPDR; fig|362976.6.peg.344; -. DR HOGENOM; Q18KI0; -. DR OMA; Q18KI0; AMIAWLG. DR BioCyc; HWAL362976:HQ1341A-MON; -. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:HAMAP. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR HAMAP; MF_01447; -; 1. DR InterPro; IPR009220; Pept_M22_Gylco. DR InterPro; IPR009180; Pept_M22_Osialgl. DR InterPro; IPR000905; Peptidase_M22. DR InterPro; IPR017860; Peptidase_M22_CS. DR InterPro; IPR017861; Peptidase_M22_subgr. DR InterPro; IPR000719; Prot_kinase_core. DR PANTHER; PTHR11735; Pept_M22_Osialgl; 1. DR Pfam; PF00814; Peptidase_M22; 1. DR PIRSF; PIRSF036401; Gcp_STYKS; 1. DR PRINTS; PR00789; OSIALOPTASE. DR ProDom; PD002367; Peptidase_M22; 1. DR ProDom; PD000001; Prot_kinase; 1. DR TIGRFAMs; TIGR00329; gcp; 1. DR PROSITE; PS01016; GLYCOPROTEASE; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Metalloprotease; KW Protease; Zinc. FT CHAIN 1 533 Putative O-sialoglycoprotein FT endopeptidase. FT /FTId=PRO_0000303649. FT DOMAIN 296 533 Protein kinase. FT REGION 1 295 Metallopeptidase. FT METAL 112 112 Zinc (Potential). FT METAL 116 116 Zinc (Potential). SQ SEQUENCE 533 AA; 57542 MW; A504147E944A27A2 CRC64; MRILGIEGTA WAASAALYNT HDETIVIESD PYQPDSGGLH PREAAEHMST ALPEVISTIL ERAVSSGNTD AIGIDAIAFS RGPGLGPCLR VVGTAARTLT QALSVPLIGV NHMIAHLEIG RHQSGFTTPV CLNASGANAH LLGYHRRQYQ VLGETMDTGV GNAIDKFTRH LGWNHPGGPK VEAAATDGSY HDLPYVVKGM DFSFSGIMSA AKDAVDNEVP VVDVCTGLQE TIFAMLTEVA ERALSLTGSN ELVLGGGVGQ NDRLREMLST MCTARGASFY APESRFLRDN AGMIAVLGAA MYEAGQTISV NDSAVDPTFR PDAVTVTWRD DETSVTRTPA TLDKTPVRGA EAIVRRINDH VVKRRVEKSY RHPKLDRRLR AERTRAEARL TSAARRLGVP TPLIFDADPE TGTLVFEYVG ETDLAADLTV SRCHAVGQHL GRIHNAGFVH GDPTTRNVRV DSAQNYLIDF GLGYHTDHVE DHAMDLHVFI QSVTGTASDP APLITAFESG YAETGISTVQ SRLRDIESRG RYH //