| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Proline iminopeptidase |
Protein Synonyms/Alias | PIP; PAP |
Gene Name | pip |
Gene Synonyms/Alias | SSO3115 |
Created Date | 3-June-2014 |
Organism | Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) |
NCBI Taxa ID | 273057 |
Phosphorylation | Position | Peptide | Code | Type | References | | 3 | *****MSYYFITMKG | Y | HTP | [1] | | 2 | ******MSYYFITMK | S | HTP | [1] | | 4 | ****MSYYFITMKGY | Y | HTP | [1] | | 7 | *MSYYFITMKGYSIN | T | HTP | [1] | |
Reference | [1]Change of carbon source causes dramatic effects in the phospho-proteome of the archaeon Sulfolobus solfataricus. Esser D,Pham TK,Reimann J,Albers SV,Siebers B,Wright PC J. Proteome Res. 2012, Oct, 5;11(10):4823-33. [ PMID:22639831] |
Functional Description From UniProt | FUNCTION: Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. In conjunction with the three factors F1, F2 and F3, Tricorn degrades oligopeptides in a sequential manner, yielding free amino acids (By similarity) |
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| Aminopeptidase; Completeproteome; Hydrolase; Protease; Referenceproteome |
Protein Sequence | MSYYFITMKG YSINVEEGYK RIFGINIYYK LYRVKGSNRN LVTLHGGPGG SHDYLIPLAD 60
LSNYGINVLF YDQFGCGRSD DPKDTSDYTI DHGLEELEEL RKQVFGNDKI VLLGHSYGGA 120
LAIAYALKYQ QFLRGLIVSS GLSSVPYTVK EMRRLIEELP DKYKTIIKRY ESLGDFKNPE 180
YLDAVNFFYS QHLLRLKEMP EPVKRTFEYI GKRRTYEIMN GPNEFTIIGT IKDWDVTEQL 240
YKITVPTLIT VGKYDEVTVN VAQLIHKNIK GSRLVIFENS SHMAMWEEKD KYLEVIKEFI 300
DQVYSLNMVK 310 |
| GO:0004177 F:aminopeptidase activity IEA:UniProtKB-KW |
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