ProGP235 (CipB (putative dipeptide-binding protein

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ProGP ID ProGP235 (CipB (putative dipeptide-binding protein
Validation Status Uncharacterized
Organism Information
Organism NamePyrococcus furiosus DSM 3638
Domain Archaea
Classification Phylum : Euryarchaeota
Class : Thermococci
Orders : Thermococcales
Family : Thermococcaceae
Genus : Pyrococcus
Species : furiosus
Strain : DSM 3639
Taxonomic ID (NCBI) 2261
Genome Information
GenBank AE009950.1
EMBL AE009950
Gene Information
Gene NamecipB (PF1408)
NCBI Gene ID 1469284
GenBank Gene Sequence NC_003413
Protein Information
Protein NameCipB (putative dipeptide-binding protein)
UniProtKB/SwissProt ID Q8U121
NCBI RefSeq WP_011012555.1
EMBL-CDSAAL81532.1
UniProtKB Sequence >tr|Q8U121|Q8U121_PYRFU Putative dipeptide-binding protein OS=Pyrococcus furiosus GN=PF1408 PE=4 SV=1 MKKGLLAILLVGVMVLGTFGSGCIGGGTQTQTQTPTETGSPTQTTTPSGVTQAILELGKV TVVDTGTAIVVVGPKGEKPSVSIPSGKKVITVTYVVDEQNTPSVKELMEQGQGFGAINPA FFRDTNVDALVIAARRETNPEVRTEIFKALYILGNYYVPEVILGQNRQLRVYWDWVKGRY YHPTLPERYDLLWEDPNAPVVDTGIGSYKNDPETYVIATIGWPESFDPAWTYETFGWEIW HEIGDTLVTYWKEETEQVTPDLAVAWAHNKEGTEWYFVIRGGVKAYDPWNDKTYPIDATD VVFTFWRVARLGHSVSWMVTEFMNVSASQALTEEEFNNYVKNNPLIAEYNGKTAEIKSLQ DLLNFFGYNGETAGVFKLVLPHPYAAVLNIVADPFLSVVPMEYLLGDKYEEALKASNYGK NPDAWEAYVQEGVDDPTHQLMHKYPVGTGPFYVKEYQENSYIVLEYNPYYWNATSNPGHK RVIYIINNDAVARVQLLTTGTADVAAIPTDKIEDVQGVTKDGYKVVVQTDILLPVLTFIV FNTQKEPFNDVKVRQALAYAIPYDQIAKVVYNNLLERNWGPIPKPWPGYTEYGIIKYEYN IAKAKQMLQEAGVDPSKYSITLIYNAGNTQREKVMTLIQNVWSQLGFRVTVESYEWPVYL SKTEHGDYDVYIVGWVPDYLDSDNWVGPFLYGATEFSEINIEVSG
Sequence length 705 AA
Subcellular LocationMembrane
Function Cold induced protein. Up-regulated in response to the cold stress.
Glycosylation Status
Technique(s) used for Glycosylation DetectionPro-Q Emerald 300 staining.
Literature
Year of Identification2005
Year of Identification Month Wise2005.1
ReferenceWeinberg, M.V., Schut, G.J., Brehm, S., Datta, S. and Adams, M.W., 2005. Cold shock of a hyperthermophilic archaeon: Pyrococcus furiosus exhibits multiple responses to a suboptimal growth temperature with a key role for membrane-bound glycoproteins. Journal of bacteriology, 187(1), pp.336-348.
Corresponding Author Michael W W Adams
ContactDepartment of Biochemistry and Molecular Biology, Life Sciences Bldg., University of Georgia, Athens, GA 30602-7229, USA