ID SAMP2_HALVD Reviewed; 66 AA. AC D4GZE7; DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 1. DT 21-SEP-2011, entry version 10. DE RecName: Full=Small archaeal modifier protein 2; DE Short=SAMP 2; DE AltName: Full=Ubiquitin-like small archaeal modifier protein 2; GN OrderedLocusNames=HVO_0202; OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC OS 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Haloferax. OX NCBI_TaxID=309800; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / RC VKM B-1768 / DS2; RX PubMed=20333302; DOI=10.1371/journal.pone.0009605; RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., RA Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M., RA Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T., RA Eisen J.A.; RT "The complete genome sequence of Haloferax volcanii DS2, a model RT archaeon."; RL PLoS ONE 5:E9605-E9605(2010). RN [2] RP FUNCTION AS A PROTEIN MODIFIER, CROSS-LINK, PROTEIN TARGETS, RP SAMPYLATION AT LYS-58, IDENTIFICATION BY MASS SPECTROMETRY, AND RP MUTAGENESIS OF 65-GLY-GLY-66. RX PubMed=20054389; DOI=10.1038/nature08659; RA Humbard M.A., Miranda H.V., Lim J.M., Krause D.J., Pritz J.R., RA Zhou G., Chen S., Wells L., Maupin-Furlow J.A.; RT "Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax RT volcanii."; RL Nature 463:54-60(2010). RN [3] RP REVIEW. RX PubMed=20547064; DOI=10.1016/j.tibs.2010.03.003; RA Darwin K.H., Hofmann K.; RT "SAMPyling proteins in archaea."; RL Trends Biochem. Sci. 35:348-351(2010). CC -!- FUNCTION: Protein modifier that is covalently attached to lysine CC residues of substrate proteins. The tagging system is termed CC SAMPylation. It is not known whether it is implicated in the CC targeting of proteins to the proteasome for degradation. Is able CC to form polymeric chains with itself at Lys-58, similar to CC ubiquitin and other ubiquitin-like proteins. 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; CP001956; ADE03392.1; -; Genomic_DNA. DR RefSeq; YP_003534279.1; NC_013967.1. DR GeneID; 8926718; -. DR GenomeReviews; CP001956_GR; HVO_0202. DR KEGG; hvo:HVO_0202; -. DR OMA; PEDQPVE; -. DR GO; GO:0031386; F:protein tag; IDA:UniProtKB. DR GO; GO:0032446; P:protein modification by small protein conjugation; IDA:UniProtKB. DR InterPro; IPR012675; Beta-grasp_ferredoxin-type. DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b. DR Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1. DR SUPFAM; SSF54285; Mo_synth/thiamin_syn_S_b-grasp; 1. PE 1: Evidence at protein level; KW Complete proteome; Isopeptide bond; Ubl conjugation; KW Ubl conjugation pathway. FT CHAIN 1 66 Small archaeal modifier protein 2. FT /FTId=PRO_0000397102. FT CROSSLNK 58 58 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SAMP2). FT CROSSLNK 66 66 Glycyl lysine isopeptide (Gly-Lys) FT (interchain with K-? in acceptor FT proteins). FT MUTAGEN 65 66 Missing: Abolishes SAMPylation of FT substrate proteins. SQ SEQUENCE 66 AA; 7118 MW; 09442B0B845C7DE0 CRC64; MNVTVEVVGE ETSEVAVDDD GTYADLVRAV DLSPHEVTVL VDGRPVPEDQ SVEVDRVKVL RLIKGG //