B0C1V4 (B0C1V4_ACAM1) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Peptidyl-prolyl cis-trans isomerase, cyclophilin-type EMBL ABW26120.1

Gene names

Ordered Locus Names:

AM1_1081

Organism

Acaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]

Taxonomic identifier

329726 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Acaryochloris

Protein attributes

Sequence length	268 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity. RuleBase RU004223
Sequence similarities	Belongs to the cyclophilin-type PPIase family. RuleBase RU004223 Contains 1 PPIase cyclophilin-type domain. RuleBase RU003420

Ontologies

Keywords
Molecular function	Isomerase Rotamase RuleBase RU003420
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	B0C1V4 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: A4898E4DA0ADD887	FASTA	268	28,550
	10 20 30 40 50 60 MLHSTKAISF FRSFWVMVLV FLLMACSAPS NSSGTSDTGG ASPSGSPPSE STQEDNSETT 70 80 90 100 110 120 GVPGSESTSP LAQLPQLQGE ATVVLQVNGK TITLAINGKD APITAGNFID LVDKKVYDGT 130 140 150 160 170 180 AFHRVVRTPS PFVVQGGDPQ SKDPNFPVQR LGTGSYIDPE TKQARYLPLE ILPEGAEQAV 190 200 210 220 230 240 YSKTLKSAGE NKPPKLRHTR GAVAMARSQL PDSASAQFYF ALADVDFLDG SYAVFGYVTE 250 260 GMDVVDQIQQ GDRIESATVT AGIENLKR

References

[1]

"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina." Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W. Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000828 Genomic DNA. Translation: ABW26120.1.
RefSeq	YP_001515434.1. NC_009925.1.
3D structure databases
ProteinModelPortal	B0C1V4.
ModBase	Search...
Protein-protein interaction databases
STRING	B0C1V4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5679906.
GenomeReviews	Gene locus AM1_1081 in contig CP000828_GR.
KEGG	amr:AM1_1081.
PATRIC	20616618. VBIAcaMar40141_0956.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG610621.
OMA	QPFVVQG.
PhylomeDB	B0C1V4.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 2 hits.
KO	K03768.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

B0C1V4_ACAM1

Accession

Primary (citable) accession number: B0C1V4

Entry history

Integrated into UniProtKB/TrEMBL:	February 26, 2008
Last sequence update:	February 26, 2008
Last modified:	January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)