Q8DMH9 (Q8DMH9_THEEB) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Peptidyl-prolyl cis-trans isomerase EMBL BAC07690.1

Gene names

Ordered Locus Names:

tlr0137

Organism

Thermosynechococcus elongatus (strain BP-1)

Taxonomic identifier

197221 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Thermosynechococcus

Protein attributes

Sequence length	243 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 Reference 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)
	Q8DMH9 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: F69BC4C6DDE8DE00	FASTA	243	26,004
	10 20 30 40 50 60 MKPLKFGTVL PLFLQRLVIV LSALLLVSCA SLSSVADTSS IPGAQSPTPM ANLPRLNGDA 70 80 90 100 110 120 TVVLTVNDRP ITIQVKGDAA PITAGNFVDL VNRGVYDGTI FHRVVREPRP FVVQGGDPQT 130 140 150 160 170 180 KDPKVSPQLY GTGSFIDPAT NRPRYIPLEI LGQGSDTPTY SQAGKVSPVL NHRRGAVAMA 190 200 210 220 230 240 RSQLPDSASA QFYIALDQLD FLDGNYAVFG YVTDGMDVVD TIQQGDRLQS AKVVAGLENL QQP

References

[1]

"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1." Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. , Takeuchi C., Yamada M., Tabata S. DNA Res. 9:123-130(2002) [PubMed: 12240834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BP-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000039 Genomic DNA. Translation: BAC07690.1.
RefSeq	NP_680928.1. NC_004113.1.
3D structure databases
HSSP	HSSP built from PDB template 1CLH based on UniProtKB P20752.
ProteinModelPortal	Q8DMH9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8DMH9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1010328.
GenomeReviews	Gene locus tlr0137 in contig BA000039_GR.
KEGG	tel:tlr0137.
NMPDR	fig|197221.1.peg.137.
PATRIC	23925464. VBITheElo119873_0143.
Phylogenomic databases
HOGENOM	HBG610621.
OMA	QPFVVQG.
ProtClustDB	CLSK538483.
Enzyme and pathway databases
BioCyc	TELO197221:TLR0137-MONOMER.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
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

Q8DMH9_THEEB

Accession

Primary (citable) accession number: Q8DMH9

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2003
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)