Q99009 (Q99009_TOLIN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Recommended name: Peptidyl-prolyl cis-trans isomerase RuleBase RU000493 EC=5.2.1.8 RuleBase RU000493
Organism	Tolypocladium inflatum (Cyclosporin fungus) (Tolypocladium niveum) EMBL CAA88041.1
Taxonomic identifier	29910 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Hypocreomycetidae › Hypocreales › Clavicipitaceae › mitosporic Clavicipitaceae › Tolypocladium

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	PPIases accelerate the folding of proteins By similarity. RuleBase RU000493 PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity. RuleBase RU004223
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0). RuleBase RU000493 SAAS SAAS020892
Sequence similarities	Belongs to the cyclophilin-type PPIase family. RuleBase RU004223 Contains 1 PPIase cyclophilin-type domain. SAAS SAAS020892 RuleBase RU003420

Ontologies

Keywords
Domain	Signal EMBL CAA88041.1
Molecular function	Isomerase Rotamase SAAS SAAS020892 RuleBase RU003420
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 48	48	Potential EMBL CAA88041.1
	Chain	49 – 227	179	Potential EMBL CAA88041.1		PRO_5000147584

Sequences

	Sequence		Length	Mass (Da)
	Q99009 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 0D023F7EBB444553	FASTA	227	24,590
	10 20 30 40 50 60 MKSTLLRPLL PRYKLCSPGS RSFPLPQLAS ASNTFRAARF FSATSAIMGN KVFFDIEWEG 70 80 90 100 110 120 PVMQGGKPTS TVKEQSGRIN FKLYDDVVPK TAENFRALCT GEKGFGYEGS SFHRIIPEFM 130 140 150 160 170 180 LQGGDFTRGN GTGGKSIYGE KFADENGQLK HDRPGLLSMA NAGPNTNGSQ FFVTTVVTSW 190 200 210 220 LNGRHVVFGE VADQESLDVV KALEATGSGS GAVKYNKRAT IVKSGEL

References

[1]	"Cloning and sequencing of a cyclophilin gene from the cyclosporin producer Tolypocladium niveum." Hornbogen T., Zocher R. Biochem. Mol. Biol. Int. 36:169-176(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: DSM 915 EMBL CAA88041.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z48002 Genomic DNA. Translation: CAA88041.1.
3D structure databases
HSSP	HSSP built from PDB template 1IST based on UniProtKB P14832.
ProteinModelPortal	Q99009.
SMR	Q99009. Positions 50-225.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR024936. Cyclophilin-type_PPIase. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PIRSF	PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTS	PR00153. CSAPPISMRASE.
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q99009_TOLIN

Accession

Primary (citable) accession number: Q99009
Secondary accession number(s): Q99010

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)