P20080 (FKB1A_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase fkr-2
Short name=PPIase fkr-2
EC=5.2.1.8

Alternative name(s):
FK506-binding protein 1A
Short name=FKBP-1A

Gene names

Name:	fkr-2
Synonyms:	fpr-1a
ORF Names:	9G6.180, NCU04140

Organism

Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

Taxonomic identifier

367110 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	120 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.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subcellular location	Cytoplasm.
Miscellaneous	Binds to the immunosuppressant drug FK506.
Sequence similarities	Belongs to the FKBP-type PPIase family. FKBP1 subfamily. Contains 1 PPIase FKBP-type domain.
Sequence caution	The sequence EAA32060.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Isomerase Rotamase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Chain	1 – 120	120	Peptidyl-prolyl cis-trans isomerase fkr-2		PRO_0000075303
Regions
	Domain	26 – 114	89	PPIase FKBP-type

Sequences

	Sequence		Length	Mass (Da)
	P20080 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: AF97183C041563B7	FASTA	120	13,037
	10 20 30 40 50 60 MTIPQLDGLQ IEVQQEGQGT RETRRGDNVD VHYKGVLTSG KKFDASYDRG EPLNFTVGQG 70 80 90 100 110 120 QVIKGWDEGL LGMKIGEKRK LTIAPHLAYG NRAVGGIIPA NSTLIFETEL VGIKGVQKGE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and sequence of an FK506-binding protein from N. crassa which catalyses protein folding." Tropschug M., Wachter E., Mayer S., Schoenbrunner E.R., Schmid F.X. Nature 346:674-677(1990) [PubMed: 1696687] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence." Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U. Nucleic Acids Res. 31:1944-1954(2003) [PubMed: 12655011] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]	"The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W. Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X55743 Genomic DNA. Translation: CAA39274.1. AL513463 Genomic DNA. Translation: CAC28766.1. AABX02000013 Genomic DNA. Translation: EAA32060.2. Different initiation.
PIR	S11090.
RefSeq	XP_961296.2. XM_956203.2.
3D structure databases
ProteinModelPortal	P20080.
ModBase	Search...
Protein-protein interaction databases
STRING	P20080.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	EFNCRT00000003914; EFNCRP00000003914; EFNCRG00000003909.
GeneID	3877460.
KEGG	ncr:NCU04140.
NMPDR	fig|5141.1.peg.1413.
Phylogenomic databases
eggNOG	fuNOG10864.
GeneTree	EFGT00050000000955.
OrthoDB	EOG4DNJF5.
Enzyme and pathway databases
BioCyc	NCRA-XX3-01:NCRA-XX3-01-007888-MONOMER.
Family and domain databases
InterPro	IPR023566. PPIase_FKBP. IPR001179. PPIase_FKBP_dom. [Graphical view]
KO	K09569.
PANTHER	PTHR10516. PPIase_FKBP. 1 hit.
Pfam	PF00254. FKBP_C. 1 hit. [Graphical view]
PROSITE	PS50059. FKBP_PPIASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FKB1A_NEUCR

Accession

Primary (citable) accession number: P20080
Secondary accession number(s): Q7S7U2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	December 14, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program