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Q9P376 (FCP1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA polymerase II subunit A C-terminal domain phosphatase
EC=3.1.3.16
Alternative name(s):
CTD phosphatase fcp1
Gene names
Name:fcp1
ORF Names:SPAC19B12.05c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length723 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Ref.2

Catalytic activity

A phosphoprotein + H2O = a protein + phosphate. Ref.2

Cofactor

Magnesium or manganese or cobalt. Ref.2

Subunit structure

Monomer. Ref.2

Subcellular location

Nucleus Probable.

Sequence similarities

Contains 1 BRCT domain.

Contains 1 FCP1 homology domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 723723RNA polymerase II subunit A C-terminal domain phosphatase
PRO_0000212567

Regions

Domain160 – 341182FCP1 homology
Domain486 – 57994BRCT

Sites

Active site1701 Ref.2
Active site1721 Ref.2

Experimental info

Mutagenesis1701D → A, N or E: No activity. Ref.2
Mutagenesis1721D → A, N or E: No activity. Ref.2

Secondary structure

1 .................................................................. 723
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9P376 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: A127A06CD2FD3435

FASTA72381,965
        10         20         30         40         50         60 
MSKRLTPIHL PNSLNYPIEI ASCLVPQGSY VKKGTPLLLY RFFTKVKEDQ EDGSEVYVDR 

        70         80         90        100        110        120 
EFVEQFECPV EGELVEWAVK KEESIENFSK IVAKLHEPCT HEVNYGGLCA ICGKNITSQD 

       130        140        150        160        170        180 
YMGYSDMARA NISMTHNTGD LTVSLEEASR LESENVKRLR QEKRLSLIVD LDQTIIHATV 

       190        200        210        220        230        240 
DPTVGEWMSD PGNVNYDVLR DVRSFNLQEG PSGYTSCYYI KFRPGLAQFL QKISELYELH 

       250        260        270        280        290        300 
IYTMGTKAYA KEVAKIIDPT GKLFQDRVLS RDDSGSLAQK SLRRLFPCDT SMVVVIDDRG 

       310        320        330        340        350        360 
DVWDWNPNLI KVVPYEFFVG IGDINSNFLA KSTPLPEQEQ LIPLEIPKDE PDSVDEINEE 

       370        380        390        400        410        420 
NEETPEYDSS NSSYAQDSST IPEKTLLKDT FLQNREALEE QNKERVTALE LQKSERPLAK 

       430        440        450        460        470        480 
QQNALLEDEG KPTPSHTLLH NRDHELERLE KVLKDIHAVY YEEENDISSR SGNHKHANVG 

       490        500        510        520        530        540 
LIIPKMKQKV LKGCRLLFSG VIPLGVDVLS SDIAKWAMSF GAEVVLDFSV PPTHLIAAKI 

       550        560        570        580        590        600 
RTEKVKKAVS MGNIKVVKLN WLTESLSQWK RLPESDYLLY PSYDLPDRNL SEHSYSSSSD 

       610        620        630        640        650        660 
DEQRISELND RELDEIDWQA ADQDVENALK DLSDDNDFDT GSISASQSQP EALEVNTPIK 

       670        680        690        700        710        720 
RKADLIQPSY NYDGEKRRKE NDNHEGYDLL PNSSTKGEES AENENELDDL ADIMEAELSK 


DTA

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Characterization of the CTD phosphatase Fcp1 from fission yeast. Preferential dephosphorylation of serine 2 versus serine 5."
Hausmann S., Shuman S.
J. Biol. Chem. 277:21213-21220(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COFACTOR, SUBUNIT, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF ASP-170 AND ASP-172.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAC00553.1.
RefSeqNP_594768.1. NM_001020195.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EF0X-ray2.10A149-580[»]
3EF1X-ray2.15A140-580[»]
ProteinModelPortalQ9P376.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1213896.
STRING4896.SPAC19B12.05c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC19B12.05c.1; SPAC19B12.05c.1:pep; SPAC19B12.05c.
GeneID2542225.
KEGGspo:SPAC19B12.05c.

Organism-specific databases

PomBaseSPAC19B12.05c.

Phylogenomic databases

eggNOGCOG5190.
HOGENOMHOG000197682.
KOK15732.
OMALYEMHIY.
OrthoDBEOG4WDHMJ.

Family and domain databases

Gene3D3.40.50.1000. 2 hits.
InterProIPR001357. BRCT_dom.
IPR011947. FCP1_euk.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view]
PfamPF03031. NIF. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 1 hit.
SM00577. CPDc. 1 hit.
[Graphical view]
SUPFAMSSF52113. BRCT. 1 hit.
SSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR02250. FCP1_euk. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS50969. FCP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9P376.
NextBio20803293.

Entry information

Entry nameFCP1_SCHPO
AccessionPrimary (citable) accession number: Q9P376
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: October 1, 2000
Last modified: May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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