Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

RNA polymerase II subunit A C-terminal domain phosphatase

Gene

fcp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

Cofactori

Mg2+1 Publication, Mn2+1 Publication, Co2+1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1701 Publication1
Active sitei1721 Publication1

GO - Molecular functioni

  • CTD phosphatase activity Source: PomBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • dephosphorylation of RNA polymerase II C-terminal domain Source: PomBase
  • negative regulation of G0 to G1 transition Source: PomBase
  • protein dephosphorylation Source: PomBase
  • regulation of transcription from RNA polymerase II promoter Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Cobalt, Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-SPO-113418. Formation of the Early Elongation Complex.
R-SPO-674695. RNA Polymerase II Pre-transcription Events.

Names & Taxonomyi

Protein namesi
Recommended name:
RNA polymerase II subunit A C-terminal domain phosphatase (EC:3.1.3.16)
Alternative name(s):
CTD phosphatase fcp1
Gene namesi
Name:fcp1
ORF Names:SPAC19B12.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC19B12.05c.
PomBaseiSPAC19B12.05c. fcp1.

Subcellular locationi

GO - Cellular componenti

  • DNA-directed RNA polymerase II, holoenzyme Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi170D → A, N or E: No activity. 1 Publication1
Mutagenesisi172D → A, N or E: No activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002125671 – 723RNA polymerase II subunit A C-terminal domain phosphataseAdd BLAST723

Proteomic databases

MaxQBiQ9P376.
PRIDEiQ9P376.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi278698. 14 interactors.
MINTiMINT-1213896.

Structurei

Secondary structure

1723
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi151 – 162Combined sources12
Beta strandi165 – 169Combined sources5
Turni172 – 174Combined sources3
Beta strandi175 – 179Combined sources5
Helixi183 – 188Combined sources6
Turni194 – 196Combined sources3
Helixi197 – 199Combined sources3
Beta strandi203 – 209Combined sources7
Turni210 – 213Combined sources4
Beta strandi214 – 222Combined sources9
Helixi226 – 234Combined sources9
Beta strandi237 – 242Combined sources6
Helixi247 – 257Combined sources11
Turni262 – 266Combined sources5
Turni271 – 273Combined sources3
Helixi282 – 284Combined sources3
Beta strandi293 – 298Combined sources6
Helixi301 – 303Combined sources3
Beta strandi309 – 311Combined sources3
Turni327 – 329Combined sources3
Helixi398 – 415Combined sources18
Helixi417 – 427Combined sources11
Helixi434 – 436Combined sources3
Helixi445 – 470Combined sources26
Turni471 – 473Combined sources3
Helixi479 – 488Combined sources10
Beta strandi495 – 502Combined sources8
Turni508 – 510Combined sources3
Helixi512 – 519Combined sources8
Beta strandi526 – 530Combined sources5
Beta strandi533 – 538Combined sources6
Beta strandi540 – 542Combined sources3
Helixi543 – 551Combined sources9
Beta strandi555 – 557Combined sources3
Helixi559 – 568Combined sources10
Helixi574 – 577Combined sources4
Beta strandi578 – 580Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EF0X-ray2.10A149-329[»]
A394-580[»]
3EF1X-ray2.15A140-580[»]
4XPZX-ray1.45A149-329[»]
A394-580[»]
4XQ0X-ray1.85A149-329[»]
A394-580[»]
ProteinModelPortaliQ9P376.
SMRiQ9P376.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P376.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini160 – 341FCP1 homologyPROSITE-ProRule annotationAdd BLAST182
Domaini486 – 579BRCTPROSITE-ProRule annotationAdd BLAST94

Sequence similaritiesi

Contains 1 BRCT domain.PROSITE-ProRule annotation
Contains 1 FCP1 homology domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000197682.
InParanoidiQ9P376.
KOiK15732.
OMAiDMARANI.
OrthoDBiEOG092C3D5H.
PhylomeDBiQ9P376.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di3.40.50.1000. 2 hits.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR004274. FCP1_dom.
IPR011947. FCP1_euk.
IPR023214. HAD-like_dom.
[Graphical view]
PfamiPF03031. NIF. 1 hit.
PF12738. PTCB-BRCT. 1 hit.
[Graphical view]
SMARTiSM00577. CPDc. 1 hit.
[Graphical view]
SUPFAMiSSF52113. SSF52113. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02250. FCP1_euk. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS50969. FCP1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P376-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKRLTPIHL PNSLNYPIEI ASCLVPQGSY VKKGTPLLLY RFFTKVKEDQ
60 70 80 90 100
EDGSEVYVDR EFVEQFECPV EGELVEWAVK KEESIENFSK IVAKLHEPCT
110 120 130 140 150
HEVNYGGLCA ICGKNITSQD YMGYSDMARA NISMTHNTGD LTVSLEEASR
160 170 180 190 200
LESENVKRLR QEKRLSLIVD LDQTIIHATV DPTVGEWMSD PGNVNYDVLR
210 220 230 240 250
DVRSFNLQEG PSGYTSCYYI KFRPGLAQFL QKISELYELH IYTMGTKAYA
260 270 280 290 300
KEVAKIIDPT GKLFQDRVLS RDDSGSLAQK SLRRLFPCDT SMVVVIDDRG
310 320 330 340 350
DVWDWNPNLI KVVPYEFFVG IGDINSNFLA KSTPLPEQEQ LIPLEIPKDE
360 370 380 390 400
PDSVDEINEE NEETPEYDSS NSSYAQDSST IPEKTLLKDT FLQNREALEE
410 420 430 440 450
QNKERVTALE LQKSERPLAK QQNALLEDEG KPTPSHTLLH NRDHELERLE
460 470 480 490 500
KVLKDIHAVY YEEENDISSR SGNHKHANVG LIIPKMKQKV LKGCRLLFSG
510 520 530 540 550
VIPLGVDVLS SDIAKWAMSF GAEVVLDFSV PPTHLIAAKI RTEKVKKAVS
560 570 580 590 600
MGNIKVVKLN WLTESLSQWK RLPESDYLLY PSYDLPDRNL SEHSYSSSSD
610 620 630 640 650
DEQRISELND RELDEIDWQA ADQDVENALK DLSDDNDFDT GSISASQSQP
660 670 680 690 700
EALEVNTPIK RKADLIQPSY NYDGEKRRKE NDNHEGYDLL PNSSTKGEES
710 720
AENENELDDL ADIMEAELSK DTA
Length:723
Mass (Da):81,965
Last modified:October 1, 2000 - v1
Checksum:iA127A06CD2FD3435
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC00553.1.
RefSeqiNP_594768.1. NM_001020195.2.

Genome annotation databases

EnsemblFungiiSPAC19B12.05c.1; SPAC19B12.05c.1:pep; SPAC19B12.05c.
GeneIDi2542225.
KEGGispo:SPAC19B12.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC00553.1.
RefSeqiNP_594768.1. NM_001020195.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EF0X-ray2.10A149-329[»]
A394-580[»]
3EF1X-ray2.15A140-580[»]
4XPZX-ray1.45A149-329[»]
A394-580[»]
4XQ0X-ray1.85A149-329[»]
A394-580[»]
ProteinModelPortaliQ9P376.
SMRiQ9P376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278698. 14 interactors.
MINTiMINT-1213896.

Proteomic databases

MaxQBiQ9P376.
PRIDEiQ9P376.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC19B12.05c.1; SPAC19B12.05c.1:pep; SPAC19B12.05c.
GeneIDi2542225.
KEGGispo:SPAC19B12.05c.

Organism-specific databases

EuPathDBiFungiDB:SPAC19B12.05c.
PomBaseiSPAC19B12.05c. fcp1.

Phylogenomic databases

HOGENOMiHOG000197682.
InParanoidiQ9P376.
KOiK15732.
OMAiDMARANI.
OrthoDBiEOG092C3D5H.
PhylomeDBiQ9P376.

Enzyme and pathway databases

ReactomeiR-SPO-113418. Formation of the Early Elongation Complex.
R-SPO-674695. RNA Polymerase II Pre-transcription Events.

Miscellaneous databases

EvolutionaryTraceiQ9P376.
PROiQ9P376.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di3.40.50.1000. 2 hits.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR004274. FCP1_dom.
IPR011947. FCP1_euk.
IPR023214. HAD-like_dom.
[Graphical view]
PfamiPF03031. NIF. 1 hit.
PF12738. PTCB-BRCT. 1 hit.
[Graphical view]
SMARTiSM00577. CPDc. 1 hit.
[Graphical view]
SUPFAMiSSF52113. SSF52113. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02250. FCP1_euk. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS50969. FCP1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFCP1_SCHPO
AccessioniPrimary (citable) accession number: Q9P376
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.