Q4WHY5 (SSU72_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RNA polymerase II subunit A C-terminal domain phosphatase ssu72
Short name=CTD phosphatase ssu72
EC=3.1.3.16

Alternative name(s):
Suppressor of SUA7 protein 2 homolog

Gene names

Name:	ssu72
ORF Names:	AFUA_2G03760

Organism

Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Neosartorya fumigata

Protein attributes

Sequence length	287 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Processively dephosphorylates Ser-5 of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (rpb1) By similarity. Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Ssu72 is required for 3'-end formation of snoRNAs By similarity.
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Subunit structure	Component of the cleavage and polyadenylation factor (CPF) complex By similarity.
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the SSU72 phosphatase family.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phosphoprotein phosphatase 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 – 287	287	RNA polymerase II subunit A C-terminal domain phosphatase ssu72		PRO_0000255603
Regions
	Compositional bias	15 – 28	14	Pro-rich

Sequences

	Sequence		Length	Mass (Da)
	Q4WHY5 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 5366D17B18D8BC1D	FASTA	287	31,559
	10 20 30 40 50 60 MAHDPRLSSA GTATPNPPPP PPPPPPEPST TGTGETQAAE PSAPAQSSDS FKLKFCTVCA 70 80 90 100 110 120 SNQNRSMEAH LRLSTAPSPF PVISFGTGSL VRLPGPSITQ PNVYNFNTTS YSQMYDELLA 130 140 150 160 170 180 KDERLYRNNG LLNMLDRNRN LKWGPERFQD WVPGMPRVDH VSKGDKGALG TEGGTVDVII 190 200 210 220 230 240 TCEERCWDAV VDDLMNKGAA LNRPVHVFNV DIRDNHEEAL VGGKAILELA TRLNDAATQE 250 260 270 280 RKIHGAEGWE NGNGEARRSF DERVPEILAS WQEKWPNLPA LWTLAWL

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAHF01000008 Genomic DNA. Translation: EAL87470.1.
RefSeq	XP_749508.1. XM_744415.1.
3D structure databases
ProteinModelPortal	Q4WHY5.
ModBase	Search...
Protein-protein interaction databases
STRING	5085.CADAFUAP00003794.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUAT00003794; CADAFUAP00003794; CADAFUAG00003794.
GeneID	3506785.
KEGG	afm:AFUA_2G03760.
Phylogenomic databases
eggNOG	COG5211.
HOGENOM	HOG000183445.
KO	K15544.
OMA	CEERCWD.
OrthoDB	EOG4DFSXT.
Family and domain databases
InterPro	IPR006811. RNA_pol_II_suA. [Graphical view]
PANTHER	PTHR20383. PTHR20383. 1 hit.
Pfam	PF04722. Ssu72. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SSU72_ASPFU

Accession

Primary (citable) accession number: Q4WHY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	July 5, 2005
Last modified:	May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program