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Protein

Probable cysteine desulfurase, mitochondrial

Gene

SPBC21D10.11c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. Plays a role in both tRNA-processing and mitochondrial metabolism. Involved in the 2-thio-modification of both 5-carboxymethylaminomethyl-2-thiouridine in mitochondrial tRNAs and 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs.By similarity

Catalytic activityi

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.By similarity

Cofactori

pyridoxal 5'-phosphateBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei252 – 2521Pyridoxal phosphateBy similarity
Binding sitei280 – 2801Pyridoxal phosphateBy similarity
Binding sitei340 – 3401Pyridoxal phosphateBy similarity
Active sitei425 – 4251Cysteine persulfide intermediateBy similarity
Metal bindingi425 – 4251Iron-sulfur (2Fe-2S); via persulfide groupBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Iron, Iron-sulfur, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-SPO-1362409. Mitochondrial iron-sulfur cluster biogenesis.
R-SPO-947581. Molybdenum cofactor biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable cysteine desulfurase, mitochondrialBy similarity (EC:2.8.1.7By similarity)
Gene namesi
ORF Names:SPBC21D10.11cImported
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC21D10.11c.
PomBaseiSPBC21D10.11c.

Subcellular locationi

  • Mitochondrion By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 501Probable cysteine desulfurase, mitochondrialPRO_0000001303
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei303 – 3031N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiO74351.

Interactioni

Protein-protein interaction databases

BioGridi276931. 9 interactions.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni172 – 1732Pyridoxal phosphate bindingBy similarity
Regioni300 – 3023Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000017510.
InParanoidiO74351.
KOiK04487.
OMAiEPIQSGG.
OrthoDBiEOG7ZKSMC.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00331. Cys_desulf_IscS.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR010240. Cys_deSase_IscS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02006. IscS. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O74351-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKMGSLMLS RARCLLELRS ALFFVKRESQ DINNVRQSLG VYGRSFMTSS
60 70 80 90 100
RMDKPSMSNK PREQMYGLGN MTAVQEPIPE NSLKTVTLDQ AQTAASTVTG
110 120 130 140 150
LHPIYMDFQA TSPLDYRVLD SMLPFFTGIY GNPHSRTHAY GWEAEKAVEN
160 170 180 190 200
ARQEIASVIN ADPREIIFTS GATESNNAIL KGVARFYKSR KKHLVSVQTE
210 220 230 240 250
HKCVLDSLRA LQEEGFEVTF LPVQTNGLIN LDELRDAIRP DTVCVSVMAV
260 270 280 290 300
NNEIGVCQPL EEIGKICRQK KVFFHSDAAQ GYGKIDIDVN RMNIDLMSIS
310 320 330 340 350
AHKIYGPKGI GAAYVRRRPR VRLEPLISGG GQERGLRSGT LAPSQVVGFG
360 370 380 390 400
TAARICKEEM KYDYAHISKL SQRLIDGLLA IPYTSLNGDP KSRYPGCVNI
410 420 430 440 450
SFNYVEGESL LMGLKNIALS SGSACTSASL EPSYVLRAIG QSDENAHSSI
460 470 480 490 500
RFGIGRFTTE AEIDYAIENV SRQVSFLRNM SPLWDLVQEG VDLSTIEWSQ

H
Length:501
Mass (Da):55,543
Last modified:October 3, 2012 - v2
Checksum:iDBE47BC3ACF8713E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA20767.2.
PIRiT11683.
RefSeqiNP_596002.2. NM_001021910.2.

Genome annotation databases

EnsemblFungiiSPBC21D10.11c.1; SPBC21D10.11c.1:pep; SPBC21D10.11c.
GeneIDi2540403.
KEGGispo:SPBC21D10.11c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA20767.2.
PIRiT11683.
RefSeqiNP_596002.2. NM_001021910.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276931. 9 interactions.

Proteomic databases

MaxQBiO74351.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC21D10.11c.1; SPBC21D10.11c.1:pep; SPBC21D10.11c.
GeneIDi2540403.
KEGGispo:SPBC21D10.11c.

Organism-specific databases

EuPathDBiFungiDB:SPBC21D10.11c.
PomBaseiSPBC21D10.11c.

Phylogenomic databases

HOGENOMiHOG000017510.
InParanoidiO74351.
KOiK04487.
OMAiEPIQSGG.
OrthoDBiEOG7ZKSMC.

Enzyme and pathway databases

ReactomeiR-SPO-1362409. Mitochondrial iron-sulfur cluster biogenesis.
R-SPO-947581. Molybdenum cofactor biosynthesis.

Miscellaneous databases

PROiO74351.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00331. Cys_desulf_IscS.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR010240. Cys_deSase_IscS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02006. IscS. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.

Entry informationi

Entry nameiNFS1_SCHPO
AccessioniPrimary (citable) accession number: O74351
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 3, 2012
Last modified: June 8, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. 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.