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

probable cardiolipin-specific deacylase, mitochondrial

Gene

SPAC6G10.03c

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

Functioni

Mitochondrial cardiolipin-specific phospholipase which deacylates de novo synthesized cardiolipin. Part of the remodeling process of cardiolipin, which involves deacylation-reacylation of premature cardiolipin (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Enzyme and pathway databases

ReactomeiR-SPO-1483152. Hydrolysis of LPE.

Protein family/group databases

ESTHERischpo-ye63. CGI-58_ABHD5_ABHD4.

Names & Taxonomyi

Protein namesi
Recommended name:
probable cardiolipin-specific deacylase, mitochondrial (EC:3.5.1.-)
Gene namesi
ORF Names:SPAC6G10.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC6G10.03c.
PomBaseiSPAC6G10.03c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • endoplasmic reticulum Source: PomBase
  • Golgi apparatus Source: PomBase
  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 428probable cardiolipin-specific deacylase, mitochondrialPRO_0000116702
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

MaxQBiO14249.

Interactioni

Protein-protein interaction databases

MINTiMINT-4671756.

Structurei

3D structure databases

ProteinModelPortaliO14249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi398 – 4036HXXXXD motifBy similarity

Domaini

The HXXXXD motif is essential for acyltransferase activity.By similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000211778.
InParanoidiO14249.
KOiK13535.
OMAiNTSAGHE.
OrthoDBiEOG7G4QQM.
PhylomeDBiO14249.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.

Sequencei

Sequence statusi: Complete.

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

O14249-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQVKVAVRS EEAANSYTQT FGMSWRQWRQ ACSEEYAKQC EREVLHTVDF
60 70 80 90 100
IRENEKDPER LVEVVDSKIY DNDGLVHEVC VSDKATGKAN KRSIVYMHGY
110 120 130 140 150
GAGLGFYFRN MDGLTKGVTK DFNSYFVDWL GMGNSSRPPF DIKGQTASEK
160 170 180 190 200
VEETERFFTE SLETWRIGHG IEKMILVGHS MGGYLSAVYA MQYPERVEKL
210 220 230 240 250
LLVSPVAIPE NPFASNDDAE VYNSVASSAV HAVMDEPPLS NVTNEVLQTQ
260 270 280 290 300
EETTGLEPSR PSKPKNPLPR FITFLWEQNV TPFSLLRLSG PLGPKLMSFW
310 320 330 340 350
SSRRFSTLPP ETFRALHNYC YSIFRLKGSS EYALGNLLAP GAFARRCIMN
360 370 380 390 400
RLRMLKCRTI FMYGDKDWMD DVAGLEATNR LKEMNIEAEH HIISNAGHHC
410 420
YLDNPEDFNE IVLKEIRMSL RSFSSISE
Length:428
Mass (Da):48,720
Last modified:January 1, 1998 - v1
Checksum:iEDB60B76D0F6B4CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11289.1.
PIRiT39053.
RefSeqiNP_594100.1. NM_001019524.2.

Genome annotation databases

EnsemblFungiiSPAC6G10.03c.1; SPAC6G10.03c.1:pep; SPAC6G10.03c.
GeneIDi2542281.
KEGGispo:SPAC6G10.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11289.1.
PIRiT39053.
RefSeqiNP_594100.1. NM_001019524.2.

3D structure databases

ProteinModelPortaliO14249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4671756.

Protein family/group databases

ESTHERischpo-ye63. CGI-58_ABHD5_ABHD4.

Proteomic databases

MaxQBiO14249.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC6G10.03c.1; SPAC6G10.03c.1:pep; SPAC6G10.03c.
GeneIDi2542281.
KEGGispo:SPAC6G10.03c.

Organism-specific databases

EuPathDBiFungiDB:SPAC6G10.03c.
PomBaseiSPAC6G10.03c.

Phylogenomic databases

HOGENOMiHOG000211778.
InParanoidiO14249.
KOiK13535.
OMAiNTSAGHE.
OrthoDBiEOG7G4QQM.
PhylomeDBiO14249.

Enzyme and pathway databases

ReactomeiR-SPO-1483152. Hydrolysis of LPE.

Miscellaneous databases

PROiO14249.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCLD1_SCHPO
AccessioniPrimary (citable) accession number: O14249
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 100 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

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  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.