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Y9086_DICDI
ID   Y9086_DICDI             Reviewed;         937 AA.
AC   Q55EQ3;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Uncharacterized abhydrolase domain-containing protein DDB_G0269086;
DE            EC=3.-.-.-;
GN   ORFNames=DDB_G0269086;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-19; 51-64 AND 171-187, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=AX2;
RA   Bienvenut W.V., Ura S., Insall R.H.;
RL   Submitted (JUL-2009) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000004; EAL73132.2; -; Genomic_DNA.
DR   RefSeq; XP_646967.2; XM_641875.2.
DR   AlphaFoldDB; Q55EQ3; -.
DR   SMR; Q55EQ3; -.
DR   STRING; 44689.DDB0252556; -.
DR   ESTHER; dicdi-y9086; Monoglyceridelipase_lysophospholip.
DR   PaxDb; Q55EQ3; -.
DR   PRIDE; Q55EQ3; -.
DR   EnsemblProtists; EAL73132; EAL73132; DDB_G0269086.
DR   GeneID; 8616659; -.
DR   KEGG; ddi:DDB_G0269086; -.
DR   dictyBase; DDB_G0269086; -.
DR   eggNOG; KOG1455; Eukaryota.
DR   HOGENOM; CLU_312958_0_0_1; -.
DR   InParanoid; Q55EQ3; -.
DR   OMA; FENIAHA; -.
DR   Reactome; R-DDI-1482883; Acyl chain remodeling of DAG and TAG.
DR   Reactome; R-DDI-426048; Arachidonate production from DAG.
DR   PRO; PR:Q55EQ3; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR022742; Hydrolase_4.
DR   Pfam; PF12146; Hydrolase_4; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Direct protein sequencing; Hydrolase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           2..937
FT                   /note="Uncharacterized abhydrolase domain-containing
FT                   protein DDB_G0269086"
FT                   /id="PRO_0000388372"
FT   REGION          281..937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          345..802
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        281..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..399
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..886
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        899..925
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        292
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000269|Ref.2"
SQ   SEQUENCE   937 AA;  103186 MW;  61DC4483C3C8A27A CRC64;
     MTSSVSNLLT SDKETLSLRT WTPKVKPIAT VTMIHGLGEH SGRYEHVFSR FAEQGIKVNA
     FDQRGHGISS GVRGHSPSLE QSLKDIQLIA STAETDVPHF IYGHSFGGCL ALHYNLKKKD
     HHPAGCIVTS PLIKPAIKVS GVKLSMGNLL GGLMPSWTIS NSIDPTLISK DSAVVNEYKQ
     DKLVHNKISL GMAKWMLQRS EQLIDLAPQF DTPLLLVHAN DDKITCPKAS QQFYDRVPST
     VDKTLKLWEN MYHEVHNEFA KEEFVTYILE WIKERIENAK NESPSSNINT TTTSTTTTTT
     TTTSSPVVEE SKPVVEESKP VVEESKPVVE ESKPVVEESK PEPVVDDSKE KEEKERLEKE
     EAAAKLEKER LEKEEAERVA KEAEEKRIKD EKEAQENLEK QQQEAAAAAQ AEKERLEKEE
     ADKLEKERLE AEAAAAAQAE KERLEAEAAA AAQAEKERLE AEAAAAVQAE KERLEKEEAD
     RLEKEKLEAE AAAATQAEKE RLEAEAAAAA QAEKERLEKE ETERLEKEKL EAEAAAAAQA
     EKEKLEAEAA AAAQAEKERL EAEAAAAAQA EKERLEAEAA AAAQAEKERL EAEAAAAAQA
     EKEEAERLEK EKLEAEAAAA QAEKERLEAE AAAAAQAEKE RLEAEAAAAA QAEKEKLEAE
     AEAAAQAEKE RLEKEEAERL EKEKLEAEAA AAQAEKERLE AEAAAAAQAE KEKLEAEAAA
     AQAEKERLEA EAAAAAQAEK ERLEKEETER LEKERLEAEA AAAQAEKERL EAEAAAAAQA
     EKERLEAEAA AEKAAEETKV EEPVQEETKV EEPVQEEIKV EEPVQEETKV EEPVQEETKV
     EEPVQEETKV EEPVQEETKV EEPVQEETKV EESTTEQAKP TETENKEETE EGEEVDEASN
     TTTEQTTTNA NQPKKPNNNN NNNKGKGKKG KGKGGRK
 
 
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