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Database: UniProt
Entry: L1JTT6_GUITC
LinkDB: L1JTT6_GUITC
Original site: L1JTT6_GUITC 
ID   L1JTT6_GUITC            Unreviewed;       855 AA.
AC   L1JTT6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Acylphosphatase-like domain-containing protein {ECO:0000259|PROSITE:PS51160};
GN   ORFNames=GUITHDRAFT_102761 {ECO:0000313|EMBL:EKX51493.1};
OS   Guillardia theta (strain CCMP2712) (Cryptophyte).
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX51493.1};
RN   [1] {ECO:0000313|EMBL:EKX51493.1, ECO:0000313|Proteomes:UP000011087}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX51493.1,
RC   ECO:0000313|Proteomes:UP000011087};
RX   PubMed=23201678; DOI=10.1038/nature11681;
RG   DOE Joint Genome Institute;
RA   Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S.,
RA   Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A.,
RA   Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA   Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA   Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA   Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F.,
RA   Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G.,
RA   Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A.,
RA   Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W.,
RA   Sarai C., Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA   Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA   Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA   Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RT   "Algal genomes reveal evolutionary mosaicism and the fate of
RT   nucleomorphs.";
RL   Nature 492:59-65(2012).
RN   [2] {ECO:0000313|Proteomes:UP000011087}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP2712 {ECO:0000313|Proteomes:UP000011087};
RA   Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M.,
RA   Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F.,
RA   Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA   Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA   Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA   Durnford D.G., Fast N.M., Green B.R., Grisdale C., Hempe F., Henrissat B.,
RA   Hoppner M.P., Ishida K.-I., Kim E., Koreny L., Kroth P.G., Liu Y.,
RA   Malik S.-B., Maier U.G., McRose D., Mock T., Neilson J.A., Onodera N.T.,
RA   Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W., Sarai C.,
RA   Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA   Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA   Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA   Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblProtists:EKX51493}
RP   IDENTIFICATION.
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC       family. {ECO:0000256|ARBA:ARBA00006499}.
CC   -!- SIMILARITY: Belongs to the acylphosphatase family.
CC       {ECO:0000256|RuleBase:RU004168}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00520}.
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DR   EMBL; JH992975; EKX51493.1; -; Genomic_DNA.
DR   RefSeq; XP_005838473.1; XM_005838416.1.
DR   AlphaFoldDB; L1JTT6; -.
DR   STRING; 905079.L1JTT6; -.
DR   PaxDb; 55529-EKX51493; -.
DR   EnsemblProtists; EKX51493; EKX51493; GUITHDRAFT_102761.
DR   GeneID; 17308208; -.
DR   KEGG; gtt:GUITHDRAFT_102761; -.
DR   eggNOG; KOG2112; Eukaryota.
DR   HOGENOM; CLU_334182_0_0_1; -.
DR   OrthoDB; 4670340at2759; -.
DR   Proteomes; UP000011087; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.100; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR003140; PLipase/COase/thioEstase.
DR   PANTHER; PTHR10655; LYSOPHOSPHOLIPASE-RELATED; 1.
DR   PANTHER; PTHR10655:SF17; PALMITOYL-PROTEIN HYDROLASE; 1.
DR   Pfam; PF02230; Abhydrolase_2; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011087};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..855
FT                   /note="Acylphosphatase-like domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008771754"
FT   DOMAIN          765..854
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   REGION          101..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..733
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   855 AA;  94286 MW;  E3B224D5C5D13470 CRC64;
     MKMGRRWAGT AMLWLHWNIA GLTHSECYVH QASCFVSSGV ATCAGRSKFV SLNPKLSGGG
     SLYLQKVKGL GCSQSRASCR GLLVLSLALS SNETDSVLLA PQNEGIQQAK SRSPESWPSG
     GKKPLFRARR RKSQRQEIPK YGKAMIVSPS QEATGVVIWL DGLDYGDGPA RWSKRLKRLG
     LDWCRLVLPS GYVEGEEKKS FWKRERRAWF DETSDEGLYS TLQYIQTLVS VEMKKGIPSD
     RIMIGGLGQG ATVAMLAGML LSARLAGVIC IGGQIPETIA GLPSAESFST PFFFFRSPDD
     FLAQEAYETL SHLGMRTEVF PPDFQTGGFR MSLSRWTRRW RPWGSRCREA VEDFVLRALP
     EDVEAIPEID LMLQDGKARA GSGSNQGIGL ARFQRFVPLW QLRPADIKDM SLVCMQYHGI
     RYDDVSNERE ARERLFAAAK LAGMKRNNAR AEKDFSVGTD GYDDGEAEGY QDPSRVVQNI
     ADRAWFMGKD IAQGLGSAVQ DEEIRRDIFQ KAWNAGATAA KFATEAATDE DARSRAAESF
     VRAGKSAADY ARASFSNPEA ARKIAETAWE AGRAAADYVQ TTGRDDNVSF LSAEEWYDRY
     NRTGSADVYG ESVDYSLEEE RQPRGVQENI YYKDDPLGTD DYRTAVDSAA MGIGDAARKG
     VGWINSIFQD PSDLPGAGRG FDQQQIPRQP PPRPYQPPRT VTYPTQSYST PDSTQFSFRQ
     DPVSSSIRTD IAASGSRSWP RPAPDPLQER KSGDQAIPGS GPLLCFNFKI FGMIEQRSFG
     AAIAYKASEL GISGSCTMTG GEVEGKVEGK FEQAEKFIQW LCSVGAPGSV IEGAIIENQT
     RGEQRQFQSF DLSNS
//
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