ID A3FQF8_CRYPI Unreviewed; 729 AA.
AC A3FQF8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Carboxylesterase, putative {ECO:0000313|EMBL:EAZ51357.1};
GN ORFNames=cgd1_3290 {ECO:0000313|EMBL:EAZ51357.1};
OS Cryptosporidium parvum (strain Iowa II).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=353152 {ECO:0000313|EMBL:EAZ51357.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAZ51357.1, ECO:0000313|Proteomes:UP000006726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX PubMed=15044751; DOI=10.1126/science.1094786;
RA Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA Anantharaman V., Aravind L., Kapur V.;
RT "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL Science 304:441-445(2004).
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC family. {ECO:0000256|ARBA:ARBA00006499}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAZ51357.1}.
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DR EMBL; AAEE01000006; EAZ51357.1; -; Genomic_DNA.
DR RefSeq; XP_001388180.1; XM_001388143.1.
DR AlphaFoldDB; A3FQF8; -.
DR STRING; 353152.A3FQF8; -.
DR EnsemblProtists; EAZ51357; EAZ51357; cgd1_3290.
DR GeneID; 3371389; -.
DR KEGG; cpv:cgd1_3290; -.
DR VEuPathDB; CryptoDB:cgd1_3290; -.
DR InParanoid; A3FQF8; -.
DR OMA; EDNCAKI; -.
DR OrthoDB; 4670340at2759; -.
DR Proteomes; UP000006726; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
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 SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006726};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..268
FT /note="Phospholipase/carboxylesterase/thioesterase"
FT /evidence="ECO:0000259|Pfam:PF02230"
FT REGION 381..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 83368 MW; 093BAA25DA4C9135 CRC64;
MLSLEIQRKI PRIYVIFIIF IIFFSNVECL LKKANQTVKF KKGDTNGGYG LNFTPSNYQN
VIVWLHGLCS SAVEWERFLI LVNKKDFLPN TKWIIPTSKY RKITAIYGNE CPAWFNITSF
SPTENIEDIN GILESVKRIR NIIKSEIDLG IDQSRIFLIG FSQGSAMALI TSMIMRDITI
GGVIGVSGWI PMISHLSLGK DSPLNNEIFD FNVSDEKKQN TRVYIFHGSK DKLIPFHIFL
QTSIFMSTEL EIQNINQRMY YNIGHTITAM QGIHIMYEIS KMIDSENIHE ELTAVQLSTL
SNSSYSMILK VTDPMDCNYT YYKFMPCNPN QQGKLLCNNI NCNCTDMLYF YDKSKFFENL
NHRDFGQNKY PYAIIQAIPS ENNKKKRNNN NNSNNKEDES QDFELTNIKI NEKDNENVST
LLSNINVNGN ESIKDNFVSG NDINQAIMND DNDNDDDNSN NNDNSDLKDQ ISKNSHNSLR
RRNTSLNNIS QRYLMSINNE KNDNSSDSSS IVDYHDKLYI SLRGNGSEDI ENDNDEYVDK
QERDQEDQVK HMDENEDKQK EEKKQKQEKN VREEEGKGRE EEEGKGKGKE EGKEEGKGEE
GEQEGEEGEE GEEKGERGAG GKEEEQQEMN ITSTLASPVD QIISDELNTS NKIFSTKISH
YSKTPLKVKH YIVSDKDNSK EGEDTNMGEN GNGIFNIGKY IDSLYNQSRD SINANNTIIS
NIYESEVGN
//