ID A0A139A1T3_GONPJ Unreviewed; 577 AA.
AC A0A139A1T3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Alpha/beta-hydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=M427DRAFT_159014 {ECO:0000313|EMBL:KXS10649.1};
OS Gonapodya prolifera (strain JEL478) (Monoblepharis prolifera).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Monoblepharidomycetes; Monoblepharidales;
OC Gonapodyaceae; Gonapodya.
OX NCBI_TaxID=1344416 {ECO:0000313|EMBL:KXS10649.1, ECO:0000313|Proteomes:UP000070544};
RN [1] {ECO:0000313|EMBL:KXS10649.1, ECO:0000313|Proteomes:UP000070544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL478 {ECO:0000313|EMBL:KXS10649.1,
RC ECO:0000313|Proteomes:UP000070544};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; KQ965819; KXS10649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139A1T3; -.
DR STRING; 1344416.A0A139A1T3; -.
DR OMA; LHWTPCP; -.
DR OrthoDB; 2407664at2759; -.
DR Proteomes; UP000070544; Unassembled WGS sequence.
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; IPR000073; AB_hydrolase_1.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF22; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000070544};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..577
FT /note="Alpha/beta-hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007295883"
FT DOMAIN 78..259
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 455..525
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 577 AA; 59912 MW; 47E810D37E7740E8 CRC64;
MASWTAIVLF LSAALASTSQ FTTAAITPSL STWTSCGSGL DCAKLTVPLE YADASSHETA
TIPLVRFNAT AAVRKGSILV NPGGPGASGV AFVSAGAGQS ISVITGGEYD IIGFDPRGVG
GAEPKFACFA NAGDEYDFNS AFPAGANLWI GAFANATERK AVASSMKDFD TAAANLAAAC
LKQNSKALFT SSASYVVRDM ASIVDALDGP GAKLNYWGFS YGPIFGVEFI QTFPNRVGRI
VLDGVYDAAA NAQTYVSQLP NDQISVRNAI KDFAQLCFEA GPSACTFAGA STSAADIEAR
FDALHKTAFR TPVVASGVPI SSSILSSFLW NFFTVPPTWP LVSALIAGLE AGDASALLNV
LVTSAGSAPA NRSAPAVGLR SLSSMGLTCV DNAPTNLVPL MYVQNLVANL TVAQQTPWLG
ADLGVLSFCR NFGSKRPKLP NVGVSKITDT DCLLAEHNTT ILIVNGIHDS STPLKSAQHL
RTMLPRSSRI ATRGGPGHTT ISFPSLGLAK TVANYFRTGA LPPDGAFYPS DMVVFPKNTT
LSVAPSTPTF NGTSYSDSDR AILNAAYGIV LAFIAIA
//
