ID A0A165K134_9BASI Unreviewed; 552 AA.
AC A0A165K134;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Alpha/beta-hydrolase {ECO:0000313|EMBL:KZT62527.1};
GN ORFNames=CALCODRAFT_426150 {ECO:0000313|EMBL:KZT62527.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT62527.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT62527.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT62527.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; KV423916; KZT62527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165K134; -.
DR STRING; 1353952.A0A165K134; -.
DR InParanoid; A0A165K134; -.
DR OrthoDB; 50200at2759; -.
DR Proteomes; UP000076842; 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:SF29; 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, ECO:0000313|EMBL:KZT62527.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT DOMAIN 55..234
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 408..510
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 552 AA; 59698 MW; 0114974C5BD8ED48 CRC64;
MGLGIPWTPC ADLTEFDCAY FSVPMDYADP QPSEHVSLAL RRWPSTAPKK DYMGTLFINP
GGPGGSGTDT VVTIGPLLGK ILKGRYDIMS WDPRGVNMTT PPLDCYPTEY DEFVAEQMST
QIGLPFQARA EGGAAAELAL MKKTDAYYLS GLGSCLKNGN AKMLASLSTA YNVRDMVRML
EALGEDERGL QYWGFSYGTI LGATFAAMFP DKVHRVLLDG VSSARLYTRD MFDWGRSGMD
DTNKVWQGFL SSCAKAGPER CALAKGDDTA ESILARFDTM VESLIEQPLP VPWGGVTSGI
ITASDVIQGV FRALYTPKQW PKLATALAAL EAGDPYPLAA DLNLPAPQGG RSDPLDNVFK
RFMIKSPSSI TTEAIMCSDT DQSVAHAGAP DAASFAEYSR ELRNLSIAGE NWAYWVGKCR
VWNITATEAY RGPWTVEEGF PLMFLGVTAD PVTPLSAAKD MSAGFGNTSA TLLIQDGFGH
CSLAHPSLCT AKTVRAYFLE GKVPEYGTVC SSPEEYLFPE GGKTDSLLSA MGAEDRELLQ
AWEKLGEGVV AW
//
