ID A0A165GZ68_9BASI Unreviewed; 606 AA.
AC A0A165GZ68;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Alpha/beta-hydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CALCODRAFT_482133 {ECO:0000313|EMBL:KZT58667.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT58667.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT58667.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT58667.1,
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV423948; KZT58667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165GZ68; -.
DR STRING; 1353952.A0A165GZ68; -.
DR InParanoid; A0A165GZ68; -.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT DOMAIN 126..310
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 468..566
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 606 AA; 66128 MW; 6E149418A274EA2E CRC64;
MPGNEKQSAP SVEVAPSHPQ RTRKLGVVIV SALLVAVYLF QEQLLASFSS TFVSGPTNGE
GDVENWTQLA PGTVKWWDCR GENGAIPGAE CGYIIVPTDY FNEYAGVTKI ALGRYKAKRR
PYHGMVLVNP GGPGGPGKPL GAVLGSMIQT AVTSETYDIV GFDPRGIGET EPATRCFTDP
RQQMLLKLNT VLNKGFNVGG NLSAPELKEG LLRQQIEADG IYRTQFALCA KNMGEKARYM
GTSTVVRDID FMTKTLAGED ALINYWGGSY GSILGQYLVN MLPDRIGRVA IDGIADAVAW
SNEPNYKWYR TWLSSTEAAY DIFLNLCAKA GDYDCPLTLF KNEEPYYIRK RLEEWIDSLY
EKPLIVDDPE FPGVVTAGMA RTFLLGTLEA PRTWPTRSAI LAAAIAGEGK LLLQQTNVFG
EAADMSRQAV SCNDAVRLTP QTAASHEEVL DEYVHVLKSV TKLTMAVVSS EPDSGCQYWP
VDPPERFSGP WNQTLRNPIV VFSNTADPVT PISSARLVKA LLGDSAVLAL QNAPGHCTLS
LPSICTLRKA RAFFEYGALP EDGHVCEISV QPFPDDDELH AFSGEDAAAL EAGMRLGEYI
QAVRRM
//
