ID A0A074RQK3_9AGAM Unreviewed; 661 AA.
AC A0A074RQK3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Putative hydrolase {ECO:0000313|EMBL:KEP46988.1};
GN ORFNames=V565_172550 {ECO:0000313|EMBL:KEP46988.1};
OS Rhizoctonia solani 123E.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=1423351 {ECO:0000313|EMBL:KEP46988.1, ECO:0000313|Proteomes:UP000027456};
RN [1] {ECO:0000313|EMBL:KEP46988.1, ECO:0000313|Proteomes:UP000027456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=123E {ECO:0000313|EMBL:KEP46988.1,
RC ECO:0000313|Proteomes:UP000027456};
RA Cubeta M., Pakala S., Fedorova N., Thomas E., Dean R., Jabaji S., Neate S.,
RA Toda T., Tavantzis S., Vilgalys R., Bharathan N., Pakala S., Losada L.S.,
RA Zafar N., Nierman W.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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:KEP46988.1}.
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DR EMBL; AZST01000876; KEP46988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074RQK3; -.
DR STRING; 1423351.A0A074RQK3; -.
DR HOGENOM; CLU_013364_5_1_1; -.
DR OrthoDB; 50200at2759; -.
DR Proteomes; UP000027456; Unassembled WGS sequence.
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; 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:KEP46988.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000027456};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..661
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001699551"
FT TRANSMEM 589..609
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..260
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 436..540
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 661 AA; 71346 MW; D8F855E4954FE341 CRC64;
MPPLLGYLAL GTTALATSVN AQHWPLPEGY HRFAPRTAGF KWGTCVPVRT SRECSRFEVP
LDWANPAAGK ASLAVARYKA TKQPKLGTLF VNPGGPGGSG VDMVLSGNAL KISEASGGQY
DIVSWDPRGI GKTVPRAECF TTGTEENAFW EGTIPRAGLE ARGNFTDQGD IDAFYEQVDE
VDHLLTQLGQ KCVAYSPDTF QYIGTAAAVR DMIAMHDILE GSDKPVHYWG FSYGTVVGIY
LVNMFPERVG RVVLDGVVDP ELWANNPSYQ KWAVKPESTD EAFTGFLKAC ATAGPSRCAI
ANKDSSEETL RKYVSDLIDA AYDYKRRLGP RANFGSSYVR SRIFRGMYSP SSWPTLALEL
AEVANEVLDS ANHETKRSLP TSPIDMQSAV EKTSANADPA PDYAFQGVTC ADALDAGNTT
TKDVFDFLVH VTRTVSPMFG PSWGDGGFYC HRWPVRAVER YTGPWNKTLA NPILVIGNKA
DPVTPYVVAK KVADALGDSA ALIQQDDYGH TSLAMHSNCT IAALQNYFLD NKLPTHELHC
GTDQPLFPGS GLTVASLDKL HPVSNSTSTS NTSSSHGELG NALQRNCNLL IATIALAAAT
GLVLIVSLVS RIHRRYKLES AYGAYIHPGA SEKTIEESGH THGPYVLSAE IKSGGYPCIG
A
//
