ID   A0A1Q7WQU0_9CHLR        Unreviewed;       696 AA.
AC   A0A1Q7WQU0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Serine aminopeptidase S33 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AUG45_08180 {ECO:0000313|EMBL:OLE33130.1};
OS   Ktedonobacter sp. 13_1_20CM_3_54_15.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Ktedonobacteraceae; Ktedonobacter.
OX   NCBI_TaxID=1805224 {ECO:0000313|EMBL:OLE33130.1, ECO:0000313|Proteomes:UP000186882};
RN   [1] {ECO:0000313|EMBL:OLE33130.1, ECO:0000313|Proteomes:UP000186882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. FUS2 hydrolase
CC       family. {ECO:0000256|ARBA:ARBA00038115}.
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:OLE33130.1}.
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DR   EMBL; MNJJ01000148; OLE33130.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7WQU0; -.
DR   Proteomes; UP000186882; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000383; Xaa-Pro-like_dom.
DR   PANTHER; PTHR22946:SF12; CONIDIAL PIGMENT BIOSYNTHESIS PROTEIN AYG1 (AFU_ORTHOLOGUE AFUA_2G17550); 1.
DR   PANTHER; PTHR22946; UNCHARACTERIZED; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF02129; Peptidase_S15; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 2.
PE   3: Inferred from homology;
FT   DOMAIN          148..344
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          431..532
FT                   /note="Xaa-Pro dipeptidyl-peptidase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02129"
SQ   SEQUENCE   696 AA;  77739 MW;  7C25ED47BD7AFF35 CRC64;
     MTKNIPLENR LASFPVGYYT LHPDASINFQ MNRFYDWVGD PSMLTEMREA GAFAQDYPTF
     TQIFLELGEK TIAEGNIYKG AAYLRMAEFF LFADDPRKLP TLRRIIKLLL LHHQVTEEQH
     FRIPYESAWL SAYRFTPPQP KGTLVAFGGF DSYCEEWLPA AFTFRDAGYD TIVFDGPGQG
     LTLEEAGLTM IPEWEKPVKA VLDFFQLDDV TLVGESLGGE LVIRAAAFEP RVQRVVAYDI
     LTDVLETNLR NFPASVGEQV RGWLESGNEN ALNAFFEQAR SQSLLLDWML KQANHVTGTQ
     TVFEALRHFQ RFETASISPK VTQDVLLLAG SEDHYVPIHQ LPDQIATLTH ARSLTARVFT
     PYEQAQNHVQ VGNYGLALRT MIEWIESLQV RGVVLANRDK KERTMIIDKR DVTFKSGDTF
     AAGWFFLPEH ATSETRVPAV AMAHGLGAVK EMYLEPFARR FAEAGIAVLV FDYRSFGASG
     GEPRQRLFPR DQIEDYRSAL TWLSLQPEID ADRLGVWGSS FSGGHVLHVA AYAEQFAALE
     QLTVQERVRH ATEGGEVYIP DIGLPGQGFA LQTDQESYDF ARGAQATIAP SWRNEVTMSS
     LDAILEHAPA KSIELIAPRP LLMILAKDDP ISPPDSIRAA FARAGEPKRL LEVEGGHYSV
     YPWSKGQSAD QASQAATEWF AEHLVASTAM GNGEVG
//