ID A0A0W1RE01_9EURY Unreviewed; 681 AA.
AC A0A0W1RE01;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Acylaminoacyl-peptidase {ECO:0000313|EMBL:KTG11663.1};
GN ORFNames=AUR64_00280 {ECO:0000313|EMBL:KTG11663.1};
OS Haloprofundus marisrubri.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloprofundus.
OX NCBI_TaxID=1514971 {ECO:0000313|EMBL:KTG11663.1, ECO:0000313|Proteomes:UP000054387};
RN [1] {ECO:0000313|EMBL:KTG11663.1, ECO:0000313|Proteomes:UP000054387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB9 {ECO:0000313|EMBL:KTG11663.1,
RC ECO:0000313|Proteomes:UP000054387};
RA Zhang G., Stingl U., Rashid M.;
RT "Haloprofundus marisrubri gen. nov., sp. nov., an extremely halophilic
RT archaeon isolated from the Discovery deep brine-seawater interface in the
RT Red Sea.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KTG11663.1}.
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DR EMBL; LOPU01000001; KTG11663.1; -; Genomic_DNA.
DR RefSeq; WP_058579948.1; NZ_LOPU01000001.1.
DR AlphaFoldDB; A0A0W1RE01; -.
DR STRING; 1514971.AUR64_00280; -.
DR OrthoDB; 25019at2157; -.
DR Proteomes; UP000054387; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR Pfam; PF07676; PD40; 2.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 442..647
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..681
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 75860 MW; EE229FB43C7FE674 CRC64;
MRHISATDYH DIAKPESPRL SPDGEQVAFV RKVPTDDQSY EATIYLVPAD GDSEPRRFTV
DEGVDSQPRW SPSGDRLAFV STRGDDDDRP QLWVVPTHGG EAQQITQVPG GVSTPEWSPD
GERIAFVQAT TEDEREEELD RSIADEEEYE RETPDPRVVD RLVYRQLARY IDGTRGHVYV
ADVESGDVER LTDGDYDHSS PAWSDETTVY YTSKRTDDPD DNVYVDVFAY DTEEGEEEHV
LQTTGWGTGL AVAGDGRVVY ARTSEDRTSM RQTDLELFDP NGEETTVLTT DIDRTVGAVG
FQWDPQEEFV YFVTPDEGDY VCRRVDASAA AIEVVAGDGH VTDISAGKDA VAFAKSEWDH
PGDVFIAHGE ETTRLTELNA DYLADLDVGE PEELRYESDD GVEVQGWVLT PPEFDESESY
PLAVEIHGGP HAMWSTAGTM WHEFQTLAAR GYVVFWSNPR GSTGYGEAFE MAIERDWGDV
TMTDVMAGAE LVADRDYVDE TNAFVTGGSF GGFMTGWIVG HTDFFAGAVA QRGVYDLSSF
YGSTDAFKLV EWDFGAKPWD EPEFLWEQSP VAHAADATTP TLVVHADNDF RVPVNNGEMF
YLFLKKNDVD TRLVRYPREG HELSRSGEPG HVVDRIERIA RWFDGYSEHH DAPRALDRGD
DGLSAGESEE ESNSSDDSSA E
//
