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Database: UniProt
Entry: A0A1H9VZX8_9PSEU
LinkDB: A0A1H9VZX8_9PSEU
Original site: A0A1H9VZX8_9PSEU 
ID   A0A1H9VZX8_9PSEU        Unreviewed;      1501 AA.
AC   A0A1H9VZX8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Subtilase family protein {ECO:0000313|EMBL:SES27256.1};
GN   ORFNames=SAMN04488000_12030 {ECO:0000313|EMBL:SES27256.1};
OS   Lentzea albida.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=65499 {ECO:0000313|EMBL:SES27256.1, ECO:0000313|Proteomes:UP000199503};
RN   [1] {ECO:0000313|EMBL:SES27256.1, ECO:0000313|Proteomes:UP000199503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44437 {ECO:0000313|EMBL:SES27256.1,
RC   ECO:0000313|Proteomes:UP000199503};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240}.
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DR   EMBL; FOFV01000020; SES27256.1; -; Genomic_DNA.
DR   STRING; 65499.SAMN04488000_12030; -.
DR   OrthoDB; 3751446at2; -.
DR   Proteomes; UP000199503; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00161; RICIN; 4.
DR   Gene3D; 2.80.10.50; -; 3.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR   InterPro; IPR010496; 3-keto-disaccharide_hydrolase.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF06439; 3keto-disac_hyd; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 3.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00458; RICIN; 3.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 3.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 3.
DR   PROSITE; PS51892; SUBTILASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1501
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011755374"
FT   DOMAIN          1125..1244
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   DOMAIN          1248..1371
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   DOMAIN          1377..1497
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   REGION          342..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..370
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        150
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        188
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        474
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1501 AA;  155677 MW;  1E1313DBC61BD8AF CRC64;
     MRRTRRVAVA AACLTLGVAG AVSPVQAAPG NGARPDVVNS ARHVVGSQDV AKDAQGRMIV
     YVEGAQESSL RAAVAKAGGV VADADAGRVK AVVPQDKLDV VASQAGVTEV RLPDRAVPMG
     VTSEGVVPSR ANEWISAGKT GAGVKVGIID VGFGDLAASQ AAGELPATGP QLAYRDAGCL
     DATTKSVHGT NVAETVHDMA PGAELYLACV EDSVSFSAAA DWMDQQGVKI ISSAVGFLSP
     SGGRGDGSGP QDSPADVVKR SRAKGVLWNV AAGNLARTHF AGTPVVTGDT RWVKFRNDTQ
     FNQIILSANQ SATISIRWDA WPTTNEDLDL YVMDQMIAPD APNAPAPRKV SLRSQKDAQG
     GLSPTEEVQI SNTAASSRPF YVYVKNNNAR FTTPFELFVA GPEQIQYWTE AGSITEPATS
     PHVLAVGATQ PGSGQVEDFS GRGPTIDGRT KPDIIGFDRT STSMWPAPDF RGTSAATAHV
     AGAAALLKSA NPALDATQLQ SALQGRAVRP ANADPNTWGS GVLNVGAATN VPTAPAGSKY
     TADPVPTRTV AGQVFAAGET RTIPFSSLPS ESTAVAITVS VRANQDSIGE FGLEIAQGDP
     AVLGGKVPTI YGRGENSWTW TTMTLFAPLD GARSIKMRNR GNGPVVVVVE RLGYFHPNGV
     STFTALKEPA RVLDTRGFPV VTGGSTRKTP LIGANDTEKT VDVPVRGVGQ VPTTATSVVV
     NLTGFEATQV QFLVVHAGGT SVPVTTSLVL GPGERRSNLV VVPIGADGKI RLTNTSSGYT
     AGAALDVVGW FADGDSGARY VPFGDVGRVA DTATGNGVPK ALIGHGQSAA FQVTGTAGIP
     DSATTAAMVL TGRDDNLGTE LSAVSKEVGW LPASQVSTRK AEPASGLALV PLGSSGEVRV
     RNERGQTKLS ADVTGYFVGS AKVTGPASDT CVTAADEPGF TSILDGRSES DLAGWRSTGT
     KMTADRCEAV TANTSDVNWY TAHTYNSDYT LKVDWKATTN NSDSGVFVGI TNPGTNAAAP
     GQSGYEINIG PTGATGTMQT GGVVGIKPPL TTTAVKPVNQ WNTFKFVFRW NTVTVYLNDT
     LVNEHGFSDA TAASRNTFIG LQNDNTGDPV RFRNVRIKRD TPVLSGVVKN SGGRCLDMFN
     ADPNQSVVEL FTCHGGFAQV WTMHGGLVLA GGRCLRAAGT TDGTEAVLGG CAGDDFQQWT
     LRGDNRLVHR QSGRCLTPRS NTDLARLELR ACNLGDASQT WVVPEANGGR VGQIVAPVGK
     CIDIFNSDVT QNRIGVHPCH GGLNQSWVMT GDGTVRGSGK CLNIASNTPG EGSAVNVADC
     NGSQHQQWLA QQEGTLVNPL TGRCLASAGG EFAPLLISTC NGTPAQSFRL SSQVVSVGQV
     VGLATKCVDV FGGTTSGKVN LHTCVGSSAH NWWSTGDGTL RALGSCLDIQ STANAALTVL
     AGCRGDGGQI WSARHDGTIV NPMSNRCLDV FGALPDDGTQ IIIGDCHGGP NQRWATPVNP
     S
//
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