ID A0A0M1JVL1_9CYAN Unreviewed; 1316 AA.
AC A0A0M1JVL1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Thiazoline oxidase {ECO:0000313|EMBL:KOR36800.1};
GN ORFNames=AM228_10440 {ECO:0000313|EMBL:KOR36800.1};
OS Planktothricoides sp. SR001.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothricoides.
OX NCBI_TaxID=1705388 {ECO:0000313|EMBL:KOR36800.1, ECO:0000313|Proteomes:UP000037054};
RN [1] {ECO:0000313|Proteomes:UP000037054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR001 {ECO:0000313|Proteomes:UP000037054};
RA Tan B., Te S.H., Thompson J., Gin K.;
RT "Draft Genome of Planktothricoides sp. SR001.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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:KOR36800.1}.
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DR EMBL; LIUQ01000014; KOR36800.1; -; Genomic_DNA.
DR RefSeq; WP_054466072.1; NZ_LIUQ01000014.1.
DR STRING; 1705388.AM228_10440; -.
DR PATRIC; fig|1705388.3.peg.6603; -.
DR OrthoDB; 9801593at2; -.
DR Proteomes; UP000037054; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02142; McbC_SagB-like_oxidoreductase; 1.
DR CDD; cd07476; Peptidases_S8_thiazoline_oxidase_subtilisin-like_protease; 1.
DR Gene3D; 3.40.109.10; NADH Oxidase; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR InterPro; IPR040636; PatG_C.
DR InterPro; IPR040483; PatG_dom.
DR InterPro; IPR034056; Pep_S8_PatG/PatA-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR023830; Peptidase_S8A_PatG.
DR InterPro; IPR020051; SagB-type_dehydrogenase.
DR NCBIfam; TIGR03605; antibiot_sagB; 1.
DR NCBIfam; TIGR03895; protease_PatA; 1.
DR PANTHER; PTHR43745; NITROREDUCTASE MJ1384-RELATED; 1.
DR PANTHER; PTHR43745:SF2; NITROREDUCTASE MJ1384-RELATED; 1.
DR Pfam; PF00881; Nitroreductase; 1.
DR Pfam; PF18065; PatG_C; 1.
DR Pfam; PF18047; PatG_D; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR SUPFAM; SSF55469; FMN-dependent nitroreductase-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Reference proteome {ECO:0000313|Proteomes:UP000037054};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01240}.
FT DOMAIN 270..463
FT /note="Nitroreductase"
FT /evidence="ECO:0000259|Pfam:PF00881"
FT DOMAIN 722..932
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 1037..1146
FT /note="PatG"
FT /evidence="ECO:0000259|Pfam:PF18047"
FT DOMAIN 1200..1307
FT /note="PatG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18065"
FT REGION 511..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 592
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 732
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 895
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1316 AA; 143990 MW; 41FA445C6A3D3B32 CRC64;
MSLHSFAVSL NPSVQVSSTE SQYTLGSVEA DPTALLTLAT TPGITMVLDS LKAGSSTPEL
LVQKLAELEG QAVGEQFGQM LKQLDERGWL SYTVLPLAVA IPMVDSAELN LAQPYWTQTR
VALSRFAYQR PYEGTMVLES PLSKFRVKLL DWRASAILTQ LAQPQSLGAV TPPPYLGAET
AYQFLNLLWV AGFLTADPEP PSLQLWDFHN LLFHSRSRGG RHDYPLQDTN IEQWSDFPVV
KPPMSDRIVP LPHPNLGALK YNDATLTEAI ERRKSIRKCD EAHPVTVEQL SELLYRTARI
KDIRSVEEYF GENWREILDF DADIDYGELA SRPYPGGGAM YELEIYPVVR RCEGLDTGLY
HYDPLNHQLE QIIGAEDNIF ALSGYKLPNN LPSNLGTPQV LLVITARFGR LFRKYRSLAY
SLVLKHVGVL QQNFYLVATN MGLAPCAWGY GDSDGFGQAA GLDYVEESAV GEFTLSSLPK
RDLRASGVEL AQDVDASEES GEVGISVSKA ELTRSETEPD PADVGFLSSI QPTETLSSSD
EGLREAAETV SKAVRSEALE TSMETTDAAV SGRETESVNL SALSESTTEV MDSKVSESQA
ESDIIPDEIE SATISASEVE SSASPALVAL HPHDLDDRVP GLAYLRNQTL GDPRITIVVL
EGNPDHSLSC FQSPEISKVF PYWHDTPEPF SAEDYAKYRA IDDSDRTKQE KEEALKAAFP
EPQIVRLKVD DHTCHVTSII VGQENTPSAG IAPHCRLINL PVNSTGIPEE SIGILNLARA
FEQALNLGAN IIHCGFCRPT QTCEGEELLA KAVQKCLDNN ILIVGPAGNG LGEYWCLPGV
LPGVLPVGAM DLGSPPAHYS NWGRNYTQEG IMAPGDDIWG AQLGSEKPKL RTGTSGSAPI
VTGIAALLMS LQLQQGKPID AEAVRMALLN TAIPCDPKRV EEPERCMRGF VNIAGAMEVL
FGRPSVTISF AGDQVTRTEW AGYALPTPTA MSASSAPSSA VVAAIAENAV TDGAIATVQE
SAEPTNIETS TAFAGDVYAL GTLGYDFGDE ARRDTFKQLM PPFELDGIMV PPDPYDARQV
VEHLDRNPDE ARSLIWTLNL EQNTLYALEP KGPFASDVYE IFLQMLAGQL EPETSDEFVE
RISVAARRTN RTVELFSGEV VPVVTVHDLR GMYGWTVNAL INPALASVRN LEPDREPIVR
EAISAFLNRV YYDLHNLGQT SRDRALNFAT TNIFQAVSVF AEAIASGRQL DTISVEKSPY
CRIRSDCWDV LLTFFDPDSS RRSRRVFRFT LDVAANLPVT IGSIKRWSIP GQSNSQ
//
