ID   A0A401Y4A2_9ACTN        Unreviewed;       952 AA.
AC   A0A401Y4A2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=F5/8 type C domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=NLS1_14610 {ECO:0000313|EMBL:GCD89455.1};
OS   Nocardioides sp. LS1.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1027620 {ECO:0000313|EMBL:GCD89455.1, ECO:0000313|Proteomes:UP000288271};
RN   [1] {ECO:0000313|EMBL:GCD89455.1, ECO:0000313|Proteomes:UP000288271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS1 {ECO:0000313|EMBL:GCD89455.1,
RC   ECO:0000313|Proteomes:UP000288271};
RA   Morimura H., Sato I., Uesaka K.;
RT   "Draft Genome sequence of the deoxynivalenol-degrading actinomycete
RT   Nocardioides sp. strain LS1, isolated from wheat leaves in Japan.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family.
CC       {ECO:0000256|ARBA:ARBA00006006}.
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:GCD89455.1}.
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DR   EMBL; BIFF01000002; GCD89455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401Y4A2; -.
DR   Proteomes; UP000288271; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 3.10.450.490; -; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001842; Peptidase_M36.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR   PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF02128; Peptidase_M36; 1.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000288271};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..952
FT                   /note="F5/8 type C domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019301022"
FT   DOMAIN          144..192
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          805..921
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|Pfam:PF00754"
SQ   SEQUENCE   952 AA;  99666 MW;  2257FCB8ECD7203F CRC64;
     MIHAKKTWVA SAAVATTALA VTMLGLPSQA AIQQPTSRLA SSSVRHDAAR TPGYLDARRL
     GNKAIVRAER QRLSGLSKAD RAWQRSLGSQ ALLDFDPLTG TVRNVGRLDG FLTGRSTAPA
     RSIALAYVRQ HASALGLDAA DLQTLRFRKD YVDDMGLHHL SWQQYAAGRP VFGNGLKVQV
     TRDGRVLAVQ GSPVHGLQAL AAAAGTGSLD AAAARSTAAR NVGGTTAAAG DQASPVWFLT
     RSGLRAGWST YVHAGGGAYQ HVVDATSGAV LFRRSTTDSA DGDSYVYDNY PGAAKGGKPK
     VVNFVGRGWL KKSATTLAGN SVVAWADIND NNQRDNNEKT PVPGTSSGAQ FSLVHFGSTA
     SKFCSSHYVC TWNPKKKDSW RTNMNADVAQ AFYLASNFHD YLTKAPISFT SAAGNFETSD
     HDPVKLNALD GADTGNGFPD GNHIDNANMD TPPDGQSPTM QMYLFHFPGA SDNQEPFLPT
     SSAFEADVLY HEYTHGLSNR LVVDAGGVST LNDIQPGSMG EAWSDYYAMD YLVKKGFQPD
     TSKSGELLVG KYVSVGQPLI RTMDVDCAVG STAKGCTRID GSRGGYTYGD FATVIPGAEV
     HASGEIWGQT LWDLRKKLGP AVADRLITRA MSISADDPSF LDMRNAIVQA DNVAYSGSHN
     AAIWNVFAHR GMGFFAGAIN GADDDPAEDF NTPPTGPADQ TISGVVTDPT TGDPVAGALV
     AVAGQGDAAT DTTAADGSYS IGGLYAGTYQ KVVAFGPGYF PQAKAVDSTS SAPTNFLITR
     DFASTSGGAE IVDFNGGDYT AYGCGPGGLI DLSLGTGWGS TAGNDQGDPT GTFVPKFAVV
     DMHTNVNITS FGVDPNATCG DDPTAATKGY RIETSVDGVT WTTAAQGTFT SADNGTLNSI
     APTAGTTGVR YVKFWILSNQ TPSFGSSCPS GPYSGCSFAD VSEMAVFGTE AP
//