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Database: UniProt
Entry: A0A0D2JXB7_9CHLO
LinkDB: A0A0D2JXB7_9CHLO
Original site: A0A0D2JXB7_9CHLO 
ID   A0A0D2JXB7_9CHLO        Unreviewed;       844 AA.
AC   A0A0D2JXB7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN   ORFNames=MNEG_4698 {ECO:0000313|EMBL:KIZ03258.1};
OS   Monoraphidium neglectum.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX   NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ03258.1, ECO:0000313|Proteomes:UP000054498};
RN   [1] {ECO:0000313|EMBL:KIZ03258.1, ECO:0000313|Proteomes:UP000054498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ03258.1,
RC   ECO:0000313|Proteomes:UP000054498};
RX   PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA   Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA   Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA   Mussgnug J.H., Kruse O.;
RT   "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT   neglectum from its genome sequence reveals characteristics suitable for
RT   biofuel production.";
RL   BMC Genomics 14:926-926(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; KK100884; KIZ03258.1; -; Genomic_DNA.
DR   RefSeq; XP_013902277.1; XM_014046823.1.
DR   AlphaFoldDB; A0A0D2JXB7; -.
DR   GeneID; 25737575; -.
DR   KEGG; mng:MNEG_4698; -.
DR   Proteomes; UP000054498; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1370.40; -; 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054498};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          575..722
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          733..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  85655 MW;  9D1F41D3C7D4F376 CRC64;
     MHRRTPERAP QRHPAADADA TQQQARLCGA LLRALEGGAP ATAGAALDGG AWAAALEAPD
     VAQQRLACLR AEEAGLLRQL DELMGDPALA PRVLLDVADI GDALGPTVSS SSASAAGGSD
     GDGSGSGAGG GRSTPDDAPA ARTVVLTRAA TAALLARAPG AAARRAAHEA GLVPRLAAGG
     AALSRLALCR DGMAQLCGAG SFPELCCARL AAPGPVEVAG FLQEAAEKLR PLAERQVERL
     LARAQRLPDE VAPGASASGL AVAERKGGGT AAAVRQEDPV PARVPALAPP FEPWDWERLF
     EAECAPDAAT LAALAPHLHL GPVLLGFSTL LRRLLGIALL PRPPAGGGGG GDGGGGELWR
     PGVWVVAMLH EQRGHLGTLY VDPGAGYGTR VLRHGPWRWA RRGRSSGSGG GGGGGRCGAG
     GDGDLSPNEL WAAAIAHLGP VGGAVGPAAA AGSPGSTRVL SWLQAHAASA PGVSIGLSSV
     PRGPQGGSAP GSTNGSAAPA DGVLSLSALW ELGHELGHAV HLLLSSSNLG PPVGPGGSFE
     EELEKQQQEQ RQGQQREGQQ QQQQEQQQQQ QQEQARPRSP HLSGRFLAPD LLELPSALFE
     RILLEPAALA TICSHRETGE PAPAELAAAL ARHYRWRYGS PLAVQDKVCA ALAEQLLGLF
     PEDAATQDTW AQTWAEFSST PPWARATSRQ LALMPVVAAH RGTYFSYITC WAWAAHMWRG
     TAATLLSPAS GGDGGGGGSG GGGGSGGGGG SGSAAGEGQG AGAEARARAR ARAAMMAVMS
     LDASMALESV FRLLLSLGGT GPPEGAAAGR EEAWRGAAEG TGSGDDFVWV PDMPAGLEGW
     VFES
//
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