ID A0A087SK67_AUXPR Unreviewed; 930 AA.
AC A0A087SK67;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Zinc-metallopeptidase, peroxisomal {ECO:0000313|EMBL:KFM26121.1};
GN ORFNames=F751_6272 {ECO:0000313|EMBL:KFM26121.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM26121.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM26121.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM26121.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; KL662126; KFM26121.1; -; Genomic_DNA.
DR RefSeq; XP_011399017.1; XM_011400715.1.
DR AlphaFoldDB; A0A087SK67; -.
DR STRING; 3075.A0A087SK67; -.
DR GeneID; 23617663; -.
DR KEGG; apro:F751_6272; -.
DR eggNOG; KOG0959; Eukaryota.
DR OrthoDB; 129328at2759; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 6.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000028924};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 39..89
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 167..318
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 319..610
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 620..800
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 930 AA; 102986 MW; C2FA8F66893D804F CRC64;
MVHARESTDL GGGAPGLLRC PTTDENGYRF VKLDNGLQVL LVHDPKTDKA AVACDVRVGS
LSDPDDLPGL AHFLEHMLFY SSEKYPVEDE YRFAQFFICP LISRDGVDRE AHAVDSEHGK
NLNSDAWKAL QLWKHTANPD HPFSRFATGN LETLLDGPAR KNVEVHTRLK EFYEKHYCSQ
LMRAVIIGRE SLDDLQALAS SAFGPVPCRG LRAPSFSPEA TPRAGLLMKA VPERSGHTLE
LQWRVEPELK HYDAAPCQYF SHLLGDEGEG SLFALLKARG WATDLCAGES GTSFSAASIF
MVRIGLTDAG QEHVPELRFD FAEKMAPSSY ATTLAGAMQV YGRHDLLLAI HHVPQRYDPE
LLDTVLSTLC PSEARVLWAS SSFQVPTDCP LKEPWYGTAH SAGPLPAEWL THWEAAWRGE
GAALGDKDGH RFCGMHLPPP NPYIPSRFDL IKESSSSPAK IHATPLYTLW HRPETGFKVP
KTAIYLHLRM PEAYLTPRAA VSTQLISRLL TDKLSEVAYP AELAGLHYGV RATTSGMLLS
FWGHSHTLPR LVQTVLDSLL EFEVLPDRFE LAKEHQAKDY ANMRHEQPYQ HGLYLLSVGL
EARRWHVRDY EAVLPGVMGD SLRAFQTAML GTVRIDALIA GNVPAADARA LLQALEARLL
AGRCSPLPAS QRTEARVVAL PSPMRAVHAV PGPNPANDNS AVVVAFQAGR DDVRRNALVD
LVGHLGKREA FHTLRTVEQL GYITHLSAFW TLTVSNILVL IQSSAHSARY LQSRIDAFLP
KLADSLRGMP AEEYAAHVEE LAKAKLEKPK RLRDAVNTDW SEIDDGTLRF PRKELEAAAV
RSITQEELVA FFEARESRGY LRVLSFWLLD TVVNPRTRRS YSVLVEGNVK EPAPEAAGSK
ASAAPPTADE VLVSDQYSFK RGQALYASFL
//