ID A0A5N5TK10_9CRUS Unreviewed; 995 AA.
AC A0A5N5TK10;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 24-JAN-2024, entry version 9.
DE SubName: Full=Presequence protease, mitochondrial {ECO:0000313|EMBL:KAB7506500.1};
GN Name=pitrm1 {ECO:0000313|EMBL:KAB7506500.1};
GN ORFNames=Anas_02779 {ECO:0000313|EMBL:KAB7506500.1};
OS Armadillidium nasatum.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Peracarida; Isopoda; Oniscidea; Crinocheta;
OC Armadillidiidae; Armadillidium.
OX NCBI_TaxID=96803 {ECO:0000313|EMBL:KAB7506500.1, ECO:0000313|Proteomes:UP000326759};
RN [1] {ECO:0000313|EMBL:KAB7506500.1, ECO:0000313|Proteomes:UP000326759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANa2 {ECO:0000313|EMBL:KAB7506500.1};
RC TISSUE=Whole body excluding digestive tract and cuticle
RC {ECO:0000313|EMBL:KAB7506500.1};
RX PubMed=31600190; DOI=.1371/journal.pbio.3000438;
RA Becking T., Chebbi M.A., Giraud I., Moumen B., Laverre T., Caubet Y.,
RA Peccoud J., Gilbert C., Cordaux R.;
RT "Sex chromosomes control vertical transmission of feminizing Wolbachia
RT symbionts in an isopod.";
RL PLoS Biol. 17:e3000438-e3000438(2019).
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:KAB7506500.1}.
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DR EMBL; SEYY01000776; KAB7506500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N5TK10; -.
DR Proteomes; UP000326759; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR013578; Peptidase_M16C_assoc.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR Pfam; PF08367; M16C_assoc; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KAB7506500.1};
KW Protease {ECO:0000313|EMBL:KAB7506500.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000326759}.
FT DOMAIN 490..738
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
SQ SEQUENCE 995 AA; 112443 MW; 8230336E0E5F2A5B CRC64;
MYHYQVDFSN NEKASALSIN SDLQKEFEIG STIHGFEVIE QKVVPELQLT AFRLNHIKTG
ADYLHIARED SNNVFCIGFK TTPKDSTGVA HILEHNVLCG SEKYPCRDPF FKMLNRSLST
FMNAMTGNDY TVYPFSTQNK VDFRNLMSVY LDAVFRPNLR EIDFMQEGWR LEHKDVIDKN
SPIIFKGVVF NEMKGVFADS QQLFMQKLQN GVLPSHTYGV VSGGDPLHIP QLTWKDLRAF
HADHYHPSNS RIYSYGDLSL KDHLDFIDSE YLSKFEKINP NTSVPEEPKW KEPQSSYISC
SADPMAPEDR QTSLAVSCVL TSITDDFENF VLAILDQLLV RGPNAPFYKS LIETSLGTSF
SPVSGFDNQT RTTTFTVGLQ GMNKDDVNKV LSIIDTTFDS VMENGFASDR IESILHNIEL
SMKHQTSNFG LGLILNLTPF WNHDGNLLKA LEINSKIEKL RNILKENPQF LQEKVYQYFK
TNNHKYSLVM SPEEHYEQKL IQAEESLLEM KVRNLSEEET KSVWEMGQLL KTQQETKEDL
SCLPTLCVSD IPKTIPNTDI GNVNINGNIP LQLCIQPTNG VSYFNAVLST KNLPVELAKF
VPLLCNILTS MGAGNLDFRD MSQKIELVSG GFCSSMHIIN HPEDSSLYEE GIHINSYCLQ
KNFVAMLDLW LNIMNELKLD DVSRFTTLIN MIATEKSNSL IHNGHKYAIS AASSSISYVC
CKKEEVGGLA YLQNLKELCN SPFLTEILEK LKEVSHHLLN KNNIRVAINT SRETADTDVC
NVEKFLQNIQ GEPSNASSMS VVPSAFTPRT ERTHHIFNLP VNYSAKAFSN IPYAHPDSGP
LRILARLMFQ FLHREIREKG GAYGGGAYAN PGNPFSFYSY RDPNSTLTLK TFDDAVDWVL
TGEFTQQDIN EAKLGVFQNV DAPVSPGERG MRQFLNHISD DMFSQQRLAI LNATSDNLIS
VCRKYLKEAS LQGTCLIGPQ NSHIDEDPEW NKKIH
//