ID A0A452IK94_9SAUR Unreviewed; 1145 AA.
AC A0A452IK94;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Nardilysin convertase {ECO:0008006|Google:ProtNLM};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000028304.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000028304.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR AlphaFoldDB; A0A452IK94; -.
DR STRING; 38772.ENSGAGP00000028304; -.
DR Ensembl; ENSGAGT00000032160.1; ENSGAGP00000028304.1; ENSGAGG00000020555.1.
DR Proteomes; UP000291020; 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; 4.
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:UP000291020};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 218..347
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 373..558
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 564..844
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 850..1031
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..55
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..201
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1145 AA; 130713 MW; FD1DF3BC6E990C65 CRC64;
MWRALGALAR RRPGTRVGAD QAFRGAGHSC PVRAAPTPPP QPSQQQRPPP RRSPAMPGRN
KASCSCPDLP SGQQVGEGGR DAKGRLLQEE SEEEGGHRRA KPNLGDPDVV KSPSDPKHYR
YIKLQNGLCA LLISDLNNMD TAPSVVSSEG EDSGESEDES DEDDDSGAEI EDDKEGGDDD
DDDYDEDDGG DDEDLNDPDN SELEELAEKE ETRKRGCTEK QSAAALCIAV GSFSDPEDLP
GLAHFLEHMV FMGSLKYPDE NGFDAFLKKH GGSDNASTDC ERTVFQFDVQ RKYFKEALDR
WAQFFIHPLM IRDAIDREVE AVDSEYQLAR PSDANRKEML FGSLARPGHP MKKFFWGNAE
TLKHEPKMNN IDTYTRLRDF WQRYYSAHYM TLVVQSKETL DTLEKWVTEI FSAIPNNGLP
RPSFGHLTQP FDTPEFHKLY RVFPVRKVHS LSITWALPPQ DQHYRVKPLH YISWLVGHEG
KGSVLSFLRK KFWALALYGG NGETGFEQNS TYSIFSISVT LTDEGYKHFY EVAHVVFQYL
KMLQQRGPDK RIWEEIQKIE ANEFHYQEQT DPVDYVESLC ENMQLFQKED FLTGDQLLFE
YKPDVIADAL NQLCPQRANL FLLSAANEGK CNLKERWFGT QYSEEDIDKY WSDLWASDFQ
LNEDLHLPEE NKYIATDFAL KAPDCPESEY PVRILSTQQG CLWYRKDDKF KIPKAYIRFH
LISPLIQQSA ENVVLFDTFV NILTHNLAEP AYEADVAQLE YKLVAGEHGL VIRVKGFNHK
LPLLFQLIID HLSDFSFTPA VFEMITEQLK KTYFNILIKP ETLAKNVRLL ILEHGRWSMI
DKYETLMKGL SIESLSSFVK TFKSQLYVEG LVQGNFTSRE SKDFLNYVVQ KLQFFPLLHP
CPVQFRVVDL PNTHLLCKVK ALNKGDANSE VTVYYQSGAR SLREYTLMEL LVMHMEEPCF
DFLRTKQTLG YHVYPTCRNT SGILGFSVTV ATQATKYNSE LVDKKIEDFL SFFEEKIKHL
TEEAFSTQVT ALIKLKECED SHLGEEVDRN WNEVVTQQYL FDRLACEIEA LKSLTKADLV
DWFQAHRGSE SKVLSVHVVG FGKHEGDAEV PAVSDDQTSS CDTPRILCNR DQLCPFTVVI
PSGCF
//
