ID A0A261CBN6_9PELO Unreviewed; 1023 AA.
AC A0A261CBN6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
DE Flags: Fragment;
GN ORFNames=FL83_06323 {ECO:0000313|EMBL:OZG19470.1};
OS Caenorhabditis latens.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG19470.1, ECO:0000313|Proteomes:UP000216463};
RN [1] {ECO:0000313|EMBL:OZG19470.1, ECO:0000313|Proteomes:UP000216463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX534 {ECO:0000313|EMBL:OZG19470.1,
RC ECO:0000313|Proteomes:UP000216463};
RA Fierst J.L.;
RT "Caenorhabditis latens genome sequence.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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:OZG19470.1}.
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DR EMBL; NIPN01000021; OZG19470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261CBN6; -.
DR STRING; 1503980.A0A261CBN6; -.
DR Proteomes; UP000216463; Unassembled WGS sequence.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 2.40.128.20; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF890; ZINC METALLOPROTEINASE NAS-30; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF50814; Lipocalins; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000216463};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 18..1023
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5011831419"
FT DOMAIN 326..521
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 534..632
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 66..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 415
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OZG19470.1"
SQ SEQUENCE 1023 AA; 113623 MW; 3642EE279C4A746F CRC64;
MKTLWIFVLL VVGFIEAQDF MSLFKPFLGG GGGGGNPFAN PQAIGGLFQQ FAGGQGGGGF
GQFLGAMAPK PPPAPAAGPA AVAPTNEDYN TDLDAVPAPP KPKARAAHHR RPQADAPPPP
QQSFRQPRTK QEKIERWKNI ARTFSPFFFD DQNTTPAPQF NNYIWQQNAP AVTPEPFTFA
PFSLATLATV APIGPTLEPM LPTTASPQLL AHNTARMIRE IATFSDGGKS RDQDFGAVQT
LMQAFFEAVA SGNNGGSSAA TGTAVGTPLG DAPMYQARRD GTELGANRAL TNKLFESDMV
LTVPQMKAVV LAAQEARNPH GRKKRKVITG SVYRWKSVIP YRFKGGDSKW KKLIREGLSL
WEKETCVRWS ENGHGKDYVI FFRGSGCYSS VGRTGGSQLI SIGYGCEDKG IVAHEVGHSL
GFWHEQSRPD RDQYIHLRKE WIIKGTDGNF EKRSWEEIED MGVPYDIGSV MHYGSNAFTK
DWDQITIETT DSRYQGTIGQ PVCPVALNCQ HGGYPDPNNC SVCKCPDGLG GKLCGRVAKG
TDHDKCGGEL VATPEWQEMI YKGKRTCNWR VKSPNGGRVR LVLTELRYQC ATSCKAYIEI
KHNTDFQQTG FRVCCFNKTY DVISDQSEAL ILSNANIVDY EVSYKLQWIQ DNGKPLPPPK
PTSTWVPGKE NRPFRGVENT GGTIEKFILQ AIPKIRDSHR PLESITSIVA EYGLATLLGV
SHNVSVGHLK LLRLLLPDAI SPVDIIITVS DQLLSFHFIR SSFTSQVMIL ICFYLLSLLN
LANAMSATVR PFTNSIPVPG RNVPIMRLFE NYAASCRPTN KRDFNMDQLA TLLQSFQMDE
VATKQYNSIF FGMADMQIEK FMGKWYTVVD SKEVHKEDCS IFYFDMVLQT PYTATFTSKQ
YALVNNDVIT NEGYGSMVGP EPGSVLITTG HERDQCPFFP VRIGGLNDDG EYQYMILSTP
LKYPTMVLTR DLELFETKWK HEVYDFVEKN GFMSPMAALN TRLHFTDTDV CRKVNKLYEN
GNI
//
