ID A0A0V0UG45_9BILA Unreviewed; 2635 AA.
AC A0A0V0UG45;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 03-MAY-2023, entry version 38.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN Name=nas-8 {ECO:0000313|EMBL:KRX49651.1};
GN ORFNames=T05_2542 {ECO:0000313|EMBL:KRX49651.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX49651.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX49651.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX49651.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:PRU01211}.
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:KRX49651.1}.
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DR EMBL; JYDJ01000014; KRX49651.1; -; Genomic_DNA.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd11304; Cadherin_repeat; 8.
DR CDD; cd15720; FYVE_Hrs; 1.
DR CDD; cd21387; GAT_Hrs; 1.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 1.20.5.1940; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 8.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR017073; HGS/VPS27.
DR InterPro; IPR024641; HRS_helical.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002014; VHS_dom.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46275; HEPATOCYTE GROWTH FACTOR-REGULATED TYROSINE KINASE SUBSTRATE; 1.
DR PANTHER; PTHR46275:SF1; HEPATOCYTE GROWTH FACTOR-REGULATED TYROSINE KINASE SUBSTRATE; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF12210; Hrs_helical; 1.
DR Pfam; PF00790; VHS; 1.
DR PRINTS; PR00480; ASTACIN.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 8.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00288; VHS; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49313; Cadherin-like; 8.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50179; VHS; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183}; Kinase {ECO:0000313|EMBL:KRX49651.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
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:UP000055048};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KRX49651.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01211};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT TRANSMEM 1647..1665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1721..1746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 134..336
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 689..810
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 828..923
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 941..1039
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1041..1147
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1147..1248
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1249..1366
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1376..1485
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1501..1604
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1878..1988
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 2005..2065
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 2083..2174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2384..2431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2298..2377
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2087..2111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2133..2161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2400..2414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 233
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 2635 AA; 297034 MW; BFF9E7035BB42B3B CRC64;
MMLMYIFCYH FFVKQLKCFI TCLVNSVAGL LKFLSIFNCY PGDCRVFGKH HHRCMTKSIR
KLCAIVIHSP FDAKAGHLFT CRDKFTISNT ARFQEWTQIG CKRFACQWFE KHLAIDSDIF
VVLADKYRGD VRGKALRRRQ FDSNSNLRGV SRNARIGSQY KWPDAASERA VIARAMQAYH
EKTCIKFVAR THEPDYLYIK KEDGCFSDVG RTGGRQTVSL DDGCIYYRTI IHELMHAIGF
WHEHERPDRD DFVDVIWYNI RAGAHSQFQK VSPSESNTFG ERYDYRSIMH YDSKSFSKNG
RDTMVAREPG MTSVMGKSDD FSPSDLRRLN TLYNCHSRPN SRPAPPPSPI IRPLVRPPVI
DDGDDDYDGA PFSIRPPPPR PIRLNLKIPF LDLICTDMWK DCYKWAAMCR TSVLEVPMRF
FYRFERTEKL FSHGAAKLPS NQSCENPHTR PRACRGKNVQ FEDGCCESWL FTCAMRYGRD
NNLLRRPTAE QGQFVLVWAN IRADRDVVTI KRPFGEHENK TQSYFEQQPL TDPLNDNVPQ
SWNMLWPAMR SDHFYATQPL SFIHPTCGPA VSICSGVQYT ASVVTGIPPE KKALKIHPLP
IKAKNIYNPN VPVTYAFFNG TPETFSKYFA INAQNAEIVQ LKIIPNKEAG PFLIYVIART
AYTGSKVSFA QLNIQALNPT ESRFEPEVQV TNTQAYIDEN ASIGTLIRTE RRQNGPPLQI
SVTDKDLKPG MPPAIYQYIL SGSGANHFAI DQRGYVFLNA LALKVDKNGD NVHELIIRAR
EVDTTPIRTS EPVKVRIEII ALDSHSPPVF GSKVYYATAY SGLPQQSLIR VKATVKDSKT
LAILKYRILS VSKGAEDLFH YNEDTNTLIA LGFLNPNAQY RVVLEVMDKF SRTATTTIMV
RVVDAATIGH LYQYSTQSVQ PIAWTTTTTT TATIPSTQPV IAAAFNITVS EEVSPDTLVM
TLTAEGAAPD QTSYRITDAT EKGKFRIDKN DGRIFTAGVL DREHIPSHRL VIEVKSGTMT
TYAEILVNIS DVNDNPPKIV NETPIKFTVN SNSPNSIIGK ITATDNDIGD NGIVRYRLKF
PNKFFSIDPM KGIIKSRADL STTGHSVHKL TIIAEDGGEP SLQSSVDATI EILNDNTDTG
PLSVPVFTGN YSVGIDENLG PTNLVQIKAK YLDGRQGPVT YILRRGDMSL FSIDQRTGML
STLVSLDAEK QKKYTLIVGT EENLSEEPPA WARVTVIVHE LNDNSPIFQE KSYSTTISEA
LPPGSSILQV SASDRDDSSP NNLIKYRLIG DEEAAKFFAV DEDSGLITIA RSLLGAGKDK
FTLSVEAKDK GNPPRSSFTT VAVHVEISTT TPLHFGSLST WMPPSSNAVH LQNNFVSSVF
NTTVYELVPS PHFVMTLPMK SSNPTWQPVV QCKILDGDSE EAFIIKTGSG GLCELETRLK
LDREEVSMYK LNISAATVLP SGAQYFDYAT VFIEVLDQND NRPEFQFDED SALLGTFIGI
VDEKASEFTP ILRIKAVDKD VGRNKQIAYS LLENDPDSSL FMIDQETGEL KTKAKLKEQR
GKSAAVYRFR VQAKDNPSYG IPLSAEANVV VNTVRNTNRF MITVDKWHAG QQDQYVKKLK
NEIRQIIERS RNKCQMIILE RIEDADYLGI VNNFGVNLIF VAVNIQTKRV CRSSDLGEIF
AKENIRRLKE RLAPALLVQN VQEMVSPSTL LFGRRLQMSE IVLISVGCFI GLACLVGVLV
LCYYWNRSQA KRASSEKAML YAGIPPFNPI LMSPSEKEYE TQMLELSVPD EPYDKRFNLT
TVGIDDGIYT IRPGDRSALY GTRSSSLSHV YIPPPDYPRN EDIYPRRPKY HFRVVIYGTW
YVRDVEEVRK VIRPSNGCYT VRGGLGKPKS AILSVRKRYH SDNPHVAHHA LLVLEALVKN
GGPKIHREIA TKEFMEDLKH VTSESADKVK DKVLELIQCW AHAFRDNPEY KIVKDTHTLM
KLEGHVFPVL RESDAMFMAE SAPDWVDADH CFRCKVQFSL ITRKHHCRNC GQIFCDKCSN
KNIPLPHLGI ERDVRVCEGC FDRIKNPIGD LIKKLGEFTP SSVESSKAAL EKERQKEKEK
KEAELREEEE LQLALALSQS EKEEKDRLKN RNSYQWKTSP PTMMNSNYGT SSASVANNPP
NHNEGKKDKG LSSAKDMENE LARYLNRQYW EKVRLEQKQA NTRKSPTPSA PFEPTSIIKQ
PLESVESENN NNNGVEMDAL QDFVNSLNES ISVFVNRIKS NQTRGRSVTA DDTIQNNFIA
LTSMHSRLLK NMQERIDRRE YYENLQDKVN QIREAREALE SLREEYRDKK KVELAEMQRQ
QQLVMLAKLQ SMRLKKYEML GLQRMEALRQ IEEKQRELFM RNKTAMQQPP PPPSQQPQQQ
QQPVIPVGLP PQQQQQHHHH HHHHQQQQQP SLLTGAMGSN TLVQPSAAFN HSCTTALQSG
HVQAEFSQTP QVVSVPHVAL MYPYTVPTNE NCAPSSQVLM PNPYSVNQPS MVPQQAAYHS
PYCPVDPSYG PSYMHAPSAY HHSPSYAVAG QMDMQSYVYP PAGAGHFPAP HAYTVSQGIP
GMVMHPQPTQ QVMPTAGQPN VSTPVTLASA STQSEPVSIL CRVAQMIKTV RDTSI
//
