ID C3YSP6_BRAFL Unreviewed; 2371 AA.
AC C3YSP6;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN ORFNames=BRAFLDRAFT_83478 {ECO:0000313|EMBL:EEN56747.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN56747.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN56747.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN56747.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:PRU01172}.
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DR EMBL; GG666549; EEN56747.1; -; Genomic_DNA.
DR RefSeq; XP_002600735.1; XM_002600689.1.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG3714; Eukaryota.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; C3YSP6; -.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 2.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 2.60.120.200; -; 5.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 2.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR004094; Antistasin-like.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001759; Pentraxin-related.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR PANTHER; PTHR19277:SF161; METALLOENDOPEPTIDASE; 1.
DR PANTHER; PTHR19277; PENTRAXIN; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00059; Lectin_C; 2.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00354; Pentaxin; 5.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00034; CLECT; 2.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00159; PTX; 5.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51252; ANTISTASIN; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 2.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 2.
DR PROSITE; PS51828; PTX_2; 5.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 26..2371
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5005124981"
FT DOMAIN 849..976
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1003..1029
FT /note="Antistasin-like"
FT /evidence="ECO:0000259|PROSITE:PS51252"
FT DOMAIN 1061..1252
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 2241..2370
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 554..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 1150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 1154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 1160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 2371 AA; 260855 MW; 7191118AE727C509 CRC64;
MAVKWVARFY LVLVVVRLVV PCVEAGDWQH CQNVSPLRCS VGDSRNGGSK YRYDIADYES
RWNRDQYMYV YGYGGPFKYN RLYPSFKSCY DCAGNGSVSG SSVTGEVQTV TLSPSQQDIT
ILVIADNNVG TMTKADATAI SKLPCGKYCS LWLVNCNITT IEVGAFAKLS QVETLIIWQS
NLQTLRSGTF EGMEGLEKLL LLGNNITCLE AGAFDGLPLL RSLYLVDNQI LTMAPGMLRG
LQLDWLDVSA NSLWYIAPGV LQGTRSVRNV YIVKNKLQSV SVGMFAELAN MQSLYLQYNE
ISRIADGAFH SNKRLGVLNL ACNKLTFLSG LWFKSAEIFK LYLKGNAIAA AYPGRGELRW
DVRLQDNPLR CTCANIGLYE QLWKRWKASR RRPRHSEMSL PTGCPASSLV ESPPVQVNVS
ALPCPAPFVE ILSIEQNHES REYKVVGNVY WEDLPQVSWD FANGSEHSMN IMYNTNTTTH
ANLAIGNLTV RVGTYLRAEG PNDSVISPYA EGRFEDHDSL DGSDICPYAV GRIEDHASLD
GSESVISPYA EGRFEDHDSL RDTDSSASSE IVPYGQGALN AAYEERRYEN TGTETSNVSD
QNCYQHPSTP PNPGATQSSA YQQRSSYENT GAETSNNSDQ NCYQHPSLLP DPGATQSSAY
QQRSSYENTG TETSNNVRPK LLPAPFDPSD PGATQSSAYQ QQCSYENTST EKSRMSEQNC
YLHPSTLPDP GATQPFASDH GSPSPLPNSD RSEATCSTAS SLPEAAADGP HAATPKETET
PGPGESVQDD SGSEQGGSEE GNARVRRADN DTKTDDPKTD DAKADDGLIR KTGCVDPKTG
DQWGSFDQAS NKCYKAFRIA KTWPEASAHC RNQGPGGNLA MPKNSDTNKL LIQLKEKISS
PEIWFGLNDR VSEGQWKWND GTSLVSYNDW SPHEPSNGGG HGWWWWNRGN EDCAEYNRQN
GWNDNDCAKR RNFICEREPN VDFEQPKDIF DINEEAGLLG RACPGFKCDK KDCNFGYDTD
EDGCFVCSCV PEGREVMYQG DIVLDRAGKN RILHGSENRG ARIGGLWPGG VVPYHIEEPL
RGSNLAVNAI NDAITDYHKY TCLRFIRRTN QTAYISFVDG LGCSSPVGYY GRVNRITLSS
VCWTRGTVIH EIAHSVGFWH EQSRPDRDDF VEIVWDNIPV ANRHNFNLKE NVNSLGSPYD
YQSIMHYKST AFGLNRRVTI RTTDASQQDK IGQREGLSER DITQLNLRYN CGYLQKITFP
APRSISNYAR LEATLAQDLR SLTLCLHMRT DMSSTSSAGV VSYAVQGQYN ELLILNERGL
SAFWVRGTRA RLFKLPVWDG ARHAVCATWR STDGAWQVYT DGVLKASGAG LNVGGKVRSG
GTWILAQDQD TVGGGFVTHQ AFSGELSQVN LWDRVLTPAE IGTDCISNYA RLEATLAQDL
RSLTLCLHMR TDMSSTSSAG VVSYAVQGQY NELLILNKPA GSEFWVQGSA ASPVNLPVWD
GERHAVCVTW RSTDGAWQVY TDGVLKASGS GLNVGGKVRS GGTWILAQDQ DTVGGGFVTH
QAFSGELSQV NLWDRVLTPA EIGTDWSDFC GQHGNVIDWE TSDINVYGRA SSAEYRCSYL
QKITFPAPRS ISNYARLEAT LAQDLRSLTL CLHMRTDMSS TSSAGVVSYA VQGQYNELLI
LNKPAGSEFW VQGSAASPVN LPVWDGERHA VCATWRSTDG AWQVYTDGVI RASGSGLNVG
GKVRSGGTWI LAQYQDTVGG GFVTHQAFSG ELSQVNLWDR VLTPAEIGTD WSDFCGQHGN
VIDWETSDIN VYGRASSAEY RCSYLQKITF PAPRSISNYA RLEATLAQDL RSLTLCLHMR
TDMSSTSSAG VVSYAVQGQY NELLIINERG LSAFWVRGNR AFVNLPVWDG ERHAVCATWR
STDGAWQVYS DGVLRASGSG LNVGRLVRSG GTWILAQDQD TVGGGFKTIK AFSGELSQVN
LWDRVLTPAE IGTDWSDFCV GQHGNVIDWE TSDINVYGRA SSAEYRCSYL QKITFPAPRS
ISNYARLEAT LAQDLRSLTL CLHMRTDMSS TSSAGVVSYA VQGQYNELLI LNKPAGSEFW
VQGSAASPVN LPVWDGERHA VCVTWRSTDG AWQVYTDGVL KASGSGLNVG GKVRSGGTWI
LAQDQDTVGG GFVTHQAFSG ELSQVNLWDR VLTPAEIGTD WSDFCGQHGN VIDWETSDIN
VYGRASSAEY RCKCTDGYTR YKEVCYKVIK ESKTHHEAST FCSRQGPSGR LAMAKDRGTN
DFLIGLKNGA CNNCQYHFGL TDTATEGQWK WADGSALGLF KDWASGEPNN GRGGWWGGRF
SEDCAEFKKG SGGGEWNDVR CSKKQFFICE V
//
