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Database: UniProt
Entry: F4XMZ4_9CYAN
LinkDB: F4XMZ4_9CYAN
Original site: F4XMZ4_9CYAN 
ID   F4XMZ4_9CYAN            Unreviewed;      1099 AA.
AC   F4XMZ4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=Matrixin family protein {ECO:0000313|EMBL:EGJ34053.1};
GN   ORFNames=LYNGBM3L_23180 {ECO:0000313|EMBL:EGJ34053.1};
OS   Moorena producens 3L.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Moorena.
OX   NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ34053.1, ECO:0000313|Proteomes:UP000003959};
RN   [1] {ECO:0000313|Proteomes:UP000003959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX   PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA   Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA   Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA   Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA   Gerwick W.H., Gerwick L.;
RT   "Genomic insights into the physiology and ecology of the marine filamentous
RT   cyanobacterium Lyngbya majuscula.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M10B family.
CC       {ECO:0000256|ARBA:ARBA00009490}.
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DR   EMBL; GL890840; EGJ34053.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4XMZ4; -.
DR   eggNOG; COG2931; Bacteria.
DR   HOGENOM; CLU_300478_0_0_3; -.
DR   OrthoDB; 1818597at2; -.
DR   Proteomes; UP000003959; Unassembled WGS sequence.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03603; CLECT_VCBS; 1.
DR   CDD; cd04277; ZnMc_serralysin_like; 1.
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; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 4.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR034007; CTLD_bac.
DR   InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR   InterPro; IPR001343; Hemolysn_Ca-bd.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001818; Pept_M10_metallopeptidase.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR034033; Serralysin-like.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR   PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR   Pfam; PF00353; HemolysinCabind; 7.
DR   Pfam; PF00059; Lectin_C; 2.
DR   Pfam; PF00413; Peptidase_M10; 1.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   SMART; SM00034; CLECT; 2.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF51120; beta-Roll; 6.
DR   SUPFAM; SSF56436; C-type lectin-like; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 2.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 6.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          540..641
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          814..929
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   REGION          360..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..394
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1099 AA;  118831 MW;  2A23852ACDC4F43F CRC64;
     MGVKRSGNND IDALLDDDYW VDTGKPVSLT YSINYSTGSD GLDLSERSMV REALTRWSEV
     ANITFREVSN KGNLRFSGQS GISGVASQKN ARKWWKPRSW RSDKLDHVNI KLGKDSATGR
     GHRFLDVALH EIGHALGLKH PGDYNGDTGK GSSPFLPYYK DNNTNTVMSY NDVGDYAATP
     MPYDIRAVQY IYGSNNFNSG NTYYRFDSVN GYSYDNGLAR RGSEKLPMKL SIWDSGGVDT
     LDFSKLGPVI FNISRSSGYY FDIRGGGILT SQHAYKSITY QPIDNTNNTS SLRYKTTRYG
     TSIAYGVVIE NVIGSLTSDT IIGNFSANHL KGGNGNDSLY GNGGSDSLFG EAGNDSLIGG
     TGRDELYGGT GNDSLDGNTG NDYLSGSSGN DFLRGGTGRD QLHGGTGNDT LSGDSGSDIL
     SGSSGHDYLY GGIGNDYMYG GSGNDTYTVD SSGDHVFEYA NQGIDIVYAS TTYGLSAHLE
     YLNLTGTNSI NGYGNNLNNV INGNSGNNNI WGGLGLDTVN GGDGDDIIYG DYIIASTGQY
     LFSLPGTWLS TQAEAQRLGG NLVTINNATE QSWLNTTFGT NEVFWIGLSD RTIEGQWQWV
     SGETSTYRNW FPGEPNDYRS SSIPDGEDYA VMGWGNQGWN DLQNYPNQHL RGIIEIPSVS
     PEIGESDILN GGAGNDRIYG GGGDDQLYGS YGNDNLYGGF GNDLLKGESG RDRMKGGFGD
     DQYVLDVDSM GDTIVEYAGQ GIDKVYTSIT YHLGDNLENL ELDGTNPING YGNNLNNVIQ
     GNSASNNIWG GRGHDTVNGG DGNDIVYGDY LVTRNGHSYL LSQPGTWFNT QAEAQRLGGN
     LVTINDEVEQ NWLNTTFGFN YDGFNVEANR FEANQLFWIG LTDHTTEGQW QWISGETSTY
     RNWAFGEPNN YTDDEDYAVL VSWFNQNWEQ TWFWVGAQNY PNKVYLHGII ELPSVIQEIA
     GNDSLYGGAG NDRIYGGAGD DLLNGGTGND VLSGGAGADK FVLNIPTEGI DYISDFVSQQ
     GDKLQISASG FGSGLVQGIL DVGQFVLGAA ALDTNDRFIY DRSSGLLSFD ADGSGTLGAV
     QVANFSNKTA LTNTDILIV
//
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