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
//