ID F4XIE4_9CYAN Unreviewed; 1485 AA.
AC F4XIE4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Matrixin {ECO:0000313|EMBL:EGJ35677.1};
GN ORFNames=LYNGBM3L_01360 {ECO:0000313|EMBL:EGJ35677.1};
OS Moorena producens 3L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Moorena.
OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ35677.1, 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; GL890816; EGJ35677.1; -; Genomic_DNA.
DR RefSeq; WP_008177784.1; NZ_MKZR01000001.1.
DR eggNOG; COG2931; Bacteria.
DR HOGENOM; CLU_249439_0_0_3; -.
DR OrthoDB; 468578at2; -.
DR Proteomes; UP000003959; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 7.
DR CDD; cd04277; ZnMc_serralysin_like; 1.
DR Gene3D; 2.60.40.60; Cadherins; 5.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 7.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
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; 6.
DR Pfam; PF13583; Reprolysin_4; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR SMART; SM00112; CA; 7.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF51120; beta-Roll; 3.
DR SUPFAM; SSF49313; Cadherin-like; 7.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50268; CADHERIN_2; 7.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 5.
PE 3: Inferred from homology;
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 447..538
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 545..636
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 643..734
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 741..832
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 839..931
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 938..1029
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1036..1128
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 1193..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1485 AA; 162099 MW; CF4506117277842B CRC64;
MSNTFSSADS LLDHHHWDTN TITYSFYNNA NSGSYYGPET GVSEISEKTK DNIRSILETL
ERYIAVDFHE VADTATDYGL LRYMVSDGPG YAYTYLPEGF NTNVGNWSDV AGDVHLNQAY
DTTGNNGFAD DPGNHGYMTV IHEIGHSLGL KHPNPYEDND HGPFLPFNED NTTNTVMSYN
FAGKSAITPM IYDIQALQSI YGAREYNHGD TTYSFDSVNY YTDGSEYYGK TKPIEEIKQT
LWDSGGVNTL DFSNLTFVEK GYHFDMNEGG ILTTQEAYND SSYKARSDDS GREYVTSEFG
TAIAFGTVFE NLINSNSNDY IIANSAANIF SGYELEISTG DDLIKGWNYL DTLDLSNYAF
SSVTQTQSGD DLILGLGSDS SITLKDYHTV SESDLLKIIF EEESQAPVWE EIIIPDTITN
ISDVQYVQEE PQTTNTAPTN ITLDGNSVKE FSKNGTTIAK LTTKDVDWGD SHTYKLLDDA
QGRFKIDGNR LKVKNGHLID FDDNSSHSIK IRTTDSGGKS YEETFTIEVL NQNFAPTDIS
LDGNSVKEFS KNGTTIARLT TKDVDWGDSH TYKLLDDAQG RFKIDGNQLK VKNGHLIDFD
DNSSHSIKIR TTDSGGKSYE EIFTIEVLNQ NFAPTDISLD GNSVKEFSKN GTTIARLTTK
DVDWGDSHTY KLLDDAQGRF KIDGNQLKVK NGHLIDFDDN SSHSIKIRTT DSGGKSYEEI
FTIEVLNQNF APTDISLDGR SVKEFSKNGT TIARLTTKDV DWGDSHTYKL LDDAQGRFKI
DGNRLKVKNG HLIDFDDNSS HSIKIRTTDS GGKSYEEIFT IEVLNQNFAP TDISLDGRSV
KEFSKNGTTI ARLTTKDVDW GDSHTYKLLD DAQGRFKIDG NRLKVKNGHL IDFDDNSSHS
IKIRTTDSGG KSYEETFSIE VLENQNSAPT DITLSGNSVK ELSENGTTIA RLTTKDVDWG
DSHTYKLLDD AQGRFKIVDD QLKVKDGTLL DFDVNSSHPI KIRTTDSGGK SYEEIFTIEV
LNQNFAPTDI SLDGNSVKEF SKNGTTIARL TTKDVDWGDS HTYKLLDDAQ GRFKIVDDQL
KVKDGTLLDF DVNSSHPIKI RTTDSGGKSY EEIFTIEVLN QNWESKSIRG DRYDNRLEGG
HGDDRLWGNR NNDTLIGGSG HDTLSGGSGD DSLVGGFGND FLRGTWGNDT LHGGSGHDTL
GGGQGDDSLS GGVGNDRIMG DVGNDTLEGS SGEDNLSGGS GDDLIEAGTE DDSLRGGKGG
DTLKGGSGND YLRGDDGNDS LEGGSGNDSL IGASGDDTLD GGSDHDTLKG SSGNNYLIGG
SGDDLLDGGR DHDSLEGGSG NDYLIGGSGD DLLDGGQHHD FLKGGSGNDY LIGGSGNDTL
NGVGNGSRGN GEIDVLVGGA WSDTFILGDD HRAFYQGKGD NDYAEIYDLE SKDIIQLYGV
ADQYDLVDAD NGLPGSTALY FKNDLIAVLH DVSVSDVSSR LEFLS
//
