ID   A0A0C2MD30_9CYAN        Unreviewed;      1245 AA.
AC   A0A0C2MD30;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=PKD domain-containing protein {ECO:0000259|PROSITE:PS50093};
GN   ORFNames=SD80_09000 {ECO:0000313|EMBL:KIJ84981.1};
OS   Scytonema tolypothrichoides VB-61278.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC   Scytonema.
OX   NCBI_TaxID=1233231 {ECO:0000313|EMBL:KIJ84981.1};
RN   [1] {ECO:0000313|EMBL:KIJ84981.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VB-61278 {ECO:0000313|EMBL:KIJ84981.1};
RA   Tripathy S., Das A., Panda A., Malar M.C., Adhikary S.P.;
RT   "Draft genome sequence of Scytonema tolypothrichoides VB-61278.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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:KIJ84981.1}.
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DR   EMBL; JXCA01000006; KIJ84981.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2MD30; -.
DR   STRING; 1233231.SD80_09000; -.
DR   OrthoDB; 472999at2; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00146; PKD; 1.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 1.
DR   InterPro; IPR025193; DUF4114.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR   InterPro; IPR001343; Hemolysn_Ca-bd.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   InterPro; IPR019960; T1SS_VCA0849.
DR   NCBIfam; TIGR03661; T1SS_VCA0849; 1.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF13448; DUF4114; 1.
DR   Pfam; PF00353; HemolysinCabind; 2.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF51120; beta-Roll; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 3.
DR   PROSITE; PS50093; PKD; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT   DOMAIN          848..943
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   REGION          479..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1245 AA;  132351 MW;  2D9623EC055F3617 CRC64;
     MENYSLGSEE FIRQAALRAL SNSPNSGYVV ISELTEKAAF TGSLQTGINF NTEKYLGEKR
     FDLRPGSRFG IMLLPNGNIQ DLLSNPNGNN PQLPLFSIAA ANLGESLQFS RLVNLKADDN
     IFSFEDTSLT KNSDKDYDDI IFRVVGASGE VPSYNQLVPP EKNLLNTLLG SVLPNPPKSK
     EYPIDLKKDL GLVDEPIQVS EGVWFLGRGI APDDLKIVKP NNLYAGYTSS TDKLWNGGGL
     GLNLDGNGLT VGVWEATEAG SWRIRDTHRE LNGRVNFGEN GTGFSNHATH VAGTIAATGI
     NRRARGMANG VNLRSFSAAD DTTEMNQNAA QLVVSNHSYG ASRGWDIGNQ QIIDGTTVNN
     TNVWLDDYSN SSTEDANFGK YDSDAQDLDT VLFNNPNLLS VWSAGNHRID FFSNRSNNNT
     FVTYFGSNPN IAGFNWTRQG WYQVATNIVA PPGSDGNGGT GYDSLTGEKT AKNTLVVGSV
     TDNKDNPYTN SNPTISNFSS WGPTDDGRVK PDVVAKGGNN LPKVQLLSSL GTADDDYNTG
     LDDYYGTSMA APVVTGTAVL LTQHYQNLFN RLPPSATTKG LLIHTATDIG NLGPDYQSGW
     GLIDGTTAAD FLTQTASQNP SYILQENTYT GTQQTFNVIS NGADPLKATI VWTDPAGSVQ
     GKGLDVNTRV LVNDLDLSIT DPNGVVHFPW TLDLTRPEQP AVRNRANNLD NVEQVLIDAP
     IAGTYTIRIG HTGNSFTQNY SLFVSAAKND QPIANANGKY IVPEGGTITL SSAGSIDPDG
     FINAFHWDLN YDDGSSFNID SANPSPVFDA SNIDAGKPSI IRTVALGIID NRGATAFSTA
     KLEIINVSPT AFVRGDTFGV PGLSRSFTFS ATDPSKADTA AGFTFNVGYG DGTSQESKSK
     DPFTLTHTYT AEGNYTTTVT AKDKDDGISK AATHTIEIKA AGILPCPKDP SKTALYVGGT
     LGTDQINVTQ QGETGIYNVL VNGQSKGSFS PNGCIIIYGQ DGDDEIDAPN SSLPVEMYAG
     IGNDRLKGGF GNVSMFGGIG DDTYYIDSTN DIATEYANEG TDTVNAAISY TLAANLENLN
     LLEGTAALNG TGNELSNTIN GNSANNTLNG GAGDDRLFGF AGGDTLQGGD GNDWIIGGQG
     NDILTGGAGN DYFVYNGITD AGDRITDFTV GSDKIVLTDL LKNLGYQGSN AIANGLLSFK
     QASSSLAVIQ IDPDGTASNL FRPAPFILLD NVSVTALNNP NNFVF
//