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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//