ID A4CWW7_SYNPV Unreviewed; 1961 AA.
AC A4CWW7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=P/Homo B domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=WH7805_09564 {ECO:0000313|EMBL:EAR17767.1};
OS Synechococcus sp. (strain WH7805).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=59931 {ECO:0000313|EMBL:EAR17767.1, ECO:0000313|Proteomes:UP000001224};
RN [1] {ECO:0000313|EMBL:EAR17767.1, ECO:0000313|Proteomes:UP000001224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7805 {ECO:0000313|Proteomes:UP000001224};
RA Scanlan D., Ostrowski M., Mazard S., Wilkinson N., Partensky F.,
RA Dufresne A., Garczarek L., Hess W., Gierga G., Voss B., Axmann I., Post A.,
RA Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K., Beeson K.,
RA Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
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:EAR17767.1}.
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; AAOK01000005; EAR17767.1; -; Genomic_DNA.
DR RefSeq; WP_006042713.1; NZ_CH724168.1.
DR STRING; 59931.WH7805_09564; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG2931; Bacteria.
DR eggNOG; COG4412; Bacteria.
DR eggNOG; COG4935; Bacteria.
DR HOGENOM; CLU_234600_0_0_3; -.
DR OrthoDB; 561585at2; -.
DR Proteomes; UP000001224; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
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:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-KW.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR CDD; cd04277; ZnMc_serralysin_like; 1.
DR Gene3D; 2.60.40.2810; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR041690; Cadherin_5.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR013858; Peptidase_M10B_C.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR040853; RapA2_cadherin-like.
DR InterPro; IPR034033; Serralysin-like.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR InterPro; IPR010221; VCBS_dom.
DR NCBIfam; TIGR01965; VCBS_repeat; 1.
DR PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF17803; Cadherin_4; 1.
DR Pfam; PF17892; Cadherin_5; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF08548; Peptidase_M10_C; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50268; CADHERIN_2; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 572..676
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1690..1814
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 20..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1407
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1444
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1614
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1961 AA; 208121 MW; 18FAC452A0EA3EE6 CRC64;
MNLSNLIESL SAYRARSLHT SLNQPEEPDP DISSIDNNPA LTPIDQPLTV ARGLLQNGAT
TPPSQQLNST ESFSEAINGN NSITTEEEAN ETTNIEFRIE SKYLHAGRCA CFACSYSRDS
LETNRESNSE LNNTLSNADP TIAFGTLNEL SDYLTTGFWE EAGTYTRRFN LGGSGLGAKN
GQLTYNITGW ADDSNGLSAE RQNLTREVFN VYEAITGIEF VEVATEGDFR FTDNDSGAYA
YLGGGWYDQD PNTGTIDYNA AIIDYSVINV ASSWFYGDSS YNSYTPQTIF HEIGHALGLG
HQGQYNAGNG NPTYENSAQY GNDTWLTTMM SYWSQTTNTN VNASRAYLQT PMTVDWIALD
KLYGSQGYGS FKAFNGNTVY GVGTNISSGT SEIMNNFATM ISDTAYTLVD GSGYDILNVS
NYSDDQFINL APSELNGTLP SSSSIGGLVN NLTIGVGTIL EEAIGGSGND TFLGNIADNV
FRGGNGGDRF YDSFGSDTYY GGSGTFDTLY FSENYSDFSI ENLGTSLAFS RNNSGLADTD
LIWNDIELVY FNDDVIKTYQ ELLADITPIN TPPTANDVFV ATSEDSNSVS GNFNANDPDS
SDQLTYTITT APTIGSVVVN SDGTFTYNFG NNFQSLGDGD STAVVFQYIA SDDNATDSAP
ATVTITINGS NDAPILSGTP SALTNGTEDI AYLLKASDLL QGYSDIDGDT LSITSVTTAS
ANGTLTPNGN GTWTYTPTQD LNGEVVFSFV VSDGNGGTAN GSTSLTLDPV EDEVLLDEDN
NGIVDGTELT AYQLFSEAGA ITLKNNAGQT YNNSSSGNSD VVAAIETDNG FQVLLEGTGS
RNDTFYVWNT NSNGVIIGGS GWKSGDIATR LGWEETFNFD TNRDGTIGAL ILDDDNNGIV
DGTELTAYQL FSEAGAITLK NNAGQTYNNS SSGNSDVVAA IETDNGFQVL LEGTGSRNDT
FYVWNTNSNG VIIGGSGWKS GDIATRLGWE ETFNFDTNRD GTIGALILDD DNNGIVDGTE
LTAYQLFSEA GAITLKNNAG QTYNNSSSGN SDVVAAIETD NGFQVLLEGT GSRNDTFYVW
NTNSNGVITG GSGWKSGDIA TRLGWEETFN FDTNRDGTIG ALILDDDNNG IVDGTELTAY
QLFSEAGAIT LKNNAGQTYN NSSSGNSDVV AAIETDNGFQ VLLEGTGSRN DTFYVWNTNS
NGVITGGSGW KSGDIATRLG WEETFNFDTN RDGTIGALIL DDDNNGIVDG TELTAYQLFS
EAGAITLKNN AGQTYNNSSS GNSDVVAAIE TDNGFQVLLE GTGSRNDTFY VWDTNSNGVI
TGGSGWKSGN IATRLGWEET FNFDTNRDGT IGLPPSLSSP TLEARFKDQW HLKDSSSGGA
NVASAWLLKN KSGSNIYGTG IHINVIDDGL DWRHQDLSTN YISASSYDYV GKDNDPTPSS
SADHGTAVAG VAAGYGHNGI GITGAAPNAN ISGQRLLGAG TARNEASALT RTMNAVDIYS
NSWGPNDNGR LQAAPARVLA ALKDGVTNGR DGKGAIYTWA GGNGRNSNDN SNYDGYANSR
YVISVAAMTN RGRYSGYSEP GANVLVSAPS NGGTDAITTT STNNSYIDNF GGTSSATPLV
SGVIALMLEA NPNLTWRDVQ HVLVNSSDVV DASSNGWFTN GAEHDFSHDY GFGRINAEAA
VALAKTWNNV GDEVSYSAST TPGIAIPDAG GGSISSTITI SQDITLESVV IPILSDHTYA
GDLTITLTSP EGTTAILSEG NRRDTSTLNF NFSAKTFWGE SSRGVWTLTI NDLASLDTGT
LDQWGLNLYG TQGTNFNAAI TDSITGNELE TFTGASGMTY ASKEALEQIE GLSSYLSHIE
DLLAESPEKA TGDWLIGTQG PQDQIMRASE LGISDSMTSQ TFNAQNGISS FSMISALDPT
EFIAQSLDSL GTNLSYAYPE LLHETTTRSL IPSLETSTFK A
//
