synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZ domain-containing protein 8 (PDZD8), also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondria membranes. PDZD8-dependent endoplasmic reticulum-mitochondria membrane tethering is essential for ER-mitochondria Ca(2+) transfer. In neurons, PDZD8 is involved in the regulation of dendritic Ca(2+) dynamics by regulating mitochondrial Ca(2+) uptake in neurons. It plays an indirect role in the regulation of cell morphology and cytoskeletal organization. PDZD8 is also a novel Gag-interacting factor that promotes retroviral infection. It may act as a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1 (HSV1). This model corresponds to the SMP domain of PDZD8, which may be implicated in lipid transport.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330428   68 ESCNSISLLLHMLFQEHKDTRALRRWVHKRLQMEMNDITTRSAAGRLIQEIRIRELSLGTKFMTINSIRVESVEMADDKN 147
Cdd:cd21674      1 ESCVWLNLLFQFLFQELRDTKRVRRWVTKKLNVEFEELLKTKTAGKFLESITVRDLSLGTSFPVIKNVTVINVKLSEDED 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330428  148 TFDKIVFILDIDYSGGFETSIDVSTIIAKKASLSVKITKLTGMVRVILSRQPYHHWTFSFVSQPIFETDINSQIQGHQLK 227
Cdd:cd21674     81 VPEELDLALDLEYSGGFQLAIDVDLVFGKSAYLSIKVVKLSGRLRLQFSRLPYTHWSFSFYEEPIIEFDVESRFEGRQLP 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1734330428  228 RLIPIIKEAIRRSLQRKHVWPNYKIRYRPFF 258
Cdd:cd21674    161 QLTSLIINQIRRVIRKKHTLPNYKIRYKPFF 191

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1734330428   354 GNNTNRAVKVCTVEDNSLADKAAFKPGDVLVAINNVPIR--SERQATRFLQSTTGDLTVLVER 414
Cdd:smart00228   21 GKDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEglTHLEAVDLLKKAGGKVTLTVLR 83

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZ domain-containing protein 8 (PDZD8), also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondria membranes. PDZD8-dependent endoplasmic reticulum-mitochondria membrane tethering is essential for ER-mitochondria Ca(2+) transfer. In neurons, PDZD8 is involved in the regulation of dendritic Ca(2+) dynamics by regulating mitochondrial Ca(2+) uptake in neurons. It plays an indirect role in the regulation of cell morphology and cytoskeletal organization. PDZD8 is also a novel Gag-interacting factor that promotes retroviral infection. It may act as a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1 (HSV1). This model corresponds to the SMP domain of PDZD8, which may be implicated in lipid transport.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330428   68 ESCNSISLLLHMLFQEHKDTRALRRWVHKRLQMEMNDITTRSAAGRLIQEIRIRELSLGTKFMTINSIRVESVEMADDKN 147
Cdd:cd21674      1 ESCVWLNLLFQFLFQELRDTKRVRRWVTKKLNVEFEELLKTKTAGKFLESITVRDLSLGTSFPVIKNVTVINVKLSEDED 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330428  148 TFDKIVFILDIDYSGGFETSIDVSTIIAKKASLSVKITKLTGMVRVILSRQPYHHWTFSFVSQPIFETDINSQIQGHQLK 227
Cdd:cd21674     81 VPEELDLALDLEYSGGFQLAIDVDLVFGKSAYLSIKVVKLSGRLRLQFSRLPYTHWSFSFYEEPIIEFDVESRFEGRQLP 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1734330428  228 RLIPIIKEAIRRSLQRKHVWPNYKIRYRPFF 258
Cdd:cd21674    161 QLTSLIINQIRRVIRKKHTLPNYKIRYKPFF 191

protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZD8, also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondrial membranes. PDZD8-dependent ER-mitochondria membrane tethering is essential for ER-mitochondria Ca2+ transfer. In neurons, it is involved in the regulation of dendritic Ca2+ dynamics by regulating mitochondrial Ca2+ uptake. PDZD8 also plays an indirect role in the regulation of cell morphology and cytoskeletal organization. It contains a PDZ domain and a C1 domain. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1734330428  997 HDWKLWYGKNSTTCAMCRGKIWLRNASSCSRCLVICHNKCVVKA 1040
Cdd:cd20825      4 HDFVLTQFQNATYCDFCKKKIWLKEAFQCRLCGMICHKKCLDKC 47

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1734330428  363 VCTVEDNSLADKAAFKPGDVLVAINNVPIRSERQATRFLQSTTGD-LTVLVER 414
Cdd:pfam17820    2 VTAVVPGSPAERAGLRVGDVILAVNGKPVRSLEDVARLLQGSAGEsVTLTVRR 54

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1734330428  354 GNNTNRAVKVCTVEDNSLADKA-AFKPGDVLVAINNVPIR--SERQATRFLQSTTGDLTVLV 412
Cdd:cd00136     19 GKDGGGGIFVSRVEPGGPAARDgRLRVGDRILEVNGVSLEglTHEEAVELLKSAGGEVTLTV 80

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734330428  359 RAVKVCTVEDNSLADKAAFKPGDVLVAINNVPIRSERQATRFLQSTT--GDLTVLVER 414
Cdd:TIGR02037  362 KGVVVTKVVSGSPAARAGLQPGDVILSVNQQPVSSVAELRKVLARAKkgGRVALLILR 419

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZ domain-containing protein 8 (PDZD8), also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondria membranes. PDZD8-dependent endoplasmic reticulum-mitochondria membrane tethering is essential for ER-mitochondria Ca(2+) transfer. In neurons, PDZD8 is involved in the regulation of dendritic Ca(2+) dynamics by regulating mitochondrial Ca(2+) uptake in neurons. It plays an indirect role in the regulation of cell morphology and cytoskeletal organization. PDZD8 is also a novel Gag-interacting factor that promotes retroviral infection. It may act as a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1 (HSV1). This model corresponds to the SMP domain of PDZD8, which may be implicated in lipid transport.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330428   68 ESCNSISLLLHMLFQEHKDTRALRRWVHKRLQMEMNDITTRSAAGRLIQEIRIRELSLGTKFMTINSIRVESVEMADDKN 147
Cdd:cd21674      1 ESCVWLNLLFQFLFQELRDTKRVRRWVTKKLNVEFEELLKTKTAGKFLESITVRDLSLGTSFPVIKNVTVINVKLSEDED 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330428  148 TFDKIVFILDIDYSGGFETSIDVSTIIAKKASLSVKITKLTGMVRVILSRQPYHHWTFSFVSQPIFETDINSQIQGHQLK 227
Cdd:cd21674     81 VPEELDLALDLEYSGGFQLAIDVDLVFGKSAYLSIKVVKLSGRLRLQFSRLPYTHWSFSFYEEPIIEFDVESRFEGRQLP 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1734330428  228 RLIPIIKEAIRRSLQRKHVWPNYKIRYRPFF 258
Cdd:cd21674    161 QLTSLIINQIRRVIRKKHTLPNYKIRYKPFF 191

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain superfamily; The SMP domain is a lipid transport domain found in phospholipid transfer proteins such as synaptotagmin family proteins, tricalbin (TCB) family proteins, maintenance of mitochondrial morphology protein 1 (MMM1), mitochondrial distribution and morphology protein 12 (MDM12), mitochondrial distribution and morphology protein 34 (MDM34), PDZ domain-containing protein 8 (PDZD8), testis-expressed protein 2 (TEX2), meiotically up-regulated gene 190 protein (Mug190), C2 domain-containing protein 2 (C2CD2) and C2 domain-containing protein 2-like (C2CD2L). The SMP domain belongs to a superfamily of lipid/hydrophobic ligand-binding domains called TULIP (tubular lipid-binding proteins). It adopts a TULIP fold with two alpha helices and a highly curved antiparallel beta sheet forming a cornucopia-like structure.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330428   90 LRRWVHKRLQMEMNDITTrsaaGRLIQEIRIRELSLGTKFMTINSIRVesvemADDKNTFDKIVFILDIDYSGGFetSID 169
Cdd:cd21669      1 LEQLIRESLQELLEEVKK----PSFIESLELTEFTLGSNPPRIKSVRV-----LDSPSSDLQLVLDLDLEYAGDF--SVV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330428  170 VSTIIAKK-----ASLSVKITKLTGMVRVILS---RQPY-HHWTFSFVSQPIFETDInsQIQGHQLKRLIPIIKEAIRRS 240
Cdd:cd21669     70 LSAKLGGGglglpVPVSVSDLSLEGRLRVRLTllpEFPYvGALSISFVEPPDIDFSI--RPLGGVDLMELPGLSSWLEKL 147

                          170
                   ....*....|...
gi 1734330428  241 LQR----KHVWPN 249
Cdd:cd21669    148 LTDalveLLVEPN 160

protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZD8, also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondrial membranes. PDZD8-dependent ER-mitochondria membrane tethering is essential for ER-mitochondria Ca2+ transfer. In neurons, it is involved in the regulation of dendritic Ca2+ dynamics by regulating mitochondrial Ca2+ uptake. PDZD8 also plays an indirect role in the regulation of cell morphology and cytoskeletal organization. It contains a PDZ domain and a C1 domain. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1734330428  997 HDWKLWYGKNSTTCAMCRGKIWLRNASSCSRCLVICHNKCVVKA 1040
Cdd:cd20825      4 HDFVLTQFQNATYCDFCKKKIWLKEAFQCRLCGMICHKKCLDKC 47

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1734330428  997 HDWKLWYGKNSTTCAMCRGKIW--LRNASSCSRCLVICHNKCVVKA 1040
Cdd:cd00029      1 HRFVPTTFSSPTFCDVCGKLIWglFKQGLKCSDCGLVCHKKCLDKA 46

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1734330428  363 VCTVEDNSLADKAAFKPGDVLVAINNVPIRSERQATRFLQSTTGD-LTVLVER 414
Cdd:pfam17820    2 VTAVVPGSPAERAGLRVGDVILAVNGKPVRSLEDVARLLQGSAGEsVTLTVRR 54

Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1734330428  354 GNNTNRAVKVCTVEDNSLADKAAFKPGDVLVAINNVPIRSERQATRFLQSTTGD-LTVLVER 414
Cdd:COG0750    123 GVPVLTPPVVGEVVPGSPAAKAGLQPGDRIVAINGQPVTSWDDLVDIIRASPGKpLTLTVER 184

protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1734330428  996 SHDWKLWYGKNSTTCAMCRGKIW--LRNASSCSRCLVICHNKCVVKA 1040
Cdd:cd20824      1 PHNFKPHSFSIPTKCDYCGEKIWglSKKGLSCKDCGFNCHIKCELKV 47

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1734330428  996 SHDWKLWYGKNSTTCAMCRGKIWlRNASSCSRCLVICHNKCVVKANSggiACTPQ 1050
Cdd:cd20826      2 SHSFKEKSFRKPRTCDVCKQIIW-NEGSSCRVCKYACHRKCEPKVTA---ACSPS 52

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1734330428  354 GNNTNRAVKVCTVEDNSLADKA-AFKPGDVLVAINNVPIR--SERQATRFLQSTTGDLTVLV 412
Cdd:cd00136     19 GKDGGGGIFVSRVEPGGPAARDgRLRVGDRILEVNGVSLEglTHEEAVELLKSAGGEVTLTV 80

protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; Munc13-1, also called protein unc-13 homolog A (Unc13A), is a diacylglycerol (DAG) receptor that plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Loss of MUNC13-1 function causes microcephaly, cortical hyperexcitability, and fatal myasthenia. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1734330428  990 PALSPASHDWKLWYGKNSTTCAMCRGKIW--LRNASSCSRCLVICHNKC 1036
Cdd:cd20858      1 PISCTTPHNFEVWTATTPTYCYECEGLLWgiARQGMRCTECGVKCHEKC 49

protein kinase C conserved region 1 (C1 domain) found in Munc13-2, Munc13-3 and similar proteins; Munc13-2, also called protein unc-13 homolog B (Unc13B), plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Munc13-2 is essential for normal release probability at hippocampal mossy fiber synapses. Munc13-3 is almost exclusively expressed in the cerebellum. It acts as a tumor suppressor and plays a critical role in the formation of release sites with calcium channel nanodomains. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1734330428  990 PALSPASHDWKLWYGKNSTTCAMCRGKIW--LRNASSCSRCLVICHNKC 1036
Cdd:cd20859     13 PISCTTPHNFEVWTATTPTYCYECEGLLWgiARQGMRCSECGVKCHEKC 61

Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1734330428  355 NNTNRAVKVCTVEDNSLADKAAFKPGDVLVAINNVPIRSERQATRFLQSTTGD-LTVLVER 414
Cdd:COG3975    490 SADGGGLVVTSVLWGSPAYKAGLSAGDELLAIDGLRVTADNLDDALAAYKPGDpIELLVFR 550

Peptidase family M50;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734330428  361 VKVCTVEDNSLADKAAFKPGDVLVAINNVPIRSERQATRFLQSTTGD-LTVLVERS 415
Cdd:pfam02163   95 PVIGGVAPGSPAAKAGLKPGDVILSINGKKITSWQDLVEALAKSPGKpITLTVERG 150

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330428  342 IGLVFDKNvaatgnntNRAVKVCTVEDNSLADKAAFKPGDVLVAINNVPIRSER--QATRFLQSTTGD-LTVLVERsldd 418
Cdd:COG0793     62 LGAELGEE--------DGKVVVVSVIPGSPAEKAGIKPGDIILAIDGKSVAGLTldDAVKLLRGKAGTkVTLTIKR---- 129

                           90       100
                   ....*....|....*....|
gi 1734330428  419 ideeeSKEAAEIVVSTVRDI 438
Cdd:COG0793    130 -----PGEGEPITVTLTRAE 144

permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping serine proteases and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Deg/HtrA-type serine proteases that participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. Typically, these proteases have an N-terminal serine protease domain and at least one C-terminal PDZ domain that recognizes substrates, and in some cases activates the protease function. An exception is yeast Nma11p which has two protease domains and four PDZ domains; its N-terminal half is comprised of a protease domain, followed by two PDZ domains, and its C-terminal half has a similar domain arrangement. HtrA-type proteases include the human HtrA1-4 and MBTPS2, tricorn protease, DegS, DegP and C-terminal processing peptidase, cyanobacterial serine proteases Hhoa, HhoB, and HtrA, and yeast Nma11p. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-termini of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This Deg/HtrA family PDZ domain is a circularly permuted PDZ domain which places beta-strand A at the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1734330428  350 VAATGNNTNRAVKVCTVEDNSLADKAAFKPGDVLVAINNVPIRS 393
Cdd:cd06779     16 AKELGLPVNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTS 59

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330428  347 DKNVA-ATGNNTNRAVKVCTVEDNSLADKAAFKPGDVLVAINNVPIRSERQatrfLQSTTGDLTVLVERSLDDIDEEESK 425
Cdd:TIGR02037  244 TSDLAkSLGLEKQRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFAD----LRRAIGTLKPGKKVTLGILRKGKEK 319

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1734330428  426 EaAEIVVstvrdidgTGSVNDTADSTSLISNNSVAN----DRDSLKDDDKTIGGIPAkdgKINATALAARR 492
Cdd:TIGR02037  320 T-ITVTL--------GASPEEQASSSNPFLGLTVANlspeIRKELRLKGDVKGVVVT---KVVSGSPAARA 378

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1734330428  997 HDWKLWYGKNSTTCAMCRGKIWL--RNASSCSRCLVICHNKCVVKANS 1042
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGlgKQGLKCSWCKLNVHKRCHEKVPP 48

circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CPP (also known as tail-specific protease, PRC protein, Protease Re, and Photosystem II D1 protein processing peptidase), and related domains. CPP belongs to the peptidase S41A family. It cleaves a C-terminal 11 residue peptide from the precursor form of penicillin-binding protein 3, and may have a role in protecting bacterium from thermal and osmotic stresses. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This CPP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330428  361 VKVCTVEDNSLADKAAFKPGDVLVAINNVPIRSER--QATRFLQSTTG-DLTVLVERslddideeeSKEAAEIVVSTVRD 437
Cdd:cd06782     16 LVVVSPIPGGPAEKAGIKPGDVIVAVDGESVRGMSldEVVKLLRGPKGtKVKLTIRR---------GGEGEPRDVTLTRE 86

                   .
gi 1734330428  438 I 438
Cdd:cd06782     87 K 87

PDZ domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1734330428  356 NTNRAVKVCTVEDNSLADKAAFKPGDVLVAINNVPIRSER 395
Cdd:pfam13180    3 DLEGGVVVVSVKSSGPAAKAGLKAGDVILSIDGRKINDLT 42