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Conserved domains on  [gi|12836118|dbj|BAB23510|]
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unnamed protein product [Mus musculus]

Protein Classification

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List of domain hits

Name Accession Description Interval E-value
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
317-398 1.92e-15

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 71.83  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12836118  317 IIIHRAGKK-YGFTLRAIRVYMGdtdvytvHHMVWHVEDGGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELVLKSGNK 395
Cdd:cd00992    4 VTLRKDPGGgLGFSLRGGKDSGG-------GIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDE 76

                 ...
gi 12836118  396 VSI 398
Cdd:cd00992   77 VTL 79
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
2-31 4.60e-05

Extension to Ser/Thr-type protein kinases;


:

Pssm-ID: 214529  Cd Length: 64  Bit Score: 41.96  E-value: 4.60e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 12836118       2 GLDWTGLLRQKAE--FIPQLESEDDTSYFDTR 31
Cdd:smart00133    2 GIDWDKLENKEIEppFVPKIKSPTDTSNFDPE 33
Peptidase_M50 pfam02163
Peptidase family M50;
347-455 1.52e-04

Peptidase family M50;


:

Pssm-ID: 308008 [Multi-domain]  Cd Length: 275  Bit Score: 44.38  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12836118    347 HMVWHVEDGGPASEAGLRQGDLITHVNGEPVHGLvhTEVVELVLKSGNKVSISTtplentsikvgpARKGSYKAKMARRS 426
Cdd:pfam02163  102 VTIGGVEPGSPAAKAGLKAGDVILSINGKKITTW--QDVVDAVAQPGKPITLTV------------ERNGQTKTVTITPE 167
                           90       100
                   ....*....|....*....|....*....
gi 12836118    427 KRSKGKDGqeSRKRSSLFRKITKQASLLH 455
Cdd:pfam02163  168 KTGRGFIG--ISPSPALGKLITGQLSLKN 194
 
Name Accession Description Interval E-value
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
317-398 1.92e-15

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 71.83  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12836118  317 IIIHRAGKK-YGFTLRAIRVYMGdtdvytvHHMVWHVEDGGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELVLKSGNK 395
Cdd:cd00992    4 VTLRKDPGGgLGFSLRGGKDSGG-------GIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDE 76

                 ...
gi 12836118  396 VSI 398
Cdd:cd00992   77 VTL 79
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
317-398 3.17e-14

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 68.56  E-value: 3.17e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12836118     317 IIIHRAGKKYGFTLRAIRVYMGdtdvytvHHMVWHVEDGGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELVLKSGNKV 396
Cdd:smart00228    5 VELEKGGGGLGFSLVGGKDEGG-------GVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKV 77

                    ..
gi 12836118     397 SI 398
Cdd:smart00228   78 TL 79
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
317-398 2.56e-07

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 334167 [Multi-domain]  Cd Length: 81  Bit Score: 48.81  E-value: 2.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12836118    317 IIIHRAGKKY-GFTLRAirvyMGDTDVYTVHhmVWHVEDGGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELVLKSGNK 395
Cdd:pfam00595    2 ITLERDGPGGlGFSLKG----GSDQGAKGIF--VSEVLPGGAAEAAGLQAGDRILSVNGVPIENLSHEEAVLALKGSGGK 75

                   ...
gi 12836118    396 VSI 398
Cdd:pfam00595   76 VTL 78
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
352-398 4.70e-06

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


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 50.02  E-value: 4.70e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 12836118  352 VEDGGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELV-LKSGNKVSI 398
Cdd:COG0793  119 PIDGSPAAKAGIKPGDVIIKIDGKSVGGVSLDEAVKLIrGKPGTKVTL 166
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
2-31 4.60e-05

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 41.96  E-value: 4.60e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 12836118       2 GLDWTGLLRQKAE--FIPQLESEDDTSYFDTR 31
Cdd:smart00133    2 GIDWDKLENKEIEppFVPKIKSPTDTSNFDPE 33
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
2-29 1.22e-04

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 45.35  E-value: 1.22e-04
                         10        20
                 ....*....|....*....|....*...
gi 12836118    2 GLDWTGLLRQKAEFIPQLESEDDTSYFD 29
Cdd:cd05573  290 GIDWENLRESPPPFVPELSSPTDTSNFD 317
prc TIGR00225
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ...
355-402 1.36e-04

C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different species including processing of D1 protein of the photosystem II reaction center in higher plants and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein in E.coli E.coli and H influenza have the most distal branch of the tree and their proteins have an N-terminal 200 amino acids that show no homology to other proteins in the database. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Protein fate, Protein modification and repair]


Pssm-ID: 272970 [Multi-domain]  Cd Length: 334  Bit Score: 45.04  E-value: 1.36e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 12836118    355 GGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELVL-KSGNKVSISTTP 402
Cdd:TIGR00225   72 GSPAEKAGIKPGDKIIKINGKSVAGMSLDDAVALIRgKKGTKVSLEILR 120
Peptidase_M50 pfam02163
Peptidase family M50;
347-455 1.52e-04

Peptidase family M50;


Pssm-ID: 308008 [Multi-domain]  Cd Length: 275  Bit Score: 44.38  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12836118    347 HMVWHVEDGGPASEAGLRQGDLITHVNGEPVHGLvhTEVVELVLKSGNKVSISTtplentsikvgpARKGSYKAKMARRS 426
Cdd:pfam02163  102 VTIGGVEPGSPAAKAGLKAGDVILSINGKKITTW--QDVVDAVAQPGKPITLTV------------ERNGQTKTVTITPE 167
                           90       100
                   ....*....|....*....|....*....
gi 12836118    427 KRSKGKDGqeSRKRSSLFRKITKQASLLH 455
Cdd:pfam02163  168 KTGRGFIG--ISPSPALGKLITGQLSLKN 194
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
355-393 3.46e-04

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 43.96  E-value: 3.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 12836118   355 GGPASEAGLRQGDLITHVNGEPVHGLVHTEV-----------VELVLKSG 393
Cdd:PLN00049  112 GGPAARAGIRPGDVILAIDGTSTEGLSLYEAadrlqgpegssVELTLRRG 161
 
Name Accession Description Interval E-value
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
317-398 1.92e-15

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 71.83  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12836118  317 IIIHRAGKK-YGFTLRAIRVYMGdtdvytvHHMVWHVEDGGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELVLKSGNK 395
Cdd:cd00992    4 VTLRKDPGGgLGFSLRGGKDSGG-------GIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDE 76

                 ...
gi 12836118  396 VSI 398
Cdd:cd00992   77 VTL 79
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
317-398 3.17e-14

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 68.56  E-value: 3.17e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12836118     317 IIIHRAGKKYGFTLRAIRVYMGdtdvytvHHMVWHVEDGGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELVLKSGNKV 396
Cdd:smart00228    5 VELEKGGGGLGFSLVGGKDEGG-------GVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKV 77

                    ..
gi 12836118     397 SI 398
Cdd:smart00228   78 TL 79
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
324-398 3.36e-09

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 53.85  E-value: 3.36e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12836118  324 KKYGFTLRairvYMGDTDVYTVHhmvwhVEDGGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELVLKS-GNKVSI 398
Cdd:cd00136    1 GGLGFSIR----GGTEGGVVVLS-----VEPGSPAERAGLQAGDVILAVNGTDVKNLTLEDVAELLKKEvGEKVTL 67
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
351-399 1.20e-08

PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 52.61  E-value: 1.20e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 12836118  351 HVEDGGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELVL-KSGNKVSIS 399
Cdd:cd00988   19 SVLPGSPAAKAGIKAGDIIVAIDGEPVDGLSLEDVVKLLRgKAGTKVRLT 68
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
348-398 7.95e-08

PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238487 [Multi-domain]  Cd Length: 90  Bit Score: 50.72  E-value: 7.95e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 12836118  348 MVWHVEDGGPASEAGLRQGDLITHVNGEPVHGLvhTEVVELV--LKSGNKVSI 398
Cdd:cd00987   27 LVASVDPGSPAAKAGLKPGDVILAVNGKPVKSV--ADLRRALaeLKPGDKVTL 77
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
317-398 2.56e-07

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 334167 [Multi-domain]  Cd Length: 81  Bit Score: 48.81  E-value: 2.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12836118    317 IIIHRAGKKY-GFTLRAirvyMGDTDVYTVHhmVWHVEDGGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELVLKSGNK 395
Cdd:pfam00595    2 ITLERDGPGGlGFSLKG----GSDQGAKGIF--VSEVLPGGAAEAAGLQAGDRILSVNGVPIENLSHEEAVLALKGSGGK 75

                   ...
gi 12836118    396 VSI 398
Cdd:pfam00595   76 VTL 78
PDZ_2 pfam13180
PDZ domain;
349-399 8.49e-07

PDZ domain;


Pssm-ID: 315771 [Multi-domain]  Cd Length: 74  Bit Score: 47.26  E-value: 8.49e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 12836118    349 VWHVEDGGPASEAGLRQGDLITHVNGEPVHGLvhTEVVELVLKS--GNKVSIS 399
Cdd:pfam13180   10 VVSVKSGSPAAKAGLKPGDVILKIDGKKIKSL--DDLNEALLNHkpGDTVKLT 60
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
352-398 4.70e-06

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


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 50.02  E-value: 4.70e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 12836118  352 VEDGGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELV-LKSGNKVSI 398
Cdd:COG0793  119 PIDGSPAAKAGIKPGDVIIKIDGKSVGGVSLDEAVKLIrGKPGTKVTL 166
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
352-395 7.75e-06

PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238489 [Multi-domain]  Cd Length: 79  Bit Score: 44.53  E-value: 7.75e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 12836118  352 VEDGGPASEAGLRQGDLITHVNGEPVHGLvhTEVVELVLKSGNK 395
Cdd:cd00989   19 VVPGSPAAKAGLKAGDRILAINGQKIKSW--EDLVDAVQENPGK 60
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
2-31 4.60e-05

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 41.96  E-value: 4.60e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 12836118       2 GLDWTGLLRQKAE--FIPQLESEDDTSYFDTR 31
Cdd:smart00133    2 GIDWDKLENKEIEppFVPKIKSPTDTSNFDPE 33
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
2-29 1.22e-04

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 45.35  E-value: 1.22e-04
                         10        20
                 ....*....|....*....|....*...
gi 12836118    2 GLDWTGLLRQKAEFIPQLESEDDTSYFD 29
Cdd:cd05573  290 GIDWENLRESPPPFVPELSSPTDTSNFD 317
prc TIGR00225
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ...
355-402 1.36e-04

C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different species including processing of D1 protein of the photosystem II reaction center in higher plants and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein in E.coli E.coli and H influenza have the most distal branch of the tree and their proteins have an N-terminal 200 amino acids that show no homology to other proteins in the database. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Protein fate, Protein modification and repair]


Pssm-ID: 272970 [Multi-domain]  Cd Length: 334  Bit Score: 45.04  E-value: 1.36e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 12836118    355 GGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELVL-KSGNKVSISTTP 402
Cdd:TIGR00225   72 GSPAEKAGIKPGDKIIKINGKSVAGMSLDDAVALIRgKKGTKVSLEILR 120
Peptidase_M50 pfam02163
Peptidase family M50;
347-455 1.52e-04

Peptidase family M50;


Pssm-ID: 308008 [Multi-domain]  Cd Length: 275  Bit Score: 44.38  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12836118    347 HMVWHVEDGGPASEAGLRQGDLITHVNGEPVHGLvhTEVVELVLKSGNKVSISTtplentsikvgpARKGSYKAKMARRS 426
Cdd:pfam02163  102 VTIGGVEPGSPAAKAGLKAGDVILSINGKKITTW--QDVVDAVAQPGKPITLTV------------ERNGQTKTVTITPE 167
                           90       100
                   ....*....|....*....|....*....
gi 12836118    427 KRSKGKDGqeSRKRSSLFRKITKQASLLH 455
Cdd:pfam02163  168 KTGRGFIG--ISPSPALGKLITGQLSLKN 194
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
355-393 3.46e-04

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 43.96  E-value: 3.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 12836118   355 GGPASEAGLRQGDLITHVNGEPVHGLVHTEV-----------VELVLKSG 393
Cdd:PLN00049  112 GGPAARAGIRPGDVILAIDGTSTEGLSLYEAadrlqgpegssVELTLRRG 161
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
352-398 3.98e-04

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]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 43.75  E-value: 3.98e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 12836118    352 VEDGGPASEAGLRQGDLITHVNGEPVHglVHTEVVELV--LKSGNKVSI 398
Cdd:TIGR02037  264 VLPGSPAEKAGLKAGDVITSVNGKPIS--SFADLRRAIgtLKPGKKVTL 310
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
2-29 7.51e-04

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 42.60  E-value: 7.51e-04
                         10        20
                 ....*....|....*....|....*...
gi 12836118    2 GLDWTGLLRQKAEFIPQLESEDDTSYFD 29
Cdd:cd05599  262 GVDWDHIRERPAPILPEVKSILDTSNFD 289
PRK10898 PRK10898
serine endoprotease; Provisional
349-405 8.30e-04

serine endoprotease; Provisional


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 42.68  E-value: 8.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12836118   349 VWHVEDGGPASEAGLRQGDLITHVNGEPVHGLVHT--EVVEL---------VLKSGNKVSISTTPLEN 405
Cdd:PRK10898  283 VNEVSPDGPAAKAGIQVNDLIISVNNKPAISALETmdQVAEIrpgsvipvvVMRDDKQLTLQVTIQEY 350
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
2-30 8.56e-04

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 42.30  E-value: 8.56e-04
                         10        20
                 ....*....|....*....|....*....
gi 12836118    2 GLDWTGLLRQKAEFIPQLESEDDTSYFDT 30
Cdd:cd05598  267 GIDWEKLRKQKAPYIPTIRHPTDTSNFDP 295
spore_IV_B TIGR02860
stage IV sporulation protein B; SpoIVB, the stage IV sporulation protein B of ...
332-419 2.32e-03

stage IV sporulation protein B; SpoIVB, the stage IV sporulation protein B of endospore-forming bacteria such as Bacillus subtilis, is a serine proteinase, expressed in the spore (rather than mother cell) compartment, that participates in a proteolytic activation cascade for Sigma-K. It appears to be universal among endospore-forming bacteria and occurs nowhere else. [Cellular processes, Sporulation and germination]


Pssm-ID: 274325 [Multi-domain]  Cd Length: 402  Bit Score: 41.17  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12836118    332 AIRVYMGDTDVYTVHHMVWHVEDG---GPASEAGLRQGDLITHVNGEPVHGLvhTEVVELVLKSGNKvSISTTPLENTSI 408
Cdd:TIGR02860   97 SIGVKLNTKGVLVVGFSDIETEKGkihSPGEEAGIQIGDRILKINGEKIKNM--DDLANLINKAGGE-KLTLTIERGGKI 173
                           90
                   ....*....|....*..
gi 12836118    409 ---KVGPARK---GSYK 419
Cdd:TIGR02860  174 ietVIKPVKDkeeGRYR 190
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
2-29 2.49e-03

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 41.17  E-value: 2.49e-03
                         10        20
                 ....*....|....*....|....*....
gi 12836118    2 GLDWTGLLRQ-KAEFIPQLESEDDTSYFD 29
Cdd:cd05600  314 NIDWDRLREGsKPPFIPELESEIDTSYFD 342
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
2-29 3.65e-03

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 40.41  E-value: 3.65e-03
                         10        20
                 ....*....|....*....|....*...
gi 12836118    2 GLDWTGLLRQKAEFIPQLESEDDTSYFD 29
Cdd:cd05597  271 GIDWDNIRDSTPPYIPEVTSPTDTSNFD 298
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
348-399 7.15e-03

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223343 [Multi-domain]  Cd Length: 347  Bit Score: 39.49  E-value: 7.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 12836118  348 MVWHVEDGGPASEAGLRQGDLITHVNGEPVHGlvHTEVVELV--LKSGNKVSIS 399
Cdd:COG0265  273 VVLGVLPGSPAAKAGIKAGDIITAVNGKPVAS--LSDLVAAVasNRPGDEVALK 324
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
314-375 9.56e-03

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


Pssm-ID: 226483 [Multi-domain]  Cd Length: 558  Bit Score: 39.73  E-value: 9.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12836118  314 RPPIIIHRAGKKYGFTLRAIR---VYMG-DTDVYTVHHMVWHVEDGGPASEAGLRQGDLITHVNGE 375
Cdd:COG3975  427 TEPPPLNPLLERFGLTFTPKPreaYYLGlKVKSEGGHEKITFVFPGGPAYKAGLSPGDKIVAINGI 492
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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