NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1622894302|ref|XP_014978773|]
View 

small conductance calcium-activated potassium channel protein 1 isoform X2 [Macaca mulatta]

Protein Classification

SK_channel and CaMBD domain-containing protein( domain architecture ID 10507664)

protein containing domains SK_channel, Ion_trans_2, and CaMBD

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
176-285 9.92e-64

Calcium-activated SK potassium channel;


:

Pssm-ID: 460958  Cd Length: 111  Bit Score: 205.52  E-value: 9.92e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302 176 LGHRRALFEKRKRLSDYALIFGMFGIVVMVTETELSW-GVYTKESLYSFALKCLISLSTAILLGLVVLYHAREIQLFMVD 254
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622894302 255 NGADDWRIAMTCERVFLISLELAVCAIHPVP 285
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 467-545 2.48e-41

Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other.


:

Pssm-ID: 198121  Cd Length: 76  Bit Score: 144.09  E-value: 2.48e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622894302  467 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQARVRKHQRKFLQAIHQaqkLRSVKIEQGKLNDQANTLTDLAKTQS 545
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQ---FRSVKMKQRKLREQANSLVDLAKTQM 76
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 374-453 7.17e-15

Ion channel; This family includes the two membrane helix type ion channels found in bacteria.


:

Pssm-ID: 462301 [Multi-domain]  Cd Length: 78  Bit Score: 69.99  E-value: 7.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302 374 ISSWIIAAWTVrvcerYHDKQEVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLE 453
Cdd:pfam07885   3 LLLVLIFGTVY-----YLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 22-146 6.06e-07

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


:

Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 49.65  E-value: 6.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302  22 PPRPQPRLRSPTGGPRPRGTLSPPalsarPGQAQQDSA-GAQPLSHAGPRAACSEPNPCTQVVMNSHSYNGSVGRPLGSG 100
Cdd:pfam15240  46 PQGPPPGGFPPQPPASDDPPGPPP-----PGGPQQPPPqGGKQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGK 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622894302 101 PgalgRDPPDPEVGRPPQPPHSPGlqvvvaksePARPSPGSPRGQP 146
Cdd:pfam15240 121 P----QGPPPQGGGPPPQGGNQQG---------PPPPPPGNPQGPP 153
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
510-589 7.73e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302 510 FLQAIHQAQKLRSVKIEQGKLNDQANTLTDLAKTQSVMYDLvSELHAQHEELEARLATLESRLDALGASLQALPGLIAQA 589
Cdd:COG4717   387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-EELEEELEELEEELEELEEELEELREELAELEAELEQL 465
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
176-285 9.92e-64

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 205.52  E-value: 9.92e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302 176 LGHRRALFEKRKRLSDYALIFGMFGIVVMVTETELSW-GVYTKESLYSFALKCLISLSTAILLGLVVLYHAREIQLFMVD 254
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622894302 255 NGADDWRIAMTCERVFLISLELAVCAIHPVP 285
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 467-545 2.48e-41

Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other.


Pssm-ID: 198121  Cd Length: 76  Bit Score: 144.09  E-value: 2.48e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622894302  467 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQARVRKHQRKFLQAIHQaqkLRSVKIEQGKLNDQANTLTDLAKTQS 545
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQ---FRSVKMKQRKLREQANSLVDLAKTQM 76
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 467-544 1.52e-40

Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other.


Pssm-ID: 460739  Cd Length: 75  Bit Score: 142.04  E-value: 1.52e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622894302 467 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQARVRKHQRKFLQAIHQaqkLRSVKIEQGKLNDQANTLTDLAKTQ 544
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSRVRKHQRKLLQAIHT---FRKVKMKQRKLRDQVNTMVDLSKMQ 75
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 374-453 7.17e-15

Ion channel; This family includes the two membrane helix type ion channels found in bacteria.


Pssm-ID: 462301 [Multi-domain]  Cd Length: 78  Bit Score: 69.99  E-value: 7.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302 374 ISSWIIAAWTVrvcerYHDKQEVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLE 453
Cdd:pfam07885   3 LLLVLIFGTVY-----YLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 22-146 6.06e-07

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 49.65  E-value: 6.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302  22 PPRPQPRLRSPTGGPRPRGTLSPPalsarPGQAQQDSA-GAQPLSHAGPRAACSEPNPCTQVVMNSHSYNGSVGRPLGSG 100
Cdd:pfam15240  46 PQGPPPGGFPPQPPASDDPPGPPP-----PGGPQQPPPqGGKQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGK 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622894302 101 PgalgRDPPDPEVGRPPQPPHSPGlqvvvaksePARPSPGSPRGQP 146
Cdd:pfam15240 121 P----QGPPPQGGGPPPQGGNQQG---------PPPPPPGNPQGPP 153
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 22-167 3.64e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.90  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302  22 PPRPQPRLrSPTGGPRPRGTlSPPALSARPGQAQQDSAGAQPLSHAGPRAACSEPNPctqvvmnSHSYNGSVGRPLGSGP 101
Cdd:PRK07764  600 PPAPASSG-PPEEAARPAAP-AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHP-------KHVAVPDASDGGDGWP 670

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622894302 102 GALGRDPPDPEVGrPPQPPHSPGLQVVVAKSEPARPSPGSPRGQPQDQDDDEDDEEDEAGRQRGSG 167
Cdd:PRK07764  671 AKAGGAAPAAPPP-APAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAA 735
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
467-590 1.11e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302 467 DTQLTKRVKNAAANVlretwliYKHTRLVKKPDQARvrkHQRKFLQAihQAQKLRSvKIEQ--GKLND--QANTLTDLAK 542
Cdd:COG3206   146 DPELAAAVANALAEA-------YLEQNLELRREEAR---KALEFLEE--QLPELRK-ELEEaeAALEEfrQKNGLVDLSE 212

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622894302 543 TQSVMYDLVSELHAQHEELEARLATLESRLDALGASLQALPGLIAQAI 590
Cdd:COG3206   213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
510-589 7.73e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302 510 FLQAIHQAQKLRSVKIEQGKLNDQANTLTDLAKTQSVMYDLvSELHAQHEELEARLATLESRLDALGASLQALPGLIAQA 589
Cdd:COG4717   387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-EELEEELEELEEELEELEEELEELREELAELEAELEQL 465
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
176-285 9.92e-64

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 205.52  E-value: 9.92e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302 176 LGHRRALFEKRKRLSDYALIFGMFGIVVMVTETELSW-GVYTKESLYSFALKCLISLSTAILLGLVVLYHAREIQLFMVD 254
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622894302 255 NGADDWRIAMTCERVFLISLELAVCAIHPVP 285
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 467-545 2.48e-41

Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other.


Pssm-ID: 198121  Cd Length: 76  Bit Score: 144.09  E-value: 2.48e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622894302  467 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQARVRKHQRKFLQAIHQaqkLRSVKIEQGKLNDQANTLTDLAKTQS 545
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQ---FRSVKMKQRKLREQANSLVDLAKTQM 76
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 467-544 1.52e-40

Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other.


Pssm-ID: 460739  Cd Length: 75  Bit Score: 142.04  E-value: 1.52e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622894302 467 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQARVRKHQRKFLQAIHQaqkLRSVKIEQGKLNDQANTLTDLAKTQ 544
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSRVRKHQRKLLQAIHT---FRKVKMKQRKLRDQVNTMVDLSKMQ 75
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 374-453 7.17e-15

Ion channel; This family includes the two membrane helix type ion channels found in bacteria.


Pssm-ID: 462301 [Multi-domain]  Cd Length: 78  Bit Score: 69.99  E-value: 7.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302 374 ISSWIIAAWTVrvcerYHDKQEVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLE 453
Cdd:pfam07885   3 LLLVLIFGTVY-----YLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 22-146 6.06e-07

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 49.65  E-value: 6.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302  22 PPRPQPRLRSPTGGPRPRGTLSPPalsarPGQAQQDSA-GAQPLSHAGPRAACSEPNPCTQVVMNSHSYNGSVGRPLGSG 100
Cdd:pfam15240  46 PQGPPPGGFPPQPPASDDPPGPPP-----PGGPQQPPPqGGKQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGK 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622894302 101 PgalgRDPPDPEVGRPPQPPHSPGlqvvvaksePARPSPGSPRGQP 146
Cdd:pfam15240 121 P----QGPPPQGGGPPPQGGNQQG---------PPPPPPGNPQGPP 153
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 22-167 3.64e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.90  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302  22 PPRPQPRLrSPTGGPRPRGTlSPPALSARPGQAQQDSAGAQPLSHAGPRAACSEPNPctqvvmnSHSYNGSVGRPLGSGP 101
Cdd:PRK07764  600 PPAPASSG-PPEEAARPAAP-AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHP-------KHVAVPDASDGGDGWP 670

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622894302 102 GALGRDPPDPEVGrPPQPPHSPGLQVVVAKSEPARPSPGSPRGQPQDQDDDEDDEEDEAGRQRGSG 167
Cdd:PRK07764  671 AKAGGAAPAAPPP-APAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAA 735
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 22-170 1.05e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302   22 PPRPQPRLRSPTGGPRPRgtlSPPALSARPGQAqqdsagaqplSHAGPRAACSEPNPCTQVVMNSHSYNGSVGRPLGSGP 101
Cdd:PHA03307   277 GPSSRPGPASSSSSPRER---SPSPSPSSPGSG----------PAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSP 343

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622894302  102 GALGRDPPDPEVGRPPQPPHSPglqvvvAKSEPARPSPGSPRgQPQDQDDDEDDEEDEAGRQRGSGKPS 170
Cdd:PHA03307   344 GPSPSRSPSPSRPPPPADPSSP------RKRPRPSRAPSSPA-ASAGRPTRRRARAAVAGRARRRDATG 405
PHA03247 PHA03247
large tegument protein UL36; Provisional
 22-143 4.58e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 4.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302   22 PPRPQPRLRSPTGGPRPRGTLSPPAlSAR---PGQAQQDSAGAQPLSHAGPRAACSEPNPCTQvvmNSHSYNGSVGRPLG 98
Cdd:PHA03247  2570 PPRPAPRPSEPAVTSRARRPDAPPQ-SARpraPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSP---SPAANEPDPHPPPT 2645

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1622894302   99 SGPGALGRDPPDPEVGRPPQPPHSPGlQVVVAKSEPARPSPGSPR 143
Cdd:PHA03247  2646 VPPPERPRDDPAPGRVSRPRRARRLG-RAAQASSPPQRPRRRAAR 2689
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 22-146 7.08e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 7.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302  22 PPRPQPRLRSPTGGPRPRGTLSPPALS---ARPGQAQQDSAGAQPLSHAGPR-------------AACSEPNPCTQVVMN 85
Cdd:pfam03154 185 SPPPPGTTQAATAGPTPSAPSVPPQGSpatSQPPNQTQSTAAPHTLIQQTPTlhpqrlpsphpplQPMTQPPPPSQVSPQ 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302  86 SH---SYNGSV---GRPLGSGPGALGRD-PPDP----------EVGRPPQP--PHSPGLQVVVAKSEPARPSPGSPRGQP 146
Cdd:pfam03154 265 PLpqpSLHGQMppmPHSLQTGPSHMQHPvPPQPfpltpqssqsQVPPGPSPaaPGQSQQRIHTPPSQSQLQSQQPPREQP 344
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 22-124 1.00e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302   22 PPRPQPRLRSPTGGPRPRgTLSPPALS--ARPGQAQQDSAGAQPLSHA---------GPRAACSEPNPcTQVVMNSHSYN 90
Cdd:PHA03307   194 PPSTPPAAASPRPPRRSS-PISASASSpaPAPGRSAADDAGASSSDSSssessgcgwGPENECPLPRP-APITLPTRIWE 271

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1622894302   91 GSVGRPLGSGPGALGRDPPDPEVGRPPQPPHSPG 124
Cdd:PHA03307   272 ASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGS 305
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
467-590 1.11e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302 467 DTQLTKRVKNAAANVlretwliYKHTRLVKKPDQARvrkHQRKFLQAihQAQKLRSvKIEQ--GKLND--QANTLTDLAK 542
Cdd:COG3206   146 DPELAAAVANALAEA-------YLEQNLELRREEAR---KALEFLEE--QLPELRK-ELEEaeAALEEfrQKNGLVDLSE 212

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622894302 543 TQSVMYDLVSELHAQHEELEARLATLESRLDALGASLQALPGLIAQAI 590
Cdd:COG3206   213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 500-590 1.58e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302 500 QARVRKHQRKFLQAIHQA-----QKLRSVKIEQGKLNDQANTLTD-LAKTQsvmyDLVSELHAQHEELEARLATLESRLD 573
Cdd:COG4942    18 QADAAAEAEAELEQLQQEiaeleKELAALKKEEKALLKQLAALERrIAALA----RRIRALEQELAALEAELAELEKEIA 93

                          90
                  ....*....|....*..
gi 1622894302 574 ALGASLQALPGLIAQAI 590
Cdd:COG4942    94 ELRAELEAQKEELAELL 110
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 27-142 7.54e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 39.28  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302  27 PRLRSPTGGPRPRGTLSPPALSARPGQAQQDSAGAQPLSHAGPRAACSepnpctqvvmnSHSYNGSVGRPLGSGPGalgr 106
Cdd:PRK14959  363 PRLMPVESLRPSGGGASAPSGSAAEGPASGGAATIPTPGTQGPQGTAP-----------AAGMTPSSAAPATPAPS---- 427

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622894302 107 DPPDPEV---GRPPQPPHSPGLQVVVAKSEPARPSPGSP 142
Cdd:PRK14959  428 AAPSPRVpwdDAPPAPPRSGIPPRPAPRMPEASPVPGAP 466
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
510-589 7.73e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302 510 FLQAIHQAQKLRSVKIEQGKLNDQANTLTDLAKTQSVMYDLvSELHAQHEELEARLATLESRLDALGASLQALPGLIAQA 589
Cdd:COG4717   387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-EELEEELEELEEELEELEEELEELREELAELEAELEQL 465
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 30-142 7.84e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 7.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894302  30 RSPTGGPRPRGTLSPPALSARPGQAQQDSAGAQPLSHAGPRAACSEPNPCTQVVMNSHSYNGSVGRPLGSGPGALGRDPP 109
Cdd:PRK07764  664 DGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPP 743

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622894302 110 DPE---VGRPPQPPHSPGLQVVVAKSEPARPSPGSP 142
Cdd:PRK07764  744 EPDdppDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH