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Conserved domains on  [gi|14043024|ref|NP_004272|]
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BAG family molecular chaperone regulator 3 [Homo sapiens]

Protein Classification

WW domain-containing protein( domain architecture ID 11269963)

WW domain-containing protein; the WW domain mediates protein-protein interaction via proline-rich motifs, such as PPxY

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAG smart00264
BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated ...
 421-498 3.18e-24

BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated athanogene 1 and silencer of death domains


:

Pssm-ID: 214591  Cd Length: 79  Bit Score: 96.22  E-value: 3.18e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14043024    421 GVLKVEAILEKVQG-LEQAVDNFEGKKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQKA 498
Cdd:smart00264   1 SIKKINEVLDEVQKkIEKEVQVADGKKDDKEYLRLSEELMKLLLKLDSVDVEGCEDIREARKRLVRLIQNLLNALDSKK 79
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 21-53 5.34e-08

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


:

Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 48.75  E-value: 5.34e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 14043024     21 PLPPGWEIKIDPQtGWPFFVDHNSRTTTWNDPR 53
Cdd:smart00456   1 PLPPGWEERKDPD-GRPYYYNHETKETQWEKPR 32
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 257-417 4.39e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043024   257 PRPLRAASPFRSSVQGASSREGSPARSSTPLHSPSPIRVHTVVdrpqQPMTHRETAPvsQPENKPESKPGPVGPELPPGH 336
Cdd:PHA03247 2650 ERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTV----GSLTSLADPP--PPPPTPEPAPHALVSATPLPP 2723

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043024   337 IPiQVIRKEVDSKPVSQKPPPPSEKVEVKVPPAPVPCPPPSPGPSAVPSSPKSVATEERAAP-----STAPAEATPPKPG 411
Cdd:PHA03247 2724 GP-AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTrpavaSLSESRESLPSPW 2802


                  ....*.
gi 14043024   412 EAEAPP 417
Cdd:PHA03247 2803 DPADPP 2808
 
Name Accession Description Interval E-value
BAG smart00264
BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated ...
 421-498 3.18e-24

BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated athanogene 1 and silencer of death domains


Pssm-ID: 214591  Cd Length: 79  Bit Score: 96.22  E-value: 3.18e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14043024    421 GVLKVEAILEKVQG-LEQAVDNFEGKKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQKA 498
Cdd:smart00264   1 SIKKINEVLDEVQKkIEKEVQVADGKKDDKEYLRLSEELMKLLLKLDSVDVEGCEDIREARKRLVRLIQNLLNALDSKK 79
BAG pfam02179
BAG domain; Domain present in Hsp70 regulators.
 425-497 1.44e-22

BAG domain; Domain present in Hsp70 regulators.


Pssm-ID: 460475 [Multi-domain]  Cd Length: 77  Bit Score: 91.52  E-value: 1.44e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14043024   425 VEAILEKVQGLEQAVDNFEG----KKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQK 497
Cdd:pfam02179   1 IDAILKEVDKLEPQVEAFEGsppsKKRDKEYKRLSEMLMKLLLKLDGIDTEGDPEAREARKAAVKEVQGLLEKLDAL 77
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 21-53 5.34e-08

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 48.75  E-value: 5.34e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 14043024     21 PLPPGWEIKIDPQtGWPFFVDHNSRTTTWNDPR 53
Cdd:smart00456   1 PLPPGWEERKDPD-GRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 23-53 1.39e-07

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 47.52  E-value: 1.39e-07
                        10        20        30
                ....*....|....*....|....*....|.
gi 14043024  23 PPGWEIKIDPQtGWPFFVDHNSRTTTWNDPR 53
Cdd:cd00201   1 PPGWEERWDPD-GRVYYYNHNTKETQWEDPR 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 22-52 1.57e-07

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 47.50  E-value: 1.57e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 14043024    22 LPPGWEIKIDPQtGWPFFVDHNSRTTTWNDP 52
Cdd:pfam00397   1 LPPGWEERWDPD-GRVYYYNHETGETQWEKP 30
PHA03247 PHA03247
large tegument protein UL36; Provisional
 257-417 4.39e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043024   257 PRPLRAASPFRSSVQGASSREGSPARSSTPLHSPSPIRVHTVVdrpqQPMTHRETAPvsQPENKPESKPGPVGPELPPGH 336
Cdd:PHA03247 2650 ERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTV----GSLTSLADPP--PPPPTPEPAPHALVSATPLPP 2723

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043024   337 IPiQVIRKEVDSKPVSQKPPPPSEKVEVKVPPAPVPCPPPSPGPSAVPSSPKSVATEERAAP-----STAPAEATPPKPG 411
Cdd:PHA03247 2724 GP-AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTrpavaSLSESRESLPSPW 2802


                  ....*.
gi 14043024   412 EAEAPP 417
Cdd:PHA03247 2803 DPADPP 2808
 
Name Accession Description Interval E-value
BAG smart00264
BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated ...
 421-498 3.18e-24

BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated athanogene 1 and silencer of death domains


Pssm-ID: 214591  Cd Length: 79  Bit Score: 96.22  E-value: 3.18e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14043024    421 GVLKVEAILEKVQG-LEQAVDNFEGKKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQKA 498
Cdd:smart00264   1 SIKKINEVLDEVQKkIEKEVQVADGKKDDKEYLRLSEELMKLLLKLDSVDVEGCEDIREARKRLVRLIQNLLNALDSKK 79
BAG pfam02179
BAG domain; Domain present in Hsp70 regulators.
 425-497 1.44e-22

BAG domain; Domain present in Hsp70 regulators.


Pssm-ID: 460475 [Multi-domain]  Cd Length: 77  Bit Score: 91.52  E-value: 1.44e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14043024   425 VEAILEKVQGLEQAVDNFEG----KKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQK 497
Cdd:pfam02179   1 IDAILKEVDKLEPQVEAFEGsppsKKRDKEYKRLSEMLMKLLLKLDGIDTEGDPEAREARKAAVKEVQGLLEKLDAL 77
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 21-53 5.34e-08

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 48.75  E-value: 5.34e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 14043024     21 PLPPGWEIKIDPQtGWPFFVDHNSRTTTWNDPR 53
Cdd:smart00456   1 PLPPGWEERKDPD-GRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 23-53 1.39e-07

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 47.52  E-value: 1.39e-07
                        10        20        30
                ....*....|....*....|....*....|.
gi 14043024  23 PPGWEIKIDPQtGWPFFVDHNSRTTTWNDPR 53
Cdd:cd00201   1 PPGWEERWDPD-GRVYYYNHNTKETQWEDPR 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 22-52 1.57e-07

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 47.50  E-value: 1.57e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 14043024    22 LPPGWEIKIDPQtGWPFFVDHNSRTTTWNDP 52
Cdd:pfam00397   1 LPPGWEERWDPD-GRVYYYNHETGETQWEKP 30
PHA03247 PHA03247
large tegument protein UL36; Provisional
 257-417 4.39e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043024   257 PRPLRAASPFRSSVQGASSREGSPARSSTPLHSPSPIRVHTVVdrpqQPMTHRETAPvsQPENKPESKPGPVGPELPPGH 336
Cdd:PHA03247 2650 ERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTV----GSLTSLADPP--PPPPTPEPAPHALVSATPLPP 2723

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043024   337 IPiQVIRKEVDSKPVSQKPPPPSEKVEVKVPPAPVPCPPPSPGPSAVPSSPKSVATEERAAP-----STAPAEATPPKPG 411
Cdd:PHA03247 2724 GP-AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTrpavaSLSESRESLPSPW 2802


                  ....*.
gi 14043024   412 EAEAPP 417
Cdd:PHA03247 2803 DPADPP 2808
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
257-421 7.38e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.45  E-value: 7.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043024  257 PRPLRAASPFRSSVQGASSREGSPARSSTPLHSPSP--------IRVHTVVDRPQQPMTHRE-TAPVSQPENKPESKPGP 327
Cdd:PRK07003 377 AGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPkaaaaaaaTRAEAPPAAPAPPATADRgDDAADGDAPVPAKANAR 456

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043024  328 VGPELPPGHIPIQ-VIRKEVDSKPVSQKPPPPSEKVEVKVPPAPVPCPPPSPGPSAVPsspkSVATEERAAPSTAPA-EA 405
Cdd:PRK07003 457 ASADSRCDERDAQpPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA----AASREDAPAAAAPPApEA 532

                        170
                 ....*....|....*.
gi 14043024  406 TPPKPGEAEAPPKHPG 421
Cdd:PRK07003 533 RPPTPAAAAPAARAGG 548
 
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.
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