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Conserved domains on  [gi|530394628|ref|XP_005270344|]
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BAG family molecular chaperone regulator 3 isoform X1 [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 ...
420-497 3.17e-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: 3.17e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530394628   420 GVLKVEAILEKVQG-LEQAVDNFEGKKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQKA 497
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 5.39e-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: 5.39e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 530394628    21 PLPPGWEIKIDPQtGWPFFVDHNSRTTTWNDPR 53
Cdd:smart00456   1 PLPPGWEERKDPD-GRPYYYNHETKETQWEKPR 32
PHA03247 super family cl33720
large tegument protein UL36; Provisional
257-416 3.40e-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: 43.77  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394628  257 PRPLRAASPFRSSVQGASSREGSPARSSTPLHSPSPIRVHTVVdrpQPMTHRETAPvsQPENKPESKPGPVGPELPPGHI 336
Cdd:PHA03247 2650 ERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTV---GSLTSLADPP--PPPPTPEPAPHALVSATPLPPG 2724
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394628  337 PiQVIRKEVDSKPVSQKPPPPSEKVEVKVPPAPVPCPPPSPGPSAVPSSPKSVATEERAAP-----STAPAEATPPKPGE 411
Cdd:PHA03247 2725 P-AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTrpavaSLSESRESLPSPWD 2803

                  ....*
gi 530394628  412 AEAPP 416
Cdd:PHA03247 2804 PADPP 2808
 
Name Accession Description Interval E-value
BAG smart00264
BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated ...
420-497 3.17e-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: 3.17e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530394628   420 GVLKVEAILEKVQG-LEQAVDNFEGKKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQKA 497
Cdd:smart00264   1 SIKKINEVLDEVQKkIEKEVQVADGKKDDKEYLRLSEELMKLLLKLDSVDVEGCEDIREARKRLVRLIQNLLNALDSKK 79
BAG pfam02179
BAG domain; Domain present in Hsp70 regulators.
424-496 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 530394628  424 VEAILEKVQGLEQAVDNFEG----KKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQK 496
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 5.39e-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: 5.39e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 530394628    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 1.40e-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: 1.40e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 530394628  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 1.56e-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: 1.56e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 530394628   22 LPPGWEIKIDPQtGWPFFVDHNSRTTTWNDP 52
Cdd:pfam00397   1 LPPGWEERWDPD-GRVYYYNHETGETQWEKP 30
PHA03247 PHA03247
large tegument protein UL36; Provisional
257-416 3.40e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394628  257 PRPLRAASPFRSSVQGASSREGSPARSSTPLHSPSPIRVHTVVdrpQPMTHRETAPvsQPENKPESKPGPVGPELPPGHI 336
Cdd:PHA03247 2650 ERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTV---GSLTSLADPP--PPPPTPEPAPHALVSATPLPPG 2724
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394628  337 PiQVIRKEVDSKPVSQKPPPPSEKVEVKVPPAPVPCPPPSPGPSAVPSSPKSVATEERAAP-----STAPAEATPPKPGE 411
Cdd:PHA03247 2725 P-AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTrpavaSLSESRESLPSPWD 2803

                  ....*
gi 530394628  412 AEAPP 416
Cdd:PHA03247 2804 PADPP 2808
 
Name Accession Description Interval E-value
BAG smart00264
BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated ...
420-497 3.17e-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: 3.17e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530394628   420 GVLKVEAILEKVQG-LEQAVDNFEGKKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQKA 497
Cdd:smart00264   1 SIKKINEVLDEVQKkIEKEVQVADGKKDDKEYLRLSEELMKLLLKLDSVDVEGCEDIREARKRLVRLIQNLLNALDSKK 79
BAG pfam02179
BAG domain; Domain present in Hsp70 regulators.
424-496 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 530394628  424 VEAILEKVQGLEQAVDNFEG----KKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQK 496
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 5.39e-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: 5.39e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 530394628    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 1.40e-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: 1.40e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 530394628  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 1.56e-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: 1.56e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 530394628   22 LPPGWEIKIDPQtGWPFFVDHNSRTTTWNDP 52
Cdd:pfam00397   1 LPPGWEERWDPD-GRVYYYNHETGETQWEKP 30
PHA03247 PHA03247
large tegument protein UL36; Provisional
257-416 3.40e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394628  257 PRPLRAASPFRSSVQGASSREGSPARSSTPLHSPSPIRVHTVVdrpQPMTHRETAPvsQPENKPESKPGPVGPELPPGHI 336
Cdd:PHA03247 2650 ERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTV---GSLTSLADPP--PPPPTPEPAPHALVSATPLPPG 2724
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394628  337 PiQVIRKEVDSKPVSQKPPPPSEKVEVKVPPAPVPCPPPSPGPSAVPSSPKSVATEERAAP-----STAPAEATPPKPGE 411
Cdd:PHA03247 2725 P-AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTrpavaSLSESRESLPSPWD 2803

                  ....*
gi 530394628  412 AEAPP 416
Cdd:PHA03247 2804 PADPP 2808
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
257-420 4.45e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.83  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394628 257 PRPLRAASPFRSSVQGASSREGSPARSSTPLHSPSP--------IRVHTVVDRPQPMTHRE--TAPVSQPENKPESKPGP 326
Cdd:PRK07003 377 AGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPkaaaaaaaTRAEAPPAAPAPPATADrgDDAADGDAPVPAKANAR 456
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394628 327 VGPELPPGHIPIQ-VIRKEVDSKPVSQKPPPPSEKVEVKVPPAPVPCPPPSPGPSAVPsspkSVATEERAAPSTAPA-EA 404
Cdd:PRK07003 457 ASADSRCDERDAQpPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA----AASREDAPAAAAPPApEA 532
                        170
                 ....*....|....*.
gi 530394628 405 TPPKPGEAEAPPKHPG 420
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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