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Conserved domains on  [gi|2462584003|ref|XP_054181180|]
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postacrosomal sheath WW domain-binding protein isoform X1 [Homo sapiens]

Protein Classification

GRAM domain-containing protein; WBP2 family GRAM domain-containing protein( domain architecture ID 12987386)

GRAM domain-containing protein is a membrane-associated protein; similar to Homo sapiens WW domain-binding protein 2, which acts as a transcriptional coactivator of estrogen and progesterone receptors (ESR1 and PGR) upon hormone activation| WBP2 family GRAM domain-containing protein similar to Homo sapiens WW domain-binding protein 2 (WBP-2) that acts as a transcriptional coactivator of estrogen and progesterone receptors (ESR1 and PGR) upon hormone activation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-GRAM_WBP2 cd13214
WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 71-166 8.19e-37

WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; WBP2 plays a number of roles including: acting as a tyrosine kinase substrate, activation of estrogen receptor alpha (ERalpha)/progesterone receptor (PR) transcription, and playing a role in breast cancer. WBP2 contain a N-terminal PH-GRAM domain and a C-terminal WWbp domain. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The WWbp domain is characterized by several short PY and PT-like motifs of the PPPPY form and binds to WW domains. WW domains contain two highly conserved tryptophans that are spaced 20-23 residues apart. They bind proline-rich peptide motifs [AP]-P-P-[AP]-Y, and/or phosphoserine- phosphothreonine-containing motifs.


:

Pssm-ID: 275401  Cd Length: 103  Bit Score: 128.06  E-value: 8.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584003  71 GSNVFSGRKTGTLFLTSYRVIFITSCSiSDPMLSFMMPFDLMTNLTVEQPVFAANFIKGTIQAAPYGGWEGQATFKLVFR 150
Cdd:cd13214     9 APPFFKGSKKGTIYLTNQRLIFVSSKP-TDNFQSFSMPLLNIRDVKFEQPVFGANYLKGKVKPVPGGGWPGEAEFKLTFK 87

                          90
                  ....*....|....*.
gi 2462584003 151 NGDAIEFAQLMVKAAS 166
Cdd:cd13214    88 DGGAIEFGQAFLRLAE 103
PTZ00436 super family cl33183
60S ribosomal protein L19-like protein; Provisional
 232-337 4.32e-10

60S ribosomal protein L19-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00436:

Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 60.35  E-value: 4.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584003 232 PVGNEGPPVGYRASPVRYGAPPLGYGAPPAGYGAPPLGYGAPPLGYGTPPLGYGAPPLGYGAPPAGNEGPPAGYRASPAG 311
Cdd:PTZ00436  243 PAKAAAAPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAAPAKAAAAPAKAAAAPAKAAAPPAK 322

                          90       100
                  ....*....|....*....|....*.
gi 2462584003 312 SGARPqeSTAAQAPENEASLPSASSS 337
Cdd:PTZ00436  323 AAAPP--AKAATPPAKAAAPPAKAAA 346
 
Name Accession Description Interval E-value
PH-GRAM_WBP2 cd13214
WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 71-166 8.19e-37

WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; WBP2 plays a number of roles including: acting as a tyrosine kinase substrate, activation of estrogen receptor alpha (ERalpha)/progesterone receptor (PR) transcription, and playing a role in breast cancer. WBP2 contain a N-terminal PH-GRAM domain and a C-terminal WWbp domain. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The WWbp domain is characterized by several short PY and PT-like motifs of the PPPPY form and binds to WW domains. WW domains contain two highly conserved tryptophans that are spaced 20-23 residues apart. They bind proline-rich peptide motifs [AP]-P-P-[AP]-Y, and/or phosphoserine- phosphothreonine-containing motifs.


Pssm-ID: 275401  Cd Length: 103  Bit Score: 128.06  E-value: 8.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584003  71 GSNVFSGRKTGTLFLTSYRVIFITSCSiSDPMLSFMMPFDLMTNLTVEQPVFAANFIKGTIQAAPYGGWEGQATFKLVFR 150
Cdd:cd13214     9 APPFFKGSKKGTIYLTNQRLIFVSSKP-TDNFQSFSMPLLNIRDVKFEQPVFGANYLKGKVKPVPGGGWPGEAEFKLTFK 87

                          90
                  ....*....|....*.
gi 2462584003 151 NGDAIEFAQLMVKAAS 166
Cdd:cd13214    88 DGGAIEFGQAFLRLAE 103
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
 232-337 4.32e-10

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 60.35  E-value: 4.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584003 232 PVGNEGPPVGYRASPVRYGAPPLGYGAPPAGYGAPPLGYGAPPLGYGTPPLGYGAPPLGYGAPPAGNEGPPAGYRASPAG 311
Cdd:PTZ00436  243 PAKAAAAPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAAPAKAAAAPAKAAAAPAKAAAPPAK 322

                          90       100
                  ....*....|....*....|....*.
gi 2462584003 312 SGARPqeSTAAQAPENEASLPSASSS 337
Cdd:PTZ00436  323 AAAPP--AKAATPPAKAAAPPAKAAA 346
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 77-167 8.39e-09

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 52.75  E-value: 8.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584003  77 GRKTGTLFLTSYRVIFiTScSISDPMLSFMMPFDLMTNltVEQPVFAANFIKGTIQAAPYGGWEgqATFKLVFRNGDAIE 156
Cdd:pfam02893  28 GPVQGRLYLTNYRLCF-RS-LPKGWSTKVVIPLVDIEE--IEKLKGGANLFPNGIQVETGSNDK--FSFAGFVTRDEAIE 101

                          90
                  ....*....|.
gi 2462584003 157 FAQLMVKAASA 167
Cdd:pfam02893 102 FILALLKNAHP 112
 
Name Accession Description Interval E-value
PH-GRAM_WBP2 cd13214
WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 71-166 8.19e-37

WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; WBP2 plays a number of roles including: acting as a tyrosine kinase substrate, activation of estrogen receptor alpha (ERalpha)/progesterone receptor (PR) transcription, and playing a role in breast cancer. WBP2 contain a N-terminal PH-GRAM domain and a C-terminal WWbp domain. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The WWbp domain is characterized by several short PY and PT-like motifs of the PPPPY form and binds to WW domains. WW domains contain two highly conserved tryptophans that are spaced 20-23 residues apart. They bind proline-rich peptide motifs [AP]-P-P-[AP]-Y, and/or phosphoserine- phosphothreonine-containing motifs.


Pssm-ID: 275401  Cd Length: 103  Bit Score: 128.06  E-value: 8.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584003  71 GSNVFSGRKTGTLFLTSYRVIFITSCSiSDPMLSFMMPFDLMTNLTVEQPVFAANFIKGTIQAAPYGGWEGQATFKLVFR 150
Cdd:cd13214     9 APPFFKGSKKGTIYLTNQRLIFVSSKP-TDNFQSFSMPLLNIRDVKFEQPVFGANYLKGKVKPVPGGGWPGEAEFKLTFK 87

                          90
                  ....*....|....*.
gi 2462584003 151 NGDAIEFAQLMVKAAS 166
Cdd:cd13214    88 DGGAIEFGQAFLRLAE 103
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
 232-337 4.32e-10

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 60.35  E-value: 4.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584003 232 PVGNEGPPVGYRASPVRYGAPPLGYGAPPAGYGAPPLGYGAPPLGYGTPPLGYGAPPLGYGAPPAGNEGPPAGYRASPAG 311
Cdd:PTZ00436  243 PAKAAAAPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAAPAKAAAAPAKAAAAPAKAAAPPAK 322

                          90       100
                  ....*....|....*....|....*.
gi 2462584003 312 SGARPqeSTAAQAPENEASLPSASSS 337
Cdd:PTZ00436  323 AAAPP--AKAATPPAKAAAPPAKAAA 346
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
 222-332 2.82e-09

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 57.65  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584003 222 GAPPAGYGAQPVGNEGPPVGYRASPVRYGAPPLGYGAPPAGYGAPPLGYGAPPLGYGTPPLGYGAPPLGYGAPPAGNEGP 301
Cdd:PTZ00436  240 AAAPAKAAAAPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAAPAKAAAAPAKAAAAPAKAAAP 319

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462584003 302 PAGYRASPAGSGARPqeSTAAQAPENEASLP 332
Cdd:PTZ00436  320 PAKAAAPPAKAATPP--AKAAAPPAKAAAAP 348
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
 221-337 6.85e-09

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 56.50  E-value: 6.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584003 221 YGAppagygaqPVGNEGPPVGYRASPVRYGAPPLGYGAPPAGYGAPPLGYGAPPLGYGTPPLGYGAPPLGYGAPPAGNEG 300
Cdd:PTZ00436  226 AAA--------PAKAAAPPAKAAAAPAKAAAAPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAA 297

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462584003 301 PPAGYRASPAGSGARPqeSTAAQAPENEASLPSASSS 337
Cdd:PTZ00436  298 APAKAAAAPAKAAAAP--AKAAAPPAKAAAPPAKAAT 332
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 77-167 8.39e-09

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 52.75  E-value: 8.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584003  77 GRKTGTLFLTSYRVIFiTScSISDPMLSFMMPFDLMTNltVEQPVFAANFIKGTIQAAPYGGWEgqATFKLVFRNGDAIE 156
Cdd:pfam02893  28 GPVQGRLYLTNYRLCF-RS-LPKGWSTKVVIPLVDIEE--IEKLKGGANLFPNGIQVETGSNDK--FSFAGFVTRDEAIE 101

                          90
                  ....*....|.
gi 2462584003 157 FAQLMVKAASA 167
Cdd:pfam02893 102 FILALLKNAHP 112
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
 214-314 4.19e-06

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 48.02  E-value: 4.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584003 214 YGAPPPGYGAPPAGYGAQPVGNEGPPVGYRASPVRYGAPPLGYGAPPAGYGAPPLGYGAPPLGYGTPPLGYGAPPLGYGA 293
Cdd:PTZ00436  253 AAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAAPAKAAAAPAKAAAAPAKAAAPPAKAAAPPAKAAT 332

                          90       100
                  ....*....|....*....|.
gi 2462584003 294 PPAGNEGPPAGYRASPAGSGA 314
Cdd:PTZ00436  333 PPAKAAAPPAKAAAAPVGKKA 353
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 77-122 2.23e-03

Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275393  Cd Length: 94  Bit Score: 36.98  E-value: 2.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2462584003  77 GRKTGTLFLTSYRVIFITscSISDPMLSFMMPFDLMTNLTVEQPVF 122
Cdd:cd10570    17 LPLEGTLYLSTYRLIFSS--KADGDETKLVIPLVDITDVEKIAGAS 60
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 231-338 2.53e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584003 231 QPVGNEGPPVGYRASPVRYGAPPLGYGAPPAGYGAPPLGYGAPPLG-YGTPPLGYGAPPLGYGAPPAGNEGPPAGYRASP 309
Cdd:PRK07764  620 APAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGgDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPA 699

                          90       100
                  ....*....|....*....|....*....
gi 2462584003 310 AGSGARPQESTAAQAPENEASLPSASSSQ 338
Cdd:PRK07764  700 QPAPAPAATPPAGQADDPAAQPPQAAQGA 728
 
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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