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Conserved domains on  [gi|195539466|ref|NP_001124200|]
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WASP homolog-associated protein with actin, membranes and microtubules [Rattus norvegicus]

Protein Classification

WHAMM-JMY_N and JMY domain-containing protein( domain architecture ID 11239840)

protein containing domains WHAMM-JMY_N, PHA03307, JMY, and COG4913

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
JMY pfam15871
Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is ...
67-435 0e+00

Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is also a WASP homolog-associated protein with actin, membranes and microtubules. This middle region is the coiled-coil region that putatively binds microtubules to the scaffold. This ability to interact with microtubules plays a role in membrane tubulation.


:

Pssm-ID: 464915  Cd Length: 357  Bit Score: 589.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466   67 WAGALSAAGFRGAHRQLAALWPALERCFPPLPPeldaasGAGWGLgrglwalvWALVWPAPANPGDAALQDLCRQLEHYL 146
Cdd:pfam15871   1 WAGLFSFQDLRAIHRQLCAVHPALEPCFPALPE------GESEGL--------WTLLFPGRPEPGEAELQELCRQLEEYL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466  147 GLAADGCGGATVRDVLFPAPGDSAD--CEGLSEFRERMLRARLDQTVARLRQLLQDHRKANTMVTLMKVYQEEDEVYQEL 224
Cdd:pfam15871  67 GYALDICGRKILLDVLFAADGDDAEeyFENLSELRKKGYEEVLQRAKERLRQVLQQHKNADTMVELMKVYQEEDEAYQEL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466  225 VTMATTFFQYLLQPFRDMREVATSCKLGILKSLEEDELGPKRVAALQKEASEWTRRAEEAVVSIQDITVNYFKETVTALT 304
Cdd:pfam15871 147 VTAATEFYQYLLQPFRDMRELATLRKLEIKKSLENDDLGPKRVEALQKEAEEWQRRAEEAVVSIQDITVNYFKETVKALS 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466  305 GMQKQMEQDQRRFGQAAWATAMPRLENLKLMLARETLQLMRAKELCLKHRQAEIQRKVEDLPDQGKNVGVVDELEIQYYE 384
Cdd:pfam15871 227 GMQKQMEQDQKRFGKAAWAAAAPRLEKLKYMLAKETLQLMRAKELCLEQKRAEIRKEMESLEEGEKAVAVVDELEIQYYE 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 195539466  385 TQLELYDVKLEILRNEETILVTRLDSVKRLIAEKQAEVVYYDPCESPEELK 435
Cdd:pfam15871 307 AQLELYEVQLEILKNEELLLTAQLDSLRRQIKEKQDEVVYYDTCESPEELK 357
WHAMM-JMY_N pfam15920
N-terminal of Junction-mediating and WASP homolog-associated; WHAMM-JMY_N is the very ...
5-47 1.84e-23

N-terminal of Junction-mediating and WASP homolog-associated; WHAMM-JMY_N is the very N-terminus of WHAMM and JMY proteins. The function of this conserved region is not known; there are two highly conserved tryptophan residues.


:

Pssm-ID: 464942  Cd Length: 49  Bit Score: 93.66  E-value: 1.84e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 195539466    5 QPDSLEGWVPLREDLFPEPERHQLRFLVAWNAAEGQFAVTCHD 47
Cdd:pfam15920   1 RPDSLEGWVAVKENLFEEPEKHKLRFIVAWNEIEGKFAVTCHN 43
 
Name Accession Description Interval E-value
JMY pfam15871
Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is ...
67-435 0e+00

Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is also a WASP homolog-associated protein with actin, membranes and microtubules. This middle region is the coiled-coil region that putatively binds microtubules to the scaffold. This ability to interact with microtubules plays a role in membrane tubulation.


Pssm-ID: 464915  Cd Length: 357  Bit Score: 589.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466   67 WAGALSAAGFRGAHRQLAALWPALERCFPPLPPeldaasGAGWGLgrglwalvWALVWPAPANPGDAALQDLCRQLEHYL 146
Cdd:pfam15871   1 WAGLFSFQDLRAIHRQLCAVHPALEPCFPALPE------GESEGL--------WTLLFPGRPEPGEAELQELCRQLEEYL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466  147 GLAADGCGGATVRDVLFPAPGDSAD--CEGLSEFRERMLRARLDQTVARLRQLLQDHRKANTMVTLMKVYQEEDEVYQEL 224
Cdd:pfam15871  67 GYALDICGRKILLDVLFAADGDDAEeyFENLSELRKKGYEEVLQRAKERLRQVLQQHKNADTMVELMKVYQEEDEAYQEL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466  225 VTMATTFFQYLLQPFRDMREVATSCKLGILKSLEEDELGPKRVAALQKEASEWTRRAEEAVVSIQDITVNYFKETVTALT 304
Cdd:pfam15871 147 VTAATEFYQYLLQPFRDMRELATLRKLEIKKSLENDDLGPKRVEALQKEAEEWQRRAEEAVVSIQDITVNYFKETVKALS 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466  305 GMQKQMEQDQRRFGQAAWATAMPRLENLKLMLARETLQLMRAKELCLKHRQAEIQRKVEDLPDQGKNVGVVDELEIQYYE 384
Cdd:pfam15871 227 GMQKQMEQDQKRFGKAAWAAAAPRLEKLKYMLAKETLQLMRAKELCLEQKRAEIRKEMESLEEGEKAVAVVDELEIQYYE 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 195539466  385 TQLELYDVKLEILRNEETILVTRLDSVKRLIAEKQAEVVYYDPCESPEELK 435
Cdd:pfam15871 307 AQLELYEVQLEILKNEELLLTAQLDSLRRQIKEKQDEVVYYDTCESPEELK 357
WHAMM-JMY_N pfam15920
N-terminal of Junction-mediating and WASP homolog-associated; WHAMM-JMY_N is the very ...
5-47 1.84e-23

N-terminal of Junction-mediating and WASP homolog-associated; WHAMM-JMY_N is the very N-terminus of WHAMM and JMY proteins. The function of this conserved region is not known; there are two highly conserved tryptophan residues.


Pssm-ID: 464942  Cd Length: 49  Bit Score: 93.66  E-value: 1.84e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 195539466    5 QPDSLEGWVPLREDLFPEPERHQLRFLVAWNAAEGQFAVTCHD 47
Cdd:pfam15920   1 RPDSLEGWVAVKENLFEEPEKHKLRFIVAWNEIEGKFAVTCHN 43
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
254-500 1.54e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466   254 LKSLEED-ELGPKRVAALQKEASEWTRRAEEAVVSIQDITvnyfketvTALTGMQKQMEQDQRRFGQAAWATAMPRLENL 332
Cdd:TIGR02168  686 IEELEEKiAELEKALAELRKELEELEEELEQLRKELEELS--------RQISALRKDLARLEAEVEQLEERIAQLSKELT 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466   333 KLMLARETLQLMRAKELCLKHRQ----AEIQRKVEDLPDQGKNVG-VVDELEIQYYETQLELYDV--KLEILRNEETILV 405
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAeaeiEELEAQIEQLKEELKALReALDELRAELTLLNEEAANLreRLESLERRIAATE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466   406 TRLDSVKRLIAEKQAEVVYY-----DPCESPEELKSlapDLELHL----GDNRELRALSQQCQQLEAQRGRICSRRAQLR 476
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLaaeieELEELIEELES---ELEALLneraSLEEALALLRSELEELSEELRELESKRSELR 914
                          250       260
                   ....*....|....*....|....*..
gi 195539466   477 NRKDHCRE---NHQLRLQQAKQNVRHF 500
Cdd:TIGR02168  915 RELEELREklaQLELRLEGLEVRIDNL 941
 
Name Accession Description Interval E-value
JMY pfam15871
Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is ...
67-435 0e+00

Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is also a WASP homolog-associated protein with actin, membranes and microtubules. This middle region is the coiled-coil region that putatively binds microtubules to the scaffold. This ability to interact with microtubules plays a role in membrane tubulation.


Pssm-ID: 464915  Cd Length: 357  Bit Score: 589.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466   67 WAGALSAAGFRGAHRQLAALWPALERCFPPLPPeldaasGAGWGLgrglwalvWALVWPAPANPGDAALQDLCRQLEHYL 146
Cdd:pfam15871   1 WAGLFSFQDLRAIHRQLCAVHPALEPCFPALPE------GESEGL--------WTLLFPGRPEPGEAELQELCRQLEEYL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466  147 GLAADGCGGATVRDVLFPAPGDSAD--CEGLSEFRERMLRARLDQTVARLRQLLQDHRKANTMVTLMKVYQEEDEVYQEL 224
Cdd:pfam15871  67 GYALDICGRKILLDVLFAADGDDAEeyFENLSELRKKGYEEVLQRAKERLRQVLQQHKNADTMVELMKVYQEEDEAYQEL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466  225 VTMATTFFQYLLQPFRDMREVATSCKLGILKSLEEDELGPKRVAALQKEASEWTRRAEEAVVSIQDITVNYFKETVTALT 304
Cdd:pfam15871 147 VTAATEFYQYLLQPFRDMRELATLRKLEIKKSLENDDLGPKRVEALQKEAEEWQRRAEEAVVSIQDITVNYFKETVKALS 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466  305 GMQKQMEQDQRRFGQAAWATAMPRLENLKLMLARETLQLMRAKELCLKHRQAEIQRKVEDLPDQGKNVGVVDELEIQYYE 384
Cdd:pfam15871 227 GMQKQMEQDQKRFGKAAWAAAAPRLEKLKYMLAKETLQLMRAKELCLEQKRAEIRKEMESLEEGEKAVAVVDELEIQYYE 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 195539466  385 TQLELYDVKLEILRNEETILVTRLDSVKRLIAEKQAEVVYYDPCESPEELK 435
Cdd:pfam15871 307 AQLELYEVQLEILKNEELLLTAQLDSLRRQIKEKQDEVVYYDTCESPEELK 357
WHAMM-JMY_N pfam15920
N-terminal of Junction-mediating and WASP homolog-associated; WHAMM-JMY_N is the very ...
5-47 1.84e-23

N-terminal of Junction-mediating and WASP homolog-associated; WHAMM-JMY_N is the very N-terminus of WHAMM and JMY proteins. The function of this conserved region is not known; there are two highly conserved tryptophan residues.


Pssm-ID: 464942  Cd Length: 49  Bit Score: 93.66  E-value: 1.84e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 195539466    5 QPDSLEGWVPLREDLFPEPERHQLRFLVAWNAAEGQFAVTCHD 47
Cdd:pfam15920   1 RPDSLEGWVAVKENLFEEPEKHKLRFIVAWNEIEGKFAVTCHN 43
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
254-500 1.54e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466   254 LKSLEED-ELGPKRVAALQKEASEWTRRAEEAVVSIQDITvnyfketvTALTGMQKQMEQDQRRFGQAAWATAMPRLENL 332
Cdd:TIGR02168  686 IEELEEKiAELEKALAELRKELEELEEELEQLRKELEELS--------RQISALRKDLARLEAEVEQLEERIAQLSKELT 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466   333 KLMLARETLQLMRAKELCLKHRQ----AEIQRKVEDLPDQGKNVG-VVDELEIQYYETQLELYDV--KLEILRNEETILV 405
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAeaeiEELEAQIEQLKEELKALReALDELRAELTLLNEEAANLreRLESLERRIAATE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466   406 TRLDSVKRLIAEKQAEVVYY-----DPCESPEELKSlapDLELHL----GDNRELRALSQQCQQLEAQRGRICSRRAQLR 476
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLaaeieELEELIEELES---ELEALLneraSLEEALALLRSELEELSEELRELESKRSELR 914
                          250       260
                   ....*....|....*....|....*..
gi 195539466   477 NRKDHCRE---NHQLRLQQAKQNVRHF 500
Cdd:TIGR02168  915 RELEELREklaQLELRLEGLEVRIDNL 941
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
265-498 6.58e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 6.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466   265 KRVAALQKEASEWTRRAEEAVVSIQDItVNYFKETVTALTGMQKQMEQDQRRFGQ--AAWATAMPRLENLKLMLARETLQ 342
Cdd:TIGR02168  288 KELYALANEISRLEQQKQILRERLANL-ERQLEELEAQLEELESKLDELAEELAEleEKLEELKEELESLEAELEELEAE 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539466   343 LMRAKELcLKHRQAEIQRKVEDLPDQGKNVGVVDElEIQYYETQLELYDVKLEILRNEETILVTRLDSVKRliAEKQAEV 422
Cdd:TIGR02168  367 LEELESR-LEELEEQLETLRSKVAQLELQIASLNN-EIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAEL 442
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 195539466   423 VyydpcESPEELKSLAPDLELHlgdNRELRALSQQCQQLEAQRGRICSRRAQLRNRKDHCrENHQLRLQQAKQNVR 498
Cdd:TIGR02168  443 E-----ELEEELEELQEELERL---EEALEELREELEEAEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVK 509
 
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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