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Conserved domains on  [gi|194389186|dbj|BAG61610|]
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unnamed protein product [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 3-98 1.31e-18

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member pfam00012:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 598  Bit Score: 86.55  E-value: 1.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194389186    3 TDQNAKEEEKMQVDQEEPHVEEQQQQTPAENKAESEEMETSQAGSKDKKMDQPPQAKKAKVKTSTVDLPIE----NQLLW 78
Cdd:pfam00012 499 EGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKSKVESAIEWLKDElegdDKEEI 578

                          90       100
                  ....*....|....*....|
gi 194389186   79 QIDREMLNLYIENEGKMIMQ 98
Cdd:pfam00012 579 EAKTEELAQVSQKIGERMYQ 598
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 89-176 1.57e-11

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member pfam00012:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 598  Bit Score: 64.98  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194389186   89 IENEGKMIMQDKLEKERNDAKNAVEEYVYEMRDKLSgEYEKFVSEDDRNsftlKLEDTENWLYEDGEDQPKQVYVDKLAE 168
Cdd:pfam00012 510 VKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLE-EEGDKVPEAEKS----KVESAIEWLKDELEGDDKEEIEAKTEE 584


                  ....*...
gi 194389186  169 LKNLGQPI 176
Cdd:pfam00012 585 LAQVSQKI 592
PTZ00009 super family cl36495
heat shock 70 kDa protein; Provisional
 215-276 8.45e-03

heat shock 70 kDa protein; Provisional


The actual alignment was detected with superfamily member PTZ00009:

Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 37.85  E-value: 8.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194389186 215 DHLDAADMTKVEKSTNEAMEWmnnklnLQNKQSLTMDpvvkskEIEAKIKELTSTCSPIISK 276
Cdd:PTZ00009 562 GKLSDSDKATIEKAIDEALEW------LEKNQLAEKE------EFEHKQKEVESVCNPIMTK 611
 
Name Accession Description Interval E-value
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 3-98 1.31e-18

Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.


Pssm-ID: 394970 [Multi-domain]  Cd Length: 598  Bit Score: 86.55  E-value: 1.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194389186    3 TDQNAKEEEKMQVDQEEPHVEEQQQQTPAENKAESEEMETSQAGSKDKKMDQPPQAKKAKVKTSTVDLPIE----NQLLW 78
Cdd:pfam00012 499 EGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKSKVESAIEWLKDElegdDKEEI 578

                          90       100
                  ....*....|....*....|
gi 194389186   79 QIDREMLNLYIENEGKMIMQ 98
Cdd:pfam00012 579 EAKTEELAQVSQKIGERMYQ 598
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 89-176 1.57e-11

Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.


Pssm-ID: 394970 [Multi-domain]  Cd Length: 598  Bit Score: 64.98  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194389186   89 IENEGKMIMQDKLEKERNDAKNAVEEYVYEMRDKLSgEYEKFVSEDDRNsftlKLEDTENWLYEDGEDQPKQVYVDKLAE 168
Cdd:pfam00012 510 VKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLE-EEGDKVPEAEKS----KVESAIEWLKDELEGDDKEEIEAKTEE 584


                  ....*...
gi 194389186  169 LKNLGQPI 176
Cdd:pfam00012 585 LAQVSQKI 592
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
 98-176 8.61e-06

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 47.48  E-value: 8.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194389186  98 QDKLEKERNDAKNAVEEYVYEMRDKLSGEYEK-FVSEDDRNSFTLKLEDTENWLyEDGEDQPKQVYVDKLAELKNLGQPI 176
Cdd:PTZ00009 530 EDEANRERVEAKNGLENYCYSMKNTLQDEKVKgKLSDSDKATIEKAIDEALEWL-EKNQLAEKEEFEHKQKEVESVCNPI 608
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
 215-276 8.45e-03

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 37.85  E-value: 8.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194389186 215 DHLDAADMTKVEKSTNEAMEWmnnklnLQNKQSLTMDpvvkskEIEAKIKELTSTCSPIISK 276
Cdd:PTZ00009 562 GKLSDSDKATIEKAIDEALEW------LEKNQLAEKE------EFEHKQKEVESVCNPIMTK 611
 
Name Accession Description Interval E-value
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 3-98 1.31e-18

Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.


Pssm-ID: 394970 [Multi-domain]  Cd Length: 598  Bit Score: 86.55  E-value: 1.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194389186    3 TDQNAKEEEKMQVDQEEPHVEEQQQQTPAENKAESEEMETSQAGSKDKKMDQPPQAKKAKVKTSTVDLPIE----NQLLW 78
Cdd:pfam00012 499 EGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKSKVESAIEWLKDElegdDKEEI 578

                          90       100
                  ....*....|....*....|
gi 194389186   79 QIDREMLNLYIENEGKMIMQ 98
Cdd:pfam00012 579 EAKTEELAQVSQKIGERMYQ 598
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 89-176 1.57e-11

Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.


Pssm-ID: 394970 [Multi-domain]  Cd Length: 598  Bit Score: 64.98  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194389186   89 IENEGKMIMQDKLEKERNDAKNAVEEYVYEMRDKLSgEYEKFVSEDDRNsftlKLEDTENWLYEDGEDQPKQVYVDKLAE 168
Cdd:pfam00012 510 VKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLE-EEGDKVPEAEKS----KVESAIEWLKDELEGDDKEEIEAKTEE 584


                  ....*...
gi 194389186  169 LKNLGQPI 176
Cdd:pfam00012 585 LAQVSQKI 592
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
 98-176 8.61e-06

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 47.48  E-value: 8.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194389186  98 QDKLEKERNDAKNAVEEYVYEMRDKLSGEYEK-FVSEDDRNSFTLKLEDTENWLyEDGEDQPKQVYVDKLAELKNLGQPI 176
Cdd:PTZ00009 530 EDEANRERVEAKNGLENYCYSMKNTLQDEKVKgKLSDSDKATIEKAIDEALEWL-EKNQLAEKEEFEHKQKEVESVCNPI 608
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
 215-276 8.45e-03

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 37.85  E-value: 8.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194389186 215 DHLDAADMTKVEKSTNEAMEWmnnklnLQNKQSLTMDpvvkskEIEAKIKELTSTCSPIISK 276
Cdd:PTZ00009 562 GKLSDSDKATIEKAIDEALEW------LEKNQLAEKE------EFEHKQKEVESVCNPIMTK 611
 
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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