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Conserved domains on  [gi|50302307|ref|XP_451088|]
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uncharacterized protein KLLA0_A01991g [Kluyveromyces lactis]

Protein Classification

V-type ATP synthase subunit D( domain architecture ID 10015578)

V-type ATP synthase subunit D is part of the catalytic core (V1) of the vacuolar (V)-type ATP synthase complex (V0/V1) that catalyzes the production of ATP from ADP in the presence of a proton gradient across the membrane

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
V_ATPase_subD TIGR00309
H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run ...
5-211 1.25e-85

H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run backwards, using a proton gradient to synthesize ATP, the primary biological role is to acidify some compartment, such as yeast vacuole (a lysosomal homolog) or the interior of a prokaryote. [Transport and binding proteins, Cations and iron carrying compounds]


:

Pssm-ID: 129409  Cd Length: 209  Bit Score: 254.75  E-value: 1.25e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307     5 REQVFPTRMTLGLMKTKLKGANQGYSLLKRKSEALTKRFRDITKRIDDSKQKMGRVMQTAAFSLAEVTYATGENIGYQVQ 84
Cdd:TIGR00309   1 MEKVNPTRMELLKLKDKLKMAKRGYSLLKLKRDALIMEFRQILERAKDIKNKMEQKLKEAISDLIEAQSVMGPFAVWIAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307    85 ENVANARFKVRATQENVSGVYLPQFESF-IDSNINDfKMTGLGRGGQQVQRAKEIYSRAVETLVELASLQTAFIILDEVI 163
Cdd:TIGR00309  81 LSVVTARFEVDMKSKNIMGVVVPVFDSYeIRRKVHE-RGYGLLFTSYKVDEAAEIYEEAVELIVELAEIETTIRLLAEEI 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 50302307   164 KVTNRRVNAIEHVIIPRTENTIAYINSELDELDREEFYRLKKVQEKKQ 211
Cdd:TIGR00309 160 EITKRRVNALEHVIIPRLKNTIKYINMRLDEMDRENFVRLKKIKSSKE 207
 
Name Accession Description Interval E-value
V_ATPase_subD TIGR00309
H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run ...
5-211 1.25e-85

H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run backwards, using a proton gradient to synthesize ATP, the primary biological role is to acidify some compartment, such as yeast vacuole (a lysosomal homolog) or the interior of a prokaryote. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 129409  Cd Length: 209  Bit Score: 254.75  E-value: 1.25e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307     5 REQVFPTRMTLGLMKTKLKGANQGYSLLKRKSEALTKRFRDITKRIDDSKQKMGRVMQTAAFSLAEVTYATGENIGYQVQ 84
Cdd:TIGR00309   1 MEKVNPTRMELLKLKDKLKMAKRGYSLLKLKRDALIMEFRQILERAKDIKNKMEQKLKEAISDLIEAQSVMGPFAVWIAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307    85 ENVANARFKVRATQENVSGVYLPQFESF-IDSNINDfKMTGLGRGGQQVQRAKEIYSRAVETLVELASLQTAFIILDEVI 163
Cdd:TIGR00309  81 LSVVTARFEVDMKSKNIMGVVVPVFDSYeIRRKVHE-RGYGLLFTSYKVDEAAEIYEEAVELIVELAEIETTIRLLAEEI 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 50302307   164 KVTNRRVNAIEHVIIPRTENTIAYINSELDELDREEFYRLKKVQEKKQ 211
Cdd:TIGR00309 160 EITKRRVNALEHVIIPRLKNTIKYINMRLDEMDRENFVRLKKIKSSKE 207
ATP-synt_D pfam01813
ATP synthase subunit D; This is a family of subunit D form various ATP synthases including ...
14-208 1.05e-71

ATP synthase subunit D; This is a family of subunit D form various ATP synthases including V-type H+ transporting and Na+ dependent. Subunit D is suggested to be an integral part of the catalytic sector of the V-ATPase.


Pssm-ID: 460343  Cd Length: 194  Bit Score: 218.63  E-value: 1.05e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307    14 TLGLMKTKLKGANQGYSLLKRKSEALTKRFRDITKRIDDSKQKMGRVMQTAAFSLAEVTYATGE-NIGYQVQENVaNARF 92
Cdd:pfam01813   1 ELIRLKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGEeDVESLALESV-PSVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307    93 KVRATQENVSGVYLPQFEsFIDSNINDFKMTGLGRGGQQVQRAKEIYSRAVETLVELASLQTAFIILDEVIKVTNRRVNA 172
Cdd:pfam01813  80 RVEVKTENIMGVKVPVFE-LVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNA 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 50302307   173 IEHVIIPRTENTIAYINSELDELDREEFYRLKKVQE 208
Cdd:pfam01813 159 LEKVVIPRLEETIKYIKSELDEREREEFFRLKKVKA 194
NtpD COG1394
Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal ...
6-210 6.35e-34

Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441004  Cd Length: 202  Bit Score: 121.88  E-value: 6.35e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307   6 EQVFPTRMTLGLMKTKLKGANQGYSLLKRKSEALTKRFRDITKRIDDSKQKMGRVMQTAAFSLAEVTYATGENiGYQVQE 85
Cdd:COG1394   2 AKVKPTKMELLRLKRQLKLAKRGHKLLKDKRDALIREFLKLIDEAEELREELEELLEEAYEALALANARMGIE-AVEELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307  86 NVANARFKVRATQENVSGVYLPQFESFIDSNINDFkmtGLGRGGQQVQRAKEIYSRAVETLVELASLQTAFIILDEVIKV 165
Cdd:COG1394  81 LSVPRVLEVEVSTRNIMGVEVPVLESEEFKEERPY---GLLGTSAWLDEAIEALEELLELLLELAELETALRRLAEEIRK 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 50302307 166 TNRRVNAIEHVIIPRTENTIAYINSELDELDREEFYRLKKVQEKK 210
Cdd:COG1394 158 TQRRVNALEKVLIPRLEETIKYIRMKLEEREREEFVRLKKVKKKL 202
PRK00373 PRK00373
V-type ATP synthase subunit D; Reviewed
5-206 5.63e-29

V-type ATP synthase subunit D; Reviewed


Pssm-ID: 178991  Cd Length: 204  Bit Score: 109.14  E-value: 5.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307    5 REQVFPTRMTLGLMKTKLKGANQGYSLLKRKSEALTKRFRDITKRIDDSKQKMGRVMQTA--AFSLAEVTYATG--ENIG 80
Cdd:PRK00373   3 RLNVKPTRMELINLKRRLKLAERGHKLLKDKRDELIMEFFDILDEAKKLREEVEEELEEAykDFLMARAVEGSLavEEAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307   81 YQVQENVanarfKVRATQENVSGVYLPQFESFIDSNINDFKMTGLGRGGQQVQRAKEiYSRAVETLVELASLQTAFIILD 160
Cdd:PRK00373  83 ASPKESL-----EVDVSSKNIMGVVVPVIELSVKRTLPERGYGFLGTSAELDEAAEK-FEELLEKILELAEVEKTIQLLA 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 50302307  161 EVIKVTNRRVNAIEHVIIPRTENTIAYINSELDELDREEFYRLKKV 206
Cdd:PRK00373 157 DEIEKTKRRVNALEYVIIPRLEETIKYIKMKLDEMERENFVRLKKI 202
 
Name Accession Description Interval E-value
V_ATPase_subD TIGR00309
H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run ...
5-211 1.25e-85

H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run backwards, using a proton gradient to synthesize ATP, the primary biological role is to acidify some compartment, such as yeast vacuole (a lysosomal homolog) or the interior of a prokaryote. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 129409  Cd Length: 209  Bit Score: 254.75  E-value: 1.25e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307     5 REQVFPTRMTLGLMKTKLKGANQGYSLLKRKSEALTKRFRDITKRIDDSKQKMGRVMQTAAFSLAEVTYATGENIGYQVQ 84
Cdd:TIGR00309   1 MEKVNPTRMELLKLKDKLKMAKRGYSLLKLKRDALIMEFRQILERAKDIKNKMEQKLKEAISDLIEAQSVMGPFAVWIAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307    85 ENVANARFKVRATQENVSGVYLPQFESF-IDSNINDfKMTGLGRGGQQVQRAKEIYSRAVETLVELASLQTAFIILDEVI 163
Cdd:TIGR00309  81 LSVVTARFEVDMKSKNIMGVVVPVFDSYeIRRKVHE-RGYGLLFTSYKVDEAAEIYEEAVELIVELAEIETTIRLLAEEI 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 50302307   164 KVTNRRVNAIEHVIIPRTENTIAYINSELDELDREEFYRLKKVQEKKQ 211
Cdd:TIGR00309 160 EITKRRVNALEHVIIPRLKNTIKYINMRLDEMDRENFVRLKKIKSSKE 207
ATP-synt_D pfam01813
ATP synthase subunit D; This is a family of subunit D form various ATP synthases including ...
14-208 1.05e-71

ATP synthase subunit D; This is a family of subunit D form various ATP synthases including V-type H+ transporting and Na+ dependent. Subunit D is suggested to be an integral part of the catalytic sector of the V-ATPase.


Pssm-ID: 460343  Cd Length: 194  Bit Score: 218.63  E-value: 1.05e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307    14 TLGLMKTKLKGANQGYSLLKRKSEALTKRFRDITKRIDDSKQKMGRVMQTAAFSLAEVTYATGE-NIGYQVQENVaNARF 92
Cdd:pfam01813   1 ELIRLKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGEeDVESLALESV-PSVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307    93 KVRATQENVSGVYLPQFEsFIDSNINDFKMTGLGRGGQQVQRAKEIYSRAVETLVELASLQTAFIILDEVIKVTNRRVNA 172
Cdd:pfam01813  80 RVEVKTENIMGVKVPVFE-LVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNA 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 50302307   173 IEHVIIPRTENTIAYINSELDELDREEFYRLKKVQE 208
Cdd:pfam01813 159 LEKVVIPRLEETIKYIKSELDEREREEFFRLKKVKA 194
NtpD COG1394
Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal ...
6-210 6.35e-34

Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441004  Cd Length: 202  Bit Score: 121.88  E-value: 6.35e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307   6 EQVFPTRMTLGLMKTKLKGANQGYSLLKRKSEALTKRFRDITKRIDDSKQKMGRVMQTAAFSLAEVTYATGENiGYQVQE 85
Cdd:COG1394   2 AKVKPTKMELLRLKRQLKLAKRGHKLLKDKRDALIREFLKLIDEAEELREELEELLEEAYEALALANARMGIE-AVEELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307  86 NVANARFKVRATQENVSGVYLPQFESFIDSNINDFkmtGLGRGGQQVQRAKEIYSRAVETLVELASLQTAFIILDEVIKV 165
Cdd:COG1394  81 LSVPRVLEVEVSTRNIMGVEVPVLESEEFKEERPY---GLLGTSAWLDEAIEALEELLELLLELAELETALRRLAEEIRK 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 50302307 166 TNRRVNAIEHVIIPRTENTIAYINSELDELDREEFYRLKKVQEKK 210
Cdd:COG1394 158 TQRRVNALEKVLIPRLEETIKYIRMKLEEREREEFVRLKKVKKKL 202
PRK00373 PRK00373
V-type ATP synthase subunit D; Reviewed
5-206 5.63e-29

V-type ATP synthase subunit D; Reviewed


Pssm-ID: 178991  Cd Length: 204  Bit Score: 109.14  E-value: 5.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307    5 REQVFPTRMTLGLMKTKLKGANQGYSLLKRKSEALTKRFRDITKRIDDSKQKMGRVMQTA--AFSLAEVTYATG--ENIG 80
Cdd:PRK00373   3 RLNVKPTRMELINLKRRLKLAERGHKLLKDKRDELIMEFFDILDEAKKLREEVEEELEEAykDFLMARAVEGSLavEEAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307   81 YQVQENVanarfKVRATQENVSGVYLPQFESFIDSNINDFKMTGLGRGGQQVQRAKEiYSRAVETLVELASLQTAFIILD 160
Cdd:PRK00373  83 ASPKESL-----EVDVSSKNIMGVVVPVIELSVKRTLPERGYGFLGTSAELDEAAEK-FEELLEKILELAEVEKTIQLLA 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 50302307  161 EVIKVTNRRVNAIEHVIIPRTENTIAYINSELDELDREEFYRLKKV 206
Cdd:PRK00373 157 DEIEKTKRRVNALEYVIIPRLEETIKYIKMKLDEMERENFVRLKKI 202
PRK02195 PRK02195
V-type ATP synthase subunit D; Provisional
93-189 3.67e-03

V-type ATP synthase subunit D; Provisional


Pssm-ID: 179382  Cd Length: 201  Bit Score: 37.61  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50302307   93 KVRATQENVSGVYLPQFESfIDSNINDFkmtGLGRGGQQVQRAKEIYSRAVETLVELASLQTAFIILDEVIKVTNRRVNA 172
Cdd:PRK02195  83 KVEKDYENIAGVEVPILDS-IEFEIIEY---SLLNTPIWVDTGIELLKELVQLKIEAEVLQERLLLLEEELRKTTQRVNL 158
                         90
                 ....*....|....*..
gi 50302307  173 IEHVIIPRTENTIAYIN 189
Cdd:PRK02195 159 FEKVLIPETKANIKKIK 175
 
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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