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Conserved domains on  [gi|58865520|ref|NP_001011972|]
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V-type proton ATPase subunit d 2 [Rattus norvegicus]

Protein Classification

V0D/AC39 family V-type ATPase subunit( domain architecture ID 10488051)

V0D/AC39 family V-type ATPase subunit such as Deinococcus radiodurans V-type ATPase subunit C, and eukaryotic V-type proton ATPase subunit d that is part of the integral membrane V0 proton pore complex of vacuolar ATPase, which is responsible for acidifying a variety of intracellular compartments in cells and providing the energy required for transport in the vacuolar system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
vATP-synt_AC39 pfam01992
ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP ...
16-338 1.24e-95

ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP synthase, and the C subunit from archaebacterial ATP synthase. The family also includes subunit C from the Sodium transporting ATP synthase from Enterococcus hirae.


:

Pssm-ID: 426553  Cd Length: 333  Bit Score: 287.24  E-value: 1.24e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520    16 LEGLVRGCKASLLTQQDYVNLVQCETLEDLKIHLQTTDYGNFLAHETNPLTVSKIDTEMRKKLCREFDYFRNHSLEPLST 95
Cdd:pfam01992   1 LNARVRAMESKLLTEEDYERLLQCESLEEAVRYLKETGYGDFLADEESPLHRGDIEKALRRELAKTFEKLRRFAPGLSRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520    96 FFTYMTCSYMIDNIILLMNGALQKKSVKEVLAKCHPLGRFT--EMEAVNIAESASELFKAVLvETPLAPFFQDCMsENTL 173
Cdd:pfam01992  81 FLDLYLYRYDIHNLKLLLRGKLSGLDLEELLEFLIPLGTLSalDLDKLIEAKDVEELVEALL-GTPYAEALEEAL-DELE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520   174 DELNIELLRNKLYKSYLEAFYKFCKDHGDVTAEVMCPILEFEADRRALIITLNSFG-TELSKEDRETLFPTCGKLYPEGL 252
Cdd:pfam01992 159 ETGDLQLIENALDKAYYEDLYKFCKKLGGKTAEILREYLGFEIDLRNIKIILRSKKyGKLSPEDIYKLLIPGGSLSPEEL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520   253 RLLAQAEDFEHMKRVAdNYGVYKPLFDAVGGSGG---KTLEDVFYEREVQMNV-LAFNRQFHYGVFYAYVKLKEQEMRNI 328
Cdd:pfam01992 239 KALAEAEDVEEVLAAL-EGTPYGELLSEALEELTgslSALERALDNYLLELAKkLARYQPFSIGPVLAYLKLKEQEIRNL 317
                         330
                  ....*....|
gi 58865520   329 VWIAECISQR 338
Cdd:pfam01992 318 RIIAEGKRYG 327
 
Name Accession Description Interval E-value
vATP-synt_AC39 pfam01992
ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP ...
16-338 1.24e-95

ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP synthase, and the C subunit from archaebacterial ATP synthase. The family also includes subunit C from the Sodium transporting ATP synthase from Enterococcus hirae.


Pssm-ID: 426553  Cd Length: 333  Bit Score: 287.24  E-value: 1.24e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520    16 LEGLVRGCKASLLTQQDYVNLVQCETLEDLKIHLQTTDYGNFLAHETNPLTVSKIDTEMRKKLCREFDYFRNHSLEPLST 95
Cdd:pfam01992   1 LNARVRAMESKLLTEEDYERLLQCESLEEAVRYLKETGYGDFLADEESPLHRGDIEKALRRELAKTFEKLRRFAPGLSRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520    96 FFTYMTCSYMIDNIILLMNGALQKKSVKEVLAKCHPLGRFT--EMEAVNIAESASELFKAVLvETPLAPFFQDCMsENTL 173
Cdd:pfam01992  81 FLDLYLYRYDIHNLKLLLRGKLSGLDLEELLEFLIPLGTLSalDLDKLIEAKDVEELVEALL-GTPYAEALEEAL-DELE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520   174 DELNIELLRNKLYKSYLEAFYKFCKDHGDVTAEVMCPILEFEADRRALIITLNSFG-TELSKEDRETLFPTCGKLYPEGL 252
Cdd:pfam01992 159 ETGDLQLIENALDKAYYEDLYKFCKKLGGKTAEILREYLGFEIDLRNIKIILRSKKyGKLSPEDIYKLLIPGGSLSPEEL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520   253 RLLAQAEDFEHMKRVAdNYGVYKPLFDAVGGSGG---KTLEDVFYEREVQMNV-LAFNRQFHYGVFYAYVKLKEQEMRNI 328
Cdd:pfam01992 239 KALAEAEDVEEVLAAL-EGTPYGELLSEALEELTgslSALERALDNYLLELAKkLARYQPFSIGPVLAYLKLKEQEIRNL 317
                         330
                  ....*....|
gi 58865520   329 VWIAECISQR 338
Cdd:pfam01992 318 RIIAEGKRYG 327
NtpC COG1527
Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]; Archaeal ...
12-335 1.97e-17

Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441136  Cd Length: 348  Bit Score: 81.93  E-value: 1.97e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520  12 DHGYLEGLVRGCKASLLTQQDYVNLVQCETLEDLKIHLQTTDYGNFLAHETNP-LTVSKIDTEMRKKLCREFDYFRNHSL 90
Cdd:COG1527   6 NYAYINARIRAMESKLLKEEDYERLLEAESLEEIARFLKETGYGEELDELAEReSGRDLLEKALNRNLAKTYRKLLEFAP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520  91 EPLSTFFTYMTCSYMIDNIILLMNGALQKKSVKEVLAKCHPLGRFTEMEAVNIAESAS-ELFKAVLVETPLAPFFQDCMS 169
Cdd:COG1527  86 GELKEFVKLYLLRYDIHNLKVILRGKYSGEDLEEIRELLIPAGELSEEDLKKLLEAKSvEELVEALEGTPYYEALEEALE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520 170 --ENTLDELNIEllrNKLYKSYLEAFYKFcKDHGDVTAEVMCPILEFEADRRALIITLNSFGTELSKEDRETLFPTCGKL 247
Cdd:COG1527 166 eyEETGDLFPIE---NALDRAYYENLLEL-AKKKGKDRKLLLEYLGTEIDLLNLRTILRLKRYGLSPEEIEAYLIPGGYR 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520 248 YPEG-LRLLAQAEDFEHMKRVADNYGVYKPLFDAVGGSGGKTLEDVfyEREVQMNVLA-FNRQFHYGVF-----YAYVKL 320
Cdd:COG1527 242 ISEKeLKELAEAEDVEELLEALEGTPYGKLLSELEELEETGSLSEF--ERALDRYLLEyAKKLSKYYPFsigpvLAYLLA 319
                       330
                ....*....|....*
gi 58865520 321 KEQEMRNIVWIAECI 335
Cdd:COG1527 320 KENEVKNLRIIAEGK 334
AhaC TIGR02923
ATP synthase A1, C subunit; The A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
15-332 1.16e-15

ATP synthase A1, C subunit; The A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The C subunit is part of the hydrophilic A1 "stalk" complex (AhaABCDEFG), which is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex.


Pssm-ID: 274352  Cd Length: 343  Bit Score: 76.71  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520    15 YLEGLVRGCKASLLTQQDYVNLVQCETLEDLKIHLQTTDYGNFLAHETNPLT-VSKIDTEMRKKLCREFDYFRNHSLEPL 93
Cdd:TIGR02923   7 YPNARVRAMESRLLKEEDFNELLEMRGTDEIVRFLEETDYKKELDELGSKSYgVDLIEHALDANLAKTYEKLFRISPGAS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520    94 STFFTYMTCSYMIDNIILLMNGALQKKSVKEVLAKCHPLGRFTE--MEAVNIAESASELFKAvLVETPLAPFFQDCMSEN 171
Cdd:TIGR02923  87 RDLIRLYLKKWDVWNIKTLIRAKYANASAEEVEDLLIPAGEFLEkrIKELAEAKTIEEIVEA-LEGTPYYGPLQEALAGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520   172 TldelNIELLRNKLYKSYLEAFYKFCKDHGDVTAEVMCPILEFEADRRALIITLNSFGTELS-KEDRETLFPTCGKLYPE 250
Cdd:TIGR02923 166 G----DLSPIENELDRMYYEKLLKYVGSPSDDETKLFTEFIKTEVDIRNLKTLLRLKAAGLSpDEIMPYTIPGGYELDEE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520   251 GLRLLAQAEDFEHMKRVADNYGvYKPLFDAVGGSGGK---TLEDVFYEREVQM-NVLAFNRQFHYGVFYAYVKLKEQEMR 326
Cdd:TIGR02923 242 KLAPLAHIESIDEVVSALDGTK-YGEDISEVLSEEEKsvaVFERALDEYLIKMaTKLSLRYPLSVGPVLGYILKKEREVR 320

                  ....*.
gi 58865520   327 NIVWIA 332
Cdd:TIGR02923 321 NLRAIA 326
PRK01198 PRK01198
V-type ATP synthase subunit C; Provisional
20-262 2.32e-04

V-type ATP synthase subunit C; Provisional


Pssm-ID: 234917  Cd Length: 352  Bit Score: 42.55  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520   20 VRGCKASLLTQQDYVNLVQCETLEDLKIHLQTTDYGNFLAHETNPLT-VSKIDTEMRKKLCREFDYFRNHSLEPLSTFFT 98
Cdd:PRK01198  18 VRVREAKLLDREKYERLLEMKSLEEIIRFLEETEYKEEIDELGSRYSgPDLIEKALNRNLAKTYELLLEISPGRLKELVD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520   99 YMTCSYMIDNIILLMNGALQKKSVKEVLAKCHPLGRFTE--MEAVNIAESASELFKAvLVETPLAPFFQDCMS--ENTLD 174
Cdd:PRK01198  98 VYLRKWDIHNIKTLLRGKILGLDAEEIEELLIPAGELDLekLKELLEAKSVEEIVKI-LEGTEYYEVLEEALEdyEETGD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520  175 ELNIEllrNKLYKSYLEAFYKFCKDHGDVTAevmcPILEF---EADRRALIITLNSFGTELSKEDRETLFPTCGKLYPEG 251
Cdd:PRK01198 177 LQPIE---NALDKYYYENLLEIASPKDIDEK----LLLEYvrtEIDITNIKTLLRLKAQGLSADFIEKVLIPGGSLDEEK 249
                        250
                 ....*....|.
gi 58865520  252 LRLLAqAEDFE 262
Cdd:PRK01198 250 LKELL-AEDIE 259
 
Name Accession Description Interval E-value
vATP-synt_AC39 pfam01992
ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP ...
16-338 1.24e-95

ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP synthase, and the C subunit from archaebacterial ATP synthase. The family also includes subunit C from the Sodium transporting ATP synthase from Enterococcus hirae.


Pssm-ID: 426553  Cd Length: 333  Bit Score: 287.24  E-value: 1.24e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520    16 LEGLVRGCKASLLTQQDYVNLVQCETLEDLKIHLQTTDYGNFLAHETNPLTVSKIDTEMRKKLCREFDYFRNHSLEPLST 95
Cdd:pfam01992   1 LNARVRAMESKLLTEEDYERLLQCESLEEAVRYLKETGYGDFLADEESPLHRGDIEKALRRELAKTFEKLRRFAPGLSRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520    96 FFTYMTCSYMIDNIILLMNGALQKKSVKEVLAKCHPLGRFT--EMEAVNIAESASELFKAVLvETPLAPFFQDCMsENTL 173
Cdd:pfam01992  81 FLDLYLYRYDIHNLKLLLRGKLSGLDLEELLEFLIPLGTLSalDLDKLIEAKDVEELVEALL-GTPYAEALEEAL-DELE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520   174 DELNIELLRNKLYKSYLEAFYKFCKDHGDVTAEVMCPILEFEADRRALIITLNSFG-TELSKEDRETLFPTCGKLYPEGL 252
Cdd:pfam01992 159 ETGDLQLIENALDKAYYEDLYKFCKKLGGKTAEILREYLGFEIDLRNIKIILRSKKyGKLSPEDIYKLLIPGGSLSPEEL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520   253 RLLAQAEDFEHMKRVAdNYGVYKPLFDAVGGSGG---KTLEDVFYEREVQMNV-LAFNRQFHYGVFYAYVKLKEQEMRNI 328
Cdd:pfam01992 239 KALAEAEDVEEVLAAL-EGTPYGELLSEALEELTgslSALERALDNYLLELAKkLARYQPFSIGPVLAYLKLKEQEIRNL 317
                         330
                  ....*....|
gi 58865520   329 VWIAECISQR 338
Cdd:pfam01992 318 RIIAEGKRYG 327
NtpC COG1527
Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]; Archaeal ...
12-335 1.97e-17

Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441136  Cd Length: 348  Bit Score: 81.93  E-value: 1.97e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520  12 DHGYLEGLVRGCKASLLTQQDYVNLVQCETLEDLKIHLQTTDYGNFLAHETNP-LTVSKIDTEMRKKLCREFDYFRNHSL 90
Cdd:COG1527   6 NYAYINARIRAMESKLLKEEDYERLLEAESLEEIARFLKETGYGEELDELAEReSGRDLLEKALNRNLAKTYRKLLEFAP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520  91 EPLSTFFTYMTCSYMIDNIILLMNGALQKKSVKEVLAKCHPLGRFTEMEAVNIAESAS-ELFKAVLVETPLAPFFQDCMS 169
Cdd:COG1527  86 GELKEFVKLYLLRYDIHNLKVILRGKYSGEDLEEIRELLIPAGELSEEDLKKLLEAKSvEELVEALEGTPYYEALEEALE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520 170 --ENTLDELNIEllrNKLYKSYLEAFYKFcKDHGDVTAEVMCPILEFEADRRALIITLNSFGTELSKEDRETLFPTCGKL 247
Cdd:COG1527 166 eyEETGDLFPIE---NALDRAYYENLLEL-AKKKGKDRKLLLEYLGTEIDLLNLRTILRLKRYGLSPEEIEAYLIPGGYR 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520 248 YPEG-LRLLAQAEDFEHMKRVADNYGVYKPLFDAVGGSGGKTLEDVfyEREVQMNVLA-FNRQFHYGVF-----YAYVKL 320
Cdd:COG1527 242 ISEKeLKELAEAEDVEELLEALEGTPYGKLLSELEELEETGSLSEF--ERALDRYLLEyAKKLSKYYPFsigpvLAYLLA 319
                       330
                ....*....|....*
gi 58865520 321 KEQEMRNIVWIAECI 335
Cdd:COG1527 320 KENEVKNLRIIAEGK 334
AhaC TIGR02923
ATP synthase A1, C subunit; The A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
15-332 1.16e-15

ATP synthase A1, C subunit; The A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The C subunit is part of the hydrophilic A1 "stalk" complex (AhaABCDEFG), which is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex.


Pssm-ID: 274352  Cd Length: 343  Bit Score: 76.71  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520    15 YLEGLVRGCKASLLTQQDYVNLVQCETLEDLKIHLQTTDYGNFLAHETNPLT-VSKIDTEMRKKLCREFDYFRNHSLEPL 93
Cdd:TIGR02923   7 YPNARVRAMESRLLKEEDFNELLEMRGTDEIVRFLEETDYKKELDELGSKSYgVDLIEHALDANLAKTYEKLFRISPGAS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520    94 STFFTYMTCSYMIDNIILLMNGALQKKSVKEVLAKCHPLGRFTE--MEAVNIAESASELFKAvLVETPLAPFFQDCMSEN 171
Cdd:TIGR02923  87 RDLIRLYLKKWDVWNIKTLIRAKYANASAEEVEDLLIPAGEFLEkrIKELAEAKTIEEIVEA-LEGTPYYGPLQEALAGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520   172 TldelNIELLRNKLYKSYLEAFYKFCKDHGDVTAEVMCPILEFEADRRALIITLNSFGTELS-KEDRETLFPTCGKLYPE 250
Cdd:TIGR02923 166 G----DLSPIENELDRMYYEKLLKYVGSPSDDETKLFTEFIKTEVDIRNLKTLLRLKAAGLSpDEIMPYTIPGGYELDEE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520   251 GLRLLAQAEDFEHMKRVADNYGvYKPLFDAVGGSGGK---TLEDVFYEREVQM-NVLAFNRQFHYGVFYAYVKLKEQEMR 326
Cdd:TIGR02923 242 KLAPLAHIESIDEVVSALDGTK-YGEDISEVLSEEEKsvaVFERALDEYLIKMaTKLSLRYPLSVGPVLGYILKKEREVR 320

                  ....*.
gi 58865520   327 NIVWIA 332
Cdd:TIGR02923 321 NLRAIA 326
PRK01198 PRK01198
V-type ATP synthase subunit C; Provisional
20-262 2.32e-04

V-type ATP synthase subunit C; Provisional


Pssm-ID: 234917  Cd Length: 352  Bit Score: 42.55  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520   20 VRGCKASLLTQQDYVNLVQCETLEDLKIHLQTTDYGNFLAHETNPLT-VSKIDTEMRKKLCREFDYFRNHSLEPLSTFFT 98
Cdd:PRK01198  18 VRVREAKLLDREKYERLLEMKSLEEIIRFLEETEYKEEIDELGSRYSgPDLIEKALNRNLAKTYELLLEISPGRLKELVD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520   99 YMTCSYMIDNIILLMNGALQKKSVKEVLAKCHPLGRFTE--MEAVNIAESASELFKAvLVETPLAPFFQDCMS--ENTLD 174
Cdd:PRK01198  98 VYLRKWDIHNIKTLLRGKILGLDAEEIEELLIPAGELDLekLKELLEAKSVEEIVKI-LEGTEYYEVLEEALEdyEETGD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865520  175 ELNIEllrNKLYKSYLEAFYKFCKDHGDVTAevmcPILEF---EADRRALIITLNSFGTELSKEDRETLFPTCGKLYPEG 251
Cdd:PRK01198 177 LQPIE---NALDKYYYENLLEIASPKDIDEK----LLLEYvrtEIDITNIKTLLRLKAQGLSADFIEKVLIPGGSLDEEK 249
                        250
                 ....*....|.
gi 58865520  252 LRLLAqAEDFE 262
Cdd:PRK01198 250 LKELL-AEDIE 259
 
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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