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Conserved domains on  [gi|16132004|ref|NP_418603|]
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PspA family protein YjfJ [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

PspA/IM30 family protein( domain architecture ID 12049156)

PspA/IM30 family protein similar to Deinococcus radiodurans phage shock protein A homolog and Arabidopsis thaliana membrane-associated protein VIPP1, which is required for plastid vesicle formation and thylakoid membrane biogenesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
3-228 3.07e-38

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


:

Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 132.11  E-value: 3.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004     3 ILKSLFTLGKSFISQAEESIEETQgvRMLEQHIRDAKAELDKAGKSRVDLLARVKLSHDKLKDLRERKASLEARALEALS 82
Cdd:pfam04012   1 IFKRLGRLVRANIHEGLDKAEDPE--KMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004    83 KNvNPSLINEVAEEIARLENLITAEEQVLSNLEVSRDGVEKAVTATAQRIAQFEQQMEVVKATEAMQRAQQAVTTSTvgA 162
Cdd:pfam04012  79 KG-NEELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTSL--G 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16132004   163 SSSVSTAAESLKRLQTRQAERQARLDAAAQLEKVAdgrDLDEKLAEAGIGGSNkssAQDVLARLQR 228
Cdd:pfam04012 156 SLSTSSATDSFERIEEKIEEREARADAAAELASAV---DLDAKLEQAGIQMEV---SEDVLARLKA 215
 
Name Accession Description Interval E-value
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
3-228 3.07e-38

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 132.11  E-value: 3.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004     3 ILKSLFTLGKSFISQAEESIEETQgvRMLEQHIRDAKAELDKAGKSRVDLLARVKLSHDKLKDLRERKASLEARALEALS 82
Cdd:pfam04012   1 IFKRLGRLVRANIHEGLDKAEDPE--KMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004    83 KNvNPSLINEVAEEIARLENLITAEEQVLSNLEVSRDGVEKAVTATAQRIAQFEQQMEVVKATEAMQRAQQAVTTSTvgA 162
Cdd:pfam04012  79 KG-NEELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTSL--G 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16132004   163 SSSVSTAAESLKRLQTRQAERQARLDAAAQLEKVAdgrDLDEKLAEAGIGGSNkssAQDVLARLQR 228
Cdd:pfam04012 156 SLSTSSATDSFERIEEKIEEREARADAAAELASAV---DLDAKLEQAGIQMEV---SEDVLARLKA 215
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
2-230 1.47e-23

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 94.12  E-value: 1.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004   2 GILKSLFTLGKSFISQAEESIEETQgvRMLEQHIRDAKAELDKAGKSRVDLLARVKLSHDKLKDLRERKASLEARALEAL 81
Cdd:COG1842   1 GIFKRLSDIIRANINALLDKAEDPE--KMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLAL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004  82 SKNvNPSLINEVAEEIARLENLITAEEQVLSNLEVSRDGVEKAVTATAQRIAQFEQQMEVVKATEAMQRAQQAVTTSTVG 161
Cdd:COG1842  79 EKG-REDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSG 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132004 162 ASSsvSTAAESLKRLQTRQAERQARLDAAAQLekvADGRDLDEKLAEAgiggSNKSSAQDVLARLQRQQ 230
Cdd:COG1842 158 IDS--DDATSALERMEEKIEEMEARAEAAAEL---AAGDSLDDELAEL----EADSEVEDELAALKAKM 217
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
12-209 1.65e-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: 42.35  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004     12 KSFISQAEESIEETQG--------VRMLEQHIRDAKAELDKAGKSRVDLLARVKLSHDKLKDLRERKASLEARalealsk 83
Cdd:TIGR02168  273 RLEVSELEEEIEELQKelyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK------- 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004     84 nvnpslINEVAEEIARLENLITAEEQVLSNLEVSRDGVEKAVTATAQRIAQFEQQMEVVKATEAMQRAQqavttstvgas 163
Cdd:TIGR02168  346 ------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR----------- 408
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 16132004    164 ssVSTAAESLKRLQTRQAERQARLDAAAQLEKVADGRDLDEKLAEA 209
Cdd:TIGR02168  409 --LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
 
Name Accession Description Interval E-value
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
3-228 3.07e-38

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 132.11  E-value: 3.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004     3 ILKSLFTLGKSFISQAEESIEETQgvRMLEQHIRDAKAELDKAGKSRVDLLARVKLSHDKLKDLRERKASLEARALEALS 82
Cdd:pfam04012   1 IFKRLGRLVRANIHEGLDKAEDPE--KMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004    83 KNvNPSLINEVAEEIARLENLITAEEQVLSNLEVSRDGVEKAVTATAQRIAQFEQQMEVVKATEAMQRAQQAVTTSTvgA 162
Cdd:pfam04012  79 KG-NEELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTSL--G 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16132004   163 SSSVSTAAESLKRLQTRQAERQARLDAAAQLEKVAdgrDLDEKLAEAGIGGSNkssAQDVLARLQR 228
Cdd:pfam04012 156 SLSTSSATDSFERIEEKIEEREARADAAAELASAV---DLDAKLEQAGIQMEV---SEDVLARLKA 215
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
2-230 1.47e-23

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 94.12  E-value: 1.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004   2 GILKSLFTLGKSFISQAEESIEETQgvRMLEQHIRDAKAELDKAGKSRVDLLARVKLSHDKLKDLRERKASLEARALEAL 81
Cdd:COG1842   1 GIFKRLSDIIRANINALLDKAEDPE--KMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLAL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004  82 SKNvNPSLINEVAEEIARLENLITAEEQVLSNLEVSRDGVEKAVTATAQRIAQFEQQMEVVKATEAMQRAQQAVTTSTVG 161
Cdd:COG1842  79 EKG-REDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSG 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132004 162 ASSsvSTAAESLKRLQTRQAERQARLDAAAQLekvADGRDLDEKLAEAgiggSNKSSAQDVLARLQRQQ 230
Cdd:COG1842 158 IDS--DDATSALERMEEKIEEMEARAEAAAEL---AAGDSLDDELAEL----EADSEVEDELAALKAKM 217
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
15-230 1.79e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004  15 ISQAEESIEET-QGVRMLEQHIRDAKAELDKAGKSRVDLLARVKLSHDKLKDLRERKASLEARALEALSKnvnpslINEV 93
Cdd:COG1196 262 LAELEAELEELrLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE------LEEL 335
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004  94 AEEIARLENLITAEEQVLSNLEVSRDGVEKAVTATAQRIAQFEQQMEVVKATEAMQRAQQAVTTStvgasssvstAAESL 173
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA----------QLEEL 405
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16132004 174 KRLQTRQAERQARLDAAAQLEKVADGRDLDEKLAEAGIGGSNKSSAQDVLARLQRQQ 230
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
31-232 3.81e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 3.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004  31 LEQHIRDAKAELDKAGKSRVDLLARVKLSHDKLKDLRERKASLEARALEALSKnvnpslINEVAEEIARLENLITAEEQV 110
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------EYELLAELARLEQDIARLEER 310
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004 111 LSNLEVSRDGVEKAVTATAQRIAQFEQQMEVVKATEAMQRAQQAVttstvgASSSVSTAAESLKRLQTRQAERQARLDAA 190
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE------AEAELAEAEEALLEAEAELAEAEEELEEL 384
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 16132004 191 AQLEKVADGRDLDEKLAEAGIGGSNKSSAQDVLARLQRQQGE 232
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
33-230 4.11e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 4.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004   33 QHIRDAKAELDKAgKSRVDLLARVKLSHDKLKDLRERKASLEA-----------RALEALSKnvnpsLINEVAEEIARLE 101
Cdd:COG4913  235 DDLERAHEALEDA-REQIELLEPIRELAERYAAARERLAELEYlraalrlwfaqRRLELLEA-----ELEELRAELARLE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004  102 NLITAEEQVLSNLEVSRDGVEKAV-TATAQRIAQFEQQMEVVKATEA---MQRAQQAVTTSTVGAsssvsTAAESLKRLQ 177
Cdd:COG4913  309 AELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEereRRRARLEALLAALGL-----PLPASAEEFA 383
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16132004  178 TRQAERQARLDAAAQLEKVADgRDLDEKLAEAGIGGSNKSSAQDVLARLQRQQ 230
Cdd:COG4913  384 ALRAEAAALLEALEEELEALE-EALAEAEAALRDLRRELRELEAEIASLERRK 435
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
12-209 1.65e-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: 42.35  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004     12 KSFISQAEESIEETQG--------VRMLEQHIRDAKAELDKAGKSRVDLLARVKLSHDKLKDLRERKASLEARalealsk 83
Cdd:TIGR02168  273 RLEVSELEEEIEELQKelyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK------- 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004     84 nvnpslINEVAEEIARLENLITAEEQVLSNLEVSRDGVEKAVTATAQRIAQFEQQMEVVKATEAMQRAQqavttstvgas 163
Cdd:TIGR02168  346 ------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR----------- 408
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 16132004    164 ssVSTAAESLKRLQTRQAERQARLDAAAQLEKVADGRDLDEKLAEA 209
Cdd:TIGR02168  409 --LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
61-232 1.79e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004   61 DKLKDLRERKASLEARALEALSKnvnpslINEVAEEIARLENLITAEEQV--LSNLEVSRDGVEKAVTATAQRIAQFEQ- 137
Cdd:COG4913  610 AKLAALEAELAELEEELAEAEER------LEALEAELDALQERREALQRLaeYSWDEIDVASAEREIAELEAELERLDAs 683
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004  138 -------QMEVVKATEAMQRAQQAVTtstvGASSSVSTAAESLKRLQTRQAERQARLDAAAQLEKVADGRDLDEKLAEAG 210
Cdd:COG4913  684 sddlaalEEQLEELEAELEELEEELD----ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
                        170       180
                 ....*....|....*....|..
gi 16132004  211 IGGSNKSSAQDVLARLQRQQGE 232
Cdd:COG4913  760 GDAVERELRENLEERIDALRAR 781
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5-192 4.65e-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: 37.73  E-value: 4.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004      5 KSLFTLGKSFISQAEESIEETQGVRMLEQHIRDAKAELDKAGKSRVDLLARVKLSHDKLKDLRERKASLEARALEALS-K 83
Cdd:TIGR02168  719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEeL 798
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004     84 NVNPSLINEVAEEIARLENLITAEEQVLSNLEVSRDGVEKAVTATAQRIAQFEQQME-VVKATEAMQRAQQAVTTSTVGA 162
Cdd:TIGR02168  799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIEsLAAEIEELEELIEELESELEAL 878
                          170       180       190
                   ....*....|....*....|....*....|
gi 16132004    163 SSSVSTAAESLKRLQTRQAERQARLDAAAQ 192
Cdd:TIGR02168  879 LNERASLEEALALLRSELEELSEELRELES 908
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
31-189 5.72e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.59  E-value: 5.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132004   31 LEQHIRDAKAELDKAGKSRVDLLARVKLSHDKLKDLRERKASLEARALEALSKnvnpsLINEVAEEIARLENLITAEEQV 110
Cdd:COG4913  293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLER-----EIERLERELEERERRRARLEAL 367
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132004  111 LSNLEVSRDGVEKAVTATAQRIAQFEQQmevvkATEAMQRAQQAVTtstvgasssvsTAAESLKRLQTRQAERQARLDA 189
Cdd:COG4913  368 LAALGLPLPASAEEFAALRAEAAALLEA-----LEEELEALEEALA-----------EAEAALRDLRRELRELEAEIAS 430
 
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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