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Conserved domains on  [gi|530362674|ref|XP_005270946|]
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nuclear autoantigenic sperm protein isoform X4 [Homo sapiens]

Protein Classification

TPR_12 and SHNi-TPR domain-containing protein( domain architecture ID 12139966)

TPR_12 and SHNi-TPR domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SHNi-TPR pfam10516
SHNi-TPR; SHNi-TPR family members contain a reiterated sequence motif that is an interrupted ...
 205-242 2.62e-09

SHNi-TPR; SHNi-TPR family members contain a reiterated sequence motif that is an interrupted form of TPR repeat.


:

Pssm-ID: 402238 [Multi-domain]  Cd Length: 38  Bit Score: 52.45  E-value: 2.62e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 530362674  205 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAH 242
Cdd:pfam10516   1 ADVYDLLGEISLENENFPQAVTDLRKALELREELLPPE 38
TPR_12 pfam13424
Tetratricopeptide repeat;
203-279 5.06e-07

Tetratricopeptide repeat;


:

Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 47.00  E-value: 5.06e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530362674  203 YAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEN 279
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 140-342 1.41e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674   140 TEGSEEDDKENDKTEEMPNDSVLENKSLqENEEEEIGNLELAWDMLDLAKIIFKRQETKEAQlYAAQAHLKLGEVSVESE 219
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDL-ARLEAEVEQLEERIAQLSKELTELEAEIEELEE-RLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674   220 NYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVLNEQVKEAEGssaeyk 299
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA------ 859

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 530362674   300 kEIEELKELLPEIREKIEDAKESQRSGNVAELALKATLVESST 342
Cdd:TIGR02168  860 -EIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
 
Name Accession Description Interval E-value
SHNi-TPR pfam10516
SHNi-TPR; SHNi-TPR family members contain a reiterated sequence motif that is an interrupted ...
 205-242 2.62e-09

SHNi-TPR; SHNi-TPR family members contain a reiterated sequence motif that is an interrupted form of TPR repeat.


Pssm-ID: 402238 [Multi-domain]  Cd Length: 38  Bit Score: 52.45  E-value: 2.62e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 530362674  205 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAH 242
Cdd:pfam10516   1 ADVYDLLGEISLENENFPQAVTDLRKALELREELLPPE 38
TPR_12 pfam13424
Tetratricopeptide repeat;
203-279 5.06e-07

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 47.00  E-value: 5.06e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530362674  203 YAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEN 279
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 205-275 3.81e-06

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 49.22  E-value: 3.81e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530362674 205 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAhdrllaetHYQLGLAYGYNSQYDEAVAQFSKSIE 275
Cdd:COG3914  146 AEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEA--------LNNLGNALQDLGRLEEAIAAYRRALE 208
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
205-321 8.08e-06

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 46.83  E-value: 8.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674 205 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRllaethyqLGLAYGYNSQYDEAVAQFSKSIEVIEN-RMAV 283
Cdd:COG4785  107 AEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLN--------RGIALYYLGRYELAIADLEKALELDPNdPERA 178

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 530362674 284 LNEQVKEAEGSSAEYKKEIEELKELLPEIREKIEDAKE 321
Cdd:COG4785  179 LWLYLAERKLDPEKALALLLEDWATAYLLQGDTEEARE 216
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 140-342 1.41e-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: 41.20  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674   140 TEGSEEDDKENDKTEEMPNDSVLENKSLqENEEEEIGNLELAWDMLDLAKIIFKRQETKEAQlYAAQAHLKLGEVSVESE 219
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDL-ARLEAEVEQLEERIAQLSKELTELEAEIEELEE-RLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674   220 NYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVLNEQVKEAEGssaeyk 299
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA------ 859

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 530362674   300 kEIEELKELLPEIREKIEDAKESQRSGNVAELALKATLVESST 342
Cdd:TIGR02168  860 -EIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
PRK02603 PRK02603
photosystem I assembly protein Ycf3; Provisional
 187-285 2.24e-03

photosystem I assembly protein Ycf3; Provisional


Pssm-ID: 179448 [Multi-domain]  Cd Length: 172  Bit Score: 38.88  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674 187 LAKIIFK----RQETKEAQLY-----AAQAHlklGEvsvesenYVQAVEEFQSCLNLQEqylEAHDRllAETHYQLGLAY 257
Cdd:PRK02603  18 MADLILKilpiNKKAKEAFVYyrdgmSAQAD---GE-------YAEALENYEEALKLEE---DPNDR--SYILYNMGIIY 82

                         90       100
                 ....*....|....*....|....*...
gi 530362674 258 GYNSQYDEAVAQFSKSIEVIENRMAVLN 285
Cdd:PRK02603  83 ASNGEHDKALEYYHQALELNPKQPSALN 110
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 247-279 8.51e-03

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 33.96  E-value: 8.51e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 530362674   247 AETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEN 279
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33
 
Name Accession Description Interval E-value
SHNi-TPR pfam10516
SHNi-TPR; SHNi-TPR family members contain a reiterated sequence motif that is an interrupted ...
 205-242 2.62e-09

SHNi-TPR; SHNi-TPR family members contain a reiterated sequence motif that is an interrupted form of TPR repeat.


Pssm-ID: 402238 [Multi-domain]  Cd Length: 38  Bit Score: 52.45  E-value: 2.62e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 530362674  205 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAH 242
Cdd:pfam10516   1 ADVYDLLGEISLENENFPQAVTDLRKALELREELLPPE 38
TPR_12 pfam13424
Tetratricopeptide repeat;
203-279 5.06e-07

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 47.00  E-value: 5.06e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530362674  203 YAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEN 279
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 205-275 3.81e-06

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 49.22  E-value: 3.81e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530362674 205 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAhdrllaetHYQLGLAYGYNSQYDEAVAQFSKSIE 275
Cdd:COG3914  146 AEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEA--------LNNLGNALQDLGRLEEAIAAYRRALE 208
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
205-321 8.08e-06

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 46.83  E-value: 8.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674 205 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRllaethyqLGLAYGYNSQYDEAVAQFSKSIEVIEN-RMAV 283
Cdd:COG4785  107 AEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLN--------RGIALYYLGRYELAIADLEKALELDPNdPERA 178

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 530362674 284 LNEQVKEAEGSSAEYKKEIEELKELLPEIREKIEDAKE 321
Cdd:COG4785  179 LWLYLAERKLDPEKALALLLEDWATAYLLQGDTEEARE 216
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
162-275 2.73e-05

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 45.29  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674 162 LENKSLQENEEEEIGNLELAWDMLDLAKIIFKRQETKEAQLYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYlea 241
Cdd:COG4785   30 LFAAVLALAIALADLALALAAAALAAAALAAERIDRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDL--- 106

                         90       100       110
                 ....*....|....*....|....*....|....
gi 530362674 242 hdrllAETHYQLGLAYGYNSQYDEAVAQFSKSIE 275
Cdd:COG4785  107 -----AEAYNNRGLAYLLLGDYDAALEDFDRALE 135
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 179-311 1.98e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 41.33  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674 179 ELAWDMLDLAKIIFKRQETKEAQLYA----------AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAhdrllae 248
Cdd:COG4783    2 ACAEALYALAQALLLAGDYDEAEALLekaleldpdnPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEA------- 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530362674 249 tHYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVLNE--QVKEAEGSSAEYKKEIEELKELLPE 311
Cdd:COG4783   75 -RLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRlaRAYRALGRPDEAIAALEKALELDPD 138
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 154-285 3.17e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 43.06  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674 154 EEMPNDSVLENKSLQENEEEEIGNLELAWDMLDLAKIIFKRQETKEA-QLYA---------AQAHLKLGEVSVESENYVQ 223
Cdd:COG3914   51 LAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEAlALYRralalnpdnAEALFNLGNLLLALGRLEE 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530362674 224 AVEEFQSCLNLQEQYLEAHdrllaethYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVLN 285
Cdd:COG3914  131 ALAALRRALALNPDFAEAY--------LNLGEALRRLGRLEEAIAALRRALELDPDNAEALN 184
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 176-309 3.84e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 42.02  E-value: 3.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674 176 GNLELAWDMLDLAKIIFkrQETKEAQLYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHdRLLAETHYQLGl 255
Cdd:COG2956   49 GNLYRRRGEYDRAIRIH--QKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEAL-RLLAEIYEQEG- 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530362674 256 aygynsQYDEAVAQFSKSIEVIENRMAVLNEQVKEAEGSSaEYKKEIEELKELL 309
Cdd:COG2956  125 ------DWEKAIEVLERLLKLGPENAHAYCELAELYLEQG-DYDEAIEALEKAL 171
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
205-275 8.68e-04

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 40.76  E-value: 8.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530362674 205 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYleahdrllAETHYQLGLAYGYNSQYDEAVAQFSKSIE 275
Cdd:COG0457    8 AEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDD--------AEALYNLGLAYLRLGRYEEALADYEQALE 70
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 140-342 1.41e-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: 41.20  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674   140 TEGSEEDDKENDKTEEMPNDSVLENKSLqENEEEEIGNLELAWDMLDLAKIIFKRQETKEAQlYAAQAHLKLGEVSVESE 219
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDL-ARLEAEVEQLEERIAQLSKELTELEAEIEELEE-RLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674   220 NYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVLNEQVKEAEGssaeyk 299
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA------ 859

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 530362674   300 kEIEELKELLPEIREKIEDAKESQRSGNVAELALKATLVESST 342
Cdd:TIGR02168  860 -EIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 145-337 1.59e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674   145 EDDKENDKTEEMPNDSVLENKSLQ-ENEEEEIGNLElawDMLDLAKIifkRQETKEAQlyaaqahlKLGEVSVESENYVQ 223
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDlHKLEEALNDLE---ARLSHSRI---PEIQAELS--------KLEEEVSRIEARLR 815

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674   224 AVEEFQSCLNLQEQYLEAHDRLLAEthyqlglaygYNSQYDEAVAQFSKSIEVIENRMAVLNEQVKEAEGSSAEY----- 298
Cdd:TIGR02169  816 EIEQKLNRLTLEKEYLEKEIQELQE----------QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLesrlg 885

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 530362674   299 --KKEIEELKELLPEIREKIEDAKESQRSGNVAELALKATL 337
Cdd:TIGR02169  886 dlKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 164-309 1.99e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 40.10  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674 164 NKSLQENEEEEIGNLELAWD-----MLDLAKIIFKRQETKEAqlYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQY 238
Cdd:COG2956   66 QKLLERDPDRAEALLELAQDylkagLLDRAEELLEKLLELDP--DDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPEN 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530362674 239 leahdrllAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVLNE--QVKEAEGssaEYKKEIEELKELL 309
Cdd:COG2956  144 --------AHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLlaELYLEQG---DYEEAIAALERAL 205
PRK02603 PRK02603
photosystem I assembly protein Ycf3; Provisional
 187-285 2.24e-03

photosystem I assembly protein Ycf3; Provisional


Pssm-ID: 179448 [Multi-domain]  Cd Length: 172  Bit Score: 38.88  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674 187 LAKIIFK----RQETKEAQLY-----AAQAHlklGEvsvesenYVQAVEEFQSCLNLQEqylEAHDRllAETHYQLGLAY 257
Cdd:PRK02603  18 MADLILKilpiNKKAKEAFVYyrdgmSAQAD---GE-------YAEALENYEEALKLEE---DPNDR--SYILYNMGIIY 82

                         90       100
                 ....*....|....*....|....*...
gi 530362674 258 GYNSQYDEAVAQFSKSIEVIENRMAVLN 285
Cdd:PRK02603  83 ASNGEHDKALEYYHQALELNPKQPSALN 110
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 205-309 2.60e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 39.71  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674 205 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAhdrllaetHYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVL 284
Cdd:COG2956   42 VEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEA--------LLELAQDYLKAGLLDRAEELLEKLLELDPDDAEAL 113

                         90       100
                 ....*....|....*....|....*..
gi 530362674 285 NEQVK--EAEGssaEYKKEIEELKELL 309
Cdd:COG2956  114 RLLAEiyEQEG---DWEKAIEVLERLL 137
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 205-291 3.84e-03

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 37.29  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674 205 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAhdrllaetHYQLGLAYGYNSQYDEAVAQFSKSIEVIEN--RMA 282
Cdd:COG4235   51 ADALLDLAEALLAAGDTEEAEELLERALALDPDNPEA--------LYLLGLAAFQQGDYAEAIAAWQKLLALLPAdaPAR 122


                 ....*....
gi 530362674 283 VLNEQVKEA 291
Cdd:COG4235  123 LLEASIAEA 131
TPR_1 pfam00515
Tetratricopeptide repeat;
247-279 5.40e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 34.32  E-value: 5.40e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 530362674  247 AETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEN 279
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPN 33
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 203-272 6.44e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 36.51  E-value: 6.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674 203 YAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQyleahDRLLAETHYQLGLAYGYNSQYDEAVAQFSK 272
Cdd:COG1729   28 LAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPD-----SPKAPDALLKLGLSYLELGDYDKARATLEE 92
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
205-324 7.03e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 38.06  E-value: 7.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362674 205 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYleahdrllAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVL 284
Cdd:COG0457  110 AEALYNLGLALLELGRYDEAIEAYERALELDPDD--------ADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAA 181

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 530362674 285 NEQVKEAEGSSAEYKKEIEELKELLPEIREKIEDAKESQR 324
Cdd:COG0457  182 ALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAE 221
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 247-279 8.51e-03

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 33.96  E-value: 8.51e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 530362674   247 AETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEN 279
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33
 
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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