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Conserved domains on  [gi|966917327|ref|XP_014994060|]
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nuclear autoantigenic sperm protein isoform X5 [Macaca mulatta]

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 ...
 203-240 2.61e-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: 2.61e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 966917327  203 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAH 240
Cdd:pfam10516   1 ADVYDLLGEISLENENFPQAVTDLRKALELREELLPPE 38
TPR_12 pfam13424
Tetratricopeptide repeat;
201-277 2.37e-07

Tetratricopeptide repeat;


:

Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 48.15  E-value: 2.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966917327  201 YAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEK 277
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 143-335 5.65e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327   143 EDDKENDKTEEMPNDSVLENKSLQ-ENEEEEIGNLElawDMLDLAKIifkRQETKEAQlyaaqahlKLGEVSVESENYVQ 221
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDlHKLEEALNDLE---ARLSHSRI---PEIQAELS--------KLEEEVSRIEARLR 815

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327   222 AVEEFQSCLNLQEQYLEAHDRLLAEthyqlglaygYNSQYDEAVAQFSKSIEVIEKRMAVLNEHVKEAEGLSAEY----- 296
Cdd:TIGR02169  816 EIEQKLNRLTLEKEYLEKEIQELQE----------QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLesrlg 885

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 966917327   297 --KKEIEELKELLPEIREKIEDAKESQHSGNVAELALKATL 335
Cdd:TIGR02169  886 dlKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
 
Name Accession Description Interval E-value
SHNi-TPR pfam10516
SHNi-TPR; SHNi-TPR family members contain a reiterated sequence motif that is an interrupted ...
 203-240 2.61e-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: 2.61e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 966917327  203 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAH 240
Cdd:pfam10516   1 ADVYDLLGEISLENENFPQAVTDLRKALELREELLPPE 38
TPR_12 pfam13424
Tetratricopeptide repeat;
201-277 2.37e-07

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 48.15  E-value: 2.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966917327  201 YAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEK 277
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 203-273 3.78e-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: 3.78e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966917327 203 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAhdrllaetHYQLGLAYGYNSQYDEAVAQFSKSIE 273
Cdd:COG3914  146 AEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEA--------LNNLGNALQDLGRLEEAIAAYRRALE 208
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
203-305 1.32e-05

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 46.06  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327 203 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRllaethyqLGLAYGYNSQYDEAVAQFSKSIEVI-EKRMAV 281
Cdd:COG4785  107 AEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLN--------RGIALYYLGRYELAIADLEKALELDpNDPERA 178

                         90       100
                 ....*....|....*....|....
gi 966917327 282 LNEHVKEAEglsAEYKKEIEELKE 305
Cdd:COG4785  179 LWLYLAERK---LDPEKALALLLE 199
PRK02603 PRK02603
photosystem I assembly protein Ycf3; Provisional
 185-283 2.31e-03

photosystem I assembly protein Ycf3; Provisional


Pssm-ID: 179448 [Multi-domain]  Cd Length: 172  Bit Score: 38.88  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327 185 LAKIIFK----RQETKEAQLY-----AAQAHlklGEvsvesenYVQAVEEFQSCLNLQEqylEAHDRllAETHYQLGLAY 255
Cdd:PRK02603  18 MADLILKilpiNKKAKEAFVYyrdgmSAQAD---GE-------YAEALENYEEALKLEE---DPNDR--SYILYNMGIIY 82

                         90       100
                 ....*....|....*....|....*...
gi 966917327 256 GYNSQYDEAVAQFSKSIEVIEKRMAVLN 283
Cdd:PRK02603  83 ASNGEHDKALEYYHQALELNPKQPSALN 110
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 143-335 5.65e-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: 39.28  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327   143 EDDKENDKTEEMPNDSVLENKSLQ-ENEEEEIGNLElawDMLDLAKIifkRQETKEAQlyaaqahlKLGEVSVESENYVQ 221
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDlHKLEEALNDLE---ARLSHSRI---PEIQAELS--------KLEEEVSRIEARLR 815

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327   222 AVEEFQSCLNLQEQYLEAHDRLLAEthyqlglaygYNSQYDEAVAQFSKSIEVIEKRMAVLNEHVKEAEGLSAEY----- 296
Cdd:TIGR02169  816 EIEQKLNRLTLEKEYLEKEIQELQE----------QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLesrlg 885

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 966917327   297 --KKEIEELKELLPEIREKIEDAKESQHSGNVAELALKATL 335
Cdd:TIGR02169  886 dlKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
 
Name Accession Description Interval E-value
SHNi-TPR pfam10516
SHNi-TPR; SHNi-TPR family members contain a reiterated sequence motif that is an interrupted ...
 203-240 2.61e-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: 2.61e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 966917327  203 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAH 240
Cdd:pfam10516   1 ADVYDLLGEISLENENFPQAVTDLRKALELREELLPPE 38
TPR_12 pfam13424
Tetratricopeptide repeat;
201-277 2.37e-07

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 48.15  E-value: 2.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966917327  201 YAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEK 277
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 203-273 3.78e-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: 3.78e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966917327 203 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAhdrllaetHYQLGLAYGYNSQYDEAVAQFSKSIE 273
Cdd:COG3914  146 AEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEA--------LNNLGNALQDLGRLEEAIAAYRRALE 208
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
203-305 1.32e-05

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 46.06  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327 203 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRllaethyqLGLAYGYNSQYDEAVAQFSKSIEVI-EKRMAV 281
Cdd:COG4785  107 AEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLN--------RGIALYYLGRYELAIADLEKALELDpNDPERA 178

                         90       100
                 ....*....|....*....|....
gi 966917327 282 LNEHVKEAEglsAEYKKEIEELKE 305
Cdd:COG4785  179 LWLYLAERK---LDPEKALALLLE 199
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
160-273 4.06e-05

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 44.52  E-value: 4.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327 160 LENKSLQENEEEEIGNLELAWDMLDLAKIIFKRQETKEAQLYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYlea 239
Cdd:COG4785   30 LFAAVLALAIALADLALALAAAALAAAALAAERIDRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDL--- 106

                         90       100       110
                 ....*....|....*....|....*....|....
gi 966917327 240 hdrllAETHYQLGLAYGYNSQYDEAVAQFSKSIE 273
Cdd:COG4785  107 -----AEAYNNRGLAYLLLGDYDAALEDFDRALE 135
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 152-273 3.68e-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: 3.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327 152 EEMPNDSVLENKSLQENEEEEIGNLELAWDMLDLAKIIFKRQETKEA-QLYA---------AQAHLKLGEVSVESENYVQ 221
Cdd:COG3914   51 LAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEAlALYRralalnpdnAEALFNLGNLLLALGRLEE 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 966917327 222 AVEEFQSCLNLQEQYLEAHdrllaethYQLGLAYGYNSQYDEAVAQFSKSIE 273
Cdd:COG3914  131 ALAALRRALALNPDFAEAY--------LNLGEALRRLGRLEEAIAALRRALE 174
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 174-307 7.54e-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: 41.25  E-value: 7.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327 174 GNLELAWDMLDLAKIIFkrQETKEAQLYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHdRLLAETHYQLGl 253
Cdd:COG2956   49 GNLYRRRGEYDRAIRIH--QKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEAL-RLLAEIYEQEG- 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 966917327 254 aygynsQYDEAVAQFSKSIEVIEKRMAVLNEHVKEAEGLSaEYKKEIEELKELL 307
Cdd:COG2956  125 ------DWEKAIEVLERLLKLGPENAHAYCELAELYLEQG-DYDEAIEALEKAL 171
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
203-273 9.45e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 40.76  E-value: 9.45e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966917327 203 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYleahdrllAETHYQLGLAYGYNSQYDEAVAQFSKSIE 273
Cdd:COG0457    8 AEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDD--------AEALYNLGLAYLRLGRYEEALADYEQALE 70
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 177-309 1.52e-03

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: 38.63  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327 177 ELAWDMLDLAKIIFKRQETKEAQLYA----------AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAhdrllae 246
Cdd:COG4783    2 ACAEALYALAQALLLAGDYDEAEALLekaleldpdnPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEA------- 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966917327 247 tHYQLGLAYGYNSQYDEAVAQFSKSIEVIEKRMAVLNE--HVKEAEGLSAEYKKEIEELKELLPE 309
Cdd:COG4783   75 -RLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRlaRAYRALGRPDEAIAALEKALELDPD 138
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
203-273 2.19e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.60  E-value: 2.19e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966917327 203 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYleahdrllAETHYQLGLAYGYNSQYDEAVAQFSKSIE 273
Cdd:COG0457   42 AEALYNLGLAYLRLGRYEEALADYEQALELDPDD--------AEALNNLGLALQALGRYEEALEDYDKALE 104
PRK02603 PRK02603
photosystem I assembly protein Ycf3; Provisional
 185-283 2.31e-03

photosystem I assembly protein Ycf3; Provisional


Pssm-ID: 179448 [Multi-domain]  Cd Length: 172  Bit Score: 38.88  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327 185 LAKIIFK----RQETKEAQLY-----AAQAHlklGEvsvesenYVQAVEEFQSCLNLQEqylEAHDRllAETHYQLGLAY 255
Cdd:PRK02603  18 MADLILKilpiNKKAKEAFVYyrdgmSAQAD---GE-------YAEALENYEEALKLEE---DPNDR--SYILYNMGIIY 82

                         90       100
                 ....*....|....*....|....*...
gi 966917327 256 GYNSQYDEAVAQFSKSIEVIEKRMAVLN 283
Cdd:PRK02603  83 ASNGEHDKALEYYHQALELNPKQPSALN 110
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 143-335 5.65e-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: 39.28  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327   143 EDDKENDKTEEMPNDSVLENKSLQ-ENEEEEIGNLElawDMLDLAKIifkRQETKEAQlyaaqahlKLGEVSVESENYVQ 221
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDlHKLEEALNDLE---ARLSHSRI---PEIQAELS--------KLEEEVSRIEARLR 815

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327   222 AVEEFQSCLNLQEQYLEAHDRLLAEthyqlglaygYNSQYDEAVAQFSKSIEVIEKRMAVLNEHVKEAEGLSAEY----- 296
Cdd:TIGR02169  816 EIEQKLNRLTLEKEYLEKEIQELQE----------QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLesrlg 885

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 966917327   297 --KKEIEELKELLPEIREKIEDAKESQHSGNVAELALKATL 335
Cdd:TIGR02169  886 dlKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 162-274 6.26e-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: 38.56  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327 162 NKSLQENEEEEIGNLELAWD-----MLDLAKIIFKRQETKEAqlYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQY 236
Cdd:COG2956   66 QKLLERDPDRAEALLELAQDylkagLLDRAEELLEKLLELDP--DDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPEN 143

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 966917327 237 leahdrllAETHYQLGLAYGYNSQYDEAVAQFSKSIEV 274
Cdd:COG2956  144 --------AHAYCELAELYLEQGDYDEAIEALEKALKL 173
TPR_1 pfam00515
Tetratricopeptide repeat;
245-274 6.61e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 34.32  E-value: 6.61e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 966917327  245 AETHYQLGLAYGYNSQYDEAVAQFSKSIEV 274
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALEL 30
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 203-307 7.96e-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: 38.17  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327 203 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAhdrllaetHYQLGLAYGYNSQYDEAVAQFSKSIEVIEKRMAVL 282
Cdd:COG2956   42 VEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEA--------LLELAQDYLKAGLLDRAEELLEKLLELDPDDAEAL 113

                         90       100
                 ....*....|....*....|....*..
gi 966917327 283 NE--HVKEAEGlsaEYKKEIEELKELL 307
Cdd:COG2956  114 RLlaEIYEQEG---DWEKAIEVLERLL 137
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 201-270 1.00e-02

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: 35.74  E-value: 1.00e-02
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966917327 201 YAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQyleahDRLLAETHYQLGLAYGYNSQYDEAVAQFSK 270
Cdd:COG1729   28 LAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPD-----SPKAPDALLKLGLSYLELGDYDKARATLEE 92
 
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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