NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568908641|ref|XP_006529443|]
View 

neuron navigator 1 isoform X13 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 683-767 2.32e-05

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: 49.28  E-value: 2.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641   683 QSEQIRKLRRELESSQEKVATLTSQLSANANLVAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKKKNSEAQA 762
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929


                   ....*
gi 568908641   763 VIQGA 767
Cdd:TIGR02168  930 RLEGL 934
IS21_help_AAA super family cl41901
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 1113-1266 2.38e-05

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


The actual alignment was detected with superfamily member NF038214:

Pssm-ID: 439516  Cd Length: 232  Bit Score: 47.47  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641 1113 RRGVNNISVALK--GLK-EKCVDSLVFETL--IPKPMMQHYISL--LLKHRRLVLSGPSGTGKTYLTNRLAEYLVERSGR 1185
Cdd:NF038214   41 ERENRRIERRLKraRFPaAKTLEDFDFTAApgLDKAQIRELATLdfIERAENVLLLGPPGTGKTHLAIALGYAACRQGYR 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641 1186 evtdgiVSTFNMHqqsckDL--QLYLSNLANQIDRE-TGIGDVPLVIlLDDL-------SEAGSISELVNgaltCKYHKC 1255
Cdd:NF038214  121 ------VRFTTAA-----DLveQLAQARADGRLGRLlRRLARYDLLI-IDELgylpfsrEGANLLFELIA----DRYERG 184

                         170
                  ....*....|.
gi 568908641 1256 PYIIgTTNQPV 1266
Cdd:NF038214  185 STII-TSNLPF 194
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 683-767 2.32e-05

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: 49.28  E-value: 2.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641   683 QSEQIRKLRRELESSQEKVATLTSQLSANANLVAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKKKNSEAQA 762
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929


                   ....*
gi 568908641   763 VIQGA 767
Cdd:TIGR02168  930 RLEGL 934
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 1113-1266 2.38e-05

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 47.47  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641 1113 RRGVNNISVALK--GLK-EKCVDSLVFETL--IPKPMMQHYISL--LLKHRRLVLSGPSGTGKTYLTNRLAEYLVERSGR 1185
Cdd:NF038214   41 ERENRRIERRLKraRFPaAKTLEDFDFTAApgLDKAQIRELATLdfIERAENVLLLGPPGTGKTHLAIALGYAACRQGYR 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641 1186 evtdgiVSTFNMHqqsckDL--QLYLSNLANQIDRE-TGIGDVPLVIlLDDL-------SEAGSISELVNgaltCKYHKC 1255
Cdd:NF038214  121 ------VRFTTAA-----DLveQLAQARADGRLGRLlRRLARYDLLI-IDELgylpfsrEGANLLFELIA----DRYERG 184

                         170
                  ....*....|.
gi 568908641 1256 PYIIgTTNQPV 1266
Cdd:NF038214  185 STII-TSNLPF 194
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 1154-1265 9.82e-05

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 44.29  E-value: 9.82e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641   1154 KHRRLVLSGPSGTGKTYLTNRLAEYLVERSGREVTdgIVSTFNMHQQSCKDLQLYLSNLANQIDRETGIGDV-------- 1225
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAlalarklk 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 568908641   1226 PLVILLDDLSEAGS---------ISELVNGALTCKYHKCPyIIGTTNQP 1265
Cdd:smart00382   79 PDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLT-VILTTNDE 126
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1149-1179 3.19e-04

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 45.15  E-value: 3.19e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568908641 1149 ISLLLKHRRLV-LSGPSGTGKTYLTNRLAEYL 1179
Cdd:COG1401   214 FLAALKTKKNViLAGPPGTGKTYLARRLAEAL 245
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 679-773 3.77e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.83  E-value: 3.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641   679 EERMQS--EQIRKLRRELESSQEKVATLTSQLS---ANANLVAAFEQSLVNMTSRLRHLAE-TAEEKD---TELLDLRET 749
Cdd:pfam20492   12 EERLKQyeEETKKAQEELEESEETAEELEEERRqaeEEAERLEQKRQEAEEEKERLEESAEmEAEEKEqleAELAEAQEE 91

                           90       100
                   ....*....|....*....|....*...
gi 568908641   750 IDFL----KKKNSEAQAVIQGALNASEA 773
Cdd:pfam20492   92 IARLeeevERKEEEARRLQEELEEAREE 119
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 685-783 3.86e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.76  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641  685 EQIRKLRRELESSQEKVATLTSQLSANANL---------VAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKK 755
Cdd:COG1579    59 KEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138

                          90       100
                  ....*....|....*....|....*...
gi 568908641  756 KNSEAQAVIQGALNASEATPKELRIKRQ 783
Cdd:COG1579   139 ELEEKKAELDEELAELEAELEELEAERE 166
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 1158-1265 4.13e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 42.52  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641 1158 LVLSGPSGTGKTYLTNRLAEYLVERSGRevtdgiVSTFNMHQqscKDLQLYLSNLANQIDRETGIGDV----PLVILLDd 1233
Cdd:cd00009    22 LLLYGPPGTGKTTLARAIANELFRPGAP------FLYLNASD---LLEGLVVAELFGHFLVRLLFELAekakPGVLFID- 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568908641 1234 lsEAGSISELVNGAL----------TCKYHKCPyIIGTTNQP 1265
Cdd:cd00009    92 --EIDSLSRGAQNALlrvletlndlRIDRENVR-VIGATNRP 130
AAA_28 pfam13521
AAA domain;
1157-1189 3.65e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 39.94  E-value: 3.65e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568908641  1157 RLVLSGPSGTGKTYLTNRLAEYL----VERSGREVTD 1189
Cdd:pfam13521    1 RIVITGGPSTGKTTLAEALAARFgypvVPEAAREILE 37
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 683-767 2.32e-05

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: 49.28  E-value: 2.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641   683 QSEQIRKLRRELESSQEKVATLTSQLSANANLVAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKKKNSEAQA 762
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929


                   ....*
gi 568908641   763 VIQGA 767
Cdd:TIGR02168  930 RLEGL 934
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 1113-1266 2.38e-05

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 47.47  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641 1113 RRGVNNISVALK--GLK-EKCVDSLVFETL--IPKPMMQHYISL--LLKHRRLVLSGPSGTGKTYLTNRLAEYLVERSGR 1185
Cdd:NF038214   41 ERENRRIERRLKraRFPaAKTLEDFDFTAApgLDKAQIRELATLdfIERAENVLLLGPPGTGKTHLAIALGYAACRQGYR 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641 1186 evtdgiVSTFNMHqqsckDL--QLYLSNLANQIDRE-TGIGDVPLVIlLDDL-------SEAGSISELVNgaltCKYHKC 1255
Cdd:NF038214  121 ------VRFTTAA-----DLveQLAQARADGRLGRLlRRLARYDLLI-IDELgylpfsrEGANLLFELIA----DRYERG 184

                         170
                  ....*....|.
gi 568908641 1256 PYIIgTTNQPV 1266
Cdd:NF038214  185 STII-TSNLPF 194
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 1154-1265 9.82e-05

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 44.29  E-value: 9.82e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641   1154 KHRRLVLSGPSGTGKTYLTNRLAEYLVERSGREVTdgIVSTFNMHQQSCKDLQLYLSNLANQIDRETGIGDV-------- 1225
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAlalarklk 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 568908641   1226 PLVILLDDLSEAGS---------ISELVNGALTCKYHKCPyIIGTTNQP 1265
Cdd:smart00382   79 PDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLT-VILTTNDE 126
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1149-1179 3.19e-04

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 45.15  E-value: 3.19e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568908641 1149 ISLLLKHRRLV-LSGPSGTGKTYLTNRLAEYL 1179
Cdd:COG1401   214 FLAALKTKKNViLAGPPGTGKTYLARRLAEAL 245
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 679-773 3.77e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.83  E-value: 3.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641   679 EERMQS--EQIRKLRRELESSQEKVATLTSQLS---ANANLVAAFEQSLVNMTSRLRHLAE-TAEEKD---TELLDLRET 749
Cdd:pfam20492   12 EERLKQyeEETKKAQEELEESEETAEELEEERRqaeEEAERLEQKRQEAEEEKERLEESAEmEAEEKEqleAELAEAQEE 91

                           90       100
                   ....*....|....*....|....*...
gi 568908641   750 IDFL----KKKNSEAQAVIQGALNASEA 773
Cdd:pfam20492   92 IARLeeevERKEEEARRLQEELEEAREE 119
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 685-783 3.86e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.76  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641  685 EQIRKLRRELESSQEKVATLTSQLSANANL---------VAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKK 755
Cdd:COG1579    59 KEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138

                          90       100
                  ....*....|....*....|....*...
gi 568908641  756 KNSEAQAVIQGALNASEATPKELRIKRQ 783
Cdd:COG1579   139 ELEEKKAELDEELAELEAELEELEAERE 166
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 1158-1265 4.13e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 42.52  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641 1158 LVLSGPSGTGKTYLTNRLAEYLVERSGRevtdgiVSTFNMHQqscKDLQLYLSNLANQIDRETGIGDV----PLVILLDd 1233
Cdd:cd00009    22 LLLYGPPGTGKTTLARAIANELFRPGAP------FLYLNASD---LLEGLVVAELFGHFLVRLLFELAekakPGVLFID- 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568908641 1234 lsEAGSISELVNGAL----------TCKYHKCPyIIGTTNQP 1265
Cdd:cd00009    92 --EIDSLSRGAQNALlrvletlndlRIDRENVR-VIGATNRP 130
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
680-783 5.95e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 5.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641  680 ERMQsEQIRKLRRELESSQEKVATLTSQLSANANLVAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETidflKKKNSE 759
Cdd:COG4372    62 EQLE-EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ----RKQLEA 136

                          90       100
                  ....*....|....*....|....
gi 568908641  760 AQAVIQGALNASEATPKELRIKRQ 783
Cdd:COG4372   137 QIAELQSEIAEREEELKELEEQLE 160
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
684-779 1.89e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641  684 SEQIRKLRRELESSQEKVATLTSQLSANANL--VAAFEQSLVNMTSRLRHLaetaEEKDTELLDLRETIDFLKKKNSEAQ 761
Cdd:COG4717   101 EEELEELEAELEELREELEKLEKLLQLLPLYqeLEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQ 176

                          90
                  ....*....|....*....
gi 568908641  762 AVIQGALN-ASEATPKELR 779
Cdd:COG4717   177 EELEELLEqLSLATEEELQ 195
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
1151-1259 2.74e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 42.48  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641 1151 LLLKHRRLVLSGPSGTGKTYLTNRLAEYLVERsGREVTDGIV---------STFNMHQQSCKDLQLYLSNLANQIDR--E 1219
Cdd:COG5635   176 LEAKKKRLLILGEPGSGKTTLLRYLALELAER-YLDAEDPIPilielrdlaEEASLEDLLAEALEKRGGEPEDALERllR 254

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568908641 1220 TGigdvPLVILLDDL---SEAGSISELVN--GALTCKYHKCPYII 1259
Cdd:COG5635   255 NG----RLLLLLDGLdevPDEADRDEVLNqlRRFLERYPKARVII 295
AAA_28 pfam13521
AAA domain;
1157-1189 3.65e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 39.94  E-value: 3.65e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568908641  1157 RLVLSGPSGTGKTYLTNRLAEYL----VERSGREVTD 1189
Cdd:pfam13521    1 RIVITGGPSTGKTTLAEALAARFgypvVPEAAREILE 37
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
1129-1267 8.72e-03

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.76  E-value: 8.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908641 1129 KCVDSLVFETL--IPKPMMQHYISL--LLKHRRLVLSGPSGTGKTYLTNRLAEYLVERsgrevtdGI-VSTFNMHqqsck 1203
Cdd:COG1484    69 KTLEDFDFDAQpgLDRRQILELATLdfIERGENLILLGPPGTGKTHLAIALGHEACRA-------GYrVRFTTAP----- 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568908641 1204 DL--QLYLSNLANQIDRE-TGIGDVPLVIlLDDL-----SEAGS------ISELvngaltckYHKCPYIIgTTNQPVK 1267
Cdd:COG1484   137 DLvnELKEARADGRLERLlKRLAKVDLLI-LDELgylplDAEGAellfelISDR--------YERRSTII-TSNLPFS 204
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH