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Conserved domains on  [gi|1952662932|ref|NP_001376542|]
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neuron navigator 1 isoform 5 [Homo sapiens]

Protein Classification

Graphical summary

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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 ...
 631-715 2.23e-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: 2.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932  631 QSEQIRKLRRELESSQEKVATLTSQLSANANLVAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKKKNSEAQA 710
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929


                   ....*
gi 1952662932  711 VIQGA 715
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 ...
 1077-1214 5.03e-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: 46.31  E-value: 5.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932 1077 KCVDSLVFETL--IPKPMMQHYISL--LLKHRRLVLSGPSGTGKTYLTNRLAEYLVERSGRevtegiVSTFNMHqqsckD 1152
Cdd:NF038214    60 KTLEDFDFTAApgLDKAQIRELATLdfIERAENVLLLGPPGTGKTHLAIALGYAACRQGYR------VRFTTAA-----D 128

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952662932 1153 L--QLYLSNLANQIDRE-TGIGDVPLVIlLDDL-------SEAGSISELVNgaltCKYHKCPYIIgTTNQPV 1214
Cdd:NF038214   129 LveQLAQARADGRLGRLlRRLARYDLLI-IDELgylpfsrEGANLLFELIA----DRYERGSTII-TSNLPF 194
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 631-715 2.23e-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: 2.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932  631 QSEQIRKLRRELESSQEKVATLTSQLSANANLVAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKKKNSEAQA 710
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929


                   ....*
gi 1952662932  711 VIQGA 715
Cdd:TIGR02168  930 RLEGL 934
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 1077-1214 5.03e-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: 46.31  E-value: 5.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932 1077 KCVDSLVFETL--IPKPMMQHYISL--LLKHRRLVLSGPSGTGKTYLTNRLAEYLVERSGRevtegiVSTFNMHqqsckD 1152
Cdd:NF038214    60 KTLEDFDFTAApgLDKAQIRELATLdfIERAENVLLLGPPGTGKTHLAIALGYAACRQGYR------VRFTTAA-----D 128

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952662932 1153 L--QLYLSNLANQIDRE-TGIGDVPLVIlLDDL-------SEAGSISELVNgaltCKYHKCPYIIgTTNQPV 1214
Cdd:NF038214   129 LveQLAQARADGRLGRLlRRLARYDLLI-IDELgylpfsrEGANLLFELIA----DRYERGSTII-TSNLPF 194
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 1102-1213 9.45e-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: 9.45e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932  1102 KHRRLVLSGPSGTGKTYLTNRLAEYLVERSGREVTegIVSTFNMHQQSCKDLQLYLSNLANQIDRETGIGDV-------- 1173
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAlalarklk 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1952662932  1174 PLVILLDDLSEAGS---------ISELVNGALTCKYHKCPyIIGTTNQP 1213
Cdd:smart00382   79 PDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLT-VILTTNDE 126
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1097-1127 3.06e-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: 3.06e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1952662932 1097 ISLLLKHRRLV-LSGPSGTGKTYLTNRLAEYL 1127
Cdd:COG1401    214 FLAALKTKKNViLAGPPGTGKTYLARRLAEAL 245
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 1106-1213 3.98e-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: 3.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932 1106 LVLSGPSGTGKTYLTNRLAEYLVERSGRevtegiVSTFNMHQqscKDLQLYLSNLANQIDRETGIGDV----PLVILLDd 1181
Cdd:cd00009     22 LLLYGPPGTGKTTLARAIANELFRPGAP------FLYLNASD---LLEGLVVAELFGHFLVRLLFELAekakPGVLFID- 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1952662932 1182 lsEAGSISELVNGAL----------TCKYHKCPyIIGTTNQP 1213
Cdd:cd00009     92 --EIDSLSRGAQNALlrvletlndlRIDRENVR-VIGATNRP 130
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 627-709 5.05e-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: 41.44  E-value: 5.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932  627 EERMQS--EQIRKLRRELESSQEKVATLTSQLS---ANANLVAAFEQSLVNMTSRLRHLAE-TAEEKD---TELLDLRET 697
Cdd:pfam20492   12 EERLKQyeEETKKAQEELEESEETAEELEEERRqaeEEAERLEQKRQEAEEEKERLEESAEmEAEEKEqleAELAEAQEE 91

                           90
                   ....*....|....*.
gi 1952662932  698 IDFL----KKKNSEAQ 709
Cdd:pfam20492   92 IARLeeevERKEEEAR 107
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
628-713 5.77e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 5.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932  628 ERMQsEQIRKLRRELESSQEKVATLTSQLSANANLVAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKKKNSE 707
Cdd:COG4372     62 EQLE-EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140


                   ....*.
gi 1952662932  708 AQAVIQ 713
Cdd:COG4372    141 LQSEIA 146
AAA_28 pfam13521
AAA domain;
1105-1137 2.02e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 40.33  E-value: 2.02e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1952662932 1105 RLVLSGPSGTGKTYLTNRLAEYL----VERSGREVTE 1137
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 ...
 631-715 2.23e-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: 2.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932  631 QSEQIRKLRRELESSQEKVATLTSQLSANANLVAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKKKNSEAQA 710
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929


                   ....*
gi 1952662932  711 VIQGA 715
Cdd:TIGR02168  930 RLEGL 934
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 1077-1214 5.03e-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: 46.31  E-value: 5.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932 1077 KCVDSLVFETL--IPKPMMQHYISL--LLKHRRLVLSGPSGTGKTYLTNRLAEYLVERSGRevtegiVSTFNMHqqsckD 1152
Cdd:NF038214    60 KTLEDFDFTAApgLDKAQIRELATLdfIERAENVLLLGPPGTGKTHLAIALGYAACRQGYR------VRFTTAA-----D 128

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952662932 1153 L--QLYLSNLANQIDRE-TGIGDVPLVIlLDDL-------SEAGSISELVNgaltCKYHKCPYIIgTTNQPV 1214
Cdd:NF038214   129 LveQLAQARADGRLGRLlRRLARYDLLI-IDELgylpfsrEGANLLFELIA----DRYERGSTII-TSNLPF 194
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 1102-1213 9.45e-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: 9.45e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932  1102 KHRRLVLSGPSGTGKTYLTNRLAEYLVERSGREVTegIVSTFNMHQQSCKDLQLYLSNLANQIDRETGIGDV-------- 1173
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAlalarklk 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1952662932  1174 PLVILLDDLSEAGS---------ISELVNGALTCKYHKCPyIIGTTNQP 1213
Cdd:smart00382   79 PDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLT-VILTTNDE 126
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1097-1127 3.06e-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: 3.06e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1952662932 1097 ISLLLKHRRLV-LSGPSGTGKTYLTNRLAEYL 1127
Cdd:COG1401    214 FLAALKTKKNViLAGPPGTGKTYLARRLAEAL 245
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 1106-1213 3.98e-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: 3.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932 1106 LVLSGPSGTGKTYLTNRLAEYLVERSGRevtegiVSTFNMHQqscKDLQLYLSNLANQIDRETGIGDV----PLVILLDd 1181
Cdd:cd00009     22 LLLYGPPGTGKTTLARAIANELFRPGAP------FLYLNASD---LLEGLVVAELFGHFLVRLLFELAekakPGVLFID- 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1952662932 1182 lsEAGSISELVNGAL----------TCKYHKCPyIIGTTNQP 1213
Cdd:cd00009     92 --EIDSLSRGAQNALlrvletlndlRIDRENVR-VIGATNRP 130
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 627-709 5.05e-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: 41.44  E-value: 5.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932  627 EERMQS--EQIRKLRRELESSQEKVATLTSQLS---ANANLVAAFEQSLVNMTSRLRHLAE-TAEEKD---TELLDLRET 697
Cdd:pfam20492   12 EERLKQyeEETKKAQEELEESEETAEELEEERRqaeEEAERLEQKRQEAEEEKERLEESAEmEAEEKEqleAELAEAQEE 91

                           90
                   ....*....|....*.
gi 1952662932  698 IDFL----KKKNSEAQ 709
Cdd:pfam20492   92 IARLeeevERKEEEAR 107
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
628-713 5.77e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 5.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932  628 ERMQsEQIRKLRRELESSQEKVATLTSQLSANANLVAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKKKNSE 707
Cdd:COG4372     62 EQLE-EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140


                   ....*.
gi 1952662932  708 AQAVIQ 713
Cdd:COG4372    141 LQSEIA 146
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 633-731 9.61e-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: 42.60  E-value: 9.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932  633 EQIRKLRRELESSQEKVATLTSQLSANANL---------VAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKK 703
Cdd:COG1579     59 KEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138

                           90       100
                   ....*....|....*....|....*...
gi 1952662932  704 KNSEAQAVIQGALNASETTPKELRIKRQ 731
Cdd:COG1579    139 ELEEKKAELDEELAELEAELEELEAERE 166
AAA_28 pfam13521
AAA domain;
1105-1137 2.02e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 40.33  E-value: 2.02e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1952662932 1105 RLVLSGPSGTGKTYLTNRLAEYL----VERSGREVTE 1137
Cdd:pfam13521    1 RIVITGGPSTGKTTLAEALAARFgypvVPEAAREILE 37
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
632-727 3.38e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932  632 SEQIRKLRRELESSQEKVATLTSQLSANANL--VAAFEQSLVNMTSRLRHLaetaEEKDTELLDLRETIDFLKKKNSEAQ 709
Cdd:COG4717    101 EEELEELEAELEELREELEKLEKLLQLLPLYqeLEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQ 176

                           90
                   ....*....|....*....
gi 1952662932  710 AVIQGALN-ASETTPKELR 727
Cdd:COG4717    177 EELEELLEqLSLATEEELQ 195
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 1104-1137 7.51e-03

Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 442405 [Multi-domain]  Cd Length: 178  Bit Score: 39.03  E-value: 7.51e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1952662932 1104 RRLVLSGPSGTGKTYLTNRLAEYL----VERSGREVTE 1137
Cdd:COG3172      9 KKIVLLGAESTGKTTLARALAAHYntpwVPEYGREYLE 46
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
1077-1215 8.38e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.76  E-value: 8.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662932 1077 KCVDSLVFETL--IPKPMMQHYISL--LLKHRRLVLSGPSGTGKTYLTNRLAEYLVERsgrevteGI-VSTFNMHqqsck 1151
Cdd:COG1484     69 KTLEDFDFDAQpgLDRRQILELATLdfIERGENLILLGPPGTGKTHLAIALGHEACRA-------GYrVRFTTAP----- 136

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952662932 1152 DL--QLYLSNLANQIDRE-TGIGDVPLVIlLDDL-----SEAGS------ISELvngaltckYHKCPYIIgTTNQPVK 1215
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.
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