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Conserved domains on  [gi|1952661637|ref|NP_001376546|]
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neuron navigator 1 isoform 9 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PHA03378 super family cl33729
EBNA-3B; Provisional
31-240 3.50e-06

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 52.38  E-value: 3.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637   31 PTPGASPQLRPRQA--GLALSPQRAASPRLGKAAGPSRNSSPRAFRGRGSPKFAGAVRESAEDGEGPFSSPwnsPRTTPK 108
Cdd:PHA03378   676 PSPTGANTMLPIQWapGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARP---PAAAPG 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637  109 AALSSRAGSGRIGERQGTQGKKKKAQ--EGTPVCQTRGR---SPSRTSFHGETQI---PGAPEGRKPPSCPGKDQRDINY 180
Cdd:PHA03378   753 RARPPAAAPGRARPPAAAPGAPTPQPppQAPPAPQQRPRgapTPQPPPQAGPTSMqlmPRAAPGQQGPTKQILRQLLTGG 832
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952661637  181 KSSGTPRSLEPDEGAASWASSPVCSPVQGKRPSPSPGAISFSSVHQQSQ------------PVTATVAPFQY 240
Cdd:PHA03378   833 VKRGRPSLKKPAALERQAAAGPTPSPGSGTSDKIVQAPVFYPPVLQPIQvmrqlgsvraaaASTVTQAPTEY 904
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1366-1450 3.55e-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: 3.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637 1366 QSEQIRKLRRELESSQEKVATLTSQLSANANLVAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKKKNSEAQA 1445
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929

                   ....*
gi 1952661637 1446 VIQGA 1450
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 ...
1812-1949 7.87e-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: 7.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637 1812 KCVDSLVFETL--IPKPMMQHYISL--LLKHRRLVLSGPSGTGKTYLTNRLAEYLVERSGRevtegiVSTFNMHqqsckD 1887
Cdd:NF038214    60 KTLEDFDFTAApgLDKAQIRELATLdfIERAENVLLLGPPGTGKTHLAIALGYAACRQGYR------VRFTTAA-----D 128
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952661637 1888 L--QLYLSNLANQIDRE-TGIGDVPLVIlLDDL-------SEAGSISELVNgaltCKYHKCPYIIgTTNQPV 1949
Cdd:NF038214   129 LveQLAQARADGRLGRLlRRLARYDLLI-IDELgylpfsrEGANLLFELIA----DRYERGSTII-TSNLPF 194
 
Name Accession Description Interval E-value
PHA03378 PHA03378
EBNA-3B; Provisional
31-240 3.50e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 52.38  E-value: 3.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637   31 PTPGASPQLRPRQA--GLALSPQRAASPRLGKAAGPSRNSSPRAFRGRGSPKFAGAVRESAEDGEGPFSSPwnsPRTTPK 108
Cdd:PHA03378   676 PSPTGANTMLPIQWapGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARP---PAAAPG 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637  109 AALSSRAGSGRIGERQGTQGKKKKAQ--EGTPVCQTRGR---SPSRTSFHGETQI---PGAPEGRKPPSCPGKDQRDINY 180
Cdd:PHA03378   753 RARPPAAAPGRARPPAAAPGAPTPQPppQAPPAPQQRPRgapTPQPPPQAGPTSMqlmPRAAPGQQGPTKQILRQLLTGG 832
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952661637  181 KSSGTPRSLEPDEGAASWASSPVCSPVQGKRPSPSPGAISFSSVHQQSQ------------PVTATVAPFQY 240
Cdd:PHA03378   833 VKRGRPSLKKPAALERQAAAGPTPSPGSGTSDKIVQAPVFYPPVLQPIQvmrqlgsvraaaASTVTQAPTEY 904
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1366-1450 3.55e-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: 3.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637 1366 QSEQIRKLRRELESSQEKVATLTSQLSANANLVAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKKKNSEAQA 1445
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929

                   ....*
gi 1952661637 1446 VIQGA 1450
Cdd:TIGR02168  930 RLEGL 934
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
1812-1949 7.87e-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: 7.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637 1812 KCVDSLVFETL--IPKPMMQHYISL--LLKHRRLVLSGPSGTGKTYLTNRLAEYLVERSGRevtegiVSTFNMHqqsckD 1887
Cdd:NF038214    60 KTLEDFDFTAApgLDKAQIRELATLdfIERAENVLLLGPPGTGKTHLAIALGYAACRQGYR------VRFTTAA-----D 128
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952661637 1888 L--QLYLSNLANQIDRE-TGIGDVPLVIlLDDL-------SEAGSISELVNgaltCKYHKCPYIIgTTNQPV 1949
Cdd:NF038214   129 LveQLAQARADGRLGRLlRRLARYDLLI-IDELgylpfsrEGANLLFELIA----DRYERGSTII-TSNLPF 194
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1837-1948 1.46e-04

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: 1.46e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637  1837 KHRRLVLSGPSGTGKTYLTNRLAEYLVERSGREVTegIVSTFNMHQQSCKDLQLYLSNLANQIDRETGIGDV-------- 1908
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAlalarklk 78
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1952661637  1909 PLVILLDDLSEAGS---------ISELVNGALTCKYHKCPyIIGTTNQP 1948
Cdd:smart00382   79 PDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLT-VILTTNDE 126
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
1832-1862 4.84e-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: 4.84e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1952661637 1832 ISLLLKHRRLV-LSGPSGTGKTYLTNRLAEYL 1862
Cdd:COG1401    214 FLAALKTKKNViLAGPPGTGKTYLARRLAEAL 245
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
1841-1948 6.15e-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: 6.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637 1841 LVLSGPSGTGKTYLTNRLAEYLVERSGRevtegiVSTFNMHQqscKDLQLYLSNLANQIDRETGIGDV----PLVILLDd 1916
Cdd:cd00009     22 LLLYGPPGTGKTTLARAIANELFRPGAP------FLYLNASD---LLEGLVVAELFGHFLVRLLFELAekakPGVLFID- 91
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1952661637 1917 lsEAGSISELVNGAL----------TCKYHKCPyIIGTTNQP 1948
Cdd:cd00009     92 --EIDSLSRGAQNALlrvletlndlRIDRENVR-VIGATNRP 130
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1363-1448 9.08e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 9.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637 1363 ERMQsEQIRKLRRELESSQEKVATLTSQLSANANLVAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKKKNSE 1442
Cdd:COG4372     62 EQLE-EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140

                   ....*.
gi 1952661637 1443 AQAVIQ 1448
Cdd:COG4372    141 LQSEIA 146
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
1362-1444 9.33e-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: 41.06  E-value: 9.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637 1362 EERMQS--EQIRKLRRELESSQEKVATLTSQLS---ANANLVAAFEQSLVNMTSRLRHLAE-TAEEKD---TELLDLRET 1432
Cdd:pfam20492   12 EERLKQyeEETKKAQEELEESEETAEELEEERRqaeEEAERLEQKRQEAEEEKERLEESAEmEAEEKEqleAELAEAQEE 91
                           90
                   ....*....|....*.
gi 1952661637 1433 IDFL----KKKNSEAQ 1444
Cdd:pfam20492   92 IARLeeevERKEEEAR 107
AAA_28 pfam13521
AAA domain;
1840-1872 3.13e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 40.33  E-value: 3.13e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1952661637 1840 RLVLSGPSGTGKTYLTNRLAEYL----VERSGREVTE 1872
Cdd:pfam13521    1 RIVITGGPSTGKTTLAEALAARFgypvVPEAAREILE 37
 
Name Accession Description Interval E-value
PHA03378 PHA03378
EBNA-3B; Provisional
31-240 3.50e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 52.38  E-value: 3.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637   31 PTPGASPQLRPRQA--GLALSPQRAASPRLGKAAGPSRNSSPRAFRGRGSPKFAGAVRESAEDGEGPFSSPwnsPRTTPK 108
Cdd:PHA03378   676 PSPTGANTMLPIQWapGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARP---PAAAPG 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637  109 AALSSRAGSGRIGERQGTQGKKKKAQ--EGTPVCQTRGR---SPSRTSFHGETQI---PGAPEGRKPPSCPGKDQRDINY 180
Cdd:PHA03378   753 RARPPAAAPGRARPPAAAPGAPTPQPppQAPPAPQQRPRgapTPQPPPQAGPTSMqlmPRAAPGQQGPTKQILRQLLTGG 832
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952661637  181 KSSGTPRSLEPDEGAASWASSPVCSPVQGKRPSPSPGAISFSSVHQQSQ------------PVTATVAPFQY 240
Cdd:PHA03378   833 VKRGRPSLKKPAALERQAAAGPTPSPGSGTSDKIVQAPVFYPPVLQPIQvmrqlgsvraaaASTVTQAPTEY 904
PHA03247 PHA03247
large tegument protein UL36; Provisional
9-264 1.48e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637    9 PASRPHYASAIPVP---RASSQTRIPTPGASPQLRPRQAGLALSPQRAASPR----LGKAAGPSrnSSPRAFRGRGSPKF 81
Cdd:PHA03247  2614 PSPLPPDTHAPDPPppsPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRrarrLGRAAQAS--SPPQRPRRRAARPT 2691
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637   82 AGAVRESAeDGEGPFSSPWNSPR-TTPKAALSSRAGSGRIGERQGTQGKKKKAQEGTPVCQTRGRSPSRtsfhgeTQIPG 160
Cdd:PHA03247  2692 VGSLTSLA-DPPPPPPTPEPAPHaLVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPAR------PPTTA 2764
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637  161 APEGRKPPSCPgkdqrdinykSSGTPRSLEPDEGAASWASSPVCSPVQGKRPSPSPGAISFSSVHQQSQPVTATVAPFQY 240
Cdd:PHA03247  2765 GPPAPAPPAAP----------AAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSA 2834
                          250       260
                   ....*....|....*....|....
gi 1952661637  241 RLQTDQKPGPLSQGSWPLDGYAEP 264
Cdd:PHA03247  2835 QPTAPPPPPGPPPPSLPLGGSVAP 2858
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1366-1450 3.55e-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: 3.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637 1366 QSEQIRKLRRELESSQEKVATLTSQLSANANLVAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKKKNSEAQA 1445
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929

                   ....*
gi 1952661637 1446 VIQGA 1450
Cdd:TIGR02168  930 RLEGL 934
PHA03247 PHA03247
large tegument protein UL36; Provisional
9-264 4.12e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 4.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637    9 PASRPH-YASAIPVPRASSQTR--IPTPGASPQLRPRQAGLALSPQRAASPRLGKAAGPSRNSSPRAFRGRGSPKFAGAV 85
Cdd:PHA03247  2708 PEPAPHaLVSATPLPPGPAAARqaSPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPA 2787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637   86 RESAEDGEGPFSSPWNSprTTPKAALSSRAGSGRIGERQGTQGKKKKAQEGTPVCQTRGRSPSRTSFHGETqIPGAPEGR 165
Cdd:PHA03247  2788 VASLSESRESLPSPWDP--ADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV-APGGDVRR 2864
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637  166 KPPSCPgkdqrdinykssgtprslepdegAASWASSPVCSPVQG-KRPSPSPGAISFSSVHQQSQPVTATVAPFQYRLQT 244
Cdd:PHA03247  2865 RPPSRS-----------------------PAAKPAAPARPPVRRlARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP 2921
                          250       260
                   ....*....|....*....|
gi 1952661637  245 DQKPGPLSQGSWPLDGYAEP 264
Cdd:PHA03247  2922 QPPPPPQPQPPPPPPPRPQP 2941
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
1812-1949 7.87e-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: 7.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637 1812 KCVDSLVFETL--IPKPMMQHYISL--LLKHRRLVLSGPSGTGKTYLTNRLAEYLVERSGRevtegiVSTFNMHqqsckD 1887
Cdd:NF038214    60 KTLEDFDFTAApgLDKAQIRELATLdfIERAENVLLLGPPGTGKTHLAIALGYAACRQGYR------VRFTTAA-----D 128
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952661637 1888 L--QLYLSNLANQIDRE-TGIGDVPLVIlLDDL-------SEAGSISELVNgaltCKYHKCPYIIgTTNQPV 1949
Cdd:NF038214   129 LveQLAQARADGRLGRLlRRLARYDLLI-IDELgylpfsrEGANLLFELIA----DRYERGSTII-TSNLPF 194
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1837-1948 1.46e-04

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: 1.46e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637  1837 KHRRLVLSGPSGTGKTYLTNRLAEYLVERSGREVTegIVSTFNMHQQSCKDLQLYLSNLANQIDRETGIGDV-------- 1908
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAlalarklk 78
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1952661637  1909 PLVILLDDLSEAGS---------ISELVNGALTCKYHKCPyIIGTTNQP 1948
Cdd:smart00382   79 PDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLT-VILTTNDE 126
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
11-269 1.81e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.79  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637   11 SRPHYASAIPVPRASSQTRIPTPgASPQLRPRQAGLALSPQRAASPRlGKAAGPSRNSSPRAfrgrgspkFAGAVRESAE 90
Cdd:PRK12323   372 AGPATAAAAPVAQPAPAAAAPAA-AAPAPAAPPAAPAAAPAAAAAAR-AVAAAPARRSPAPE--------ALAAARQASA 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637   91 DGEGPFSSPWNSPRTTPKAAlssragsgrigERQGTQGKKKKAQEGTPVcqTRGRSPSRTSFHGETQIPGAPEGRKPPSC 170
Cdd:PRK12323   442 RGPGGAPAPAPAPAAAPAAA-----------ARPAAAGPRPVAAAAAAA--PARAAPAAAPAPADDDPPPWEELPPEFAS 508
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637  171 PGKDQRDINYKSSGTPRSLEPDEGAASWASSPvcspvqgkrPSPSPGAISFSSVHQQSQPVTATVAPFQYRLQTDqkpgP 250
Cdd:PRK12323   509 PAPAQPDAAPAGWVAESIPDPATADPDDAFET---------LAPAPAAAPAPRAAAATEPVVAPRPPRASASGLP----D 575
                          250       260
                   ....*....|....*....|....*..
gi 1952661637  251 LSQGSW-------PLDGYAEPL-HETE 269
Cdd:PRK12323   576 MFDGDWpalaarlPVRGLAQQLaRQSE 602
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
9-257 2.83e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 2.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637    9 PASRPHYASAIPVPRASSQT----------RIPTPGASPQLRPRQAGLALSPQRAASPRLGKAAGPSRNSSPRAFRGRGS 78
Cdd:PHA03307   166 AASSRQAALPLSSPEETARApssppaepppSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESS 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637   79 PKFAGAVRESAEDGEGPFSSP--------WNSPRTTPKAALSSRAGSGRIGERQGTQGKKKKAQEGTPVCQTRGR----- 145
Cdd:PHA03307   246 GCGWGPENECPLPRPAPITLPtriweasgWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSsress 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637  146 --SPSRTSFHGETQI--PGAPEGRKPPSCPGKDQRDinykSSGTPRSLEPDEGAASWASSPVCSPVQGKRPSPSPGAI-- 219
Cdd:PHA03307   326 ssSTSSSSESSRGAAvsPGPSPSRSPSPSRPPPPAD----PSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARrr 401
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1952661637  220 --SFSSVHQQSQPVTATVAPFQYRLQTDQKPGPLSQGSWP 257
Cdd:PHA03307   402 daTGRFPAGRPRPSPLDAGAASGAFYARYPLLTPSGEPWP 441
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
1832-1862 4.84e-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: 4.84e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1952661637 1832 ISLLLKHRRLV-LSGPSGTGKTYLTNRLAEYL 1862
Cdd:COG1401    214 FLAALKTKKNViLAGPPGTGKTYLARRLAEAL 245
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
1841-1948 6.15e-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: 6.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637 1841 LVLSGPSGTGKTYLTNRLAEYLVERSGRevtegiVSTFNMHQqscKDLQLYLSNLANQIDRETGIGDV----PLVILLDd 1916
Cdd:cd00009     22 LLLYGPPGTGKTTLARAIANELFRPGAP------FLYLNASD---LLEGLVVAELFGHFLVRLLFELAekakPGVLFID- 91
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1952661637 1917 lsEAGSISELVNGAL----------TCKYHKCPyIIGTTNQP 1948
Cdd:cd00009     92 --EIDSLSRGAQNALlrvletlndlRIDRENVR-VIGATNRP 130
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1363-1448 9.08e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 9.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637 1363 ERMQsEQIRKLRRELESSQEKVATLTSQLSANANLVAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKKKNSE 1442
Cdd:COG4372     62 EQLE-EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140

                   ....*.
gi 1952661637 1443 AQAVIQ 1448
Cdd:COG4372    141 LQSEIA 146
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
1362-1444 9.33e-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: 41.06  E-value: 9.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637 1362 EERMQS--EQIRKLRRELESSQEKVATLTSQLS---ANANLVAAFEQSLVNMTSRLRHLAE-TAEEKD---TELLDLRET 1432
Cdd:pfam20492   12 EERLKQyeEETKKAQEELEESEETAEELEEERRqaeEEAERLEQKRQEAEEEKERLEESAEmEAEEKEqleAELAEAQEE 91
                           90
                   ....*....|....*.
gi 1952661637 1433 IDFL----KKKNSEAQ 1444
Cdd:pfam20492   92 IARLeeevERKEEEAR 107
PHA03247 PHA03247
large tegument protein UL36; Provisional
24-220 1.46e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637   24 ASSQTRIPTPGASPQLRPRQAGLALSPQRAAsPRLGKAAGPSRNSSPRAFRGRGSPKFAGAVRESAEDGEGPFSSPWNSP 103
Cdd:PHA03247  2544 ASDDAGDPPPPLPPAAPPAAPDRSVPPPRPA-PRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTH 2622
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637  104 RTTPKAALSSRAGSgrigerqgTQGKKKKAQEGTPVCQTRGRSPSRTSFHGETQIPG-APEGRKPPSCPgkdqrdinyks 182
Cdd:PHA03247  2623 APDPPPPSPSPAAN--------EPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGrAAQASSPPQRP----------- 2683
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1952661637  183 sgTPRSLEPDEGAASWASSPvcsPVQGKRPSPSPGAIS 220
Cdd:PHA03247  2684 --RRRAARPTVGSLTSLADP---PPPPPTPEPAPHALV 2716
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1368-1466 1.50e-03

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: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637 1368 EQIRKLRRELESSQEKVATLTSQLSANANL---------VAAFEQSLVNMTSRLRHLAETAEEKDTELLDLRETIDFLKK 1438
Cdd:COG1579     59 KEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
                           90       100
                   ....*....|....*....|....*...
gi 1952661637 1439 KNSEAQAVIQGALNASETTPKELRIKRQ 1466
Cdd:COG1579    139 ELEEKKAELDEELAELEAELEELEAERE 166
AAA_28 pfam13521
AAA domain;
1840-1872 3.13e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 40.33  E-value: 3.13e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1952661637 1840 RLVLSGPSGTGKTYLTNRLAEYL----VERSGREVTE 1872
Cdd:pfam13521    1 RIVITGGPSTGKTTLAEALAARFgypvVPEAAREILE 37
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1367-1462 5.33e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 5.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637 1367 SEQIRKLRRELESSQEKVATLTSQLSANANL--VAAFEQSLVNMTSRLRHLaetaEEKDTELLDLRETIDFLKKKNSEAQ 1444
Cdd:COG4717    101 EEELEELEAELEELREELEKLEKLLQLLPLYqeLEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQ 176
                           90
                   ....*....|....*....
gi 1952661637 1445 AVIQGALN-ASETTPKELR 1462
Cdd:COG4717    177 EELEELLEqLSLATEEELQ 195
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
20-229 9.41e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 9.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637   20 PVPRASSQTRIPTP--GASPQLRPRQAGLALSP---QRAASPRLGKAAGPSRNSSPRAFRGR--------GSPKFAGAVR 86
Cdd:PHA03307    22 PRPPATPGDAADDLlsGSQGQLVSDSAELAAVTvvaGAAACDRFEPPTGPPPGPGTEAPANEsrstptwsLSTLAPASPA 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952661637   87 ESAEDGEGPFSSPWNSPRTTPKAALSSRAGSGRIGERQGTQG---KKKKAQEGTPVCQTRGRSPSRTSFHGETQIPGAPE 163
Cdd:PHA03307   102 REGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSpgpPPAASPPAAGASPAAVASDAASSRQAALPLSSPEE 181
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952661637  164 GRKPPSCPGKDQRDINYKSSGTPRSLEPDEGAASWASSPvcSPVQGKRPSPSPGAISFSSVHQQSQ 229
Cdd:PHA03307   182 TARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSP--APAPGRSAADDAGASSSDSSSSESS 245
 
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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