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Conserved domains on  [gi|446496653|ref|WP_000574507|]
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FtsK/SpoIIIE domain-containing protein, partial [Streptococcus mitis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
T7_EssCb_Firm super family cl37349
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 1-173 2.69e-80

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


The actual alignment was detected with superfamily member TIGR03928:

Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 258.38  E-value: 2.69e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653     1 KDGHVLLYGSPGTGKTTFLQTAGMDLARKFSPKALTMYLMDFGTNGLAPLSKLPQVADTMLLDQAEKISKFVRIMERELN 80
Cdd:TIGR03928  809 KDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPHVADYFTLDEEEKIEKLIRRIKKEID 888

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653    81 RRKKLLADYGVGTLELYREASGQQEPAIVILLDSYEAIKEEAYEAELFKLLVRISREGLSIGVHLLMTASRQSNLRAQLY 160
Cdd:TIGR03928  889 RRKKLFSEYGVASISMYNKASGEKLPQIVIIIDNYDAVKEEPFYEDFEELLIQLAREGASLGIYLVMTAGRQNAVRMPLM 968

                          170
                   ....*....|...
gi 446496653   161 SNFKHQLSLPQND 173
Cdd:TIGR03928  969 NNIKTKIALYLID 981
 
Name Accession Description Interval E-value
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 1-173 2.69e-80

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 258.38  E-value: 2.69e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653     1 KDGHVLLYGSPGTGKTTFLQTAGMDLARKFSPKALTMYLMDFGTNGLAPLSKLPQVADTMLLDQAEKISKFVRIMERELN 80
Cdd:TIGR03928  809 KDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPHVADYFTLDEEEKIEKLIRRIKKEID 888

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653    81 RRKKLLADYGVGTLELYREASGQQEPAIVILLDSYEAIKEEAYEAELFKLLVRISREGLSIGVHLLMTASRQSNLRAQLY 160
Cdd:TIGR03928  889 RRKKLFSEYGVASISMYNKASGEKLPQIVIIIDNYDAVKEEPFYEDFEELLIQLAREGASLGIYLVMTAGRQNAVRMPLM 968

                          170
                   ....*....|...
gi 446496653   161 SNFKHQLSLPQND 173
Cdd:TIGR03928  969 NNIKTKIALYLID 981
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
 3-153 6.37e-18

FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.


Pssm-ID: 279863 [Multi-domain]  Cd Length: 219  Bit Score: 77.42  E-value: 6.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653    3 GHVLLYGSPGTGKTTFLQTAGMDLARKFSPKALTMYLMDFGTNGLAPLSKLPQVADTMLLDQAEKISKFVRIMERELNRR 82
Cdd:pfam01580  39 VHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHLLSVPVATDPKRALRALEWLVDEMERR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653   83 KKLLADYGVGTLELYRE---------------------------ASGQQEPAIVILLDSY-----EAIKEEAYEAElfKL 130
Cdd:pfam01580 119 YALFRALGVRSIAGYNGeiaedpldgfgdvflviygvhvmctagRWLEILPYLVVIVDERaelrlAAPKDSEMRVE--DA 196

                         170       180
                  ....*....|....*....|...
gi 446496653  131 LVRISREGLSIGVHLLMTASRQS 153
Cdd:pfam01580 197 IVRLAQKGRAAGIHLLLATQRPS 219
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 5-30 5.99e-05

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 42.13  E-value: 5.99e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446496653   5 VLLYGSPGTGKT------------TFLQTAGMDLARKF 30
Cdd:PRK03992 168 VLLYGPPGTGKTllakavahetnaTFIRVVGSELVQKF 205
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 1-156 2.78e-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: 39.28  E-value: 2.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653     1 KDGHVLLYGSPGTGKTTFLQTagmdLARKFSPKALTMYLMDfgtnglaplsklpqvadtmlldqAEKISKFVRIMERELN 80
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARA----LARELGPPGGGVIYID-----------------------GEDILEEVLDQLLLII 53

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446496653    81 RRKKLLADYGVGTLELYREASgQQEPAIVILLDSYEAIKEEAYEAELFKLLVRISREGLSI--GVHLLMTASRQSNLR 156
Cdd:smart00382  54 VGGKKASGSGELRLRLALALA-RKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSekNLTVILTTNDEKDLG 130
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 5-30 1.35e-03

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 38.06  E-value: 1.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446496653   5 VLLYGSPGTGKT------------TFLQTAGMDLARKF 30
Cdd:COG1222  115 VLLYGPPGTGKTllakavagelgaPFIRVRGSELVSKY 152
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 1-32 1.90e-03

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: 36.74  E-value: 1.90e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446496653   1 KDGHVLLYGSPGTGKTTFLQTAGMDLARKFSP 32
Cdd:cd00009   18 PPKNLLLYGPPGTGKTTLARAIANELFRPGAP 49
 
Name Accession Description Interval E-value
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 1-173 2.69e-80

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 258.38  E-value: 2.69e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653     1 KDGHVLLYGSPGTGKTTFLQTAGMDLARKFSPKALTMYLMDFGTNGLAPLSKLPQVADTMLLDQAEKISKFVRIMERELN 80
Cdd:TIGR03928  809 KDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPHVADYFTLDEEEKIEKLIRRIKKEID 888

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653    81 RRKKLLADYGVGTLELYREASGQQEPAIVILLDSYEAIKEEAYEAELFKLLVRISREGLSIGVHLLMTASRQSNLRAQLY 160
Cdd:TIGR03928  889 RRKKLFSEYGVASISMYNKASGEKLPQIVIIIDNYDAVKEEPFYEDFEELLIQLAREGASLGIYLVMTAGRQNAVRMPLM 968

                          170
                   ....*....|...
gi 446496653   161 SNFKHQLSLPQND 173
Cdd:TIGR03928  969 NNIKTKIALYLID 981
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
 3-173 2.75e-27

type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274859 [Multi-domain]  Cd Length: 566  Bit Score: 106.62  E-value: 2.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653    3 GHVLLYGSPGTGKTTFLQTAGMDLARKFSPKALTMYLMDFGTNGLAPLSKLPQVADTMLLDQAEKISKFVRIMERELNRR 82
Cdd:TIGR03925  80 GHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPHVGGVAGRLDPERVRRTVAEVEGLLRRR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653   83 KKLLADYGVGTLELYREASGQQEPA------IVILLDSYEAIKEEaYEAeLFKLLVRISREGLSIGVHLLMTASRQSNLR 156
Cdd:TIGR03925 160 ERLFRTHGIDSMAQYRARRAAGRLPedpfgdVFLVIDGWGTLRQD-FED-LEDKVTDLAARGLAYGVHVVLTASRWSEIR 237

                         170
                  ....*....|....*..
gi 446496653  157 AQLYSNFKHQLSLPQND 173
Cdd:TIGR03925 238 PALRDLIGTRIELRLGD 254
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
 3-153 6.37e-18

FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.


Pssm-ID: 279863 [Multi-domain]  Cd Length: 219  Bit Score: 77.42  E-value: 6.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653    3 GHVLLYGSPGTGKTTFLQTAGMDLARKFSPKALTMYLMDFGTNGLAPLSKLPQVADTMLLDQAEKISKFVRIMERELNRR 82
Cdd:pfam01580  39 VHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHLLSVPVATDPKRALRALEWLVDEMERR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653   83 KKLLADYGVGTLELYRE---------------------------ASGQQEPAIVILLDSY-----EAIKEEAYEAElfKL 130
Cdd:pfam01580 119 YALFRALGVRSIAGYNGeiaedpldgfgdvflviygvhvmctagRWLEILPYLVVIVDERaelrlAAPKDSEMRVE--DA 196

                         170       180
                  ....*....|....*....|...
gi 446496653  131 LVRISREGLSIGVHLLMTASRQS 153
Cdd:pfam01580 197 IVRLAQKGRAAGIHLLLATQRPS 219
T7SS_EccC_a TIGR03924
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ...
 4-151 9.25e-14

type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274858 [Multi-domain]  Cd Length: 658  Bit Score: 68.08  E-value: 9.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653    4 HVLLYGSPGTGKTTFLQTAGMDLARKFSPKALTMYLMDF-GTNGLAPLSKLPQVAD--TMLLDQAEKISKFVRIMERELN 80
Cdd:TIGR03924 437 HGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFkGGATFLGLEGLPHVSAviTNLADEAPLVDRMQDALAGEMN 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653   81 RRKKLLADYG----VGTLELYREASGQQE--PAIVILLDSYE---AIKEEAyeAELFkllVRISREGLSIGVHLLMTASR 151
Cdd:TIGR03924 517 RRQELLRAAGnfanVAEYEKARAAGADLPplPALFVVVDEFSellSQHPDF--ADLF---VAIGRLGRSLGVHLLLASQR 591
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 4-169 3.04e-12

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 63.85  E-value: 3.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653     4 HVLLYGSPGTGKTTFLQTAGMDLARKFSPKALTMYLMDFGTNGLA-PLSKLPQVADTML-LDQAEKISKFVRImERELNR 81
Cdd:TIGR03928  471 HGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMAnLFKNLPHLLGTITnLDGAQSMRALASI-KAELKK 549

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653    82 RKKLLADYGVGTLELYREASGQQE-----PAIVILLDSYEAIKEEayEAELFKLLVRISREGLSIGVHLLMTASRQSNL- 155
Cdd:TIGR03928  550 RQRLFGENNVNHINQYQKLYKQGKakepmPHLFLISDEFAELKSE--QPEFMKELVSTARIGRSLGVHLILATQKPSGVv 627

                          170
                   ....*....|....
gi 446496653   156 RAQLYSNFKHQLSL 169
Cdd:TIGR03928  628 DDQIWSNSRFKLAL 641
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 5-30 5.99e-05

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 42.13  E-value: 5.99e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446496653   5 VLLYGSPGTGKT------------TFLQTAGMDLARKF 30
Cdd:PRK03992 168 VLLYGPPGTGKTllakavahetnaTFIRVVGSELVQKF 205
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 1-156 2.78e-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: 39.28  E-value: 2.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653     1 KDGHVLLYGSPGTGKTTFLQTagmdLARKFSPKALTMYLMDfgtnglaplsklpqvadtmlldqAEKISKFVRIMERELN 80
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARA----LARELGPPGGGVIYID-----------------------GEDILEEVLDQLLLII 53

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446496653    81 RRKKLLADYGVGTLELYREASgQQEPAIVILLDSYEAIKEEAYEAELFKLLVRISREGLSI--GVHLLMTASRQSNLR 156
Cdd:smart00382  54 VGGKKASGSGELRLRLALALA-RKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSekNLTVILTTNDEKDLG 130
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 5-30 1.35e-03

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 38.06  E-value: 1.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446496653   5 VLLYGSPGTGKT------------TFLQTAGMDLARKF 30
Cdd:COG1222  115 VLLYGPPGTGKTllakavagelgaPFIRVRGSELVSKY 152
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
 4-150 1.52e-03

type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274859 [Multi-domain]  Cd Length: 566  Bit Score: 38.05  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653    4 HVLLYGSPGTGKTTFLQTAGMDLARKFSPKALTMYLMDFGTnglaplSKLPQVADTMLLDQA---EKISKFVRIMERELN 80
Cdd:TIGR03925 365 HLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRR------TLLGAVPEDYLAGYAatsAALTELIAALAALLE 438

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446496653   81 RRkklLADYGVGTLELyREASGQQEPAIVILLDSYEAIkeEAYEAELFKLLVRISREGLSIGVHLLMTAS 150
Cdd:TIGR03925 439 RR---LPGPDVTPQQL-RARSWWSGPEIYVVVDDYDLV--ATGSGNPLAPLVELLPHARDIGLHVVVARR 502
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 1-32 1.90e-03

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: 36.74  E-value: 1.90e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446496653   1 KDGHVLLYGSPGTGKTTFLQTAGMDLARKFSP 32
Cdd:cd00009   18 PPKNLLLYGPPGTGKTTLARAIANELFRPGAP 49
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 5-30 3.89e-03

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 36.16  E-value: 3.89e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446496653   5 VLLYGSPGTGKT------------TFLQTAGMDLARKF 30
Cdd:cd19502   40 VLLYGPPGTGKTllakavanhtdaTFIRVVGSELVQKY 77
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
4-17 4.40e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 36.65  E-value: 4.40e-03
                         10
                 ....*....|....
gi 446496653   4 HVLLYGSPGTGKTT 17
Cdd:PRK00080  53 HVLLYGPPGLGKTT 66
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 5-38 8.91e-03

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 34.12  E-value: 8.91e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 446496653    5 VLLYGSPGTGKTTFLQTAGMDLARKFSPKALTMY 38
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDSVY 34
AAA_24 pfam13479
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
 5-23 9.21e-03

AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.


Pssm-ID: 433243  Cd Length: 199  Bit Score: 35.38  E-value: 9.21e-03
                          10
                  ....*....|....*....
gi 446496653    5 VLLYGSPGTGKTTFLQTAG 23
Cdd:pfam13479   5 ILIYGPSGIGKTTFAKTLP 23
 
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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