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Conserved domains on  [gi|1952716300|ref|XP_038313438|]
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filensin isoform X4 [Canis lupus familiaris]

Protein Classification

AAA family ATPase( domain architecture ID 1003843)

AAA family ATPase containing an AAA (ATPases Associated with various cellular Activities) domain, may function as an ATP-dependent endonuclease or the ATPase component of an ABC-type transporter; similar to Bacillus subtilis protein YhaN

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  15037234|18208389|16828312|18466635|15037233

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
38-212 7.46e-09

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 7.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  38 LKEMLERLNKEADEALLHNLRLQIEAQFLQDDISAAKDRYKKnLLEIQTYVTILQQIVQTTPQASAITSGMREekLLTER 117
Cdd:COG4717   349 LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA-LEQAEEYQELKEELEELEEQLEELLGELEE--LLEAL 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 118 EAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAHEcyDDEIQLYNEQIENLRKEIEEAERSLERssydcrqLV 197
Cdd:COG4717   426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAA-------LK 496

                         170
                  ....*....|....*
gi 1952716300 198 VAQQTLKNELERYHR 212
Cdd:COG4717   497 LALELLEEAREEYRE 511
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 401-516 1.35e-05

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.15  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 401 EEDSLHRDSPAEpSPEQPGPPlENGQEDLQGKEGGH-PSNQHTADKENEINAEGLKGP-GEKQDDQKEDEESRgpCPVVT 478
Cdd:PTZ00449  501 EEDSDKHDEPPE-GPEASGLP-PKAPGDKEGEEGEHeDSKESDEPKEGGKPGETKEGEvGKKPGPAKEHKPSK--IPTLS 576

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1952716300 479 PGPEGPSTPQSQRSGVSPSGSEgRGVRSSSPQERSPPR 516
Cdd:PTZ00449  577 KKPEFPKDPKHPKDPEEPKKPK-RPRSAQRPTRPKSPK 613
 
Name Accession Description Interval E-value
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
38-212 7.46e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 7.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  38 LKEMLERLNKEADEALLHNLRLQIEAQFLQDDISAAKDRYKKnLLEIQTYVTILQQIVQTTPQASAITSGMREekLLTER 117
Cdd:COG4717   349 LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA-LEQAEEYQELKEELEELEEQLEELLGELEE--LLEAL 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 118 EAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAHEcyDDEIQLYNEQIENLRKEIEEAERSLERssydcrqLV 197
Cdd:COG4717   426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAA-------LK 496

                         170
                  ....*....|....*
gi 1952716300 198 VAQQTLKNELERYHR 212
Cdd:COG4717   497 LALELLEEAREEYRE 511
Filament pfam00038
Intermediate filament protein;
27-220 7.98e-08

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 54.16  E-value: 7.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  27 RYENECECQLLLKEMLERLNKEADEALLHNLRLQIEAQFLQDDISAAKDRYKKNLLEIQTYVTILQQIVQT----TPQAS 102
Cdd:pfam00038  90 KYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMdaarKLDLT 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 103 AITSGMREE-----------------------KLLTEREAAALQSQLEEGREVVSLLQAQRTELQA---QTAALEQSIKD 156
Cdd:pfam00038 170 SALAEIRAQyeeiaaknreeaeewyqskleelQQAAARNGDALRSAKEEITELRRTIQSLEIELQSlkkQKASLERQLAE 249

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952716300 157 AHECYDDEIQLYNEQIENLRKEIEEAERSLERSSYDCRQLVVAQQTLKNELERYHRIIENEGNR 220
Cdd:pfam00038 250 TEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 38-228 1.64e-06

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 50.06  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  38 LKEMLERLNKEADEallhnlrLQIEAQFLQDDISAAKDRYKKNLLEIQTYVTILQQIVQTtpqasaitsgmrEEKLLTER 117
Cdd:cd22656   119 IKALLDDLLKEAKK-------YQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTD------------EGGAIARK 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 118 EAAALQSQLEEGR-EVVSLLQAQRTELQAQTAALEQSIKDAHECYDDeIQLYNEQIENLRKEIEEAERSLERssydcrqL 196
Cdd:cd22656   180 EIKDLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIAD-LTAADTDLDNLLALIGPAIPALEK-------L 251

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1952716300 197 VVAQQTLKNELERYHRIIENEGNRLSSAFIET 228
Cdd:cd22656   252 QGAWQAIATDLDSLKDLLEDDISKIPAAILAK 283
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 401-516 1.35e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.15  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 401 EEDSLHRDSPAEpSPEQPGPPlENGQEDLQGKEGGH-PSNQHTADKENEINAEGLKGP-GEKQDDQKEDEESRgpCPVVT 478
Cdd:PTZ00449  501 EEDSDKHDEPPE-GPEASGLP-PKAPGDKEGEEGEHeDSKESDEPKEGGKPGETKEGEvGKKPGPAKEHKPSK--IPTLS 576

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1952716300 479 PGPEGPSTPQSQRSGVSPSGSEgRGVRSSSPQERSPPR 516
Cdd:PTZ00449  577 KKPEFPKDPKHPKDPEEPKKPK-RPRSAQRPTRPKSPK 613
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 14-227 1.75e-04

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: 44.66  E-value: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300   14 NVEQLSFKRRNVPRYENECECQL-LLKEMLERLNKEADEALLHNLRLQIEAQFLQDDISAAKDRykknLLEIQTYVTILQ 92
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIeELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA----LDELRAELTLLN 816

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300   93 QIVQTTPQASAitsGMREEKLLTEREAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAHECYD---DEIQLYN 169
Cdd:TIGR02168  817 EEAANLRERLE---SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleEALALLR 893

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952716300  170 EQIENLRKEIEEAERSLERSSYDCRQLVVAQQTLKNELERyhriIENEGNRLSSAFIE 227
Cdd:TIGR02168  894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEG----LEVRIDNLQERLSE 947
 
Name Accession Description Interval E-value
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
38-212 7.46e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 7.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  38 LKEMLERLNKEADEALLHNLRLQIEAQFLQDDISAAKDRYKKnLLEIQTYVTILQQIVQTTPQASAITSGMREekLLTER 117
Cdd:COG4717   349 LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA-LEQAEEYQELKEELEELEEQLEELLGELEE--LLEAL 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 118 EAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAHEcyDDEIQLYNEQIENLRKEIEEAERSLERssydcrqLV 197
Cdd:COG4717   426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAA-------LK 496

                         170
                  ....*....|....*
gi 1952716300 198 VAQQTLKNELERYHR 212
Cdd:COG4717   497 LALELLEEAREEYRE 511
Filament pfam00038
Intermediate filament protein;
27-220 7.98e-08

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 54.16  E-value: 7.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  27 RYENECECQLLLKEMLERLNKEADEALLHNLRLQIEAQFLQDDISAAKDRYKKNLLEIQTYVTILQQIVQT----TPQAS 102
Cdd:pfam00038  90 KYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMdaarKLDLT 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 103 AITSGMREE-----------------------KLLTEREAAALQSQLEEGREVVSLLQAQRTELQA---QTAALEQSIKD 156
Cdd:pfam00038 170 SALAEIRAQyeeiaaknreeaeewyqskleelQQAAARNGDALRSAKEEITELRRTIQSLEIELQSlkkQKASLERQLAE 249

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952716300 157 AHECYDDEIQLYNEQIENLRKEIEEAERSLERSSYDCRQLVVAQQTLKNELERYHRIIENEGNR 220
Cdd:pfam00038 250 TEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-224 9.33e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 9.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300   38 LKEMLERLNkEADEALLhNLRLQIEAqfLQDdISAAKDRYKKNLLEIQtyvtILQQIVQTTPQASAitsgmreeklltER 117
Cdd:COG4913    230 LVEHFDDLE-RAHEALE-DAREQIEL--LEP-IRELAERYAAARERLA----ELEYLRAALRLWFA------------QR 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  118 EAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAHECYD----DEIQLYNEQIENLRKEIEEAERSLERSSYDC 193
Cdd:COG4913    289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEALL 368

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1952716300  194 RQLVVAQQTLKNELERYHRIIENEGNRLSSA 224
Cdd:COG4913    369 AALGLPLPASAEEFAALRAEAAALLEALEEE 399
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 38-228 1.64e-06

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 50.06  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  38 LKEMLERLNKEADEallhnlrLQIEAQFLQDDISAAKDRYKKNLLEIQTYVTILQQIVQTtpqasaitsgmrEEKLLTER 117
Cdd:cd22656   119 IKALLDDLLKEAKK-------YQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTD------------EGGAIARK 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 118 EAAALQSQLEEGR-EVVSLLQAQRTELQAQTAALEQSIKDAHECYDDeIQLYNEQIENLRKEIEEAERSLERssydcrqL 196
Cdd:cd22656   180 EIKDLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIAD-LTAADTDLDNLLALIGPAIPALEK-------L 251

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1952716300 197 VVAQQTLKNELERYHRIIENEGNRLSSAFIET 228
Cdd:cd22656   252 QGAWQAIATDLDSLKDLLEDDISKIPAAILAK 283
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-203 1.12e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.84  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 115 TEREAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAHE---CYDDEIQLYNEQIENLRKEIEEAERSLERSSY 191
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEAQKE 104

                          90
                  ....*....|..
gi 1952716300 192 DCRQLVVAQQTL 203
Cdd:COG4942   105 ELAELLRALYRL 116
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 38-224 1.14e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  38 LKEMLERLnkEADEALLHNLRLQIEAQFLQDDISAAKDRYKKNLLEIQTYVTILQQIVQTTPQASAITSGMREEKLLTER 117
Cdd:COG1196   218 LKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 118 EAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAHEcyddEIQLYNEQIENLRKEIEEAERSLERSSydcRQLV 197
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE----ELEELEEELEEAEEELEEAEAELAEAE---EALL 368

                         170       180
                  ....*....|....*....|....*..
gi 1952716300 198 VAQQTLKNELERYHRIIENEGNRLSSA 224
Cdd:COG1196   369 EAEAELAEAEEELEELAEELLEALRAA 395
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 401-516 1.35e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.15  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 401 EEDSLHRDSPAEpSPEQPGPPlENGQEDLQGKEGGH-PSNQHTADKENEINAEGLKGP-GEKQDDQKEDEESRgpCPVVT 478
Cdd:PTZ00449  501 EEDSDKHDEPPE-GPEASGLP-PKAPGDKEGEEGEHeDSKESDEPKEGGKPGETKEGEvGKKPGPAKEHKPSK--IPTLS 576

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1952716300 479 PGPEGPSTPQSQRSGVSPSGSEgRGVRSSSPQERSPPR 516
Cdd:PTZ00449  577 KKPEFPKDPKHPKDPEEPKKPK-RPRSAQRPTRPKSPK 613
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 29-227 1.55e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  29 ENECECQLLLKEM---LERLNKEADEALLHnLRLQIEAQFLqdDISAAKDRYKKNLLEIQTYVTILQQIVQTTPQASAIT 105
Cdd:COG1196   186 ENLERLEDILGELerqLEPLERQAEKAERY-RELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAEL 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 106 SGMREEKLLTEREAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAHEC---YDDEIQLYNEQIENLRKEIEEA 182
Cdd:COG1196   263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERleeLEEELAELEEELEELEEELEEL 342

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1952716300 183 ERSLERSSYDCRQLVVAQQTLKNELERYHRIIENEGNRLSSAFIE 227
Cdd:COG1196   343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
115-215 1.46e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.85  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 115 TEREAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAHECY------DDEIQLYNEQIENLRKEIEEAERSLER 188
Cdd:COG2433   411 EEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEErreirkDREISRLDREIERLERELEEERERIEE 490

                          90       100
                  ....*....|....*....|....*..
gi 1952716300 189 ssydcrqlvvaqqtLKNELERYHRIIE 215
Cdd:COG2433   491 --------------LKRKLERLKELWK 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 14-227 1.75e-04

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: 44.66  E-value: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300   14 NVEQLSFKRRNVPRYENECECQL-LLKEMLERLNKEADEALLHNLRLQIEAQFLQDDISAAKDRykknLLEIQTYVTILQ 92
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIeELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA----LDELRAELTLLN 816

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300   93 QIVQTTPQASAitsGMREEKLLTEREAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAHECYD---DEIQLYN 169
Cdd:TIGR02168  817 EEAANLRERLE---SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleEALALLR 893

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952716300  170 EQIENLRKEIEEAERSLERSSYDCRQLVVAQQTLKNELERyhriIENEGNRLSSAFIE 227
Cdd:TIGR02168  894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEG----LEVRIDNLQERLSE 947
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-266 1.86e-04

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: 44.66  E-value: 1.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300   33 ECQLLLKEMLERLNKEADEALLHNLRLQIEAQFLQDDISAAKDRYKKNLLEIQTYVTILQQIVQttpqasaitsgmREEK 112
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED------------RRER 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  113 LLTEREaaALQSQLEEgrevvsllqAQRTELQAQTAALEQSIKDAHECYDDEIQLYnEQIENLRKEIEEAERSLERSSYD 192
Cdd:TIGR02168  419 LQQEIE--ELLKKLEE---------AELKELQAELEELEEELEELQEELERLEEAL-EELREELEEAEQALDAAERELAQ 486

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  193 CRQLVVAQQTLKNELERYHR---IIENEGNRLS------SAFIEtpvtlFTPSHGTSISSRLGG-------KDLARAVQD 256
Cdd:TIGR02168  487 LQARLDSLERLQENLEGFSEgvkALLKNQSGLSgilgvlSELIS-----VDEGYEAAIEAALGGrlqavvvENLNAAKKA 561

                          250
                   ....*....|
gi 1952716300  257 ITTAKPRQKG 266
Cdd:TIGR02168  562 IAFLKQNELG 571
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 38-209 2.70e-04

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: 43.89  E-value: 2.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300   38 LKEMLERLNKEAD--EALLHNLRLQI--------EAQFLQDDISAAKDRYKKnllEIQTYVTILQQIVQTTPQASAITSG 107
Cdd:TIGR02168  251 AEEELEELTAELQelEEKLEELRLEVseleeeieELQKELYALANEISRLEQ---QKQILRERLANLERQLEELEAQLEE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  108 MREEKLLTEREAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAHECYD---DEIQLYNEQIENLRKEIEEAER 184
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQLELQIASLNNEIERLEA 407

                          170       180
                   ....*....|....*....|....*
gi 1952716300  185 SLERSSYDCRQLVVAQQTLKNELER 209
Cdd:TIGR02168  408 RLERLEDRRERLQQEIEELLKKLEE 432
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
38-209 2.80e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  38 LKEMLERLNKEADEAL--LHNLR-------LQIEAQFLQDDISAAKDRY---KKNLLEIQTYVTILQQIVQTTPQA---- 101
Cdd:COG3206   180 LEEQLPELRKELEEAEaaLEEFRqknglvdLSEEAKLLLQQLSELESQLaeaRAELAEAEARLAALRAQLGSGPDAlpel 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 102 --SAITSGMREEKLLTEREAAALQSQLEEGREVVSLLQAQRTELQAQtaaLEQSIKDAHECYDDEIQLYNEQIENLRKEI 179
Cdd:COG3206   260 lqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ---LQQEAQRILASLEAELEALQAREASLQAQL 336

                         170       180       190
                  ....*....|....*....|....*....|
gi 1952716300 180 EEAERSLerssydcRQLVVAQQTLkNELER 209
Cdd:COG3206   337 AQLEARL-------AELPELEAEL-RRLER 358
PHA03381 PHA03381
tegument protein VP22; Provisional
 408-515 3.73e-04

tegument protein VP22; Provisional


Pssm-ID: 177618 [Multi-domain]  Cd Length: 290  Bit Score: 42.69  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 408 DSPAEPSPEQPGPPLENGQEDLQGKEGGHPSNQHTADKENEINAEGlkgpgekqDDQKEDEESRGPCPVVTP--GPEGPS 485
Cdd:PHA03381   30 ASPARVSFEEPADRARRGAGQARGRSQAERRFHHYDEARADYPYYT--------GSSSEDERPADPRPSRRPhaQPEASG 101

                          90       100       110
                  ....*....|....*....|....*....|
gi 1952716300 486 tPQSQRSGVSPSGSEGRGVRSSSPQERSPP 515
Cdd:PHA03381  102 -PGPARGARGPAGSRGRGRRAESPSPRDPP 130
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 38-216 7.35e-04

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: 42.74  E-value: 7.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300   38 LKEMLERLNKEADEAllhnlrlqIEAQFLQDDISAakdrykknlLEIQTYVTILQQIVQTTPQASAITSGMREEKLLTER 117
Cdd:TIGR02168  198 LERQLKSLERQAEKA--------ERYKELKAELRE---------LELALLVLRLEELREELEELQEELKEAEEELEELTA 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  118 EAAALQSQLEEGR----EVVSLLQAQRTELQAQTAALE------QSIKDAHECYDDEIQLYNEQIENLRKEIEEAERSLE 187
Cdd:TIGR02168  261 ELQELEEKLEELRlevsELEEEIEELQKELYALANEISrleqqkQILRERLANLERQLEELEAQLEELESKLDELAEELA 340

                          170       180
                   ....*....|....*....|....*....
gi 1952716300  188 RSSYDCRQLVVAQQTLKNELERYHRIIEN 216
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEE 369
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-212 7.93e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 7.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300   38 LKEMLERLNKEADEALLHNL--RLQIEAQFLQDDISAAKDRYKKNLLEIQTYVTILQQIvqttpqasaitSGMREEKLlt 115
Cdd:COG4913    277 LRAALRLWFAQRRLELLEAEleELRAELARLEAELERLEARLDALREELDELEAQIRGN-----------GGDRLEQL-- 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  116 EREAAALQSQLEEgrevvslLQAQRTELQAQTAALEQSIKDAHECYDD---EIQLYNEQIENLRKEIEEAERSLERSSYD 192
Cdd:COG4913    344 EREIERLERELEE-------RERRRARLEALLAALGLPLPASAEEFAAlraEAAALLEALEEELEALEEALAEAEAALRD 416

                          170       180
                   ....*....|....*....|
gi 1952716300  193 CRQlvvAQQTLKNELERYHR 212
Cdd:COG4913    417 LRR---ELRELEAEIASLER 433
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
116-234 1.04e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  116 EREAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAHECYD---------------DEIQLYNEQIENLRKEIE 180
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaereiaeleaelERLDASSDDLAALEEQLE 695

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1952716300  181 EAERSLERSSYDCRQLVVAQQTLKNELERYHRIIENEGNRLSSAFIETPVTLFT 234
Cdd:COG4913    696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 38-208 1.23e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300   38 LKEMLERLNKEADEALLHNLRLQIEAQFLQDDISAAKDRYKKNLLEIQTYVTILQQIVQTTPQASAITSGMREEKLLTER 117
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  118 EAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAH-ECYDDEIQLYNEQIENLRKEIEEAERSLERSSYDCRQL 196
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831

                          170
                   ....*....|..
gi 1952716300  197 VVAQQTLKNELE 208
Cdd:TIGR02169  832 EKEIQELQEQRI 843
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 38-181 1.29e-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: 40.68  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  38 LKEMLERLNKEADEALLHNLRLQIEAQFLQDDIsaakDRYKKNLLEIQT---YVTILQQIvqttpqasaitSGMREEKLL 114
Cdd:COG1579    43 LEARLEAAKTELEDLEKEIKRLELEIEEVEARI----KKYEEQLGNVRNnkeYEALQKEI-----------ESLKRRISD 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952716300 115 TEREAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAHECYDDEIQLYNEQIENLRKEIEE 181
Cdd:COG1579   108 LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
37-201 1.87e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  37 LLKEMLERLNKEADEALLHNLRLQIEAQFLQDDISAAKDRYKKNLLEIQTYVTILQQIVQTTPQASAITSGMREEKLLTE 116
Cdd:COG4372    28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 117 REAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAhecyDDEIQLYNEQIENLRKEIEEAERSLERSSYDCRQL 196
Cdd:COG4372   108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER----EEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183


                  ....*
gi 1952716300 197 VVAQQ 201
Cdd:COG4372   184 ALDEL 188
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
39-186 2.85e-03

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 40.22  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  39 KEMLERLNKEAdEALLHNL--RLQIEA-QFLQDDISAAKDRykknLLEIQTYVTILQQivqttpqasaitsgmrEEKLL- 114
Cdd:COG3524   153 QAIAEALLAES-EELVNQLseRAREDAvRFAEEEVERAEER----LRDAREALLAFRN----------------RNGILd 211

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952716300 115 TEREAAALQSQleegrevVSLLQAQRTELQAQTAALEQSIKDAHEcyddEIQLYNEQIENLRKEIEEAERSL 186
Cdd:COG3524   212 PEATAEALLQL-------IATLEGQLAELEAELAALRSYLSPNSP----QVRQLRRRIAALEKQIAAERARL 272
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 29-181 2.90e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 2.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300   29 ENECECQLLLKEM---LERLNKEADEALLHNLRLQIEAQFLQDDISAAKDRYKKNLLEIQTYV-TILQQIVQTTPQASAI 104
Cdd:TIGR02169  184 ENIERLDLIIDEKrqqLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLaSLEEELEKLTEEISEL 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  105 --TSGMREEKL---------LTEREAAALQSQLEEgrevvslLQAQRTELQAQTAALEQSIKDAHE---CYDDEIQLYNE 170
Cdd:TIGR02169  264 ekRLEEIEQLLeelnkkikdLGEEEQLRVKEKIGE-------LEAEIASLERSIAEKERELEDAEErlaKLEAEIDKLLA 336

                          170
                   ....*....|.
gi 1952716300  171 QIENLRKEIEE 181
Cdd:TIGR02169  337 EIEELEREIEE 347
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
42-211 3.87e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  42 LERLNKEADEALLHNLRLQIEAQFLQDDISAAKDRYKknllEIQTYVTILQQIVQTTPQASAITSGMREEKLLTEReAAA 121
Cdd:COG4717    76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELE----ELREELEKLEKLLQLLPLYQELEALEAELAELPER-LEE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 122 LQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDAHECYDDEIQLYNEQIENLRKEIEEAERSLERSSYDCRQLVVAQQ 201
Cdd:COG4717   151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230

                         170
                  ....*....|
gi 1952716300 202 TLKNELERYH 211
Cdd:COG4717   231 QLENELEAAA 240
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
42-187 6.06e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 6.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  42 LERLNKEADEALLHNLRLQIEAQFLQDDISAAKDRyKKNLLEIQTYVTILQQIVQTTPQASAITSGMREE----KLLTER 117
Cdd:COG3206   221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDA-LPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQ 299

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952716300 118 EAAALQSQLEEGREVVSLLQAQRTELQAQTAALEQSIKDahecYDDEIQLYNE---QIENLRKEIEEAERSLE 187
Cdd:COG3206   300 IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQ----LEARLAELPEleaELRRLEREVEVARELYE 368
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 47-209 7.09e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  47 KEADEALLHNLRLQIEAqfLQDDISAAKDRYKKNLLEIQTyvtILQQIVQTTPQASAITSGMR--EEKL-LTEREAAALQ 123
Cdd:COG4942    22 AAEAEAELEQLQQEIAE--LEKELAALKKEEKALLKQLAA---LERRIAALARRIRALEQELAalEAELaELEKEIAELR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300 124 SQLEEGREVVS--LLQAQRTELQAQTAAL------EQSIKDAH--ECYDDEIQLYNEQIENLRKEIEEAERSLERSSYDC 193
Cdd:COG4942    97 AELEAQKEELAelLRALYRLGRQPPLALLlspedfLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAEL 176

                         170
                  ....*....|....*.
gi 1952716300 194 RQLVVAQQTLKNELER 209
Cdd:COG4942   177 EALLAELEEERAALEA 192
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 142-209 7.87e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.44  E-value: 7.87e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952716300  142 ELQAQTAALEQSIKDAHECY---DDEIQLYNEQIENLRKEIEEAERSLERSSYDCRQLVVAQQTLKNELER 209
Cdd:pfam12128  601 ELRERLDKAEEALQSAREKQaaaEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNK 671
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
44-189 8.78e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 38.49  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952716300  44 RLNKEADEALLHNLRLQIEAQFLQDDISAAKDRYKKNLLEIQTYVTILQQIVQttpqasaitsgmREEKLLtEREAAAlQ 123
Cdd:COG1566    82 QAALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELE------------RYQALY-KKGAVS-Q 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952716300 124 SQLEEGREVVSLLQAQRTELQAQTAALEQSIKDahecyDDEIQLYNEQIENLRKEIEEAERSLERS 189
Cdd:COG1566   148 QELDEARAALDAAQAQLEAAQAQLAQAQAGLRE-----EEELAAAQAQVAQAEAALAQAELNLART 208
 
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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