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Conserved domains on  [gi|12853633|dbj|BAB29801|]
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unnamed protein product [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
57-267 3.35e-82

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


:

Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 251.12  E-value: 3.35e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    57 VIYALNTRNDEHDAAIQALKDAHEEEIQQILAETREKILLYKSKVTEELDLRRKIQVLEASLEDHMKMKQEALTEFEAYK 136
Cdd:pfam15665   1 VIYALNTKNDEHEAEIQALKEAHEEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQYK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633   137 RRVEDMQLCAEAQHVQRIVTMSREVEEIRKKFEERLRSFGQLQVQFENDKQAALEDLRTTHRLEVQELLKSQQNHSSSVK 216
Cdd:pfam15665  81 RRVEERELKAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRAKHRQEIQELLTTQRAQSASSL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 12853633   217 LGQEKAEGLHRMEVEALNNTVKELRLEKKQLIEEYEGKLSKAQVFYERELD 267
Cdd:pfam15665 161 AEQEKLEELHKAELESLRKEVEDLRKEKKKLAEEYEQKLSKAQAFYERELE 211
Surf_Exclu_PgrA super family cl25629
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
295-382 7.74e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


The actual alignment was detected with superfamily member TIGR04320:

Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 38.17  E-value: 7.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633   295 QGQEAILRKTIGKLKTELQMVQDEASSLLDKCQKLQMALATAENNVQVLQKQLDDAKEGEMALLSKH-KEVESELAAARE 373
Cdd:TIGR04320 253 PNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNlATAQAALANAEA 332

                  ....*....
gi 12853633   374 RLQEQASDL 382
Cdd:TIGR04320 333 RLAKAKEAL 341
 
Name Accession Description Interval E-value
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
57-267 3.35e-82

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 251.12  E-value: 3.35e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    57 VIYALNTRNDEHDAAIQALKDAHEEEIQQILAETREKILLYKSKVTEELDLRRKIQVLEASLEDHMKMKQEALTEFEAYK 136
Cdd:pfam15665   1 VIYALNTKNDEHEAEIQALKEAHEEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQYK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633   137 RRVEDMQLCAEAQHVQRIVTMSREVEEIRKKFEERLRSFGQLQVQFENDKQAALEDLRTTHRLEVQELLKSQQNHSSSVK 216
Cdd:pfam15665  81 RRVEERELKAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRAKHRQEIQELLTTQRAQSASSL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 12853633   217 LGQEKAEGLHRMEVEALNNTVKELRLEKKQLIEEYEGKLSKAQVFYERELD 267
Cdd:pfam15665 161 AEQEKLEELHKAELESLRKEVEDLRKEKKKLAEEYEQKLSKAQAFYERELE 211
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
30-388 3.44e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 3.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633  30 AQLAGHNMDYSQDMHLKMSKKIAQLTKVIYALNTRNDEHDAAIQALKDAHEEEIQQIlaetrekillyKSKVTEELDLRR 109
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-----------EEAQAEEYELLA 295
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633 110 KIQVLEASLEDHMKMKQEALTEFEAYKRRVEDMQLcAEAQHVQRIVTMSREVEEIRKKFEERLRSFGQLQVQFENDKQAA 189
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEE-ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633 190 LEDLRTTHRLEVQEL--------LKSQQNHSSSVKLGQEKAEGLHRMEVEALNNTVKELRLEKKQLIEEYEGKLSKAQVF 261
Cdd:COG1196 375 AEAEEELEELAEELLealraaaeLAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633 262 YERE------LDNLKRSQLFTAESLQASRDKEADLRKEFQGQEAILRKTIGKLKTELQMVQDEASSLL----------DK 325
Cdd:COG1196 455 EEEEeallelLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLagavavligvEA 534
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12853633 326 CQKLQMALATAENNVQVLQKQLDDAKEGEMALLSKHKEVESELAAARERLQEQASDLVLKASM 388
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAI 597
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
106-377 5.70e-06

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: 48.90  E-value: 5.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    106 DLRRKIQVLEASLEDHMKMKQEALTEFEAYKRRVEDMQlcaeaqhvqrivtmsREVEEIRKKFEERLRSFGQLQVQFEND 185
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR---------------KELEELSRQISALRKDLARLEAEVEQL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    186 KQAALEDLRTTHRLEVQELLKSQQNHSSSVKLGQEKAEglhrmeVEALNNTVKELRLEKKQLIEEYEGKlskaqvfyERE 265
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE------IEELEAQIEQLKEELKALREALDEL--------RAE 811
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    266 LDNLKRSQLFTAESLQASRDKEADLRKEFQgqeaILRKTIGKLKTELQMVQDEASSLLDKCQKLQMALATAENNVQVLQK 345
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLE----DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887
                          250       260       270
                   ....*....|....*....|....*....|..
gi 12853633    346 QLDDAKEGEMALLSKHKEVESELAAARERLQE 377
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRSELRRELEE 919
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
49-382 1.43e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633   49 KKIAQLTKVIYALNTRNDEHDAAIQalkdaHEEEIQQILAETREKIllyKSKVTEELDLRRKIQVLEASLEDHMKMKQEA 128
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIE-----RYEEQREQARETRDEA---DEVLEEHEERREELETLEAEIEDLRETIAET 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633  129 LTEFEAYKRRVEDMQlcaeaqhvqrivtmsREVEEIRKKFEERLRSFG----------QLQVQFENDKQAALEDLRTtHR 198
Cdd:PRK02224 271 EREREELAEEVRDLR---------------ERLEELEEERDDLLAEAGlddadaeaveARREELEDRDEELRDRLEE-CR 334
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633  199 LEVQELLKSQQNHSSSVKLGQEKAEGLHR------MEVEALNNTVKELRLEKKQLIEEYEgKLSKAQVFYERELDNLKRS 272
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREeaaeleSELEEAREAVEDRREEIEELEEEIE-ELRERFGDAPVDLGNAEDF 413
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633  273 QLFTAESLQASRDKEADLRKEFQGQEAILRKT-------------------------------IGKLKTELQMVQDEASS 321
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAealleagkcpecgqpvegsphvetieedrerVEELEAELEDLEEEVEE 493
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12853633  322 LLDKCQKLQmALATAENNVQVLQKQLDDAKEgemaLLSKHKEVESELAAARERLQEQASDL 382
Cdd:PRK02224 494 VEERLERAE-DLVEAEDRIERLEERREDLEE----LIAERRETIEEKRERAEELRERAAEL 549
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
295-382 7.74e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 38.17  E-value: 7.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633   295 QGQEAILRKTIGKLKTELQMVQDEASSLLDKCQKLQMALATAENNVQVLQKQLDDAKEGEMALLSKH-KEVESELAAARE 373
Cdd:TIGR04320 253 PNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNlATAQAALANAEA 332

                  ....*....
gi 12853633   374 RLQEQASDL 382
Cdd:TIGR04320 333 RLAKAKEAL 341
 
Name Accession Description Interval E-value
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
57-267 3.35e-82

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 251.12  E-value: 3.35e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    57 VIYALNTRNDEHDAAIQALKDAHEEEIQQILAETREKILLYKSKVTEELDLRRKIQVLEASLEDHMKMKQEALTEFEAYK 136
Cdd:pfam15665   1 VIYALNTKNDEHEAEIQALKEAHEEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQYK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633   137 RRVEDMQLCAEAQHVQRIVTMSREVEEIRKKFEERLRSFGQLQVQFENDKQAALEDLRTTHRLEVQELLKSQQNHSSSVK 216
Cdd:pfam15665  81 RRVEERELKAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRAKHRQEIQELLTTQRAQSASSL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 12853633   217 LGQEKAEGLHRMEVEALNNTVKELRLEKKQLIEEYEGKLSKAQVFYERELD 267
Cdd:pfam15665 161 AEQEKLEELHKAELESLRKEVEDLRKEKKKLAEEYEQKLSKAQAFYERELE 211
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
30-388 3.44e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 3.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633  30 AQLAGHNMDYSQDMHLKMSKKIAQLTKVIYALNTRNDEHDAAIQALKDAHEEEIQQIlaetrekillyKSKVTEELDLRR 109
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-----------EEAQAEEYELLA 295
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633 110 KIQVLEASLEDHMKMKQEALTEFEAYKRRVEDMQLcAEAQHVQRIVTMSREVEEIRKKFEERLRSFGQLQVQFENDKQAA 189
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEE-ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633 190 LEDLRTTHRLEVQEL--------LKSQQNHSSSVKLGQEKAEGLHRMEVEALNNTVKELRLEKKQLIEEYEGKLSKAQVF 261
Cdd:COG1196 375 AEAEEELEELAEELLealraaaeLAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633 262 YERE------LDNLKRSQLFTAESLQASRDKEADLRKEFQGQEAILRKTIGKLKTELQMVQDEASSLL----------DK 325
Cdd:COG1196 455 EEEEeallelLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLagavavligvEA 534
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12853633 326 CQKLQMALATAENNVQVLQKQLDDAKEGEMALLSKHKEVESELAAARERLQEQASDLVLKASM 388
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAI 597
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
106-377 5.70e-06

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: 48.90  E-value: 5.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    106 DLRRKIQVLEASLEDHMKMKQEALTEFEAYKRRVEDMQlcaeaqhvqrivtmsREVEEIRKKFEERLRSFGQLQVQFEND 185
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR---------------KELEELSRQISALRKDLARLEAEVEQL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    186 KQAALEDLRTTHRLEVQELLKSQQNHSSSVKLGQEKAEglhrmeVEALNNTVKELRLEKKQLIEEYEGKlskaqvfyERE 265
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE------IEELEAQIEQLKEELKALREALDEL--------RAE 811
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    266 LDNLKRSQLFTAESLQASRDKEADLRKEFQgqeaILRKTIGKLKTELQMVQDEASSLLDKCQKLQMALATAENNVQVLQK 345
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLE----DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887
                          250       260       270
                   ....*....|....*....|....*....|..
gi 12853633    346 QLDDAKEGEMALLSKHKEVESELAAARERLQE 377
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRSELRRELEE 919
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
49-373 4.42e-05

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: 45.83  E-value: 4.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633     49 KKIAQLTKVIYALNTRNDEHDAAIQALKDAHEEEIQQILAETREKILLYKSKV----TEELDLRRKIQVLEASLEDHMKM 124
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIgeleAEIASLERSIAEKERELEDAEER 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    125 KQEALTEFEAYKRRVEDMQLCAEAQHVQRIVTMSrEVEEIRKKfeerlrsfgqlqvqfENDKQAALEDLRTTHRLEVQEL 204
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE-EYAELKEE---------------LEDLRAELEEVDKEFAETRDEL 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    205 LKSQQnhsssvklgqekaeglhrmEVEALNNTVKELRLEKKQLIEEYEgKLSKAQVFYERELDNLKRSQLFTAESLQASR 284
Cdd:TIGR02169  388 KDYRE-------------------KLEKLKREINELKRELDRLQEELQ-RLSEELADLNAAIAGIEAKINELEEEKEDKA 447
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    285 DKEADLRKEFQGQEAIL---RKTIGKLKTELQMVQDEASSL---LDKCQKLQMALATAENNVQVLQKQLDDAKEGEMALL 358
Cdd:TIGR02169  448 LEIKKQEWKLEQLAADLskyEQELYDLKEEYDRVEKELSKLqreLAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTV 527
                          330
                   ....*....|....*
gi 12853633    359 SKHKEVESELAAARE 373
Cdd:TIGR02169  528 AQLGSVGERYATAIE 542
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
70-382 1.35e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 44.34  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633     70 AAIQAlKDAHEEEIQQILAETREKILLYKsKVTEELDLR--------RKIQVLEASLEDHMKMKQEALTEFEAYKRRV-- 139
Cdd:pfam15921  451 AAIQG-KNESLEKVSSLTAQLESTKEMLR-KVVEELTAKkmtlesseRTVSDLTASLQEKERAIEATNAEITKLRSRVdl 528
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    140 ---EDMQLCAEAQHVQRIVTmsrEVEEIRKKFEERLRSFGQLQVQFENDKQAALEDLRTTHRLEVQELLKSQQNHSSSVK 216
Cdd:pfam15921  529 klqELQHLKNEGDHLRNVQT---ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE 605
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    217 LGQEKA-EGLHRMEVEALNNTVKELRLEKKQLIEEYEGKLsKAQVFYERELDNLKRSQLFTAESLQASRDKEADLRKEFQ 295
Cdd:pfam15921  606 LQEFKIlKDKKDAKIRELEARVSDLELEKVKLVNAGSERL-RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFR 684
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633    296 GQEAILRKTIGKLKTELQMVQDEASSLLDKCQKLQMALATAENNVQVLQKQLdDAKEGEM-ALLSKHKEVESELAAARER 374
Cdd:pfam15921  685 NKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQI-TAKRGQIdALQSKIQFLEEAMTNANKE 763
                          330
                   ....*....|.
gi 12853633    375 ---LQEQASDL 382
Cdd:pfam15921  764 khfLKEEKNKL 774
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
96-322 4.33e-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: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633   96 LYKSKVTEELDLRRKIQVLEASLEDHMKMKQEALTEfeayKRRVEdmQLCAEAQHVQRIVTMSREVEEIrkkfeERLRSf 175
Cdd:COG4913  212 FVREYMLEEPDTFEAADALVEHFDDLERAHEALEDA----REQIE--LLEPIRELAERYAAARERLAEL-----EYLRA- 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633  176 gQLQVQFENDKQAALEDLRTTHRLEVQELLKSQQNHSSSVKLGQEKAEGLHRMEVEALNNTVKELRLEKKQLIEEYEGKL 255
Cdd:COG4913  280 -ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERE 358
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12853633  256 SKAQVfYERELDNLKRSQLFTAESLQASRDKEADLRKEFQGQEAILRKTIGKLKTELQMVQDEASSL 322
Cdd:COG4913  359 RRRAR-LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
106-338 8.52e-04

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: 41.29  E-value: 8.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633 106 DLRRKIQVLEASLEDHMKMKQEALTEFEAYKRRVEDMQlcaeaqhvQRIVTMSREVEEIRKKFEERLRSFGQLQVQFEND 185
Cdd:COG4942  31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA--------RRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633 186 KQAALEDLRTTHRLEVQ---ELLKSQQNHSSSVKLGQekaegLHRMEVEALNNTVKELRLEKKQLIEEyegklskaqvfy 262
Cdd:COG4942 103 KEELAELLRALYRLGRQpplALLLSPEDFLDAVRRLQ-----YLKYLAPARREQAEELRADLAELAAL------------ 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12853633 263 ERELDNLKRSQLFTAESLQASRDKEADLRKEFQGQEAILRKTIGKLKTELQMVQDEASSLLDKCQKLQMALATAEN 338
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
49-382 1.43e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633   49 KKIAQLTKVIYALNTRNDEHDAAIQalkdaHEEEIQQILAETREKIllyKSKVTEELDLRRKIQVLEASLEDHMKMKQEA 128
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIE-----RYEEQREQARETRDEA---DEVLEEHEERREELETLEAEIEDLRETIAET 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633  129 LTEFEAYKRRVEDMQlcaeaqhvqrivtmsREVEEIRKKFEERLRSFG----------QLQVQFENDKQAALEDLRTtHR 198
Cdd:PRK02224 271 EREREELAEEVRDLR---------------ERLEELEEERDDLLAEAGlddadaeaveARREELEDRDEELRDRLEE-CR 334
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633  199 LEVQELLKSQQNHSSSVKLGQEKAEGLHR------MEVEALNNTVKELRLEKKQLIEEYEgKLSKAQVFYERELDNLKRS 272
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREeaaeleSELEEAREAVEDRREEIEELEEEIE-ELRERFGDAPVDLGNAEDF 413
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633  273 QLFTAESLQASRDKEADLRKEFQGQEAILRKT-------------------------------IGKLKTELQMVQDEASS 321
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAealleagkcpecgqpvegsphvetieedrerVEELEAELEDLEEEVEE 493
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12853633  322 LLDKCQKLQmALATAENNVQVLQKQLDDAKEgemaLLSKHKEVESELAAARERLQEQASDL 382
Cdd:PRK02224 494 VEERLERAE-DLVEAEDRIERLEERREDLEE----LIAERRETIEEKRERAEELRERAAEL 549
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
106-345 7.65e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.46  E-value: 7.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633 106 DLRRKIQVLEASLEDHMKMKQEALTEFEAYKRRVEDMQLCAEAQ-HVQRIVTMSREVEEIRKKFEERLRSFGQLQVQFEN 184
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKlLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633 185 DKQAALEDLRTThrlEVQELLKSQQnhsssvKLGQEKAEGLHRMEVEalNNTVKELRLEKKQLIEEYEGKLSKAQVFYER 264
Cdd:COG3206 252 GPDALPELLQSP---VIQQLRAQLA------ELEAELAELSARYTPN--HPDVIALRAQIAALRAQLQQEAQRILASLEA 320
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633 265 ELDNLKRsqlfTAESLQASRDKEADLRKEFQGQEAILRKtigkLKTELQMVQDEASSLLDKCQKLQMALATAENNVQVLQ 344
Cdd:COG3206 321 ELEALQA----REASLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYESLLQRLEEARLAEALTVGNVRVID 392

                .
gi 12853633 345 K 345
Cdd:COG3206 393 P 393
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
295-382 7.74e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 38.17  E-value: 7.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853633   295 QGQEAILRKTIGKLKTELQMVQDEASSLLDKCQKLQMALATAENNVQVLQKQLDDAKEGEMALLSKH-KEVESELAAARE 373
Cdd:TIGR04320 253 PNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNlATAQAALANAEA 332

                  ....*....
gi 12853633   374 RLQEQASDL 382
Cdd:TIGR04320 333 RLAKAKEAL 341
 
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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