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Conserved domains on  [gi|1907140512|ref|XP_036018187|]
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protein GOLM2 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
42-195 1.16e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512   42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAKEGLGKRCEDDKVKLQNNISYQMA 121
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907140512  122 DIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLE-YESFQCGQQIKELRAQHEENIKKLADqfLQEQKETH 195
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEeLLKKLEEAELKELQAELEELEEELEE--LQEELERL 459
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
42-195 1.16e-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: 50.83  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512   42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAKEGLGKRCEDDKVKLQNNISYQMA 121
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907140512  122 DIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLE-YESFQCGQQIKELRAQHEENIKKLADqfLQEQKETH 195
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEeLLKKLEEAELKELQAELEELEEELEE--LQEELERL 459
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
29-178 3.57e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 3.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512   29 AFNYWSISSRHVLLQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQkeADYGRLsSRLQAKEglgKRCEDD 108
Cdd:COG4913    280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG--NGGDRL-EQLEREI---ERLERE 353
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512  109 KVKLQNNISYQMADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEYESFQCGQQIKELRAQHEE 178
Cdd:COG4913    354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
42-196 3.41e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512  42 LQEEVAELQGQVQrtEVARGRLEKRNSDLLLLVDTHKKQIDQKEADygrlsSRLQAKEGLGKRCEDDKVKLQNNISYQMA 121
Cdd:PRK03918  568 LEEELAELLKELE--ELGFESVEELEERLKELEPFYNEYLELKDAE-----KELEREEKELKKLEEELDKAFEELAETEK 640
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907140512 122 DIHHLKEQLAELRQEFLRQEDQlqdyRKNNTYLVKRLEYESFQcgQQIKELRAQHEEnIKKLADqFLQEQKETHK 196
Cdd:PRK03918  641 RLEELRKELEELEKKYSEEEYE----ELREEYLELSRELAGLR--AELEELEKRREE-IKKTLE-KLKEELEERE 707
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
121-200 4.35e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 38.82  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512 121 ADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEYESFQCGQQ----IKELRAQHEENIKKLADQFLQEQKETHK 196
Cdd:pfam03961 149 VDFPELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQLPPEKREqlekLLETKNKLSEELEELEEELKELKEELES 228

                  ....
gi 1907140512 197 IQSN 200
Cdd:pfam03961 229 LLGE 232
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
42-195 1.16e-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: 50.83  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512   42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAKEGLGKRCEDDKVKLQNNISYQMA 121
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907140512  122 DIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLE-YESFQCGQQIKELRAQHEENIKKLADqfLQEQKETH 195
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEeLLKKLEEAELKELQAELEELEEELEE--LQEELERL 459
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
29-178 3.57e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 3.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512   29 AFNYWSISSRHVLLQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQkeADYGRLsSRLQAKEglgKRCEDD 108
Cdd:COG4913    280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG--NGGDRL-EQLEREI---ERLERE 353
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512  109 KVKLQNNISYQMADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEYESFQCGQQIKELRAQHEE 178
Cdd:COG4913    354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
42-201 3.10e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 3.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512   42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAKEGLGKRCEDDKVK-------LQN 114
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIlrerlanLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512  115 NISYQMADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYL---VKRLEYESFQCGQQIKELRAQHEENIKKLADQFLQEQ 191
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLeaeLEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                          170
                   ....*....|
gi 1907140512  192 KETHKIQSND 201
Cdd:TIGR02168  397 SLNNEIERLE 406
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
42-195 3.84e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 3.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512   42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADygrlsSRLQAKEGLGKRCEDDKVKLQnnisyqma 121
Cdd:COG4913    622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-----REIAELEAELERLDASSDDLA-------- 688
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512  122 dihHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEyesfQCGQQIKELRAQHEENIKK--------LADQFLQEQKE 193
Cdd:COG4913    689 ---ALEEQLEELEAELEELEEELDELKGEIGRLEKELE----QAEEELDELQDRLEAAEDLarlelralLEERFAAALGD 761

                   ..
gi 1907140512  194 TH 195
Cdd:COG4913    762 AV 763
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
41-198 2.51e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512  41 LLQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAKEGLGKRCEDDKVKLQNNISYQM 120
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907140512 121 ADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEyesfQCGQQIKELRAQHEENIKKLADQFLQEQKETHKIQ 198
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELA----EAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
42-196 3.41e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512  42 LQEEVAELQGQVQrtEVARGRLEKRNSDLLLLVDTHKKQIDQKEADygrlsSRLQAKEGLGKRCEDDKVKLQNNISYQMA 121
Cdd:PRK03918  568 LEEELAELLKELE--ELGFESVEELEERLKELEPFYNEYLELKDAE-----KELEREEKELKKLEEELDKAFEELAETEK 640
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907140512 122 DIHHLKEQLAELRQEFLRQEDQlqdyRKNNTYLVKRLEYESFQcgQQIKELRAQHEEnIKKLADqFLQEQKETHK 196
Cdd:PRK03918  641 RLEELRKELEELEKKYSEEEYE----ELREEYLELSRELAGLR--AELEELEKRREE-IKKTLE-KLKEELEERE 707
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
42-214 4.73e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512  42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAKEGLGKRCEDDKVKLQNNISYQMA 121
Cdd:COG1196   321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512 122 DIHHLKEQLAELRQEFLRQEDQLQDYRKN-NTYLVKRLEYESFQcgQQIKELRAQHEENIKKLADQFLQEQKETHKIQSN 200
Cdd:COG1196   401 QLEELEEAEEALLERLERLEEELEELEEAlAELEEEEEEEEEAL--EEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
                         170
                  ....*....|....
gi 1907140512 201 DGKELGRNDHGAPK 214
Cdd:COG1196   479 LAELLEELAEAAAR 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
42-199 6.33e-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: 41.97  E-value: 6.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512   42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLS----------------------------S 93
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaeveqleeriaqlskelteleaeieeleE 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512   94 RLQAKEGLGKRCEDDKVKLQNNISYQMADIHHLKEQLAELRQEFlrqeDQLQDYRKNNTYLVKRLEYESFQCGQQIKELR 173
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL----TLLNEEAANLRERLESLERRIAATERRLEDLE 844
                          170       180
                   ....*....|....*....|....*....
gi 1907140512  174 AQHE---ENIKKLADQFLQEQKETHKIQS 199
Cdd:TIGR02168  845 EQIEelsEDIESLAAEIEELEELIEELES 873
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
42-208 1.71e-03

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: 40.81  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512   42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAKEGLGKRCEDD-------KVKLQN 114
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQleeleskLDELAE 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512  115 NISYQMADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEYES---FQCGQQIKELRAQHEENIKKLAD-----Q 186
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRskvAQLELQIASLNNEIERLEARLERledrrE 417
                          170       180
                   ....*....|....*....|....
gi 1907140512  187 FLQEQKETH--KIQSNDGKELGRN 208
Cdd:TIGR02168  418 RLQQEIEELlkKLEEAELKELQAE 441
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
34-180 2.98e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512  34 SISSRHVLLQEEVAELQGQVQRTEVARGRLEKRNSDLLL--LVDTHKKQIDQKEADYGRLSSRL---------------Q 96
Cdd:COG3206   223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYtpnhpdvialraqiaA 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512  97 AKEGLGKRCEDDKVKLQNNISYQMADIHHLKEQLAELRQEFLRQEDQLQDYRK-NNTYLVKRLEYESFQcgQQIKELRAQ 175
Cdd:COG3206   303 LRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRlEREVEVARELYESLL--QRLEEARLA 380

                  ....*
gi 1907140512 176 HEENI 180
Cdd:COG3206   381 EALTV 385
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
42-190 3.32e-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: 38.75  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512  42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQ----AKE--GLGKRCE---DDKVKL 112
Cdd:COG1579    29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnNKEyeALQKEIEslkRRISDL 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907140512 113 QNNISYQMADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEyesfqcgQQIKELRAQHEENIKKLADQFLQE 190
Cdd:COG1579   109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE-------AELEELEAEREELAAKIPPELLAL 179
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
42-193 3.54e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512  42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAKEGLGKRCEDDKVKLQNNISYQMA 121
Cdd:COG1196   286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907140512 122 DIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEYESFQCgQQIKELRAQHEENIKKLADQFLQEQKE 193
Cdd:COG1196   366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE-EALLERLERLEEELEELEEALAELEEE 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
34-187 3.55e-03

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: 39.65  E-value: 3.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512   34 SISSRHVLLQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAKEGLGKRCEDDKVKLQ 113
Cdd:TIGR02168  800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907140512  114 NNISYQMADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEyesfQCGQQIKELRAQHEENIKKLADQF 187
Cdd:TIGR02168  880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA----QLELRLEGLEVRIDNLQERLSEEY 949
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
121-200 4.35e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 38.82  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512 121 ADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEYESFQCGQQ----IKELRAQHEENIKKLADQFLQEQKETHK 196
Cdd:pfam03961 149 VDFPELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQLPPEKREqlekLLETKNKLSEELEELEEELKELKEELES 228

                  ....
gi 1907140512 197 IQSN 200
Cdd:pfam03961 229 LLGE 232
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
42-193 8.51e-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: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512  42 LQEEVAELQGQVQRTEVARGRLEKRN---------SDLLLLVDTHKKQIDQKEADYGRLSSRLQAKEGLGKRCEDDKVKL 112
Cdd:COG3206   180 LEEQLPELRKELEEAEAALEEFRQKNglvdlseeaKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140512 113 QNNISYQM--ADIHHLKEQLAELRQEFLRQ-------EDQLQDYRKNNTYLVKRL------EYESFQcgQQIKELRAQhE 177
Cdd:COG3206   260 LQSPVIQQlrAQLAELEAELAELSARYTPNhpdvialRAQIAALRAQLQQEAQRIlasleaELEALQ--AREASLQAQ-L 336
                         170
                  ....*....|....*.
gi 1907140512 178 ENIKKLADQFLQEQKE 193
Cdd:COG3206   337 AQLEARLAELPELEAE 352
 
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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