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Conserved domains on  [gi|404312698|ref|NP_001258212|]
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protein GOLM2 [Rattus norvegicus]

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 4.17e-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: 49.28  E-value: 4.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698    42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAREGLGKRCEDDKVKLQNNISYQMA 121
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404312698   122 DIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLE-YESFQCGQQIKELRAQHEENIKKLADqfLQEQKENH 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 4.17e-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: 49.28  E-value: 4.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698    42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAREGLGKRCEDDKVKLQNNISYQMA 121
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404312698   122 DIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLE-YESFQCGQQIKELRAQHEENIKKLADqfLQEQKENH 195
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEeLLKKLEEAELKELQAELEELEEELEE--LQEELERL 459
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
29-178 4.82e-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: 4.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698   29 AFNYWSISSRHVLLQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQkeADYGRLSSRLQAREGLgkrcEDD 108
Cdd:COG4913   280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG--NGGDRLEQLEREIERL----ERE 353
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698  109 KVKLQNNISYQMADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEYESFQCGQQIKELRAQHEE 178
Cdd:COG4913   354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
42-196 6.99e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 6.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698  42 LQEEVAELQGQVQrtEVARGRLEKRNSDLLLLVDTHKKQIDQKEADygrlsSRLQAREGLGKRCEDDKVKLQNNISYQMA 121
Cdd:PRK03918 568 LEEELAELLKELE--ELGFESVEELEERLKELEPFYNEYLELKDAE-----KELEREEKELKKLEEELDKAFEELAETEK 640
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404312698 122 DIHHLKEQLAELRQEFLRQEDQlqdyRKNNTYLVKRLEYESFQcgQQIKELRAQHEEnIKKLADqFLQEQKENHK 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 ...
121-196 5.95e-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: 38.44  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698  121 ADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEYESFQCGQQ----IKELRAQHEENIKKLADQF--LQEQKEN 194
Cdd:pfam03961 149 VDFPELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQLPPEKREqlekLLETKNKLSEELEELEEELkeLKEELES 228

                  ..
gi 404312698  195 HK 196
Cdd:pfam03961 229 LL 230
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
42-195 4.17e-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: 49.28  E-value: 4.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698    42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAREGLGKRCEDDKVKLQNNISYQMA 121
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404312698   122 DIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLE-YESFQCGQQIKELRAQHEENIKKLADqfLQEQKENH 195
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEeLLKKLEEAELKELQAELEELEEELEE--LQEELERL 459
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
29-178 4.82e-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: 4.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698   29 AFNYWSISSRHVLLQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQkeADYGRLSSRLQAREGLgkrcEDD 108
Cdd:COG4913   280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG--NGGDRLEQLEREIERL----ERE 353
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698  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 4.48e-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: 45.82  E-value: 4.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698    42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAREGLGKRCEDDKVK-------LQN 114
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIlrerlanLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698   115 NISYQMADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYL---VKRLEYESFQCGQQIKELRAQHEENIKKLADQFLQEQ 191
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLeaeLEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                          170
                   ....*....|
gi 404312698   192 KENHKIQSND 201
Cdd:TIGR02168  397 SLNNEIERLE 406
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
42-195 6.72e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 6.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698   42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADygrlsSRLQAREGLGKRCEDDKVKLQnnisyqma 121
Cdd:COG4913   622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-----REIAELEAELERLDASSDDLA-------- 688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698  122 dihHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEyesfQCGQQIKELRAQHEENIKK--------LADQFLQEQKE 193
Cdd:COG4913   689 ---ALEEQLEELEAELEELEEELDELKGEIGRLEKELE----QAEEELDELQDRLEAAEDLarlelralLEERFAAALGD 761

                  ..
gi 404312698  194 NH 195
Cdd:COG4913   762 AV 763
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
42-196 6.99e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 6.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698  42 LQEEVAELQGQVQrtEVARGRLEKRNSDLLLLVDTHKKQIDQKEADygrlsSRLQAREGLGKRCEDDKVKLQNNISYQMA 121
Cdd:PRK03918 568 LEEELAELLKELE--ELGFESVEELEERLKELEPFYNEYLELKDAE-----KELEREEKELKKLEEELDKAFEELAETEK 640
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404312698 122 DIHHLKEQLAELRQEFLRQEDQlqdyRKNNTYLVKRLEYESFQcgQQIKELRAQHEEnIKKLADqFLQEQKENHK 196
Cdd:PRK03918 641 RLEELRKELEELEKKYSEEEYE----ELREEYLELSRELAGLR--AELEELEKRREE-IKKTLE-KLKEELEERE 707
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
42-199 1.01e-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: 41.58  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698    42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQARE---------------------- 99
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEeriaqlskelteleaeieelee 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698   100 ------GLGKRCEDDKVKLQNNISYQMADIHHLKEQLAELRQEFlrqeDQLQDYRKNNTYLVKRLEYESFQCGQQIKELR 173
Cdd:TIGR02168  769 rleeaeEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL----TLLNEEAANLRERLESLERRIAATERRLEDLE 844
                          170       180
                   ....*....|....*....|....*....
gi 404312698   174 AQHE---ENIKKLADQFLQEQKENHKIQS 199
Cdd:TIGR02168  845 EQIEelsEDIESLAAEIEELEELIEELES 873
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
41-200 1.12e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698  41 LLQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAREGLGKRCEDDKVKLQNNISYQM 120
Cdd:COG1196  243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698 121 ADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEyESFQCGQQIKELRAQHEENIKKLADQFLQEQKENHKIQSN 200
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
42-214 1.69e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698  42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAREGLGKRCEDDKVKLQNNISYQMA 121
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698 122 DIHHLKEQLAELRQEFLRQEDQLQDYRKN-NTYLVKRLEYESFQcgQQIKELRAQHEENIKKLADQFLQEQKENHKIQSN 200
Cdd:COG1196  401 QLEELEEAEEALLERLERLEEELEELEEAlAELEEEEEEEEEAL--EEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
                        170
                 ....*....|....
gi 404312698 201 DGKELGRNDHVAPK 214
Cdd:COG1196  479 LAELLEELAEAAAR 492
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
34-180 4.15e-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: 4.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698  34 SISSRHVLLQEEVAELQGQVQRTEVARGRLEKRNSDLLL--LVDTHKKQIDQKEADYGRLSSRL---------------Q 96
Cdd:COG3206  223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYtpnhpdvialraqiaA 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698  97 AREGLGKRCEDDKVKLQNNISYQMADIHHLKEQLAELRQEFLRQEDQLQDYRK-NNTYLVKRLEYESFQcgQQIKELRAQ 175
Cdd:COG3206  303 LRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRlEREVEVARELYESLL--QRLEEARLA 380

                 ....*
gi 404312698 176 HEENI 180
Cdd:COG3206  381 EALTV 385
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
42-208 4.95e-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: 39.27  E-value: 4.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698    42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAREGLGKRCEDD-------KVKLQN 114
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQleeleskLDELAE 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698   115 NISYQMADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEYES---FQCGQQIKELRAQHEENIKKLAD------ 185
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRskvAQLELQIASLNNEIERLEARLERledrre 417
                          170       180
                   ....*....|....*....|....
gi 404312698   186 QFLQEQKE-NHKIQSNDGKELGRN 208
Cdd:TIGR02168  418 RLQQEIEElLKKLEEAELKELQAE 441
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
121-196 5.95e-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: 38.44  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698  121 ADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEYESFQCGQQ----IKELRAQHEENIKKLADQF--LQEQKEN 194
Cdd:pfam03961 149 VDFPELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQLPPEKREqlekLLETKNKLSEELEELEEELkeLKEELES 228

                  ..
gi 404312698  195 HK 196
Cdd:pfam03961 229 LL 230
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
42-193 6.16e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 6.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698  42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAREGLGKRCEDDKVKLQNNISYQMA 121
Cdd:COG1196  286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 404312698 122 DIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEYESFQCgQQIKELRAQHEENIKKLADQFLQEQKE 193
Cdd:COG1196  366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE-EALLERLERLEEELEELEEALAELEEE 436
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
42-190 9.53e-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: 37.60  E-value: 9.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312698  42 LQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQ----ARE--GLGKRCE---DDKVKL 112
Cdd:COG1579   29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnNKEyeALQKEIEslkRRISDL 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404312698 113 QNNISYQMADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEyesfqcgQQIKELRAQHEENIKKLADQFLQE 190
Cdd:COG1579  109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE-------AELEELEAEREELAAKIPPELLAL 179
 
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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