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Conserved domains on  [gi|10438288|dbj|BAB15218|]
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unnamed protein product [Homo sapiens]

Protein Classification

FapA and Grip domain-containing protein( domain architecture ID 13378395)

FapA and Grip domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
376-419 2.11e-13

GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.


:

Pssm-ID: 460221 [Multi-domain]  Cd Length: 44  Bit Score: 63.91  E-value: 2.11e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 10438288   376 GANLEYLKNIIYRFLTLPDSLGRQQTLTAILTILHFSPEEKQVI 419
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSERKQLLPVIATLLKFSPEEEQKI 44
Golgin_A5 super family cl25511
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
143-267 7.61e-07

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


The actual alignment was detected with superfamily member pfam09787:

Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 50.53  E-value: 7.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288   143 ELKQLKEEFERYKMRAQVVLKSK-----NTKDGN-----------------LGKELEAAQEQLAELKEKYISLRLSCEEL 200
Cdd:pfam09787   1 NLESAKQELADYKQKAARILQSKekliaSLKEGSgvegldsstaltleleeLRQERDLLREEIQKLRGQIQQLRTELQEL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10438288   201 EHQHQQEADDWKQELARLQ----------QLHRQELERCQLDFRdrtlKLEEELHKQRDRALAVLTEKDLELEQLRS 267
Cdd:pfam09787  81 EAQQQEEAESSREQLQELEeqlatersarREAEAELERLQEELR----YLEEELRRSKATLQSRIKDREAEIEKLRN 153
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
40-361 2.60e-04

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 2.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288  40 EKAKQ----KDQLAIQKLKERILQLDLENKTLALAASSRSPLDSHGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDV 115
Cdd:COG1196 210 EKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 116 EKLCDLEIMPSSEAADGEKATALYYQQELKQLKEEferykmraqvvLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRL 195
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEE-----------LAELEEELEELEEELEELEEELEEAEEELEEAEA 358
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 196 S---CEELEHQHQQEADDWKQELARLQQLHRQELERcQLDFRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSVALAs 272
Cdd:COG1196 359 ElaeAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE- 436
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 273 glpgRRSPVGGGGPGDPADTSSSDSLTQALQLAAANEPTFFLYAEQLARKEVEITSLRKQKHRLEVEVHQLQDRLLEEGE 352
Cdd:COG1196 437 ----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512

                ....*....
gi 10438288 353 RHREEVAAL 361
Cdd:COG1196 513 ALLLAGLRG 521
 
Name Accession Description Interval E-value
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
376-419 2.11e-13

GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.


Pssm-ID: 460221 [Multi-domain]  Cd Length: 44  Bit Score: 63.91  E-value: 2.11e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 10438288   376 GANLEYLKNIIYRFLTLPDSLGRQQTLTAILTILHFSPEEKQVI 419
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSERKQLLPVIATLLKFSPEEEQKI 44
Grip smart00755
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;
376-421 1.00e-10

golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;


Pssm-ID: 197860  Cd Length: 46  Bit Score: 56.46  E-value: 1.00e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 10438288    376 GANLEYLKNIIYRFLTLPDSLgRQQTLTAILTILHFSPEEKQVIMR 421
Cdd:smart00755   1 EANFEYLKNVLLQFLTLRESE-RETLLPVISTVLQLSPEEMQKLLE 45
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
143-267 7.61e-07

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 50.53  E-value: 7.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288   143 ELKQLKEEFERYKMRAQVVLKSK-----NTKDGN-----------------LGKELEAAQEQLAELKEKYISLRLSCEEL 200
Cdd:pfam09787   1 NLESAKQELADYKQKAARILQSKekliaSLKEGSgvegldsstaltleleeLRQERDLLREEIQKLRGQIQQLRTELQEL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10438288   201 EHQHQQEADDWKQELARLQ----------QLHRQELERCQLDFRdrtlKLEEELHKQRDRALAVLTEKDLELEQLRS 267
Cdd:pfam09787  81 EAQQQEEAESSREQLQELEeqlatersarREAEAELERLQEELR----YLEEELRRSKATLQSRIKDREAEIEKLRN 153
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
145-380 1.69e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 145 KQLKEEFERYKMRAQVV-LKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLhR 223
Cdd:COG1196 216 RELKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL-L 294
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 224 QELERCQLDfRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSvALASGLPGRRSPVGGGGPGDPADTSSSDSLTQALQ 303
Cdd:COG1196 295 AELARLEQD-IARLEERRRELEERLEELEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10438288 304 LAAANEPTFFLYAEQLARKEVEITSLRKQKHRLEvevhQLQDRLLEEGERHREEVAALQSHIEKNIRDQSREGANLE 380
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELE----EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
40-361 2.60e-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: 2.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288  40 EKAKQ----KDQLAIQKLKERILQLDLENKTLALAASSRSPLDSHGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDV 115
Cdd:COG1196 210 EKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 116 EKLCDLEIMPSSEAADGEKATALYYQQELKQLKEEferykmraqvvLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRL 195
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEE-----------LAELEEELEELEEELEELEEELEEAEEELEEAEA 358
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 196 S---CEELEHQHQQEADDWKQELARLQQLHRQELERcQLDFRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSVALAs 272
Cdd:COG1196 359 ElaeAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE- 436
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 273 glpgRRSPVGGGGPGDPADTSSSDSLTQALQLAAANEPTFFLYAEQLARKEVEITSLRKQKHRLEVEVHQLQDRLLEEGE 352
Cdd:COG1196 437 ----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512

                ....*....
gi 10438288 353 RHREEVAAL 361
Cdd:COG1196 513 ALLLAGLRG 521
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
32-347 5.61e-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: 5.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288     32 VSELLGTYEKAKQKDQLAiQKLKEriLQLDLENKTLALAASSRSPLDSHGEESSLDVNVLKDKMEKLKRLLQvaarKSQV 111
Cdd:TIGR02168  195 LNELERQLKSLERQAEKA-ERYKE--LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQ----ELEE 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288    112 TLDVEKLCDLEIMPSSEAADGEKATALYYQQELKQLKEEFERYKMRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYI 191
Cdd:TIGR02168  268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288    192 SLRLSCEELEHQHQQEADDWkQELARLQQLHRQELERCQLDFRDRTLKlEEELHKQRDRALAVLTEKDLELEQLRSVALA 271
Cdd:TIGR02168  348 ELKEELESLEAELEELEAEL-EELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEIEE 425
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10438288    272 sglpgrRSPVGGGGPGDPADTSSSDSLTQALQLAAANEPTfflyAEQLARKEVEITSLRKQKHRLEVEVHQLQDRL 347
Cdd:TIGR02168  426 ------LLKKLEEAELKELQAELEELEEELEELQEELERL----EEALEELREELEEAEQALDAAERELAQLQARL 491
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
9-200 6.33e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 38.76  E-value: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288    9 DQLRQQSQVE--------EQRVAALENQISEVSELLGTYEKAkqkdqlaIQKLKERILQLDLENKTLALAASSRSPLdsh 80
Cdd:PRK05771  60 DKLRSYLPKLnplreekkKVSVKSLEELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEPW--- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288   81 geeSSLDVnvlkdKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPS---SEAADGEKATAL------YYQQELKQLKE-E 150
Cdd:PRK05771 130 ---GNFDL-----DLSLLLGFKYVSVFVGTVPEDKLEELKLESDVEnveYISTDKGYVYVVvvvlkeLSDEVEEELKKlG 201
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 10438288  151 FERYKM----RAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEEL 200
Cdd:PRK05771 202 FERLELeeegTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY 255
PRK12704 PRK12704
phosphodiesterase; Provisional
130-228 8.60e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 8.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288  130 ADGEKATALYYQQELKQLKEEFERYKMRAQVVLKSKNTKDGNLGKELEAAQEQL----AELKEKYISLRLSCEELEHQhQ 205
Cdd:PRK12704  45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLdrklELLEKREEELEKKEKELEQK-Q 123
                         90       100
                 ....*....|....*....|...
gi 10438288  206 QEADDWKQELARLQQLHRQELER 228
Cdd:PRK12704 124 QELEKKEEELEELIEEQLQELER 146
 
Name Accession Description Interval E-value
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
376-419 2.11e-13

GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.


Pssm-ID: 460221 [Multi-domain]  Cd Length: 44  Bit Score: 63.91  E-value: 2.11e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 10438288   376 GANLEYLKNIIYRFLTLPDSLGRQQTLTAILTILHFSPEEKQVI 419
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSERKQLLPVIATLLKFSPEEEQKI 44
Grip smart00755
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;
376-421 1.00e-10

golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;


Pssm-ID: 197860  Cd Length: 46  Bit Score: 56.46  E-value: 1.00e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 10438288    376 GANLEYLKNIIYRFLTLPDSLgRQQTLTAILTILHFSPEEKQVIMR 421
Cdd:smart00755   1 EANFEYLKNVLLQFLTLRESE-RETLLPVISTVLQLSPEEMQKLLE 45
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
143-267 7.61e-07

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 50.53  E-value: 7.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288   143 ELKQLKEEFERYKMRAQVVLKSK-----NTKDGN-----------------LGKELEAAQEQLAELKEKYISLRLSCEEL 200
Cdd:pfam09787   1 NLESAKQELADYKQKAARILQSKekliaSLKEGSgvegldsstaltleleeLRQERDLLREEIQKLRGQIQQLRTELQEL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10438288   201 EHQHQQEADDWKQELARLQ----------QLHRQELERCQLDFRdrtlKLEEELHKQRDRALAVLTEKDLELEQLRS 267
Cdd:pfam09787  81 EAQQQEEAESSREQLQELEeqlatersarREAEAELERLQEELR----YLEEELRRSKATLQSRIKDREAEIEKLRN 153
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
145-380 1.69e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 145 KQLKEEFERYKMRAQVV-LKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLhR 223
Cdd:COG1196 216 RELKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL-L 294
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 224 QELERCQLDfRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSvALASGLPGRRSPVGGGGPGDPADTSSSDSLTQALQ 303
Cdd:COG1196 295 AELARLEQD-IARLEERRRELEERLEELEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10438288 304 LAAANEPTFFLYAEQLARKEVEITSLRKQKHRLEvevhQLQDRLLEEGERHREEVAALQSHIEKNIRDQSREGANLE 380
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELE----EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
171-350 5.30e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 5.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288  171 NLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQ----EADDWKQELARLQQlHRQELERCQLDFRDRTLKLEEElhk 246
Cdd:COG4913  299 ELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLER-ELEERERRRARLEALLAALGLP--- 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288  247 qrdralAVLTEKDLELEQLRSVALASGLPGRRSPVGGGGPGDPAdtsssdsltqalQLAAANEptfflyaeQLARKEVEI 326
Cdd:COG4913  375 ------LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA------------ALRDLRR--------ELRELEAEI 428
                        170       180
                 ....*....|....*....|....
gi 10438288  327 TSLRKQKHRLEVEVHQLQDRLLEE 350
Cdd:COG4913  429 ASLERRKSNIPARLLALRDALAEA 452
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
40-361 2.60e-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: 2.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288  40 EKAKQ----KDQLAIQKLKERILQLDLENKTLALAASSRSPLDSHGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDV 115
Cdd:COG1196 210 EKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 116 EKLCDLEIMPSSEAADGEKATALYYQQELKQLKEEferykmraqvvLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRL 195
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEE-----------LAELEEELEELEEELEELEEELEEAEEELEEAEA 358
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 196 S---CEELEHQHQQEADDWKQELARLQQLHRQELERcQLDFRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSVALAs 272
Cdd:COG1196 359 ElaeAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE- 436
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 273 glpgRRSPVGGGGPGDPADTSSSDSLTQALQLAAANEPTFFLYAEQLARKEVEITSLRKQKHRLEVEVHQLQDRLLEEGE 352
Cdd:COG1196 437 ----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512

                ....*....
gi 10438288 353 RHREEVAAL 361
Cdd:COG1196 513 ALLLAGLRG 521
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
13-220 1.58e-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: 40.52  E-value: 1.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288  13 QQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLdleNKTLALAASSRSPLDSHGEESSLDVNVLK 92
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL---ARRIRALEQELAALEAELAELEKEIAELR 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288  93 DKMEKLKRLLQVAARKSQVTLDVEKLcdlEIMPSSEAADGEKATALYYQQELKQLKEEFERYKmRAQVVLKSKNTKDGNL 172
Cdd:COG4942  97 AELEAQKEELAELLRALYRLGRQPPL---ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR-ADLAELAALRAELEAE 172
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 10438288 173 GKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQ 220
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
32-347 5.61e-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: 5.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288     32 VSELLGTYEKAKQKDQLAiQKLKEriLQLDLENKTLALAASSRSPLDSHGEESSLDVNVLKDKMEKLKRLLQvaarKSQV 111
Cdd:TIGR02168  195 LNELERQLKSLERQAEKA-ERYKE--LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQ----ELEE 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288    112 TLDVEKLCDLEIMPSSEAADGEKATALYYQQELKQLKEEFERYKMRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYI 191
Cdd:TIGR02168  268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288    192 SLRLSCEELEHQHQQEADDWkQELARLQQLHRQELERCQLDFRDRTLKlEEELHKQRDRALAVLTEKDLELEQLRSVALA 271
Cdd:TIGR02168  348 ELKEELESLEAELEELEAEL-EELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEIEE 425
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10438288    272 sglpgrRSPVGGGGPGDPADTSSSDSLTQALQLAAANEPTfflyAEQLARKEVEITSLRKQKHRLEVEVHQLQDRL 347
Cdd:TIGR02168  426 ------LLKKLEEAELKELQAELEELEEELEELQEELERL----EEALEELREELEEAEQALDAAERELAQLQARL 491
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
174-267 5.68e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.17  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288  174 KELEAAQEQLAELKEKYISLRlscEELEHQHQQEAD---------DWkqeLARLQQLHRQE--LERCQLDFRDRTLKLEE 242
Cdd:COG3096  292 RELFGARRQLAEEQYRLVEMA---RELEELSARESDleqdyqaasDH---LNLVQTALRQQekIERYQEDLEELTERLEE 365
                         90       100       110
                 ....*....|....*....|....*....|.
gi 10438288  243 ------ELHKQRDRALAVLTEKDLELEQLRS 267
Cdd:COG3096  366 qeevveEAAEQLAEAEARLEAAEEEVDSLKS 396
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
9-200 6.33e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 38.76  E-value: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288    9 DQLRQQSQVE--------EQRVAALENQISEVSELLGTYEKAkqkdqlaIQKLKERILQLDLENKTLALAASSRSPLdsh 80
Cdd:PRK05771  60 DKLRSYLPKLnplreekkKVSVKSLEELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEPW--- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288   81 geeSSLDVnvlkdKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPS---SEAADGEKATAL------YYQQELKQLKE-E 150
Cdd:PRK05771 130 ---GNFDL-----DLSLLLGFKYVSVFVGTVPEDKLEELKLESDVEnveYISTDKGYVYVVvvvlkeLSDEVEEELKKlG 201
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 10438288  151 FERYKM----RAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEEL 200
Cdd:PRK05771 202 FERLELeeegTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY 255
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
171-381 6.72e-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: 38.88  E-value: 6.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288    171 NLGKELEAAQEQLAELKEKYISLRLSCEELE---HQHQQEADDWKQELARLQQLHRQELERCQldfrdRTLKLEEELHKQ 247
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVE-----QLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288    248 RDRALAVLTEKDLELEQLRS--VALASGLPGRRSPVGGGGPGDPADTSSSDSLTQALQL----AAANEPTFFLYAEQLAR 321
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEelAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeAANLRERLESLERRIAA 835
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10438288    322 KEVEITSLRKQKHRLEVEVHQLQDRLLEEGERHREEVAALQSH-IEKNIRDQSREGANLEY 381
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlNERASLEEALALLRSEL 896
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
172-385 7.17e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 7.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 172 LGKELEAAQEQlAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLHRQELERCQLDFRDRTLKLEEELHKQRDRA 251
Cdd:COG1196 198 LERQLEPLERQ-AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288 252 LAVltEKDLELEQLRSVALASGLPGRRSPVGGGGPGDPADTSSSDSLTQALQLAAANEptfFLYAEQLARKEVEITSLRK 331
Cdd:COG1196 277 EEL--ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL---EELEEELEELEEELEEAEE 351
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 10438288 332 QKHRLEVEVHQLQDRLLEEGERHREEVAALQSHIEKNIRDQSREGANLEYLKNI 385
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
PRK12704 PRK12704
phosphodiesterase; Provisional
130-228 8.60e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 8.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10438288  130 ADGEKATALYYQQELKQLKEEFERYKMRAQVVLKSKNTKDGNLGKELEAAQEQL----AELKEKYISLRLSCEELEHQhQ 205
Cdd:PRK12704  45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLdrklELLEKREEELEKKEKELEQK-Q 123
                         90       100
                 ....*....|....*....|...
gi 10438288  206 QEADDWKQELARLQQLHRQELER 228
Cdd:PRK12704 124 QELEKKEEELEELIEEQLQELER 146
 
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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