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Conserved domains on  [gi|1387253735|ref|XP_010819591|]
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EF-hand calcium-binding domain-containing protein 4A isoform X1 [Bos taurus]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 12144783)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

CATH:  1.10.238.10
Gene Ontology:  GO:0005509
PubMed:  2479149|10191494
SCOP:  3001983

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-417 1.08e-09

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: 60.72  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 179 VEEDEELLSSALEQLG--VARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRESEHQ 256
Cdd:COG1196   237 LEAELEELEAELEELEaeLEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 257 REvrclyeemeQQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLA 336
Cdd:COG1196   317 RL---------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 337 NEALRTQLEGVQEQLRRLEGDAQGRREQAQRDVVAVSRNMQKEKLSLLRQLELLRELNTRLRDERDVCEAQRLGSSRRKA 416
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                  .
gi 1387253735 417 L 417
Cdd:COG1196   468 L 468
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
57-146 1.31e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 53.26  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  57 APGAGEAQEEEgWEHGRTSGPLATMLEQAQELFLLCDKEAKGFITRHDLQGLQSDLPLTPEQLEAVFESLDQAHTGFLTA 136
Cdd:COG5126    44 TDGDGRISREE-FVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISF 122

                          90
                  ....*....|
gi 1387253735 137 REFCLGLGKF 146
Cdd:COG5126   123 EEFVAAVRDY 132
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-417 1.08e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 179 VEEDEELLSSALEQLG--VARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRESEHQ 256
Cdd:COG1196   237 LEAELEELEAELEELEaeLEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 257 REvrclyeemeQQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLA 336
Cdd:COG1196   317 RL---------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 337 NEALRTQLEGVQEQLRRLEGDAQGRREQAQRDVVAVSRNMQKEKLSLLRQLELLRELNTRLRDERDVCEAQRLGSSRRKA 416
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                  .
gi 1387253735 417 L 417
Cdd:COG1196   468 L 468
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
57-146 1.31e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 53.26  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  57 APGAGEAQEEEgWEHGRTSGPLATMLEQAQELFLLCDKEAKGFITRHDLQGLQSDLPLTPEQLEAVFESLDQAHTGFLTA 136
Cdd:COG5126    44 TDGDGRISREE-FVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISF 122

                          90
                  ....*....|
gi 1387253735 137 REFCLGLGKF 146
Cdd:COG5126   123 EEFVAAVRDY 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 180-397 1.22e-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: 51.21  E-value: 1.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  180 EEDEELLSSALEQLGVARVLGEQQAIRALWTRLQRERPELLG---SFEDVLMRASACLEEAARERDGLEHALRRRESEHQ 256
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAeieELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  257 revrclyeemeqQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLA 336
Cdd:TIGR02168  800 ------------ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387253735  337 NEALRTQLEGVQEQLRRLEGD---AQGRREQAQRDVVAVSRNMQKEKLSLLRQLELLRELNTRL 397
Cdd:TIGR02168  868 IEELESELEALLNERASLEEAlalLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
PRK12309 PRK12309
transaldolase;
85-144 9.47e-06

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 47.81  E-value: 9.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  85 AQELFLLCDKEAKGFITRHDLQGlqSDlpltpeqleAVFESLDQAHTGFLTAREFCLGLG 144
Cdd:PRK12309  336 AQEIFRLYDLDGDGFITREEWLG--SD---------AVFDALDLNHDGKITPEEMRAGLG 384
PTZ00121 PTZ00121
MAEBL; Provisional
 235-368 2.34e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  235 EEAARERDGLEHALRRRESEHQREVRCLYEEMEQQLREQRQRLRgQGLPQEERRGRLElelQSREQELERAGLRQRELEQ 314
Cdd:PTZ00121  1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAE---ELKKAEEEKKKVEQLKKKE 1642

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1387253735  315 QLQARTSEQLEAQAQNAQLWLANEALRTQLEGVQ-EQLRRLEGDAQGRREQAQRD 368
Cdd:PTZ00121  1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaEEAKKAEEDEKKAAEALKKE 1697
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 210-372 3.01e-04

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 43.21  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 210 TRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRESEH------------QREVRCLYEEMEQQLREQRQRL 277
Cdd:pfam09731 294 REIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVraadeaqlrlefEREREEIRESYEEKLRTELERQ 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 278 RgqglpqEERRGRLELELQSREQELERAGLRQ-----------------------RELEQQLQARTSEQLEA-QAQnaQL 333
Cdd:pfam09731 374 A------EAHEEHLKDVLVEQEIELQREFLQDikekveeeragrllklnellanlKGLEKATSSHSEVEDENrKAQ--QL 445

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1387253735 334 WLANEALRTQLEgvqeqlrrlEGDAQGRREQAQRDVVAV 372
Cdd:pfam09731 446 WLAVEALRSTLE---------DGSADSRPRPLVRELKAL 475
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 86-143 5.68e-03

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 35.27  E-value: 5.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  86 QELFLLCDKEAKGFITRHDLQG--LQSDLPltPEQLEAVFESLDQAHTGFLTAREFCLGL 143
Cdd:cd00052     2 DQIFRSLDPDGDGLISGDEARPflGKSGLP--RSVLAQIWDLADTDKDGKLDKEEFAIAM 59
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-417 1.08e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 179 VEEDEELLSSALEQLG--VARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRESEHQ 256
Cdd:COG1196   237 LEAELEELEAELEELEaeLEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 257 REvrclyeemeQQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLA 336
Cdd:COG1196   317 RL---------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 337 NEALRTQLEGVQEQLRRLEGDAQGRREQAQRDVVAVSRNMQKEKLSLLRQLELLRELNTRLRDERDVCEAQRLGSSRRKA 416
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                  .
gi 1387253735 417 L 417
Cdd:COG1196   468 L 468
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
57-146 1.31e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 53.26  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  57 APGAGEAQEEEgWEHGRTSGPLATMLEQAQELFLLCDKEAKGFITRHDLQGLQSDLPLTPEQLEAVFESLDQAHTGFLTA 136
Cdd:COG5126    44 TDGDGRISREE-FVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISF 122

                          90
                  ....*....|
gi 1387253735 137 REFCLGLGKF 146
Cdd:COG5126   123 EEFVAAVRDY 132
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 180-368 2.12e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 180 EEDEELLSSALEQLGVARVLGEQQAIRAlwtRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRESEHQREV 259
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELE---ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 260 RCLYEEMEQQLREQRQRLRGQGLpqEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANEA 339
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEAL--LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467

                         170       180
                  ....*....|....*....|....*....
gi 1387253735 340 LRTQLEGVQEQLRRLEGDAQGRREQAQRD 368
Cdd:COG1196   468 LLEEAALLEAALAELLEELAEAAARLLLL 496
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 180-380 3.27e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 180 EEDEELLSSALEQLgvARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRESEHQREV 259
Cdd:COG1196   301 EQDIARLEERRREL--EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 260 RCLYEEMEQQLREQRQRLRgqglpQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANEA 339
Cdd:COG1196   379 EELEELAEELLEALRAAAE-----LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1387253735 340 LRTQLEGVQEQLRRLEGDAQGRREQAQRDVVAVSRNMQKEK 380
Cdd:COG1196   454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 180-397 1.22e-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: 51.21  E-value: 1.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  180 EEDEELLSSALEQLGVARVLGEQQAIRALWTRLQRERPELLG---SFEDVLMRASACLEEAARERDGLEHALRRRESEHQ 256
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAeieELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  257 revrclyeemeqQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLA 336
Cdd:TIGR02168  800 ------------ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387253735  337 NEALRTQLEGVQEQLRRLEGD---AQGRREQAQRDVVAVSRNMQKEKLSLLRQLELLRELNTRL 397
Cdd:TIGR02168  868 IEELESELEALLNERASLEEAlalLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
176-370 1.82e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  176 GGSVEEDEELLSSALEQLgvARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACL--EEAARERDGLEHALRRRES 253
Cdd:COG4913    605 GFDNRAKLAALEAELAEL--EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDA 682

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  254 EHQrEVRclyeemeqQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQL 333
Cdd:COG4913    683 SSD-DLA--------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1387253735  334 WLANEALRTQLEGVQEQLRRLEGDAQGRREQAQRDVV 370
Cdd:COG4913    754 RFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 141-355 4.47e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 4.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 141 LGLGKFVGAEATAGALPSRAPEETFESGWLDVQGAGGSVEEDEELLSSALEQLGVARVLGEQQAIRALWTRLQRERPELL 220
Cdd:COG1196   571 AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT 650

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 221 GSFEDVLMRASACLEEAARERDGLEHALRRRESEHQREVRCLYEEMEQQLREQRQRLRgqglpQEERRGRLELELQSREQ 300
Cdd:COG1196   651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE-----LAEAEEERLEEELEEEA 725

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1387253735 301 ELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANEALRTQLEGVQEQLRRLE 355
Cdd:COG1196   726 LEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 179-380 6.07e-06

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: 48.91  E-value: 6.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  179 VEEDEELLSSALEQLGVARvlGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHaLRRRESEHQRE 258
Cdd:TIGR02169  697 LRRIENRLDELSQELSDAS--RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE-LEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  259 VrclyEEMEQQLREQRQRLRGQGLPQ--------EERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQN 330
Cdd:TIGR02169  774 L----HKLEEALNDLEARLSHSRIPEiqaelsklEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1387253735  331 AQLWLANEALRTQLEGVQEQLRRLEG---DAQGRREQAQRDVvavsRNMQKEK 380
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELEELEAalrDLESRLGDLKKER----DELEAQL 898
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
183-374 8.78e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 8.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  183 EELLSSALEQLGV-ARVLGEQQAIRALWTRLQRERPELLGSfedVLMRASACLEEAARERDGLEHALRRREsEHQREVRC 261
Cdd:COG4913    241 HEALEDAREQIELlEPIRELAERYAAARERLAELEYLRAAL---RLWFAQRRLELLEAELEELRAELARLE-AELERLEA 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  262 LYEEMEQQLREQRQRLRGQGLPQ----EERRGRLELELQSREQELERAGLRQRELEQQLQArTSEQLEAQAQNAQlwlan 337
Cdd:COG4913    317 RLDALREELDELEAQIRGNGGDRleqlEREIERLERELEERERRRARLEALLAALGLPLPA-SAEEFAALRAEAA----- 390

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1387253735  338 eALRTQLEGVQEQLRRLEGDAQGRREQAQRDVVAVSR 374
Cdd:COG4913    391 -ALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
PRK12309 PRK12309
transaldolase;
85-144 9.47e-06

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 47.81  E-value: 9.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  85 AQELFLLCDKEAKGFITRHDLQGlqSDlpltpeqleAVFESLDQAHTGFLTAREFCLGLG 144
Cdd:PRK12309  336 AQEIFRLYDLDGDGFITREEWLG--SD---------AVFDALDLNHDGKITPEEMRAGLG 384
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
218-369 1.86e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 1.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  218 ELLGSFEDvLMRASACLEEAARERDGLEHALRRRESehqrevrclYEEMEQQLREQRQRLRGQGLPQEERR-GRLELELQ 296
Cdd:COG4913    229 ALVEHFDD-LERAHEALEDAREQIELLEPIRELAER---------YAAARERLAELEYLRAALRLWFAQRRlELLEAELE 298

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387253735  297 SREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLAN-EALRTQLEGVQEQLRRLEGdaqgRREQAQRDV 369
Cdd:COG4913    299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERER----RRARLEALL 368
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-352 4.19e-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: 4.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  117 EQLEAVFESLDQAhtGFLTAREFCLGLGKFVGAEATAGALPSRAPEETFESGWLDVQGAGGS--VEEDEELLSSALEQLG 194
Cdd:TIGR02168  708 EELEEELEQLRKE--LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEerLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  195 -----VARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRE--SEHQREVRCLYEEME 267
Cdd:TIGR02168  786 eleaqIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelSEDIESLAAEIEELE 865

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  268 QQLREQRQRLRGQglpqEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANEALRTQLEGV 347
Cdd:TIGR02168  866 ELIEELESELEAL----LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941


                   ....*
gi 1387253735  348 QEQLR 352
Cdd:TIGR02168  942 QERLS 946
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-368 4.25e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 179 VEEDEELLSSALEQLgvARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRREsehqre 258
Cdd:COG1196   346 LEEAEEELEEAEAEL--AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE------ 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 259 vrclyeemeqQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANE 338
Cdd:COG1196   418 ----------RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487

                         170       180       190
                  ....*....|....*....|....*....|
gi 1387253735 339 ALRTQLEGVQEQLRRLEGDAQGRREQAQRD 368
Cdd:COG1196   488 EAAARLLLLLEAEADYEGFLEGVKAALLLA 517
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 181-367 6.18e-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: 45.43  E-value: 6.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  181 EDEELLSSALEQLGVARVLGEQQAIRALwTRLQRERPELlGSFEDVLMRASACLEEAARERDGLEHALRRRESEHQREVR 260
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELA-EELAELEEKL-EELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  261 CLYeemeqQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQlwLANEAL 340
Cdd:TIGR02168  387 KVA-----QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ--EELERL 459

                          170       180
                   ....*....|....*....|....*..
gi 1387253735  341 RTQLEGVQEQLRRLEGDAQGRREQAQR 367
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQ 486
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 180-366 6.97e-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: 45.43  E-value: 6.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  180 EEDEELLSSALEQLGVARVlgEQQAIRALWTRLQRERPELLGSFEDvlmrasacLEEAARERDGLEHALRRRESEHQREV 259
Cdd:TIGR02168  333 DELAEELAELEEKLEELKE--ELESLEAELEELEAELEELESRLEE--------LEEQLETLRSKVAQLELQIASLNNEI 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  260 RCLYEEMEQ-QLREQRQRLRGQGL---PQEERRGRLELELQSREQELERAGLRQRELEQQLqaRTSEQLEAQAQNAQLWL 335
Cdd:TIGR02168  403 ERLEARLERlEDRRERLQQEIEELlkkLEEAELKELQAELEELEEELEELQEELERLEEAL--EELREELEEAEQALDAA 480

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1387253735  336 ANEA--LRTQLEGVQEQLRRLEGDAQGRREQAQ 366
Cdd:TIGR02168  481 ERELaqLQARLDSLERLQENLEGFSEGVKALLK 513
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-365 1.35e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  102 RHDLQGLQSDLPLTPEQLEAVFESLDQAHTGFLTAREFCLGLGKFVgAEATAGALPSRAPEETFESGWLDVQGAGGSVEE 181
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI-SALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  182 DEELLSSALEQLGVARVLGEQQairalWTRLQRERPELLGSFEDvLMRASACLEEAARERDGLEHALRRRESEHQREVRC 261
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAE-----IEELEAQIEQLKEELKA-LREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  262 LYEEMEQ------QLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWL 335
Cdd:TIGR02168  836 TERRLEDleeqieELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915

                          250       260       270
                   ....*....|....*....|....*....|
gi 1387253735  336 ANEALRTQLEGVQEQLRRLEGDAQGRREQA 365
Cdd:TIGR02168  916 ELEELREKLAQLELRLEGLEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 209-366 2.04e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  209 WTRLQRERPELLGSFEDV---LMRASACLEEAARERDGLEHALRRRESEHQREVRCLYE------EMEQQLREQRQRLRG 279
Cdd:TIGR02168  234 LEELREELEELQEELKEAeeeLEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaneisRLEQQKQILRERLAN 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  280 QGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLwlanEALRTQLEGVQEQLRRLEGDAQ 359
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL----EELESRLEELEEQLETLRSKVA 389


                   ....*..
gi 1387253735  360 GRREQAQ 366
Cdd:TIGR02168  390 QLELQIA 396
PTZ00121 PTZ00121
MAEBL; Provisional
 235-368 2.34e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  235 EEAARERDGLEHALRRRESEHQREVRCLYEEMEQQLREQRQRLRgQGLPQEERRGRLElelQSREQELERAGLRQRELEQ 314
Cdd:PTZ00121  1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAE---ELKKAEEEKKKVEQLKKKE 1642

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1387253735  315 QLQARTSEQLEAQAQNAQLWLANEALRTQLEGVQ-EQLRRLEGDAQGRREQAQRD 368
Cdd:PTZ00121  1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaEEAKKAEEDEKKAAEALKKE 1697
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 210-372 3.01e-04

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 43.21  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 210 TRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRESEH------------QREVRCLYEEMEQQLREQRQRL 277
Cdd:pfam09731 294 REIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVraadeaqlrlefEREREEIRESYEEKLRTELERQ 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 278 RgqglpqEERRGRLELELQSREQELERAGLRQ-----------------------RELEQQLQARTSEQLEA-QAQnaQL 333
Cdd:pfam09731 374 A------EAHEEHLKDVLVEQEIELQREFLQDikekveeeragrllklnellanlKGLEKATSSHSEVEDENrKAQ--QL 445

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1387253735 334 WLANEALRTQLEgvqeqlrrlEGDAQGRREQAQRDVVAV 372
Cdd:pfam09731 446 WLAVEALRSTLE---------DGSADSRPRPLVRELKAL 475
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
117-356 3.11e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  117 EQLEAVFESLDQAHTGFLTAREfclglgkfvgaeaTAGAL-PSRAPEETFESGWLDVQgaggsveedeellssALEQLGV 195
Cdd:COG4913    228 DALVEHFDDLERAHEALEDARE-------------QIELLePIRELAERYAAARERLA---------------ELEYLRA 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  196 ARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALR----RRESEHQREVrclyeEMEQQLR 271
Cdd:COG4913    280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREI-----ERLEREL 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  272 EQRQRLRGQglpQEERRGRLELELQSREQELERAglrQRELEQQLQARTSEQLEAQAQNAQLWLANEALRTQLEGVQEQL 351
Cdd:COG4913    355 EERERRRAR---LEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428


                   ....*
gi 1387253735  352 RRLEG 356
Cdd:COG4913    429 ASLER 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-379 3.34e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 188 SALEQLGVARVLGEQQAIRALWTRLQRERPELLGSFEDVLmrasacLEEAARERDGLEHALRRRESEHQREVRCLYEEME 267
Cdd:COG1196   583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL------LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 268 QQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANEALRTQLEGV 347
Cdd:COG1196   657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1387253735 348 QEQLRRLEGDAQGRREQAQRDVVAVSRNMQKE 379
Cdd:COG1196   737 LLEELLEEEELLEEEALEELPEPPDLEELERE 768
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 213-368 3.72e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.57  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 213 QRERPELLGSFEDVLMRASACLEEAARERDGLEH---ALRRRESEHQREVRCLYEEMEQQLREQRQRLRGQGLPQEERRG 289
Cdd:pfam07888  40 LQERAELLQAQEAANRQREKEKERYKRDREQWERqrrELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 290 RLELELQS----REQELERAGLRQR--ELEQQLQARTSEQLEAQAQNAQLWLANEALRTQLEGVQEQLRRLEGDAQG-RR 362
Cdd:pfam07888 120 LLAQRAAHeariRELEEDIKTLTQRvlERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQElRN 199


                  ....*.
gi 1387253735 363 EQAQRD 368
Cdd:pfam07888 200 SLAQRD 205
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 248-325 7.64e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 39.48  E-value: 7.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387253735 248 LRRRESEHQREVrclyEEMEQQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAglrQRELEQQLQARTSEQLE 325
Cdd:pfam03938  24 LEKKFKKRQAEL----EAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQL---QQKAQQELQKKQQELLQ 94
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 248-331 8.72e-04

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 39.82  E-value: 8.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 248 LRRRESEHQREVrclyEEMEQQLREQRQRL--RGQGLPQEERRgRLELELQSREQELERaglRQRELEQQLQARTSE--- 322
Cdd:COG2825    48 LEKEFKKRQAEL----QKLEKELQALQEKLqkEAATLSEEERQ-KKERELQKKQQELQR---KQQEAQQDLQKRQQEllq 119


                  ....*....
gi 1387253735 323 QLEAQAQNA 331
Cdd:COG2825   120 PILEKIQKA 128
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
202-380 1.46e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 202 QQAIRALWT-RLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALR--RRESEHQREVRCLYEEMEQQLREQRQRLR 278
Cdd:COG4717    40 LAFIRAMLLeRLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELREELE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 279 GqgLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANEALRTQLEGVQEQLRRLEGDA 358
Cdd:COG4717   120 K--LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197

                         170       180
                  ....*....|....*....|..
gi 1387253735 359 QGRREQAQRDVVAVSRNMQKEK 380
Cdd:COG4717   198 AEELEELQQRLAELEEELEEAQ 219
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
268-367 1.94e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 268 QQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANEALRTQLEGV 347
Cdd:COG4372    55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134

                          90       100
                  ....*....|....*....|
gi 1387253735 348 QEQLRRLEGDAQGRREQAQR 367
Cdd:COG4372   135 EAQIAELQSEIAEREEELKE 154
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 180-366 2.91e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.93  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 180 EEDEELLSSAL------EQLGVARVLGEQQAIRALWT-RLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALR--- 249
Cdd:pfam15709 314 ERSEEDPSKALlekreqEKASRDRLRAERAEMRRLEVeRKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRlrk 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 250 -RRESEHQREVRclyEEMEQQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGL---RQRELEQQLqARTSEQLE 325
Cdd:pfam15709 394 qRLEEERQRQEE---EERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAekqRQKELEMQL-AEEQKRLM 469

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1387253735 326 AQAQNAQLwlanEALRTQLEgvQEQLRRLEGDAQGRREQAQ 366
Cdd:pfam15709 470 EMAEEERL----EYQRQKQE--AEEKARLEAEERRQKEEEA 504
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 236-416 3.44e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.72  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 236 EAARERDGLEHALRRRESEHQREVRCLYEEMEQQLREQRQRLRgqglpqeerrgrlelelQSREQELERagLRQRELEQQ 315
Cdd:pfam17380 399 EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLE-----------------EERAREMER--VRLEEQERQ 459

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 316 LQARTSEQLEAQAQNAQLWLANEAlRTQLEGVQEQLRRLEGDAQGRRE---QAQRDVVAVSRNMQKEKLSLLRQLELLRE 392
Cdd:pfam17380 460 QQVERLRQQEEERKRKKLELEKEK-RDRKRAEEQRRKILEKELEERKQamiEEERKRKLLEKEMEERQKAIYEEERRREA 538

                         170       180
                  ....*....|....*....|....
gi 1387253735 393 LNTRlRDERDVCEAQRLGSSRRKA 416
Cdd:pfam17380 539 EEER-RKQQEMEERRRIQEQMRKA 561
PRK09039 PRK09039
peptidoglycan -binding protein;
262-371 4.73e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.79  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 262 LYEEMEQQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANEALR 341
Cdd:PRK09039   71 LERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALR 150

                          90       100       110
                  ....*....|....*....|....*....|
gi 1387253735 342 TQLEGVQEQLrrlegDAQGRREQAQRDVVA 371
Cdd:PRK09039  151 RQLAALEAAL-----DASEKRDRESQAKIA 175
PRK12704 PRK12704
phosphodiesterase; Provisional
 229-365 4.92e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 229 RASACLEEAARErdgLEHALRRRESEHQREVRCLYEEMEQQLREQRQRLRgqglPQEERRGRLELELQSREQELERaglR 308
Cdd:PRK12704   39 EAKRILEEAKKE---AEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQ----KLEKRLLQKEENLDRKLELLEK---R 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1387253735 309 QRELEQQLQARTSEQLEAQAQNAQLwlanEALrtqlegVQEQLRRLEGDAQGRREQA 365
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEEEL----EEL------IEEQLQELERISGLTAEEA 155
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
222-372 5.34e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.07  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 222 SFEDVLMRASACLEEAARERDGLE-HALRRRESEHQREVRCLyEEMEQQLREQRQRLRGQGLPQEERRGRLELELQSREQ 300
Cdd:COG2433   377 SIEEALEELIEKELPEEEPEAEREkEHEERELTEEEEEIRRL-EEQVERLEAEVEELEAELEEKDERIERLERELSEARS 455

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387253735 301 ELERAGLRQRELeQQLQARTsEQLEAQAQNAQlwLANEALRTQLegvqEQLRRLegdaqgRREQAQRDVVAV 372
Cdd:COG2433   456 EERREIRKDREI-SRLDREI-ERLERELEEER--ERIEELKRKL----ERLKEL------WKLEHSGELVPV 513
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 86-143 5.68e-03

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 35.27  E-value: 5.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  86 QELFLLCDKEAKGFITRHDLQG--LQSDLPltPEQLEAVFESLDQAHTGFLTAREFCLGL 143
Cdd:cd00052     2 DQIFRSLDPDGDGLISGDEARPflGKSGLP--RSVLAQIWDLADTDKDGKLDKEEFAIAM 59
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
169-353 6.58e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 6.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 169 WLDVQGAGGSVEEDE-ELLSSALEQLGVARVLGEQQAIRALWTRLQRERPELLGsfedvlmRASACLEEAARERdgLEHA 247
Cdd:COG4717   324 LLAALGLPPDLSPEElLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA-------EAGVEDEEELRAA--LEQA 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 248 LRRRESEHQREVrcLYEEMEQQLREQRQRLRGQGLPQ-EERRGRLELELQSREQELERAGLRQRELEQQLQARTS----- 321
Cdd:COG4717   395 EEYQELKEELEE--LEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAELEAELEQLEEdgela 472

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1387253735 322 ------EQLEAQ-AQNAQLWLANEALRTQLEGVQEQLRR 353
Cdd:COG4717   473 ellqelEELKAElRELAEEWAALKLALELLEEAREEYRE 511
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
256-414 7.20e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 7.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  256 QREVRCLYEEMeQQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQR--ELEQQLQA--RTSEQLEA-QAQN 330
Cdd:COG4913    616 EAELAELEEEL-AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELERldASSDDLAAlEEQL 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735  331 AQLWLANEALRTQLEGVQEQLRRLEG---DAQGRREQAQRDVVAVSRNMQK-------EKLSLLRQLELLRELNTRLRDE 400
Cdd:COG4913    695 EELEAELEELEEELDELKGEIGRLEKeleQAEEELDELQDRLEAAEDLARLelralleERFAAALGDAVERELRENLEER 774

                          170
                   ....*....|....
gi 1387253735  401 RDVCEAQRLGSSRR 414
Cdd:COG4913    775 IDALRARLNRAEEE 788
PRK12705 PRK12705
hypothetical protein; Provisional
 249-371 8.49e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 38.54  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 249 RRRESEHQREVRCLYEEMEQQLREQRQRLRgqglPQEERRGRLELElqsreqELERAGLRQRELEQQLQARTSEQLEAQA 328
Cdd:PRK12705   36 ERILQEAQKEAEEKLEAALLEAKELLLRER----NQQRQEARRERE------ELQREEERLVQKEEQLDARAEKLDNLEN 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1387253735 329 QNAQLWLANEALRTQLEGVQEQLR-RLEGDAQGRREQAQRDVVA 371
Cdd:PRK12705  106 QLEEREKALSARELELEELEKQLDnELYRVAGLTPEQARKLLLK 149
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
199-382 8.99e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 8.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 199 LGEQQAIRALWTRLQRERPELlgsfEDVLMRASACLEEAARERDGLEHALRRRESEHQREvrclyeEMEQQLREQRQRLR 278
Cdd:COG4717    80 LKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLLPLYQELE------ALEAELAELPERLE 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253735 279 gQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAqlwlanEALRTQLEGVQEQLRRLEGDA 358
Cdd:COG4717   150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL------EELQQRLAELEEELEEAQEEL 222

                         170       180
                  ....*....|....*....|....
gi 1387253735 359 QGRREQAQRDVVAVSRNMQKEKLS 382
Cdd:COG4717   223 EELEEELEQLENELEAAALEERLK 246
 
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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