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Conserved domains on  [gi|1387253741|ref|XP_024843393|]
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EF-hand calcium-binding domain-containing protein 4A isoform X3 [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]; ...
 126-364 2.89e-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: 59.18  E-value: 2.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 126 VEEDEELLSSALEQLG--VARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRESEHQ 203
Cdd:COG1196   237 LEAELEELEAELEELEaeLEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 204 REvrclyeemeQQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLA 283
Cdd:COG1196   317 RL---------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 284 NEALRTQLEGVQEQLRRLEGDAQGRREQAQRDVVAVSRNMQKEKLSLLRQLELLRELNTRLRDERDVCEAQRLGSSRRKA 363
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                  .
gi 1387253741 364 L 364
Cdd:COG1196   468 L 468
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4-93 2.84e-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: 52.10  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741   4 APGAGEAQEEEgWEHGRTSGPLATMLEQAQELFLLCDKEAKGFITRHDLQGLQSDLPLTPEQLEAVFESLDQAHTGFLTA 83
Cdd:COG5126    44 TDGDGRISREE-FVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISF 122

                          90
                  ....*....|
gi 1387253741  84 REFCLGLGKF 93
Cdd:COG5126   123 EEFVAAVRDY 132
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 126-364 2.89e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 2.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 126 VEEDEELLSSALEQLG--VARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRESEHQ 203
Cdd:COG1196   237 LEAELEELEAELEELEaeLEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 204 REvrclyeemeQQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLA 283
Cdd:COG1196   317 RL---------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 284 NEALRTQLEGVQEQLRRLEGDAQGRREQAQRDVVAVSRNMQKEKLSLLRQLELLRELNTRLRDERDVCEAQRLGSSRRKA 363
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                  .
gi 1387253741 364 L 364
Cdd:COG1196   468 L 468
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4-93 2.84e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.10  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741   4 APGAGEAQEEEgWEHGRTSGPLATMLEQAQELFLLCDKEAKGFITRHDLQGLQSDLPLTPEQLEAVFESLDQAHTGFLTA 83
Cdd:COG5126    44 TDGDGRISREE-FVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISF 122

                          90
                  ....*....|
gi 1387253741  84 REFCLGLGKF 93
Cdd:COG5126   123 EEFVAAVRDY 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 127-344 3.66e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 3.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  127 EEDEELLSSALEQLGVARVLGEQQAIRALWTRLQRERPELLG---SFEDVLMRASACLEEAARERDGLEHALRRRESEHQ 203
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAeieELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  204 revrclyeemeqQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLA 283
Cdd:TIGR02168  800 ------------ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387253741  284 NEALRTQLEGVQEQLRRLEGD---AQGRREQAQRDVVAVSRNMQKEKLSLLRQLELLRELNTRL 344
Cdd:TIGR02168  868 IEELESELEALLNERASLEEAlalLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
PRK12309 PRK12309
transaldolase;
32-91 9.92e-06

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 47.42  E-value: 9.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  32 AQELFLLCDKEAKGFITRHDLQGlqSDlpltpeqleAVFESLDQAHTGFLTAREFCLGLG 91
Cdd:PRK12309  336 AQEIFRLYDLDGDGFITREEWLG--SD---------AVFDALDLNHDGKITPEEMRAGLG 384
PTZ00121 PTZ00121
MAEBL; Provisional
 182-315 4.74e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 4.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  182 EEAARERDGLEHALRRRESEHQREVRCLYEEMEQQLREQRQRLRgQGLPQEERRGRLElelQSREQELERAGLRQRELEQ 261
Cdd:PTZ00121  1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAE---ELKKAEEEKKKVEQLKKKE 1642

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1387253741  262 QLQARTSEQLEAQAQNAQLWLANEALRTQLEGVQ-EQLRRLEGDAQGRREQAQRD 315
Cdd:PTZ00121  1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaEEAKKAEEDEKKAAEALKKE 1697
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 157-319 1.01e-03

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: 41.28  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 157 TRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRESEH------------QREVRCLYEEMEQQLREQRQRL 224
Cdd:pfam09731 294 REIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVraadeaqlrlefEREREEIRESYEEKLRTELERQ 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 225 RgqglpqEERRGRLELELQSREQELERAGLRQ-----------------------RELEQQLQARTSEQLEA-QAQnaQL 280
Cdd:pfam09731 374 A------EAHEEHLKDVLVEQEIELQREFLQDikekveeeragrllklnellanlKGLEKATSSHSEVEDENrKAQ--QL 445

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1387253741 281 WLANEALRTQLEgvqeqlrrlEGDAQGRREQAQRDVVAV 319
Cdd:pfam09731 446 WLAVEALRSTLE---------DGSADSRPRPLVRELKAL 475
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 33-90 4.98e-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: 4.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  33 QELFLLCDKEAKGFITRHDLQG--LQSDLPltPEQLEAVFESLDQAHTGFLTAREFCLGL 90
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]; ...
 126-364 2.89e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 2.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 126 VEEDEELLSSALEQLG--VARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRESEHQ 203
Cdd:COG1196   237 LEAELEELEAELEELEaeLEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 204 REvrclyeemeQQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLA 283
Cdd:COG1196   317 RL---------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 284 NEALRTQLEGVQEQLRRLEGDAQGRREQAQRDVVAVSRNMQKEKLSLLRQLELLRELNTRLRDERDVCEAQRLGSSRRKA 363
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                  .
gi 1387253741 364 L 364
Cdd:COG1196   468 L 468
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4-93 2.84e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.10  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741   4 APGAGEAQEEEgWEHGRTSGPLATMLEQAQELFLLCDKEAKGFITRHDLQGLQSDLPLTPEQLEAVFESLDQAHTGFLTA 83
Cdd:COG5126    44 TDGDGRISREE-FVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISF 122

                          90
                  ....*....|
gi 1387253741  84 REFCLGLGKF 93
Cdd:COG5126   123 EEFVAAVRDY 132
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 127-315 6.25e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 6.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 127 EEDEELLSSALEQLGVARVLGEQQAIRAlwtRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRESEHQREV 206
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELE---ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 207 RCLYEEMEQQLREQRQRLRGQGLpqEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANEA 286
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEAL--LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467

                         170       180
                  ....*....|....*....|....*....
gi 1387253741 287 LRTQLEGVQEQLRRLEGDAQGRREQAQRD 315
Cdd:COG1196   468 LLEEAALLEAALAELLEELAEAAARLLLL 496
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 127-327 8.87e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 8.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 127 EEDEELLSSALEQLgvARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRESEHQREV 206
Cdd:COG1196   301 EQDIARLEERRREL--EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 207 RCLYEEMEQQLREQRQRLRgqglpQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANEA 286
Cdd:COG1196   379 EELEELAEELLEALRAAAE-----LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1387253741 287 LRTQLEGVQEQLRRLEGDAQGRREQAQRDVVAVSRNMQKEK 327
Cdd:COG1196   454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 127-344 3.66e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 3.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  127 EEDEELLSSALEQLGVARVLGEQQAIRALWTRLQRERPELLG---SFEDVLMRASACLEEAARERDGLEHALRRRESEHQ 203
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAeieELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  204 revrclyeemeqQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLA 283
Cdd:TIGR02168  800 ------------ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387253741  284 NEALRTQLEGVQEQLRRLEGD---AQGRREQAQRDVVAVSRNMQKEKLSLLRQLELLRELNTRL 344
Cdd:TIGR02168  868 IEELESELEALLNERASLEEAlalLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
123-317 4.69e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 4.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  123 GGSVEEDEELLSSALEQLgvARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACL--EEAARERDGLEHALRRRES 200
Cdd:COG4913    605 GFDNRAKLAALEAELAEL--EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDA 682

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  201 EHQrEVRclyeemeqQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQL 280
Cdd:COG4913    683 SSD-DLA--------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1387253741  281 WLANEALRTQLEGVQEQLRRLEGDAQGRREQAQRDVV 317
Cdd:COG4913    754 RFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790
PRK12309 PRK12309
transaldolase;
32-91 9.92e-06

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 47.42  E-value: 9.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  32 AQELFLLCDKEAKGFITRHDLQGlqSDlpltpeqleAVFESLDQAHTGFLTAREFCLGLG 91
Cdd:PRK12309  336 AQEIFRLYDLDGDGFITREEWLG--SD---------AVFDALDLNHDGKITPEEMRAGLG 384
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 93-302 1.13e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  93 FVGAEATAGALPSRAPEETFESGWLDVQGAGGSVEEDEELLSSALEQLGVARVLGEQQAIRALWTRLQRERPELLGSFED 172
Cdd:COG1196   576 FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEG 655

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 173 VLMRASACLEEAARERDGLEHALRRRESEHQREVRCLYEEMEQQLREQRQRLRgqglpQEERRGRLELELQSREQELERA 252
Cdd:COG1196   656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE-----LAEAEEERLEEELEEEALEEQL 730

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1387253741 253 GLRQRELEQQLQARTSEQLEAQAQNAQLWLANEALRTQLEGVQEQLRRLE 302
Cdd:COG1196   731 EAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
130-321 2.62e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 2.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  130 EELLSSALEQLGV-ARVLGEQQAIRALWTRLQRERPELLGSfedVLMRASACLEEAARERDGLEHALRRREsEHQREVRC 208
Cdd:COG4913    241 HEALEDAREQIELlEPIRELAERYAAARERLAELEYLRAAL---RLWFAQRRLELLEAELEELRAELARLE-AELERLEA 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  209 LYEEMEQQLREQRQRLRGQGLPQ----EERRGRLELELQSREQELERAGLRQRELEQQLQArTSEQLEAQAQNAQlwlan 284
Cdd:COG4913    317 RLDALREELDELEAQIRGNGGDRleqlEREIERLERELEERERRRARLEALLAALGLPLPA-SAEEFAALRAEAA----- 390

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1387253741  285 eALRTQLEGVQEQLRRLEGDAQGRREQAQRDVVAVSR 321
Cdd:COG4913    391 -ALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 126-327 3.11e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 3.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  126 VEEDEELLSSALEQLGVARvlGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHaLRRRESEHQRE 205
Cdd:TIGR02169  697 LRRIENRLDELSQELSDAS--RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE-LEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  206 VrclyEEMEQQLREQRQRLRGQGLPQ--------EERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQN 277
Cdd:TIGR02169  774 L----HKLEEALNDLEARLSHSRIPEiqaelsklEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1387253741  278 AQLWLANEALRTQLEGVQEQLRRLEG---DAQGRREQAQRDVvavsRNMQKEK 327
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELEELEAalrDLESRLGDLKKER----DELEAQL 898
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
165-316 4.80e-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: 4.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  165 ELLGSFEDvLMRASACLEEAARERDGLEHALRRRESehqrevrclYEEMEQQLREQRQRLRGQGLPQEERR-GRLELELQ 243
Cdd:COG4913    229 ALVEHFDD-LERAHEALEDAREQIELLEPIRELAER---------YAAARERLAELEYLRAALRLWFAQRRlELLEAELE 298

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387253741  244 SREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLAN-EALRTQLEGVQEQLRRLEGdaqgRREQAQRDV 316
Cdd:COG4913    299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERER----RRARLEALL 368
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 126-315 1.15e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 126 VEEDEELLSSALEQLgvARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRREsehqre 205
Cdd:COG1196   346 LEEAEEELEEAEAEL--AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE------ 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 206 vrclyeemeqQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANE 285
Cdd:COG1196   418 ----------RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487

                         170       180       190
                  ....*....|....*....|....*....|
gi 1387253741 286 ALRTQLEGVQEQLRRLEGDAQGRREQAQRD 315
Cdd:COG1196   488 EAAARLLLLLEAEADYEGFLEGVKAALLLA 517
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 64-299 1.69e-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: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741   64 EQLEAVFESLDQAhtGFLTAREFCLGLGKFVGAEATAGALPSRAPEETFESGWLDVQGAGGS--VEEDEELLSSALEQLG 141
Cdd:TIGR02168  708 EELEEELEQLRKE--LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEerLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  142 -----VARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRE--SEHQREVRCLYEEME 214
Cdd:TIGR02168  786 eleaqIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelSEDIESLAAEIEELE 865

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  215 QQLREQRQRLRGQglpqEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANEALRTQLEGV 294
Cdd:TIGR02168  866 ELIEELESELEAL----LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941


                   ....*
gi 1387253741  295 QEQLR 299
Cdd:TIGR02168  942 QERLS 946
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 128-314 2.01e-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: 43.51  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  128 EDEELLSSALEQLGVARVLGEQQAIRALwTRLQRERPELlGSFEDVLMRASACLEEAARERDGLEHALRRRESEHQREVR 207
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELA-EELAELEEKL-EELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  208 CLYeemeqQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQlwLANEAL 287
Cdd:TIGR02168  387 KVA-----QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ--EELERL 459

                          170       180
                   ....*....|....*....|....*..
gi 1387253741  288 RTQLEGVQEQLRRLEGDAQGRREQAQR 314
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQ 486
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 127-313 2.91e-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: 43.12  E-value: 2.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  127 EEDEELLSSALEQLGVARVlgEQQAIRALWTRLQRERPELLGSFEDvlmrasacLEEAARERDGLEHALRRRESEHQREV 206
Cdd:TIGR02168  333 DELAEELAELEEKLEELKE--ELESLEAELEELEAELEELESRLEE--------LEEQLETLRSKVAQLELQIASLNNEI 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  207 RCLYEEMEQ-QLREQRQRLRGQGL---PQEERRGRLELELQSREQELERAGLRQRELEQQLqaRTSEQLEAQAQNAQLWL 282
Cdd:TIGR02168  403 ERLEARLERlEDRRERLQQEIEELlkkLEEAELKELQAELEELEEELEELQEELERLEEAL--EELREELEEAEQALDAA 480

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1387253741  283 ANEA--LRTQLEGVQEQLRRLEGDAQGRREQAQ 313
Cdd:TIGR02168  481 ERELaqLQARLDSLERLQENLEGFSEGVKALLK 513
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 49-312 4.61e-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: 42.35  E-value: 4.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741   49 RHDLQGLQSDLPLTPEQLEAVFESLDQAHTGFLTAREFCLGLGKFVgAEATAGALPSRAPEETFESGWLDVQGAGGSVEE 128
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI-SALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  129 DEELLSSALEQLGVARVLGEQQairalWTRLQRERPELLGSFEDvLMRASACLEEAARERDGLEHALRRRESEHQREVRC 208
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAE-----IEELEAQIEQLKEELKA-LREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  209 LYEEMEQ------QLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWL 282
Cdd:TIGR02168  836 TERRLEDleeqieELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915

                          250       260       270
                   ....*....|....*....|....*....|
gi 1387253741  283 ANEALRTQLEGVQEQLRRLEGDAQGRREQA 312
Cdd:TIGR02168  916 ELEELREKLAQLELRLEGLEVRIDNLQERL 945
PTZ00121 PTZ00121
MAEBL; Provisional
 182-315 4.74e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 4.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  182 EEAARERDGLEHALRRRESEHQREVRCLYEEMEQQLREQRQRLRgQGLPQEERRGRLElelQSREQELERAGLRQRELEQ 261
Cdd:PTZ00121  1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAE---ELKKAEEEKKKVEQLKKKE 1642

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1387253741  262 QLQARTSEQLEAQAQNAQLWLANEALRTQLEGVQ-EQLRRLEGDAQGRREQAQRD 315
Cdd:PTZ00121  1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaEEAKKAEEDEKKAAEALKKE 1697
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 156-313 5.87e-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: 42.35  E-value: 5.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  156 WTRLQRERPELLGSFEDV---LMRASACLEEAARERDGLEHALRRRESEHQREVRCLYE------EMEQQLREQRQRLRG 226
Cdd:TIGR02168  234 LEELREELEELQEELKEAeeeLEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaneisRLEQQKQILRERLAN 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  227 QGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLwlanEALRTQLEGVQEQLRRLEGDAQ 306
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL----EELESRLEELEEQLETLRSKVA 389


                   ....*..
gi 1387253741  307 GRREQAQ 313
Cdd:TIGR02168  390 QLELQIA 396
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 135-326 6.81e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 135 SALEQLGVARVLGEQQAIRALWTRLQRERPELLGSFEDVLmrasacLEEAARERDGLEHALRRRESEHQREVRCLYEEME 214
Cdd:COG1196   583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL------LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 215 QQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANEALRTQLEGV 294
Cdd:COG1196   657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1387253741 295 QEQLRRLEGDAQGRREQAQRDVVAVSRNMQKE 326
Cdd:COG1196   737 LLEELLEEEELLEEEALEELPEPPDLEELERE 768
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 157-319 1.01e-03

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: 41.28  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 157 TRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALRRRESEH------------QREVRCLYEEMEQQLREQRQRL 224
Cdd:pfam09731 294 REIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVraadeaqlrlefEREREEIRESYEEKLRTELERQ 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 225 RgqglpqEERRGRLELELQSREQELERAGLRQ-----------------------RELEQQLQARTSEQLEA-QAQnaQL 280
Cdd:pfam09731 374 A------EAHEEHLKDVLVEQEIELQREFLQDikekveeeragrllklnellanlKGLEKATSSHSEVEDENrKAQ--QL 445

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1387253741 281 WLANEALRTQLEgvqeqlrrlEGDAQGRREQAQRDVVAV 319
Cdd:pfam09731 446 WLAVEALRSTLE---------DGSADSRPRPLVRELKAL 475
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
64-303 1.02e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741   64 EQLEAVFESLDQAHTGFLTAREfclglgkfvgaeaTAGAL-PSRAPEETFESGWLDVQgaggsveedeellssALEQLGV 142
Cdd:COG4913    228 DALVEHFDDLERAHEALEDARE-------------QIELLePIRELAERYAAARERLA---------------ELEYLRA 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  143 ARVLGEQQAIRALWTRLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALR----RRESEHQREVrclyeEMEQQLR 218
Cdd:COG4913    280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREI-----ERLEREL 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  219 EQRQRLRGQglpQEERRGRLELELQSREQELERAglrQRELEQQLQARTSEQLEAQAQNAQLWLANEALRTQLEGVQEQL 298
Cdd:COG4913    355 EERERRRAR---LEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428


                   ....*
gi 1387253741  299 RRLEG 303
Cdd:COG4913    429 ASLER 433
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 160-315 1.49e-03

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: 40.65  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 160 QRERPELLGSFEDVLMRASACLEEAARERDGLEH---ALRRRESEHQREVRCLYEEMEQQLREQRQRLRGQGLPQEERRG 236
Cdd:pfam07888  40 LQERAELLQAQEAANRQREKEKERYKRDREQWERqrrELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 237 RLELELQS----REQELERAGLRQR--ELEQQLQARTSEQLEAQAQNAQLWLANEALRTQLEGVQEQLRRLEGDAQG-RR 309
Cdd:pfam07888 120 LLAQRAAHeariRELEEDIKTLTQRvlERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQElRN 199


                  ....*.
gi 1387253741 310 EQAQRD 315
Cdd:pfam07888 200 SLAQRD 205
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 195-272 3.14e-03

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: 37.56  E-value: 3.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387253741 195 LRRRESEHQREVrclyEEMEQQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAglrQRELEQQLQARTSEQLE 272
Cdd:pfam03938  24 LEKKFKKRQAEL----EAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQL---QQKAQQELQKKQQELLQ 94
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 211-278 3.27e-03

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: 38.28  E-value: 3.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387253741 211 EEMEQQLREQRQRL--RGQGLPQEERRgRLELELQSREQELERaglRQRELEQQLQARTSE---QLEAQAQNA 278
Cdd:COG2825    60 QKLEKELQALQEKLqkEAATLSEEERQ-KKERELQKKQQELQR---KQQEAQQDLQKRQQEllqPILEKIQKA 128
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
149-349 4.71e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 149 QQAIRALWT-RLQRERPELLGSFEDVLMRASACLEEAARERDGLEHALR--RRESEHQREVRCLYEEMEQQLREQRQRLR 225
Cdd:COG4717    40 LAFIRAMLLeRLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELREELE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 226 GqgLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANEALRTQLEGVQEQLRRLEGDA 305
Cdd:COG4717   120 K--LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1387253741 306 QGRREQAQRDVVAVSRNMQKEKLSLLRQLELLRELNTRLRDERD 349
Cdd:COG4717   198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 33-90 4.98e-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: 4.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741  33 QELFLLCDKEAKGFITRHDLQG--LQSDLPltPEQLEAVFESLDQAHTGFLTAREFCLGL 90
Cdd:cd00052     2 DQIFRSLDPDGDGLISGDEARPflGKSGLP--RSVLAQIWDLADTDKDGKLDKEEFAIAM 59
PRK09039 PRK09039
peptidoglycan -binding protein;
209-318 6.29e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.41  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 209 LYEEMEQQLREQRQRLRGQGLPQEERRGRLELELQSREQELERAGLRQRELEQQLQARTSEQLEAQAQNAQLWLANEALR 288
Cdd:PRK09039   71 LERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALR 150

                          90       100       110
                  ....*....|....*....|....*....|
gi 1387253741 289 TQLEGVQEQLrrlegDAQGRREQAQRDVVA 318
Cdd:PRK09039  151 RQLAALEAAL-----DASEKRDRESQAKIA 175
PRK12704 PRK12704
phosphodiesterase; Provisional
 176-312 7.83e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 7.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 176 RASACLEEAARErdgLEHALRRRESEHQREVRCLYEEMEQQLREQRQRLRgqglPQEERRGRLELELQSREQELERaglR 255
Cdd:PRK12704   39 EAKRILEEAKKE---AEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQ----KLEKRLLQKEENLDRKLELLEK---R 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1387253741 256 QRELEQQLQARTSEQLEAQAQNAQLwlanEALrtqlegVQEQLRRLEGDAQGRREQA 312
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEEEL----EEL------IEEQLQELERISGLTAEEA 155
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 183-316 8.19e-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: 38.57  E-value: 8.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 183 EAARERDGLEHALRRRESEHQREVRCLYEEMEQQLREQRQRLrgqglpqEERRGRlELElQSREQELERAGLRQReLEQQ 262
Cdd:pfam17380 399 EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL-------EEERAR-EME-RVRLEEQERQQQVER-LRQQ 468

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1387253741 263 LQARTSEQLEAQAQNAQLWLANEALRTQLEGVQEQLRRLEGDAQGRREQAQRDV 316
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEM 522
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
169-303 8.47e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.30  E-value: 8.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387253741 169 SFEDVLMRASACLEEAARERDGLE-HALRRRESEHQREVRCLyEEMEQQLREQRQRLRGQGLPQEERRGRLELELQSREQ 247
Cdd:COG2433   377 SIEEALEELIEKELPEEEPEAEREkEHEERELTEEEEEIRRL-EEQVERLEAEVEELEAELEEKDERIERLERELSEARS 455

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387253741 248 ELERAGLRQRELeQQLQARtseqleaqaqnaqlwlaNEALRTQLEGVQEQLRRLEG 303
Cdd:COG2433   456 EERREIRKDREI-SRLDRE-----------------IERLERELEEERERIEELKR 493
 
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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