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Conserved domains on  [gi|568952325|ref|XP_006536237|]
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EF-hand calcium-binding domain-containing protein 4A isoform X1 [Mus musculus]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 11473824)

EF-hand (EFh) domain-containing protein similar to Homo sapiens guanylyl cyclase-activating proteins (GCAP1 and GCAP2), myosin regulatory light chain proteins, (MYL2, MYL5, MYL9, MYL10, and MYL12), and Kv channel-interacting proteins (KChIP1, KChIP2 and KChIP4)

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]; ...
 168-324 3.77e-10

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: 61.88  E-value: 3.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 168 LEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLYEELEQ--QLGEQRHRRQSQNLPREEQRGHLELELQTREQ 245
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952325 246 ELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRNMQKE 324
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
21-94 4.92e-09

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.41  E-value: 4.92e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952325  21 VSARHGVEVLQQAQELFLLCDKDAKGFITRQDLQGLQSDLPLTPEQLEAVFESLDQAHTGFLTAREFCLGLGKF 94
Cdd:COG5126   59 MESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDY 132
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 168-324 3.77e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 3.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 168 LEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLYEELEQ--QLGEQRHRRQSQNLPREEQRGHLELELQTREQ 245
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952325 246 ELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRNMQKE 324
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
21-94 4.92e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.41  E-value: 4.92e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952325  21 VSARHGVEVLQQAQELFLLCDKDAKGFITRQDLQGLQSDLPLTPEQLEAVFESLDQAHTGFLTAREFCLGLGKF 94
Cdd:COG5126   59 MESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDY 132
PRK12309 PRK12309
transaldolase;
26-92 3.91e-07

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 51.66  E-value: 3.91e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952325  26 GVEVLQQAQELFLLCDKDAKGFITRQDLQGlqSDlpltpeqleAVFESLDQAHTGFLTAREFCLGLG 92
Cdd:PRK12309 329 GEAFTHAAQEIFRLYDLDGDGFITREEWLG--SD---------AVFDALDLNHDGKITPEEMRAGLG 384
EF-hand_7 pfam13499
EF-hand domain pair;
31-88 9.32e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 45.71  E-value: 9.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952325   31 QQAQELFLLCDKDAKGFITRQDL----QGLQSDLPLTPEQLEAVFESLDQAHTGFLTAREFC 88
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELkkllRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFL 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 168-322 5.89e-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: 48.51  E-value: 5.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325   168 LEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLyEELEQQLgeQRHRRQSQNLprEEQRGHLELELQTREQEL 247
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI-SALRKDL--ARLEAEVEQL--EERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325   248 ERAGLRQRELEQQLQARAAE--QLEAQAQhiQLQRAYEAIRAQLDQAQEQLSRLEGEA---QGRQEQTQRDVVAVSRNMQ 322
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEieELEAQIE--QLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLE 841
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 32-88 1.27e-05

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 42.53  E-value: 1.27e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568952325  32 QAQELFLLCDKDAKGFITRQDLQGL--QSDLPLTPEQLEAVFESLDQAHTGFLTAREFC 88
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAAlkSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
PTZ00121 PTZ00121
MAEBL; Provisional
 158-348 4.62e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  158 QRERPELLGSLEEVLMRASAcLEAAAREREGLEQALRRRESEHEREVRGLYEELEQQLGEQRHRRQSQNLPREEQRGHLE 237
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEE-AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  238 LELQTREQELERAGLRQRELEQQLQARAAEQleAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAV 317
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEA--KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568952325  318 SRNMQKEKLSLLRQLELLRELNLRLRDERDA 348
Cdd:PTZ00121 1749 AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 35-91 2.75e-03

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 36.87  E-value: 2.75e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568952325    35 ELFLLCDKDAKGFITRQDLQG--LQSDLPltPEQLEAVFESLDQAHTGFLTAREFCLGL 91
Cdd:smart00027  14 QIFRSLDKNQDGTVTGAQAKPilLKSGLP--QTLLAKIWNLADIDNDGELDKDEFALAM 70
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 236-320 3.23e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 39.33  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  236 LELELQTREQELERAGL---RQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLE-----GEAQGRQ 307
Cdd:pfam00529  63 AEAQLAKAQAQVARLQAeldRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapiGGISRES 142

                          90
                  ....*....|...
gi 568952325  308 EQTQRDVVAVSRN 320
Cdd:pfam00529 143 LVTAGALVAQAQA 155
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 168-324 3.77e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 3.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 168 LEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLYEELEQ--QLGEQRHRRQSQNLPREEQRGHLELELQTREQ 245
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952325 246 ELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRNMQKE 324
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
21-94 4.92e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.41  E-value: 4.92e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952325  21 VSARHGVEVLQQAQELFLLCDKDAKGFITRQDLQGLQSDLPLTPEQLEAVFESLDQAHTGFLTAREFCLGLGKF 94
Cdd:COG5126   59 MESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDY 132
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-325 6.51e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 6.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 158 QRERPELLGSLEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLYEELEQQLGEQRHRRQSQNlpreeQRGHLE 237
Cdd:COG1196  332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA-----QLEELE 406

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 238 LELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAV 317
Cdd:COG1196  407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486


                 ....*...
gi 568952325 318 SRNMQKEK 325
Cdd:COG1196  487 AEAAARLL 494
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 163-366 1.28e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 163 ELLGSLEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLYEELEQ--QLGEQRHRRQSQNLPREEQRGHLELEL 240
Cdd:COG1196  246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEEL 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 241 QTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRN 320
Cdd:COG1196  326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568952325 321 MQKEKLSLLRQLELLRELNLRLRDERDACETKLLGSSHRKALAIAH 366
Cdd:COG1196  406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
PRK12309 PRK12309
transaldolase;
26-92 3.91e-07

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 51.66  E-value: 3.91e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952325  26 GVEVLQQAQELFLLCDKDAKGFITRQDLQGlqSDlpltpeqleAVFESLDQAHTGFLTAREFCLGLG 92
Cdd:PRK12309 329 GEAFTHAAQEIFRLYDLDGDGFITREEWLG--SD---------AVFDALDLNHDGKITPEEMRAGLG 384
EF-hand_7 pfam13499
EF-hand domain pair;
31-88 9.32e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 45.71  E-value: 9.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952325   31 QQAQELFLLCDKDAKGFITRQDL----QGLQSDLPLTPEQLEAVFESLDQAHTGFLTAREFC 88
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELkkllRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFL 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 208-313 9.67e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 9.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 208 YEELEQQLGEQRHRRQSQnlprEEQRGHLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRA 287
Cdd:COG1196  234 LRELEAELEELEAELEEL----EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                         90       100
                 ....*....|....*....|....*.
gi 568952325 288 QLDQAQEQLSRLEGEAQGRQEQTQRD 313
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEEL 335
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 168-322 5.89e-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: 48.51  E-value: 5.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325   168 LEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLyEELEQQLgeQRHRRQSQNLprEEQRGHLELELQTREQEL 247
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI-SALRKDL--ARLEAEVEQL--EERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325   248 ERAGLRQRELEQQLQARAAE--QLEAQAQhiQLQRAYEAIRAQLDQAQEQLSRLEGEA---QGRQEQTQRDVVAVSRNMQ 322
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEieELEAQIE--QLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLE 841
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
174-320 1.25e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  174 RASACLEAAAREREGLEQALRRRESEHEREVRGLyEELEQQLGEQRHRRQSQNLPR----EEQRGHLELELQTREQELER 249
Cdd:COG4913   285 FAQRRLELLEAELEELRAELARLEAELERLEARL-DALREELDELEAQIRGNGGDRleqlEREIERLERELEERERRRAR 363

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952325  250 AGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRN 320
Cdd:COG4913   364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 32-88 1.27e-05

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 42.53  E-value: 1.27e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568952325  32 QAQELFLLCDKDAKGFITRQDLQGL--QSDLPLTPEQLEAVFESLDQAHTGFLTAREFC 88
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAAlkSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 163-309 1.49e-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: 47.37  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325   163 ELLGSLEEVLMRasacLEAAAREREGLEQALRRRESeherevrgLYEELEQQLGEQRHRRQSQNLPREEQRGHLELELQT 242
Cdd:TIGR02169  798 AELSKLEEEVSR----IEARLREIEQKLNRLTLEKE--------YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952325   243 REQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQ 309
Cdd:TIGR02169  866 LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-309 1.80e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 179 LEAAAREREGLEQALRRRESEHEREVRGLyEELEQQLGEQRHRRQSQNLpREEQRGHLELELQTREQELERAGLRQRELE 258
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERR 311

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568952325 259 QQLQARAAEqleAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQ 309
Cdd:COG1196  312 RELEERLEE---LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 207-353 2.61e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 207 LYEELEQQLGE--------QRHRRQSQNLpREEQRGHLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQL 278
Cdd:COG1196  194 ILGELERQLEPlerqaekaERYRELKEEL-KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952325 279 QRAYEAIRAQLDQAQEQLSRLEGEAQgRQEQTQRDVVAVSRNMQKEKLSLLRQLELLRELNLRLRDERDACETKL 353
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
209-311 2.89e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 45.42  E-value: 2.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 209 EELEQQLGEQRHRRQSQ--NLPREEQRGHLELELQTREQELERAGLRQRELEQQLQAR---AAEQLEAQAQHIQLQRAYE 283
Cdd:COG1566   79 TDLQAALAQAEAQLAAAeaQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYqalYKKGAVSQQELDEARAALD 158

                         90       100
                 ....*....|....*....|....*...
gi 568952325 284 AIRAQLDQAQEQLSRLEGEAQGRQEQTQ 311
Cdd:COG1566  159 AAQAQLEAAQAQLAQAQAGLREEEELAA 186
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-346 4.14e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 167 SLEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLYEELEQQLGEQRHRRQSQNLPREEQRGHLELELQTREQE 246
Cdd:COG1196  306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 247 LERAGLRQRELE-----QQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRNM 321
Cdd:COG1196  386 EELLEALRAAAElaaqlEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465

                        170       180
                 ....*....|....*....|....*
gi 568952325 322 QKEKLSLLRQLELLRELNLRLRDER 346
Cdd:COG1196  466 AELLEEAALLEAALAELLEELAEAA 490
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
179-316 5.91e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  179 LEAAAREREGLEQALRRRESEHEREvrglyEELEQQLGEQRHRRQSQNLPREEQRGHLELELQTREQELERAGLRQ---- 254
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEAL-----EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssdd 686

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952325  255 -RELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVA 316
Cdd:COG4913   687 lAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
136-313 9.77e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 9.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  136 EKLGVARVLGEQWAVRTLWVGLQRERPELLGSLEEvLMRASACLEAAAREREGLEQALrrreseherevrglyEELEQQL 215
Cdd:COG4913   645 ERREALQRLAEYSWDEIDVASAEREIAELEAELER-LDASSDDLAALEEQLEELEAEL---------------EELEEEL 708

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  216 GEQRHRRQSqnlpreeqrghLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQ 295
Cdd:COG4913   709 DELKGEIGR-----------LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDA 777

                         170
                  ....*....|....*...
gi 568952325  296 LSRLEGEAQGRQEQTQRD 313
Cdd:COG4913   778 LRARLNRAEEELERAMRA 795
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 157-313 1.96e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 157 LQRERPELLGSLEEVLMRASACLEAAAREREGLEQALRrreseherevrglyeeLEQQLGEQRHRRQSQNLPREEQRGHL 236
Cdd:COG1196  377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE----------------RLERLEEELEELEEALAELEEEEEEE 440

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952325 237 ELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRD 313
Cdd:COG1196  441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 34-91 2.47e-04

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: 39.13  E-value: 2.47e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  34 QELFLLCDKDAKGFITRQDLQG--LQSDLPltPEQLEAVFESLDQAHTGFLTAREFCLGL 91
Cdd:cd00052    2 DQIFRSLDPDGDGLISGDEARPflGKSGLP--RSVLAQIWDLADTDKDGKLDKEEFAIAM 59
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 213-325 3.34e-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: 3.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325   213 QQLGEQRHRRQSQNLPREEQRGHLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQA 292
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568952325   293 QEQLSRLegEAQGRQEQTQRDVVAVSRNMQKEK 325
Cdd:TIGR02168  315 ERQLEEL--EAQLEELESKLDELAEELAELEEK 345
PTZ00121 PTZ00121
MAEBL; Provisional
 158-348 4.62e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  158 QRERPELLGSLEEVLMRASAcLEAAAREREGLEQALRRRESEHEREVRGLYEELEQQLGEQRHRRQSQNLPREEQRGHLE 237
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEE-AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  238 LELQTREQELERAGLRQRELEQQLQARAAEQleAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAV 317
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEA--KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568952325  318 SRNMQKEKLSLLRQLELLRELNLRLRDERDA 348
Cdd:PTZ00121 1749 AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
165-319 4.98e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 4.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 165 LGSLEEVLMRASACLEAAAREREGLEQALRRRESEHEREVR-GLYEELEQQLGEQRHRRQS------------------- 224
Cdd:COG3206  221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQsPVIQQLRAQLAELEAELAElsarytpnhpdvialraqi 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 225 ----QNLPREEQRGHLELELQTREQELERAGLRQREleQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAqeqLSRLE 300
Cdd:COG3206  301 aalrAQLQQEAQRILASLEAELEALQAREASLQAQL--AQLEARLAELPELEAELRRLEREVEVARELYESL---LQRLE 375

                        170
                 ....*....|....*....
gi 568952325 301 gEAQGRQEQTQRDVVAVSR 319
Cdd:COG3206  376 -EARLAEALTVGNVRVIDP 393
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
160-312 5.87e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  160 ERPELLGSLEEV------LMRASACLEAAAREREGLEQALRRRESeherevrglYEELEQQLGEQRHRRQSQNLpreeQR 233
Cdd:COG4913   219 EEPDTFEAADALvehfddLERAHEALEDAREQIELLEPIRELAER---------YAAARERLAELEYLRAALRL----WF 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  234 GHLELELQTREQELERAglrqrELEQQLQARAAEQLEAQAQHIQLQRAYEAIR----AQLDQAQEQLSRLEGEAQGRQEQ 309
Cdd:COG4913   286 AQRRLELLEAELEELRA-----ELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERR 360


                  ...
gi 568952325  310 TQR 312
Cdd:COG4913   361 RAR 363
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 229-322 7.55e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 7.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 229 REEQRGHLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQE 308
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                         90
                 ....*....|....
gi 568952325 309 QTQRDVVAVSRNMQ 322
Cdd:COG4942  105 ELAELLRALYRLGR 118
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
239-300 7.94e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 41.19  E-value: 7.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952325 239 ELQTREQELERAGLRQRELEQQLQArAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLE 300
Cdd:COG1566  149 ELDEARAALDAAQAQLEAAQAQLAQ-AQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 236-319 1.10e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.09  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  236 LELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQlsRLEGEAQGRQEQTQRDVV 315
Cdd:PRK11448  147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEK--AAETSQERKQKRKEITDQ 224


                  ....
gi 568952325  316 AVSR 319
Cdd:PRK11448  225 AAKR 228
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 208-312 1.12e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.48  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  208 YEELEQQLGEQR---------HRRQSQNLPREEQRGHLELELQTR----EQELERAGLRQRELEQQLQARAA--EQLEAQ 272
Cdd:COG3096   521 LAELEQRLRQQQnaerlleefCQRIGQQLDAAEELEELLAELEAQleelEEQAAEAVEQRSELRQQLEQLRAriKELAAR 600

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568952325  273 AQH-IQLQRAYEAIRAQLDQA-----------QEQLSRLEGEAQGRQEQTQR 312
Cdd:COG3096   601 APAwLAAQDALERLREQSGEAladsqevtaamQQLLEREREATVERDELAAR 652
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
165-311 1.16e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 165 LGSLEEVLMRASACLEAAAREREGLEQALRRRESEHEREV--------RGLYEELEQQLGEQRHrrqsqnlpREEQRGHL 236
Cdd:COG4717   97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleaelaelPERLEELEERLEELRE--------LEEELEEL 168

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952325 237 ELELQTREQELERAGLRQRELEQQLQARAAEQLE-AQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQ 311
Cdd:COG4717  169 EAELAELQEELEELLEQLSLATEEELQDLAEELEeLQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 163-324 1.41e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 163 ELLGSLEEVLMRASACLEAAAREREGLEQALRRRESEHEREVR-GLYEELEQQLGEQRHRRQSQNLPREEQRGHLELELQ 241
Cdd:COG1196  606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREvTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 242 TREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRNM 321
Cdd:COG1196  686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765


                 ...
gi 568952325 322 QKE 324
Cdd:COG1196  766 ERE 768
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 239-312 1.49e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 1.49e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952325   239 ELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQR 312
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 139-302 1.50e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 139 GVARVLGEQWAVRTLWVGLQRERPELLGSLEEVLMRASacLEAAAREREGLEQALRRRESEHEREVRglyEELEQQLGEQ 218
Cdd:COG1196  613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT--LEGEGGSAGGSLTGGSRRELLAALLEA---EAELEELAER 687

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 219 RHRRQSQNLPREEQRGHLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIR----AQLDQAQE 294
Cdd:COG1196  688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEElpepPDLEELER 767


                 ....*...
gi 568952325 295 QLSRLEGE 302
Cdd:COG1196  768 ELERLERE 775
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
231-312 1.63e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 231 EQRGHLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQT 310
Cdd:COG4372   38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117


                 ..
gi 568952325 311 QR 312
Cdd:COG4372  118 EE 119
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 236-300 2.06e-03

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 39.93  E-value: 2.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952325 236 LELELQTREQELERAGLRQRELEQQLQ---------ARAAEQLE-AQAQHIQLQRAYEAIRAQLDQAQEQLSRLE 300
Cdd:COG0845   59 LQAALAQAQAQLAAAQAQLELAKAELErykallkkgAVSQQELDqAKAALDQAQAALAAAQAALEQARANLAYTT 133
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 35-91 2.75e-03

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 36.87  E-value: 2.75e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568952325    35 ELFLLCDKDAKGFITRQDLQG--LQSDLPltPEQLEAVFESLDQAHTGFLTAREFCLGL 91
Cdd:smart00027  14 QIFRSLDKNQDGTVTGAQAKPilLKSGLP--QTLLAKIWNLADIDNDGELDKDEFALAM 70
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 209-304 2.88e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 209 EELEQQLGEQRHRRQSQnlprEEQRGHLELELQTREQELERAGLRQRELEQQLQaraaeqlEAQAQHIQLQRAYEAIRAQ 288
Cdd:COG4942   30 EQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELA-------ALEAELAELEKEIAELRAE 98

                         90
                 ....*....|....*.
gi 568952325 289 LDQAQEQLSRLEGEAQ 304
Cdd:COG4942   99 LEAQKEELAELLRALY 114
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
208-363 3.19e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 208 YEELEQQLGEQRHRRQSQnlprEEQRGHLELELQTREQELERAGLRQR--ELEQQLQA--RAAEQLEAQAQHI-QLQRAY 282
Cdd:COG4717   90 YAELQEELEELEEELEEL----EAELEELREELEKLEKLLQLLPLYQEleALEAELAElpERLEELEERLEELrELEEEL 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 283 EAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRNMQKEKLSLLRQLELLRELNLRLRDERDACETKLLGSSHRKAL 362
Cdd:COG4717  166 EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL 245


                 .
gi 568952325 363 A 363
Cdd:COG4717  246 K 246
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 236-320 3.23e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 39.33  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  236 LELELQTREQELERAGL---RQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLE-----GEAQGRQ 307
Cdd:pfam00529  63 AEAQLAKAQAQVARLQAeldRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapiGGISRES 142

                          90
                  ....*....|...
gi 568952325  308 EQTQRDVVAVSRN 320
Cdd:pfam00529 143 LVTAGALVAQAQA 155
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 140-304 4.55e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 4.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325   140 VARVLGEQWAVRTLWVGLQRERPEL---LGSLEEVLMRASACLEAAAREREGLEQALRRreseherevrglYEELEQQLG 216
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELsrqISALRKDLARLEAEVEQLEERIAQLSKELTE------------LEAEIEELE 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325   217 EQRHRRQSQNLPREEQRGHLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQL 296
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847


                   ....*...
gi 568952325   297 SRLEGEAQ 304
Cdd:TIGR02168  848 EELSEDIE 855
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 238-313 4.71e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.37  E-value: 4.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952325 238 LELQTREQELERAGLRQRELEQQLQaraaeqlEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRD 313
Cdd:COG1579   10 LDLQELDSELDRLEHRLKELPAELA-------ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 168-325 5.19e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 38.95  E-value: 5.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325   168 LEEVLMRASACLEAAAREREGLEQalrrreseherEVRGLYEELEQQLGEQRHRRQSQNLPREEQR-------------G 234
Cdd:pfam15921  347 LEKQLVLANSELTEARTERDQFSQ-----------ESGNLDDQLQKLLADLHKREKELSLEKEQNKrlwdrdtgnsitiD 415

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325   235 HLELELQTREQELERAGLRQRELEQQLQARAAEQLEA-QAQHIQLQRAyEAIRAQLDQAQEQLSRLEGEAQGRQ---EQT 310
Cdd:pfam15921  416 HLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAiQGKNESLEKV-SSLTAQLESTKEMLRKVVEELTAKKmtlESS 494

                          170
                   ....*....|....*
gi 568952325   311 QRDVVAVSRNMQKEK 325
Cdd:pfam15921  495 ERTVSDLTASLQEKE 509
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 209-312 6.10e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 6.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325   209 EELEQQLGEQRHRR---QSQNLPREEQRGHLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAI 285
Cdd:TIGR02168  298 SRLEQQKQILRERLanlERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377

                           90       100
                   ....*....|....*....|....*..
gi 568952325   286 RAQLDQAQEQLSRLEGEAQGRQEQTQR 312
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNNEIER 404
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 209-324 6.92e-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: 38.39  E-value: 6.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325  209 EELEQQLGEQRHRRQSQNLPREEQRGHLELELQTREQELEragLRQRELEQQLQARAAEQleaQAQHIQLQRAYEAIRAQ 288
Cdd:pfam15709 351 ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIR---LRKQRLEEERQRQEEEE---RKQRLQLQAAQERARQQ 424

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568952325  289 ldqaQEQLSRLEGEAQGRQEQTQRDVVAVSRNMQKE 324
Cdd:pfam15709 425 ----QEEFRRKLQELQRKKQQEEAERAEAEKQRQKE 456
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
209-324 6.96e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.34  E-value: 6.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 209 EELEQQLGEQRHRRQSQNLPREEQRGHLE---LELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAI 285
Cdd:COG4372   62 EQLEEELEQARSELEQLEEELEELNEQLQaaqAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568952325 286 RAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRNMQKE 324
Cdd:COG4372  142 QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 168-297 7.13e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.50  E-value: 7.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325   168 LEEVLMRASACLEAAAREREGLEQALrrreseherevrglyEELEQQLGEQRHRRQSQnlprEEQRGHLELELQTREQEL 247
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELI---------------EELESELEALLNERASL----EEALALLRSELEELSEEL 903

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 568952325   248 ERAGLRQRELEQQLQaraaeqlEAQAQHIQLQRAYEAIRAQLDQAQEQLS 297
Cdd:TIGR02168  904 RELESKRSELRRELE-------ELREKLAQLELRLEGLEVRIDNLQERLS 946
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 237-320 7.75e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 7.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 237 ELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVA 316
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94


                 ....
gi 568952325 317 VSRN 320
Cdd:COG3883   95 LYRS 98
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 212-312 8.13e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 38.25  E-value: 8.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952325 212 EQQLGEQR--HRRQSQNLPREEQRGHLELELQTREQELERAglRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQL 289
Cdd:PRK09510  69 QQQKSAKRaeEQRKKKEQQQAEELQQKQAAEQERLKQLEKE--RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK 146

                         90       100
                 ....*....|....*....|...
gi 568952325 290 DQAQEQLSRLEGEAQGRQEQTQR 312
Cdd:PRK09510 147 AKAEAEAKRAAAAAKKAAAEAKK 169
 
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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