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Conserved domains on  [gi|189011645|ref|NP_001121013|]
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EF-hand calcium-binding domain-containing protein 4A [Rattus norvegicus]

Protein Classification

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

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

Gene Ontology:  GO:0005509
PubMed:  2479149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
8-94 1.38e-11

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.73  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645   8 GAGQGQEEEERAGVSAGHQAEVLQQAQELFVLCDKDAKGFITRQDLQGLQSDLPLTPEQLEAVFESLDQAHTGFLTAREF 87
Cdd:COG5126   46 GDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEF 125


                 ....*..
gi 189011645  88 CLGLGKF 94
Cdd:COG5126  126 VAAVRDY 132
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 229-345 4.79e-07

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: 51.86  E-value: 4.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 229 EEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQEQ 308
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 189011645 309 TQRDVVAVSRNMQKE-KLSLLRQLELLRELNLRLRDER 345
Cdd:COG1196  381 LEELAEELLEALRAAaELAAQLEELEEAEEALLERLER 418
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
8-94 1.38e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.73  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645   8 GAGQGQEEEERAGVSAGHQAEVLQQAQELFVLCDKDAKGFITRQDLQGLQSDLPLTPEQLEAVFESLDQAHTGFLTAREF 87
Cdd:COG5126   46 GDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEF 125


                 ....*..
gi 189011645  88 CLGLGKF 94
Cdd:COG5126  126 VAAVRDY 132
EF-hand_7 pfam13499
EF-hand domain pair;
31-88 4.28e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.86  E-value: 4.28e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011645   31 QQAQELFVLCDKDAKGFITRQDL----QGLQSDLPLTPEQLEAVFESLDQAHTGFLTAREFC 88
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELkkllRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFL 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 229-345 4.79e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 4.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 229 EEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQEQ 308
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 189011645 309 TQRDVVAVSRNMQKE-KLSLLRQLELLRELNLRLRDER 345
Cdd:COG1196  381 LEELAEELLEALRAAaELAAQLEELEEAEEALLERLER 418
PRK12309 PRK12309
transaldolase;
26-92 1.25e-06

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 50.12  E-value: 1.25e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011645  26 QAEVLQQAQELFVLCDKDAKGFITRQDLQGlqSDlpltpeqleAVFESLDQAHTGFLTAREFCLGLG 92
Cdd:PRK12309 329 GEAFTHAAQEIFRLYDLDGDGFITREEWLG--SD---------AVFDALDLNHDGKITPEEMRAGLG 384
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 32-88 1.56e-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: 42.15  E-value: 1.56e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189011645  32 QAQELFVLCDKDAKGFITRQDLQGL--QSDLPLTPEQLEAVFESLDQAHTGFLTAREFC 88
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAAlkSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 229-303 7.10e-05

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 43.00  E-value: 7.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011645  229 EEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQ 303
Cdd:pfam08614  84 NEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENR 158
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 228-308 4.87e-04

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: 42.36  E-value: 4.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645   228 REEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQE 307
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931


                   .
gi 189011645   308 Q 308
Cdd:TIGR02169  932 E 932
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 226-318 5.16e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 42.25  E-value: 5.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645  226 PPREEERG--HLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQliRLEGEAQ 303
Cdd:PRK11448  136 PPEDPENLlhALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEK--AAETSQE 213

                          90
                  ....*....|....*
gi 189011645  304 GRQEQTQRDVVAVSR 318
Cdd:PRK11448  214 RKQKRKEITDQAAKR 228
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
8-94 1.38e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.73  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645   8 GAGQGQEEEERAGVSAGHQAEVLQQAQELFVLCDKDAKGFITRQDLQGLQSDLPLTPEQLEAVFESLDQAHTGFLTAREF 87
Cdd:COG5126   46 GDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEF 125


                 ....*..
gi 189011645  88 CLGLGKF 94
Cdd:COG5126  126 VAAVRDY 132
EF-hand_7 pfam13499
EF-hand domain pair;
31-88 4.28e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.86  E-value: 4.28e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011645   31 QQAQELFVLCDKDAKGFITRQDL----QGLQSDLPLTPEQLEAVFESLDQAHTGFLTAREFC 88
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELkkllRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFL 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 229-345 4.79e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 4.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 229 EEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQEQ 308
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 189011645 309 TQRDVVAVSRNMQKE-KLSLLRQLELLRELNLRLRDER 345
Cdd:COG1196  381 LEELAEELLEALRAAaELAAQLEELEEAEEALLERLER 418
PRK12309 PRK12309
transaldolase;
26-92 1.25e-06

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 50.12  E-value: 1.25e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011645  26 QAEVLQQAQELFVLCDKDAKGFITRQDLQGlqSDlpltpeqleAVFESLDQAHTGFLTAREFCLGLG 92
Cdd:PRK12309 329 GEAFTHAAQEIFRLYDLDGDGFITREEWLG--SD---------AVFDALDLNHDGKITPEEMRAGLG 384
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 229-312 2.18e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 229 EEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQEQ 308
Cdd:COG1196  252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331


                 ....
gi 189011645 309 TQRD 312
Cdd:COG1196  332 LEEL 335
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 229-311 2.67e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 229 EEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQEQ 308
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429


                 ...
gi 189011645 309 TQR 311
Cdd:COG1196  430 LAE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 157-324 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 189011645 157 QRERPELLGSLEEILMRASACLEAAARERDGLEQALRRRESEHEREVRGLYEELEQQLREQRQRRQSQNppreeERGHLE 236
Cdd:COG1196  332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA-----QLEELE 406

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 237 LELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQEQTQRDVVAV 316
Cdd:COG1196  407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486


                 ....*...
gi 189011645 317 SRNMQKEK 324
Cdd:COG1196  487 AEAAARLL 494
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 32-88 1.56e-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: 42.15  E-value: 1.56e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189011645  32 QAQELFVLCDKDAKGFITRQDLQGL--QSDLPLTPEQLEAVFESLDQAHTGFLTAREFC 88
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAAlkSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 229-303 7.10e-05

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 43.00  E-value: 7.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011645  229 EEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQ 303
Cdd:pfam08614  84 NEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENR 158
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 234-308 1.48e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.48e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011645 234 HLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQEQ 308
Cdd:COG1196  215 YRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
229-319 1.90e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645  229 EEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQEQ 308
Cdd:COG4913   344 EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423

                          90
                  ....*....|.
gi 189011645  309 TQRDVVAVSRN 319
Cdd:COG4913   424 LEAEIASLERR 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 215-347 3.25e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 215 REQRQRRQSQNPPREEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQ 294
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189011645 295 LIRLEGEAQGRQEQTQRDVVAVSRNMQKEKLSLLRQLELLRELNLRLRDERDA 347
Cdd:COG1196  395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 34-91 3.64e-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: 38.35  E-value: 3.64e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645  34 QELFVLCDKDAKGFITRQDLQG--LQSDLPltPEQLEAVFESLDQAHTGFLTAREFCLGL 91
Cdd:cd00052    2 DQIFRSLDPDGDGLISGDEARPflGKSGLP--RSVLAQIWDLADTDKDGKLDKEEFAIAM 59
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 178-323 4.84e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 4.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 178 LEAAARERDGLEQALRRRESEHEREVRGLyEELEQQLREQRQRRQSQN----------PPREEERGHLELELQTREQELE 247
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAEL-EELRLELEELELELEEAQaeeyellaelARLEQDIARLEERRRELEERLE 319

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189011645 248 RAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQEQTQRDVVAVSRNMQKE 323
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 228-308 4.87e-04

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: 42.36  E-value: 4.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645   228 REEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQE 307
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931


                   .
gi 189011645   308 Q 308
Cdd:TIGR02169  932 E 932
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 226-318 5.16e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 42.25  E-value: 5.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645  226 PPREEERG--HLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQliRLEGEAQ 303
Cdd:PRK11448  136 PPEDPENLlhALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEK--AAETSQE 213

                          90
                  ....*....|....*
gi 189011645  304 GRQEQTQRDVVAVSR 318
Cdd:PRK11448  214 RKQKRKEITDQAAKR 228
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 228-321 6.47e-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: 41.67  E-value: 6.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 228 REEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQE 307
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                         90
                 ....*....|....
gi 189011645 308 QTQRDVVAVSRNMQ 321
Cdd:COG4942  105 ELAELLRALYRLGR 118
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 238-311 1.04e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 1.04e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011645   238 ELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQEQTQR 311
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
238-299 1.97e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 40.03  E-value: 1.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011645 238 ELQTREQELERAALRQRELEQQLQArAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLE 299
Cdd:COG1566  149 ELDEARAALDAAQAQLEAAQAQLAQ-AQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
234-304 2.00e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011645  234 HLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQG 304
Cdd:COG4913   264 YAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG 334
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
235-315 2.54e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645  235 LELELQTREQELERAALRQ---RELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQEQTQR 311
Cdd:COG4913   666 AEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745


                  ....
gi 189011645  312 DVVA 315
Cdd:COG4913   746 ELRA 749
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
228-318 2.84e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 228 REEERGHLELELQTREQELERAALRQREleQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLirleGEAQGRQE 307
Cdd:COG3206  309 QEAQRILASLEAELEALQAREASLQAQL--AQLEARLAELPELEAELRRLEREVEVARELYESLLQRL----EEARLAEA 382

                         90
                 ....*....|.
gi 189011645 308 QTQRDVVAVSR 318
Cdd:COG3206  383 LTVGNVRVIDP 393
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
228-310 3.44e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 39.26  E-value: 3.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 228 REEERGHLELELQTREQELERAALRQRELEQQLQAR---AAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQG 304
Cdd:COG1566  101 RLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYqalYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLRE 180


                 ....*.
gi 189011645 305 RQEQTQ 310
Cdd:COG1566  181 EEELAA 186
PRK12704 PRK12704
phosphodiesterase; Provisional
 228-303 4.03e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 228 REEERGHLELELQTREQELER----AALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQL--------DQAQEQL 295
Cdd:PRK12704  80 RRNELQKLEKRLLQKEENLDRklelLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisgltaEEAKEIL 159


                 ....*....
gi 189011645 296 I-RLEGEAQ 303
Cdd:PRK12704 160 LeKVEEEAR 168
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-347 5.10e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 5.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 167 LEEILMRASACLEAAARERDGLEQALRRRESEHEREVRGLYEELEQQLREQRQRRQSQNPPREEERGHLELELQTREQEL 246
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 247 ERAALRQRELE--QQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQEQTQRDVVAVSRNMQKEK 324
Cdd:COG1196  380 ELEELAEELLEalRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                        170       180
                 ....*....|....*....|...
gi 189011645 325 LSLLRQLELLRELNLRLRDERDA 347
Cdd:COG1196  460 ALLELLAELLEEAALLEAALAEL 482
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
228-311 6.09e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 6.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 228 REEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEvqaqhiQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQE 307
Cdd:COG4717  154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ------DLAEELEELQQRLAELEEELEEAQEELEELEE 227


                 ....
gi 189011645 308 QTQR 311
Cdd:COG4717  228 ELEQ 231
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 229-318 8.16e-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: 38.21  E-value: 8.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 229 EEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQEQ 308
Cdd:COG4942  163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242

                         90
                 ....*....|
gi 189011645 309 TQRDVVAVSR 318
Cdd:COG4942  243 TPAAGFAALK 252
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 237-312 8.83e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.60  E-value: 8.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189011645 237 LELQTREQELERAALRQRELEQQLQaraaeqlEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQEQTQRD 312
Cdd:COG1579   10 LDLQELDSELDRLEHRLKELPAELA-------ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 235-295 8.99e-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: 37.62  E-value: 8.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011645 235 LELELQTREQELERA----ALRQRELE--QQLQAR---AAEQLEV-QAQHIQLQRAYEALRAQLDQAQEQL 295
Cdd:COG0845   59 LQAALAQAQAQLAAAqaqlELAKAELEryKALLKKgavSQQELDQaKAALDQAQAALAAAQAALEQARANL 129
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
228-311 9.19e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.96  E-value: 9.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011645 228 REEERGHLELELQTREQELERAALRQRELEQQLQARAAEQLEVQAQHIQLQRAYEALRAQLDQAQEQLIRLEGEAQGRQE 307
Cdd:COG4372   71 ARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150


                 ....
gi 189011645 308 QTQR 311
Cdd:COG4372  151 ELKE 154
 
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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