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Conserved domains on  [gi|1063741477|ref|NP_001331530|]
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inner centromere protein, ARK-binding region protein [Arabidopsis thaliana]

Protein Classification

tolA_full and INCENP_ARK-bind domain-containing protein( domain architecture ID 11495112)

tolA_full and INCENP_ARK-bind domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1438-1615 2.91e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


:

Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 48.30  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1438 VQQQKPAPALITGKRDVKVKALE----AAEASKRIAEQKENDRKLKKEAMKLeRAKQEQENlkkqeiekkkkeedrkkke 1513
Cdd:TIGR02794   73 LEQQAEEAEKQRAAEQARQKELEqraaAEKAAKQAEQAAKQAEEKQKQAEEA-KAKQAAEA------------------- 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1514 aemawkqemekKKKEEERKRKEFEmADRKRQREEEDKrLKEAKKRQRIADFQRQQREADEKLQAEKELKRQAMDARIKA- 1592
Cdd:TIGR02794  133 -----------KAKAEAEAERKAK-EEAAKQAEEEAK-AKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAe 199

                          170       180
                   ....*....|....*....|...
gi 1063741477 1593 QKELKEDQNNAEKTRQANSRIPA 1615
Cdd:TIGR02794  200 AAKAKAAAEAAAKAEAEAAAAAA 222
INCENP_ARK-bind super family cl04337
Inner centromere protein, ARK binding region; This region of the inner centromere protein has ...
 1685-1721 1.17e-03

Inner centromere protein, ARK binding region; This region of the inner centromere protein has been found to be necessary and sufficient for binding to aurora-related kinase. This interaction has been implicated in the coordination of chromosome segregation with cell division in yeast.


The actual alignment was detected with superfamily member pfam03941:

Pssm-ID: 461100 [Multi-domain]  Cd Length: 53  Bit Score: 38.33  E-value: 1.17e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1063741477 1685 KKFAPTWASKSNVRLAVISQQNIDPDVTFPAKSACDI 1721
Cdd:pfam03941   13 RKPVPSWAQSPNLRQALIRQEPIDPDEIFGPIPPLNL 49
 
Name Accession Description Interval E-value
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1438-1615 2.91e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 48.30  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1438 VQQQKPAPALITGKRDVKVKALE----AAEASKRIAEQKENDRKLKKEAMKLeRAKQEQENlkkqeiekkkkeedrkkke 1513
Cdd:TIGR02794   73 LEQQAEEAEKQRAAEQARQKELEqraaAEKAAKQAEQAAKQAEEKQKQAEEA-KAKQAAEA------------------- 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1514 aemawkqemekKKKEEERKRKEFEmADRKRQREEEDKrLKEAKKRQRIADFQRQQREADEKLQAEKELKRQAMDARIKA- 1592
Cdd:TIGR02794  133 -----------KAKAEAEAERKAK-EEAAKQAEEEAK-AKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAe 199

                          170       180
                   ....*....|....*....|...
gi 1063741477 1593 QKELKEDQNNAEKTRQANSRIPA 1615
Cdd:TIGR02794  200 AAKAKAAAEAAAKAEAEAAAAAA 222
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 1538-1609 2.89e-04

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 43.88  E-value: 2.89e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063741477 1538 MADRKRQREEEdkrlKEAKKRQRIAdfQRQQREADEKLQAEKELKRQAMDARIKAQKELKEDQNNAEKTRQA 1609
Cdd:pfam09756    3 LGAKKRAKLEL----KEAKRQQREA--EEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQE 68
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1539-1656 5.39e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.65  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1539 ADRKRQREEEDKRLKEAKK---RQRIADFQRQQREADEKLQAEKELKRQAMDARIKAQKElKEDQNNAEKTRQANSRIPA 1615
Cdd:COG3064     88 EAEKKAAAEKAKAAKEAEAaaaAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAE-AAAKAEAEAARAAAAAAAA 166

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1063741477 1616 VRSKSNSSDDTNASRSSRENDFKVISNPGNMSEEANMGIEE 1656
Cdd:COG3064    167 AAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAA 207
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1439-1625 5.58e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.41  E-value: 5.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1439 QQQKPAPALITGKRDVKVKALEAAEASKRIAEQKENDRKLKKEAMKLERAKQEQENLKKQEIEKKKKEEDRKKKEAEMAW 1518
Cdd:PRK09510    67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1519 KQEMEKKKKEEERKRKEFEMADRKRQREEEDKRLKEAKKR------QRIADFQRQQREADEKLQAEKELKRQA-MDARIK 1591
Cdd:PRK09510   147 AKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKaeaeaaAKAAAEAKKKAEAEAKKKAAAEAKKKAaAEAKAA 226

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1063741477 1592 AQKELKEDQNNAEKTRQANSRIPAVRSKSNSS-DD 1625
Cdd:PRK09510   227 AAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEvDD 261
INCENP_ARK-bind pfam03941
Inner centromere protein, ARK binding region; This region of the inner centromere protein has ...
 1685-1721 1.17e-03

Inner centromere protein, ARK binding region; This region of the inner centromere protein has been found to be necessary and sufficient for binding to aurora-related kinase. This interaction has been implicated in the coordination of chromosome segregation with cell division in yeast.


Pssm-ID: 461100 [Multi-domain]  Cd Length: 53  Bit Score: 38.33  E-value: 1.17e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1063741477 1685 KKFAPTWASKSNVRLAVISQQNIDPDVTFPAKSACDI 1721
Cdd:pfam03941   13 RKPVPSWAQSPNLRQALIRQEPIDPDEIFGPIPPLNL 49
ClassIIa_HDAC4_Gln-rich-N cd10162
Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This ...
 1539-1608 3.85e-03

Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 4 (HDAC4). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197398 [Multi-domain]  Cd Length: 90  Bit Score: 38.25  E-value: 3.85e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063741477 1539 ADRKRQREEEDKRLKEAKKRQR---IADFQRQQREADEKLQAE--KELKRQAMDARIKAQKELKEDQNNAEKTRQ 1608
Cdd:cd10162      3 ALREQQLQQELLALKQKQQIQRqllIAEFQRQHEQLSRQHEAQlhEHIKQQQELLAMKHQQELLEHQRKLERHRQ 77
 
Name Accession Description Interval E-value
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1438-1615 2.91e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 48.30  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1438 VQQQKPAPALITGKRDVKVKALE----AAEASKRIAEQKENDRKLKKEAMKLeRAKQEQENlkkqeiekkkkeedrkkke 1513
Cdd:TIGR02794   73 LEQQAEEAEKQRAAEQARQKELEqraaAEKAAKQAEQAAKQAEEKQKQAEEA-KAKQAAEA------------------- 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1514 aemawkqemekKKKEEERKRKEFEmADRKRQREEEDKrLKEAKKRQRIADFQRQQREADEKLQAEKELKRQAMDARIKA- 1592
Cdd:TIGR02794  133 -----------KAKAEAEAERKAK-EEAAKQAEEEAK-AKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAe 199

                          170       180
                   ....*....|....*....|...
gi 1063741477 1593 QKELKEDQNNAEKTRQANSRIPA 1615
Cdd:TIGR02794  200 AAKAKAAAEAAAKAEAEAAAAAA 222
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 1538-1609 2.89e-04

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 43.88  E-value: 2.89e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063741477 1538 MADRKRQREEEdkrlKEAKKRQRIAdfQRQQREADEKLQAEKELKRQAMDARIKAQKELKEDQNNAEKTRQA 1609
Cdd:pfam09756    3 LGAKKRAKLEL----KEAKRQQREA--EEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQE 68
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1539-1656 5.39e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.65  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1539 ADRKRQREEEDKRLKEAKK---RQRIADFQRQQREADEKLQAEKELKRQAMDARIKAQKElKEDQNNAEKTRQANSRIPA 1615
Cdd:COG3064     88 EAEKKAAAEKAKAAKEAEAaaaAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAE-AAAKAEAEAARAAAAAAAA 166

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1063741477 1616 VRSKSNSSDDTNASRSSRENDFKVISNPGNMSEEANMGIEE 1656
Cdd:COG3064    167 AAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAA 207
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1439-1625 5.58e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.41  E-value: 5.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1439 QQQKPAPALITGKRDVKVKALEAAEASKRIAEQKENDRKLKKEAMKLERAKQEQENLKKQEIEKKKKEEDRKKKEAEMAW 1518
Cdd:PRK09510    67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1519 KQEMEKKKKEEERKRKEFEMADRKRQREEEDKRLKEAKKR------QRIADFQRQQREADEKLQAEKELKRQA-MDARIK 1591
Cdd:PRK09510   147 AKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKaeaeaaAKAAAEAKKKAEAEAKKKAAAEAKKKAaAEAKAA 226

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1063741477 1592 AQKELKEDQNNAEKTRQANSRIPAVRSKSNSS-DD 1625
Cdd:PRK09510   227 AAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEvDD 261
PTZ00121 PTZ00121
MAEBL; Provisional
 1455-1656 8.44e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 8.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1455 KVKALEAAEASKRIAE-QKENDRKLKKEAMKLERAKQEQENlKKQEIEKKKKEEDRKKKEAEMAWKQEMEKKKKEEERKR 1533
Cdd:PTZ00121  1201 KAEAARKAEEERKAEEaRKAEDAKKAEAVKKAEEAKKDAEE-AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK 1279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1534 KEFEMADRKRQREEEDKRLKEAKKRQRIADFQRQQREADEKLQAEKELKRQAMDARIKAQKELKEDQNNAEKTRQANSRI 1613
Cdd:PTZ00121  1280 ADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA 1359

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1063741477 1614 PAVRSKSNSSDDTNASRSSRENDFKVISNPGNMSEEANMGIEE 1656
Cdd:PTZ00121  1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
INCENP_ARK-bind pfam03941
Inner centromere protein, ARK binding region; This region of the inner centromere protein has ...
 1685-1721 1.17e-03

Inner centromere protein, ARK binding region; This region of the inner centromere protein has been found to be necessary and sufficient for binding to aurora-related kinase. This interaction has been implicated in the coordination of chromosome segregation with cell division in yeast.


Pssm-ID: 461100 [Multi-domain]  Cd Length: 53  Bit Score: 38.33  E-value: 1.17e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1063741477 1685 KKFAPTWASKSNVRLAVISQQNIDPDVTFPAKSACDI 1721
Cdd:pfam03941   13 RKPVPSWAQSPNLRQALIRQEPIDPDEIFGPIPPLNL 49
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1460-1609 1.38e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1460 EAAEASKRIAEQKENDRKLKKEAMKLERAKQEQENLKKQEIekkkkeedrkkkeaemAWKQEMEKKKKEEERKRKEFEMA 1539
Cdd:COG4717     72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE----------------ELREELEKLEKLLQLLPLYQELE 135

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063741477 1540 DRKRQREEEDKRLKEAKKR-QRIADFQRQQREADEKL-QAEKELKRQAMDARIKAQKELKEDQNNAEKTRQA 1609
Cdd:COG4717    136 ALEAELAELPERLEELEERlEELRELEEELEELEAELaELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
PTZ00121 PTZ00121
MAEBL; Provisional
 1453-1634 2.08e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1453 DVKVKALEA--AEASKRIAEQK---ENDRKLKKEAMKLERAKQEQENLKKQEIEKKKKEEDRKKkeaemawkqemekkkk 1527
Cdd:PTZ00121  1435 EAKKKAEEAkkADEAKKKAEEAkkaEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK---------------- 1498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1528 eeerkrkefemADRKRQREEEDKRLKEAKKRQriadfqrQQREADEKLQAEKelKRQAMDARIKAQKELKEDQNNAEKTR 1607
Cdd:PTZ00121  1499 -----------ADEAKKAAEAKKKADEAKKAE-------EAKKADEAKKAEE--AKKADEAKKAEEKKKADELKKAEELK 1558

                          170       180
                   ....*....|....*....|....*..
gi 1063741477 1608 QANSRIPAVRSKSNSSDDTNASRSSRE 1634
Cdd:PTZ00121  1559 KAEEKKKAEEAKKAEEDKNMALRKAEE 1585
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1539-1600 3.27e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 3.27e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063741477 1539 ADRKRQREEEdkRLKEAKKRQRIADFQRQQREADEKLQAEKELKRQAMD---ARIKAQKELKEDQ 1600
Cdd:pfam13868  137 EEQAEWKELE--KEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEreiARLRAQQEKAQDE 199
ClassIIa_HDAC4_Gln-rich-N cd10162
Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This ...
 1539-1608 3.85e-03

Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 4 (HDAC4). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197398 [Multi-domain]  Cd Length: 90  Bit Score: 38.25  E-value: 3.85e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063741477 1539 ADRKRQREEEDKRLKEAKKRQR---IADFQRQQREADEKLQAE--KELKRQAMDARIKAQKELKEDQNNAEKTRQ 1608
Cdd:cd10162      3 ALREQQLQQELLALKQKQQIQRqllIAEFQRQHEQLSRQHEAQlhEHIKQQQELLAMKHQQELLEHQRKLERHRQ 77
PTZ00121 PTZ00121
MAEBL; Provisional
 1439-1609 4.18e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 4.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1439 QQQKPAPALITGKRDVKVKALEAAEASKRIAEQKENDRKLKKEAMKLERAKQEQENLKKQEIEKKKKEEDRKKKEAEMAW 1518
Cdd:PTZ00121  1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741477 1519 KQEMEKKKKEEERKRKE-FEMADRKRQREEEDKRLKEAKKRQRIADFQRQQREADE-KLQAEK-----ELKRQAMDARIK 1591
Cdd:PTZ00121  1419 KADEAKKKAEEKKKADEaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEaKKKAEEakkadEAKKKAEEAKKK 1498

                          170       180
                   ....*....|....*....|
gi 1063741477 1592 AQ--KELKEDQNNAEKTRQA 1609
Cdd:PTZ00121  1499 ADeaKKAAEAKKKADEAKKA 1518
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1540-1609 5.26e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 39.25  E-value: 5.26e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063741477 1540 DRKRQREEEDKRLKEAKKRQRIADfQRQQRE------ADEKLQAEKELKRQAMDARIKAQKELKEDQNNAEKTRQA 1609
Cdd:pfam05672   31 EQERLEKEEEERLRKEELRRRAEE-ERARREeearrlEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEE 105
ClassIIa_HDAC_Gln-rich-N cd10149
Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, ...
 1541-1608 6.89e-03

Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, HDAC5 and HDCA9); This superfamily consists of a glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDAC9; it is missing in HDAC7. It is referred to as the glutamine-rich domain, and confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors. This domain is able to repress transcription independently of the HDAC's C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197397 [Multi-domain]  Cd Length: 90  Bit Score: 37.75  E-value: 6.89e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063741477 1541 RKRQREEEDKRLKEAKKRQR---IADFQRQQREADEKLQAE--KELKRQAMDARIKAQKELKEDQNNAEKTRQ 1608
Cdd:cd10149      5 REQQLQQELLALKQQQQIQKqllIAEFQKQHENLTRQHEAQlqEHIKQQQEMLAIKQQQELLEKQRKLEQQRQ 77
 
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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