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Conserved domains on  [gi|929273847|ref|XP_014013614|]
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galactokinase isoform X1 [Salmo salar]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GalK COG0153
Galactokinase [Carbohydrate transport and metabolism];
11-370 8.69e-164

Galactokinase [Carbohydrate transport and metabolism];


:

Pssm-ID: 439923 [Multi-domain]  Cd Length: 380  Bit Score: 475.03  E-value: 8.69e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  11 LVAEARRVYEQSFGGDgPQVAVCAPGRVNLIGEHIDYNQGFVLPMALPMVTVVVGS-RTSGQsasIITAAKDVEEprRVD 89
Cdd:COG0153    1 RLERLIEAFEEAFGEE-PEGVFSAPGRVNLIGEHTDYNGGFVLPAAIDRGTYAAARpRDDRK---VRVYSADFDE--EVE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  90 FDLPNdkalLSPGK-PSWANYVKGVVQHYRA--PPVPGFRAVIASSVPLGGGLSSSASLEVAMYTFLQQLKPDDGDKVAK 166
Cdd:COG0153   75 FDLDD----LEPGEeDGWANYVRGVAWALQErgYKLGGFDLVIDGDVPLGAGLSSSAALEVAVALALNDLFGLGLDPVEL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 167 AVACQKAEHTHAGVPCGIMDQFVSVLGREAHALLIDCRSLEATPVPLSDPGLVILISNSNVKHSLTGSEYPSRRRQCEEA 246
Cdd:COG0153  151 AKIGQRAENEFVGVPCGIMDQFASALGKKGHALLLDCRSLEYEYVPLPLEGYALVIVDTNVKHSLADSEYNERRAECEAA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 247 AAILEKASLRDATLKDLEDAKSRLDDET-YRRARHVIEEIERTAQAAEALKKGAYKEFGKLMVESHNSLRDLYEVSCKEL 325
Cdd:COG0153  231 AAILGVKSLRDVTLEDLEAARARLGDEVlRRRARHVVTENQRVLEAVEALRAGDLEAFGKLMNASHASLRDDYEVSCPEL 310

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 929273847 326 DELVSAAVEVEGVFGSRMTGGGFGGCTVTLLQAEAIDRTMQNMQR 370
Cdd:COG0153  311 DTLVELALAEAGVLGARMTGGGFGGCTIALVPKDAVDEFIEAVAE 355
BTB_POZ_KCTD6_like cd18365
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 396-489 1.47e-50

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins, KCTD6, KCTD21 and similar proteins; KCTD6, also called KCASH3 (KCTD containing, Cullin3 adaptor, suppressor of Hedgehog 3), is a substrate-specific adaptor of cullin-3, effectively regulating protein levels of the muscle small ankyrin-1 isoform 5 (sAnk1.5). KCTD21, also called KCASH2, functions as a substrate-specific adaptor of cullin-3, promoting the ubiquitination and degradation of histone deacetylase HDAC1, thereby inhibiting the deacetylation-mediated transcriptional activation of the Hedgehog effectors Gli1 and Gli2. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


:

Pssm-ID: 349674 [Multi-domain]  Cd Length: 94  Bit Score: 170.65  E-value: 1.47e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 396 DPVSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRR 475
Cdd:cd18365    1 DIVNLNVGGVHYTTTLATLTRFPDSMLGAMFSGSMPTTRDDQGNYFIDRDGTLFRYILNFLRSSQLSLPEDFKEYDLLLR 80

                         90
                 ....*....|....
gi 929273847 476 EADFFQIRPLLDEI 489
Cdd:cd18365   81 EADFYQIEPLIEAL 94
KCTD11_21_C super family cl44759
BTB/POZ domain-containing protein KCTD11/21 C-terminus; This family represents the C-terminal ...
 505-674 8.66e-26

BTB/POZ domain-containing protein KCTD11/21 C-terminus; This family represents the C-terminal region of BTB/POZ domain-containing protein KCTD11 (known as REN: EGF-, NGF- and retinoic acid-responsive gene) and one homolog, a member of KCTD containing, Cullin3 adaptor, suppressor of Hedgehog (KCASH) family, KCASH2-KCTD21 protein. They share high similarity and a BTB domain responsible for oligomerization and formation of a Cullin3 ubiquitin ligase complex, specific expression in brain and cerebellum where they have a role in neuronal differentiation, and suppressor activity on acetylation-dependent Hedgehog/Gli signalling through ubiquitination and degradation of histone deacetylase 1. These proteins have been described as tumor suppressors that inhibit medulloblastoma growth by antagonizing Hedgehog signalling.


The actual alignment was detected with superfamily member pfam19329:

Pssm-ID: 466043  Cd Length: 154  Bit Score: 103.87  E-value: 8.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  505 RGAMLLVDVDCQVRVLHFNLRRAPENYELRTCSVRILTAEIFCTWRAFLVLLCERFSYrTTQGPTSPLPSD-QRHNRLKL 583
Cdd:pfam19329   2 KNAMLNISLDQKMQTVHFTVREAPQIYSLSSSTMEVFNANIFCTSGLFLKLLGSQLCY-FFNGNLSPICSElEDQNHLTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  584 EWVPRPDELPQDQYEKQQYRGLvvsdsWATQTHSgdlcdvimprcspcEVKDTRGFVEELLTVSLAEGFRVDSVTPDPMD 663
Cdd:pfam19329  81 QWVAAVEGLPEEEYTLQNLKRL-----WVFPANK--------------QINSFQAFVEEVLKIAMNDGFCMDSSHPSSLD 141

                         170
                  ....*....|.
gi 929273847  664 ILNCRTLQLVR 674
Cdd:pfam19329 142 FMNNKIIRLIR 152
 
Name Accession Description Interval E-value
GalK COG0153
Galactokinase [Carbohydrate transport and metabolism];
11-370 8.69e-164

Galactokinase [Carbohydrate transport and metabolism];


Pssm-ID: 439923 [Multi-domain]  Cd Length: 380  Bit Score: 475.03  E-value: 8.69e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  11 LVAEARRVYEQSFGGDgPQVAVCAPGRVNLIGEHIDYNQGFVLPMALPMVTVVVGS-RTSGQsasIITAAKDVEEprRVD 89
Cdd:COG0153    1 RLERLIEAFEEAFGEE-PEGVFSAPGRVNLIGEHTDYNGGFVLPAAIDRGTYAAARpRDDRK---VRVYSADFDE--EVE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  90 FDLPNdkalLSPGK-PSWANYVKGVVQHYRA--PPVPGFRAVIASSVPLGGGLSSSASLEVAMYTFLQQLKPDDGDKVAK 166
Cdd:COG0153   75 FDLDD----LEPGEeDGWANYVRGVAWALQErgYKLGGFDLVIDGDVPLGAGLSSSAALEVAVALALNDLFGLGLDPVEL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 167 AVACQKAEHTHAGVPCGIMDQFVSVLGREAHALLIDCRSLEATPVPLSDPGLVILISNSNVKHSLTGSEYPSRRRQCEEA 246
Cdd:COG0153  151 AKIGQRAENEFVGVPCGIMDQFASALGKKGHALLLDCRSLEYEYVPLPLEGYALVIVDTNVKHSLADSEYNERRAECEAA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 247 AAILEKASLRDATLKDLEDAKSRLDDET-YRRARHVIEEIERTAQAAEALKKGAYKEFGKLMVESHNSLRDLYEVSCKEL 325
Cdd:COG0153  231 AAILGVKSLRDVTLEDLEAARARLGDEVlRRRARHVVTENQRVLEAVEALRAGDLEAFGKLMNASHASLRDDYEVSCPEL 310

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 929273847 326 DELVSAAVEVEGVFGSRMTGGGFGGCTVTLLQAEAIDRTMQNMQR 370
Cdd:COG0153  311 DTLVELALAEAGVLGARMTGGGFGGCTIALVPKDAVDEFIEAVAE 355
PRK05101 PRK05101
galactokinase; Provisional
 11-362 1.42e-121

galactokinase; Provisional


Pssm-ID: 179937 [Multi-domain]  Cd Length: 382  Bit Score: 366.94  E-value: 1.42e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  11 LVAEARRVYEQSFGGDgPQVAVCAPGRVNLIGEHIDYNQGFVLPMALPMVTVVVGSRTSGQSASIITAAKDVEeprRVDF 90
Cdd:PRK05101   3 LKQKTQSLFAQQFGYP-PTHTIQAPGRVNLIGEHTDYNDGFVLPCAIDYQTVISCAKRDDRIVRVIAADYDNQ---QDEF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  91 DLpnDKALLSPGKPSWANYVKGVVQHY--RAPPVPGFRAVIASSVPLGGGLSSSASLEVAMYTFLQQLKPDDGDKVAKAV 168
Cdd:PRK05101  79 SL--DAPIVPHPEQQWANYVRGVVKHLqeRNPDFGGADLVISGNVPQGAGLSSSASLEVAVGQTFQQLYHLPLSGAEIAL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 169 ACQKAEHTHAGVPCGIMDQFVSVLGREAHALLIDCRSLEATPVPLSDpGLVILISNSNVKHSLTGSEYPSRRRQCEEAAA 248
Cdd:PRK05101 157 NGQEAENQFVGCNCGIMDQLISALGKKDHALLIDCRSLETKAVPMPE-GVAVVIINSNVKRGLVDSEYNTRRQQCETAAR 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 249 ILEKASLRDATLKDLEDAKSRLDDETYRRARHVIEEIERTAQAAEALKKGAYKEFGKLMVESHNSLRDLYEVSCKELDEL 328
Cdd:PRK05101 236 FFGVKALRDVTLEQFNAVAAELDPVVAKRARHVITENARTLEAASALAAGDLKRMGELMAESHASMRDDFEITVPQIDTL 315

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 929273847 329 VSAAVEV---EGvfGSRMTGGGFGGCTVTLLQAEAID 362
Cdd:PRK05101 316 VEIVKAVigdQG--GVRMTGGGFGGCIVALVPEELVE 350
gal_kin TIGR00131
galactokinase; Galactokinase is a member of the GHMP kinases (Galactokinase, Homoserine kinase, ...
 14-366 6.64e-113

galactokinase; Galactokinase is a member of the GHMP kinases (Galactokinase, Homoserine kinase, Mevalonate kinase, Phosphomevalonate kinase) and shares with them an amino-terminal domain probably related to ATP binding.The galactokinases found by this model are divided into two sets. Prokaryotic forms are generally shorter. The eukaryotic forms are longer because of additional central regions and in some cases are known to be bifunctional, with regulatory activities that are independent of galactokinase activity. [Energy metabolism, Sugars]


Pssm-ID: 272924 [Multi-domain]  Cd Length: 386  Bit Score: 344.89  E-value: 6.64e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847   14 EARRVYEQSFGgDGPQVAVCAPGRVNLIGEHIDYNQGFVLPMALPMVTVVVGSRTSGQSASIITAAKDVEEPRRvDFDLP 93
Cdd:TIGR00131   3 SIQKIFASAFG-AKPDFTARAPGRVNLIGEHTDYNDGSVLPCAIDFGTLCAVAVRDDKNVRIYLANADNKFAER-SLDLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847   94 NDKALLSpgkpSWANYVKGVVQHY--RAPPVP-GFRAVIASSVPLGGGLSSSASLEVAMYTFLQQL--KPDDGDKVAKAV 168
Cdd:TIGR00131  81 LDGSEVS----DWANYFKGVLHVAqeRFNSFPlGADIVCSGNVPTGSGLSSSAAFECAVGAVLQNMghLPLDSKQILLRI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  169 acQKAEHTHAGVPCGIMDQFVSVLGREAHALLIDCRSLEATPVPLSDPGLVILISNSNVKHSLTGSEYPSRRRQCEEAAA 248
Cdd:TIGR00131 157 --QVAENHFVGVNCGIMDQAASVLGKEDHALLVECRSLKATPFKFPQLGIAFVIANTNVKRTLAPSNYNTRRQECTTAAN 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  249 IL---EKASLRDATLKDLEDAKSRL---DDETYRRARHVIEEIERTAQAAEALKKGAYKEFGKLMVESHNSLRDLYEVSC 322
Cdd:TIGR00131 235 FLaatDKGALRDFMNEYFARYIARLtkmLPLVEERAKHVVSENLRVLKAVKAMKDNDFKQFGALMNESHASCDDDYECTC 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 929273847  323 KELDELVSAAVEVEGVFGSRMTGGGFGGCTVTLLQAEAIDRTMQ 366
Cdd:TIGR00131 315 PEIDELVCSAALVNGSGGSRMTGAGFGGCTVHLVPNENVDKVRQ 358
BTB_POZ_KCTD6_like cd18365
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 396-489 1.47e-50

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins, KCTD6, KCTD21 and similar proteins; KCTD6, also called KCASH3 (KCTD containing, Cullin3 adaptor, suppressor of Hedgehog 3), is a substrate-specific adaptor of cullin-3, effectively regulating protein levels of the muscle small ankyrin-1 isoform 5 (sAnk1.5). KCTD21, also called KCASH2, functions as a substrate-specific adaptor of cullin-3, promoting the ubiquitination and degradation of histone deacetylase HDAC1, thereby inhibiting the deacetylation-mediated transcriptional activation of the Hedgehog effectors Gli1 and Gli2. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349674 [Multi-domain]  Cd Length: 94  Bit Score: 170.65  E-value: 1.47e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 396 DPVSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRR 475
Cdd:cd18365    1 DIVNLNVGGVHYTTTLATLTRFPDSMLGAMFSGSMPTTRDDQGNYFIDRDGTLFRYILNFLRSSQLSLPEDFKEYDLLLR 80

                         90
                 ....*....|....
gi 929273847 476 EADFFQIRPLLDEI 489
Cdd:cd18365   81 EADFYQIEPLIEAL 94
KCTD11_21_C pfam19329
BTB/POZ domain-containing protein KCTD11/21 C-terminus; This family represents the C-terminal ...
 505-674 8.66e-26

BTB/POZ domain-containing protein KCTD11/21 C-terminus; This family represents the C-terminal region of BTB/POZ domain-containing protein KCTD11 (known as REN: EGF-, NGF- and retinoic acid-responsive gene) and one homolog, a member of KCTD containing, Cullin3 adaptor, suppressor of Hedgehog (KCASH) family, KCASH2-KCTD21 protein. They share high similarity and a BTB domain responsible for oligomerization and formation of a Cullin3 ubiquitin ligase complex, specific expression in brain and cerebellum where they have a role in neuronal differentiation, and suppressor activity on acetylation-dependent Hedgehog/Gli signalling through ubiquitination and degradation of histone deacetylase 1. These proteins have been described as tumor suppressors that inhibit medulloblastoma growth by antagonizing Hedgehog signalling.


Pssm-ID: 466043  Cd Length: 154  Bit Score: 103.87  E-value: 8.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  505 RGAMLLVDVDCQVRVLHFNLRRAPENYELRTCSVRILTAEIFCTWRAFLVLLCERFSYrTTQGPTSPLPSD-QRHNRLKL 583
Cdd:pfam19329   2 KNAMLNISLDQKMQTVHFTVREAPQIYSLSSSTMEVFNANIFCTSGLFLKLLGSQLCY-FFNGNLSPICSElEDQNHLTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  584 EWVPRPDELPQDQYEKQQYRGLvvsdsWATQTHSgdlcdvimprcspcEVKDTRGFVEELLTVSLAEGFRVDSVTPDPMD 663
Cdd:pfam19329  81 QWVAAVEGLPEEEYTLQNLKRL-----WVFPANK--------------QINSFQAFVEEVLKIAMNDGFCMDSSHPSSLD 141

                         170
                  ....*....|.
gi 929273847  664 ILNCRTLQLVR 674
Cdd:pfam19329 142 FMNNKIIRLIR 152
BTB_2 pfam02214
BTB/POZ domain; In voltage-gated K+ channels this domain is responsible for subfamily-specific ...
 398-486 2.05e-20

BTB/POZ domain; In voltage-gated K+ channels this domain is responsible for subfamily-specific assembly of alpha-subunits into functional tetrameric channels. In KCTD1 this domain functions as a transcriptional repressor. It also mediates homomultimerization of KCTD1 and interaction of KCTD1 with the transcription factor AP-2-alpha.


Pssm-ID: 426665 [Multi-domain]  Cd Length: 93  Bit Score: 86.11  E-value: 2.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRsSSLDLPEGFS-EMRLLRRE 476
Cdd:pfam02214   1 VKLNVGGTRFETLKSTLTRFPDTRLGRLLELECDDYDDDTNEYFFDRSPKHFETILNFYR-TGGKLHRPEEvCLDEFLEE 79

                          90
                  ....*....|
gi 929273847  477 ADFFQIRPLL 486
Cdd:pfam02214  80 AEFYGLDELA 89
GalKase_gal_bdg pfam10509
Galactokinase galactose-binding signature; This is the highly conserved galactokinase ...
 19-67 3.00e-20

Galactokinase galactose-binding signature; This is the highly conserved galactokinase signature sequence which appears to be present in all galactokinases irrespective of how many other ATP binding sites, etc that they carry. The function of this domain appears to be to bind galactose, and the domain is normally at the N-terminus of the enzymes, EC:2.7.1.6. This domain is associated with the families GHMP_kinases_C, pfam08544 and GHMP_kinases_N, pfam00288.


Pssm-ID: 463125 [Multi-domain]  Cd Length: 50  Bit Score: 84.43  E-value: 3.00e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 929273847   19 YEQSFGGDgPQVAVCAPGRVNLIGEHIDYNQGFVLPMALPMVTVVVGSR 67
Cdd:pfam10509   3 FEELFGKE-PVGVASAPGRVNLIGEHTDYNGGFVLPAAINLDTYVAVSP 50
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
 398-487 5.42e-12

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


Pssm-ID: 197585 [Multi-domain]  Cd Length: 97  Bit Score: 62.32  E-value: 5.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847   398 VSLNVGGEIYTTTLDTLTRYqDSMLGAMFTGQIStLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEgfSEMRLLRREA 477
Cdd:smart00225   2 VTLVVGGKKFHAHKAVLAAH-SPYFKALFSSDFK-ESDKSEIYLDDVSPEDFRALLNFLYTGKLDLPE--ENVEELLELA 77

                           90
                   ....*....|
gi 929273847   478 DFFQIRPLLD 487
Cdd:smart00225  78 DYLQIPGLVE 87
 
Name Accession Description Interval E-value
GalK COG0153
Galactokinase [Carbohydrate transport and metabolism];
11-370 8.69e-164

Galactokinase [Carbohydrate transport and metabolism];


Pssm-ID: 439923 [Multi-domain]  Cd Length: 380  Bit Score: 475.03  E-value: 8.69e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  11 LVAEARRVYEQSFGGDgPQVAVCAPGRVNLIGEHIDYNQGFVLPMALPMVTVVVGS-RTSGQsasIITAAKDVEEprRVD 89
Cdd:COG0153    1 RLERLIEAFEEAFGEE-PEGVFSAPGRVNLIGEHTDYNGGFVLPAAIDRGTYAAARpRDDRK---VRVYSADFDE--EVE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  90 FDLPNdkalLSPGK-PSWANYVKGVVQHYRA--PPVPGFRAVIASSVPLGGGLSSSASLEVAMYTFLQQLKPDDGDKVAK 166
Cdd:COG0153   75 FDLDD----LEPGEeDGWANYVRGVAWALQErgYKLGGFDLVIDGDVPLGAGLSSSAALEVAVALALNDLFGLGLDPVEL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 167 AVACQKAEHTHAGVPCGIMDQFVSVLGREAHALLIDCRSLEATPVPLSDPGLVILISNSNVKHSLTGSEYPSRRRQCEEA 246
Cdd:COG0153  151 AKIGQRAENEFVGVPCGIMDQFASALGKKGHALLLDCRSLEYEYVPLPLEGYALVIVDTNVKHSLADSEYNERRAECEAA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 247 AAILEKASLRDATLKDLEDAKSRLDDET-YRRARHVIEEIERTAQAAEALKKGAYKEFGKLMVESHNSLRDLYEVSCKEL 325
Cdd:COG0153  231 AAILGVKSLRDVTLEDLEAARARLGDEVlRRRARHVVTENQRVLEAVEALRAGDLEAFGKLMNASHASLRDDYEVSCPEL 310

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 929273847 326 DELVSAAVEVEGVFGSRMTGGGFGGCTVTLLQAEAIDRTMQNMQR 370
Cdd:COG0153  311 DTLVELALAEAGVLGARMTGGGFGGCTIALVPKDAVDEFIEAVAE 355
PRK05101 PRK05101
galactokinase; Provisional
 11-362 1.42e-121

galactokinase; Provisional


Pssm-ID: 179937 [Multi-domain]  Cd Length: 382  Bit Score: 366.94  E-value: 1.42e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  11 LVAEARRVYEQSFGGDgPQVAVCAPGRVNLIGEHIDYNQGFVLPMALPMVTVVVGSRTSGQSASIITAAKDVEeprRVDF 90
Cdd:PRK05101   3 LKQKTQSLFAQQFGYP-PTHTIQAPGRVNLIGEHTDYNDGFVLPCAIDYQTVISCAKRDDRIVRVIAADYDNQ---QDEF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  91 DLpnDKALLSPGKPSWANYVKGVVQHY--RAPPVPGFRAVIASSVPLGGGLSSSASLEVAMYTFLQQLKPDDGDKVAKAV 168
Cdd:PRK05101  79 SL--DAPIVPHPEQQWANYVRGVVKHLqeRNPDFGGADLVISGNVPQGAGLSSSASLEVAVGQTFQQLYHLPLSGAEIAL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 169 ACQKAEHTHAGVPCGIMDQFVSVLGREAHALLIDCRSLEATPVPLSDpGLVILISNSNVKHSLTGSEYPSRRRQCEEAAA 248
Cdd:PRK05101 157 NGQEAENQFVGCNCGIMDQLISALGKKDHALLIDCRSLETKAVPMPE-GVAVVIINSNVKRGLVDSEYNTRRQQCETAAR 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 249 ILEKASLRDATLKDLEDAKSRLDDETYRRARHVIEEIERTAQAAEALKKGAYKEFGKLMVESHNSLRDLYEVSCKELDEL 328
Cdd:PRK05101 236 FFGVKALRDVTLEQFNAVAAELDPVVAKRARHVITENARTLEAASALAAGDLKRMGELMAESHASMRDDFEITVPQIDTL 315

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 929273847 329 VSAAVEV---EGvfGSRMTGGGFGGCTVTLLQAEAID 362
Cdd:PRK05101 316 VEIVKAVigdQG--GVRMTGGGFGGCIVALVPEELVE 350
gal_kin TIGR00131
galactokinase; Galactokinase is a member of the GHMP kinases (Galactokinase, Homoserine kinase, ...
 14-366 6.64e-113

galactokinase; Galactokinase is a member of the GHMP kinases (Galactokinase, Homoserine kinase, Mevalonate kinase, Phosphomevalonate kinase) and shares with them an amino-terminal domain probably related to ATP binding.The galactokinases found by this model are divided into two sets. Prokaryotic forms are generally shorter. The eukaryotic forms are longer because of additional central regions and in some cases are known to be bifunctional, with regulatory activities that are independent of galactokinase activity. [Energy metabolism, Sugars]


Pssm-ID: 272924 [Multi-domain]  Cd Length: 386  Bit Score: 344.89  E-value: 6.64e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847   14 EARRVYEQSFGgDGPQVAVCAPGRVNLIGEHIDYNQGFVLPMALPMVTVVVGSRTSGQSASIITAAKDVEEPRRvDFDLP 93
Cdd:TIGR00131   3 SIQKIFASAFG-AKPDFTARAPGRVNLIGEHTDYNDGSVLPCAIDFGTLCAVAVRDDKNVRIYLANADNKFAER-SLDLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847   94 NDKALLSpgkpSWANYVKGVVQHY--RAPPVP-GFRAVIASSVPLGGGLSSSASLEVAMYTFLQQL--KPDDGDKVAKAV 168
Cdd:TIGR00131  81 LDGSEVS----DWANYFKGVLHVAqeRFNSFPlGADIVCSGNVPTGSGLSSSAAFECAVGAVLQNMghLPLDSKQILLRI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  169 acQKAEHTHAGVPCGIMDQFVSVLGREAHALLIDCRSLEATPVPLSDPGLVILISNSNVKHSLTGSEYPSRRRQCEEAAA 248
Cdd:TIGR00131 157 --QVAENHFVGVNCGIMDQAASVLGKEDHALLVECRSLKATPFKFPQLGIAFVIANTNVKRTLAPSNYNTRRQECTTAAN 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  249 IL---EKASLRDATLKDLEDAKSRL---DDETYRRARHVIEEIERTAQAAEALKKGAYKEFGKLMVESHNSLRDLYEVSC 322
Cdd:TIGR00131 235 FLaatDKGALRDFMNEYFARYIARLtkmLPLVEERAKHVVSENLRVLKAVKAMKDNDFKQFGALMNESHASCDDDYECTC 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 929273847  323 KELDELVSAAVEVEGVFGSRMTGGGFGGCTVTLLQAEAIDRTMQ 366
Cdd:TIGR00131 315 PEIDELVCSAALVNGSGGSRMTGAGFGGCTVHLVPNENVDKVRQ 358
PRK05322 PRK05322
galactokinase; Provisional
 19-362 2.95e-106

galactokinase; Provisional


Pssm-ID: 235407 [Multi-domain]  Cd Length: 387  Bit Score: 327.59  E-value: 2.95e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  19 YEQSFGGDGPQVAVcAPGRVNLIGEHIDYNQGFVLPMALPMVTV-VVGSRTSGQsasIITAAKDVEEPRRVDFDLPN--- 94
Cdd:PRK05322  10 FAEVFGEEAEDVFF-SPGRINLIGEHTDYNGGHVFPAAITLGTYgAARKRDDKK---VRLYSANFEDLGIIEFDLDDlsf 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  95 DKallspgKPSWANYVKGVVQHYRA---PPVPGFRAVIASSVPLGGGLSSSASLEVAMYTFLQQLKPDDGDKVAKAVACQ 171
Cdd:PRK05322  86 DK------EDDWANYPKGVLKFLQEagyKIDHGFDILIYGNIPNGAGLSSSASIELLTGVILKDLFNLDLDRLELVKLGQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 172 KAEHTHAGVPCGIMDQFVSVLGREAHALLIDCRSLEATPVPLSDPGLVILISNSNVKHSLTGSEYPSRRRQCEEAAAILE 251
Cdd:PRK05322 160 KTENEFIGVNSGIMDQFAIGMGKKDHAILLDCNTLEYEYVPLDLGDYVIVIMNTNKRRELADSKYNERRAECEKALEELQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 252 K----ASLRDATLKDLEDAKSRLDDET-YRRARHVIEEIERTAQAAEALKKGAYKEFGKLMVESHNSLRDLYEVSCKELD 326
Cdd:PRK05322 240 KkldiKSLGELTEEEFDEYSYLIKDETlLKRARHAVTENQRTLKAVKALKAGDLEKFGRLMNASHVSLRDDYEVTGLELD 319

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 929273847 327 ELVSAAVEVEGVFGSRMTGGGFGGCTVTLLQAEAID 362
Cdd:PRK05322 320 TLVEAAWKQEGVLGARMTGAGFGGCAIAIVKKDKVE 355
PRK03817 PRK03817
galactokinase; Provisional
 32-363 1.26e-93

galactokinase; Provisional


Pssm-ID: 235163 [Multi-domain]  Cd Length: 351  Bit Score: 293.44  E-value: 1.26e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  32 VCAPGRVNLIGEHIDYNQGFVLPMALPMVTVVVGSRtsgqSASIITAAKDVEEPRRVDFDLpndkalLSPGKpSWANYVK 111
Cdd:PRK03817   3 VKSPGRVNLIGEHTDYNDGYVLPFAINLYTFLEIEK----SEKFIFYSENFNEEKTFELDK------LEKLN-SWADYIK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 112 GVV-----QHYRappVPGFRAVIASSVPLGGGLSSSASLEVAMYTFLQQLKPDDGDKVAKAVACQKAEHTHAGVPCGIMD 186
Cdd:PRK03817  72 GVIwvlekRGYE---VGGVKGKVSSNLPIGAGLSSSASLEVAVAYALNEAYNLNLSKLELALLAREAENEFVGVPCGIMD 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 187 QFVSVLGREAHALLIDCRSLEATPVPLSDpGLVILISNSNVKHSLTGSEYPSRRRQCEEAAAILEKASLRDATLKDLeda 266
Cdd:PRK03817 149 QFAVAFGKKDHAIFLDTMTLEYEYVPFPE-DYEILVFDTGVKRELASSEYNERRQECEEALKILGKKSSKEVTEEDL--- 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 267 kSRLDDETYRRARHVIEEIERTAQAAEALKKGAYKEFGKLMVESHNSLRDLYEVSCKELDELVSAAVEVeGVFGSRMTGG 346
Cdd:PRK03817 225 -SKLPPLLRKRAGYVLRENERVLKVRDALKEGDIETLGELLTESHWDLADNYEVSCEELDFFVEFALEL-GAYGARLTGA 302

                        330
                 ....*....|....*..
gi 929273847 347 GFGGCTVTLLQAEAIDR 363
Cdd:PRK03817 303 GFGGSAIALVDKGKFES 319
PRK00555 PRK00555
galactokinase; Provisional
 34-371 8.35e-84

galactokinase; Provisional


Pssm-ID: 179063 [Multi-domain]  Cd Length: 363  Bit Score: 268.65  E-value: 8.35e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  34 APGRVNLIGEHIDYNQGFVLPMALPMVTVVvgSRTSGQSASIITAAKDVEEPRRVDFDLpndkallSPGKPS-WANYVKG 112
Cdd:PRK00555   7 APGRINLIGEHTDYNLGFALPIALPQRTVV--TFTPEHTDAITASSDRADGSARIPLDT-------TPGQVTgWAAYAAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 113 VVQHYRAP--PVPGFRAVIASSVPLGGGLSSSASLEVAMYTFLQQLKPDDGDKVAKAVACQKAEHTHAGVPCGIMDQFVS 190
Cdd:PRK00555  78 VIWALRGAghPVPGGAMSITSDVEIGSGLSSSAALECAVLGAVGAATGTRIDRLEQARLAQRAENEYVGAPTGLLDQLAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 191 VLGREAHALLIDCRSLEATPVPLsDP---GLVILISNSNVKHSLTGSEYPSRRRQCEEAAAILEKASLRDATLKDLEDAK 267
Cdd:PRK00555 158 LFGAPKTALLIDFRDLTVRPVAF-DPdaaGVVLLLMDSRARHRHAGGEYAARRASCERAAADLGVSSLRAVQDRGLAALG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 268 SRLDDETYRRARHVIEEIERTAQAAEALKKGAYKEFGKLMVESHNSLRDLYEVSCKELDELVSAAVEVeGVFGSRMTGGG 347
Cdd:PRK00555 237 AIADPIDARRARHVLTENQRVLDFAAALADSDFTAAGQLLTASHASMRDDFEITTERIDLIADSAVRA-GALGARMTGGG 315

                        330       340
                 ....*....|....*....|....
gi 929273847 348 FGGCTVTLLQAEAIDRTMQNMQRS 371
Cdd:PRK00555 316 FGGCVIALVPADRAEDVADTVRRA 339
BTB_POZ_KCTD6_like cd18365
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 396-489 1.47e-50

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins, KCTD6, KCTD21 and similar proteins; KCTD6, also called KCASH3 (KCTD containing, Cullin3 adaptor, suppressor of Hedgehog 3), is a substrate-specific adaptor of cullin-3, effectively regulating protein levels of the muscle small ankyrin-1 isoform 5 (sAnk1.5). KCTD21, also called KCASH2, functions as a substrate-specific adaptor of cullin-3, promoting the ubiquitination and degradation of histone deacetylase HDAC1, thereby inhibiting the deacetylation-mediated transcriptional activation of the Hedgehog effectors Gli1 and Gli2. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349674 [Multi-domain]  Cd Length: 94  Bit Score: 170.65  E-value: 1.47e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 396 DPVSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRR 475
Cdd:cd18365    1 DIVNLNVGGVHYTTTLATLTRFPDSMLGAMFSGSMPTTRDDQGNYFIDRDGTLFRYILNFLRSSQLSLPEDFKEYDLLLR 80

                         90
                 ....*....|....
gi 929273847 476 EADFFQIRPLLDEI 489
Cdd:cd18365   81 EADFYQIEPLIEAL 94
PLN02521 PLN02521
galactokinase
 2-368 3.10e-49

galactokinase


Pssm-ID: 215285 [Multi-domain]  Cd Length: 497  Bit Score: 179.90  E-value: 3.10e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847   2 ASPVPSVSEL---------VAEARRVY-------EQSFGGDgPQVAVCAPGRVNLIGEHIDYNQGFVLPMALPMVTVVVG 65
Cdd:PLN02521   6 EEPVPVFSSLepvygdgslLEEARLRYarlkaafVEVYGAK-PDLFARSPGRVNLIGEHIDYEGYSVLPMAIRQDTIVAI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  66 SRTSGQSASIITaakdveeprRVDFDLPNDKALLSP------GKPSWANYV----KGVVQHYRA-----PPVPGFRAVIA 130
Cdd:PLN02521  85 RRAEGSKKLRIA---------NVNDKYTTCTFPADPdqevdlANHKWGNYFicgyKGVFEFLKSkgvdvGPPVGLDVVVD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 131 SSVPLGGGLSSSASLEVAMYTFLQQLKPDDGDKVAKAVACQKAEHtHAGVPCGIMDQFVSVLGREAHALLIDCRSLEATP 210
Cdd:PLN02521 156 GTVPTGSGLSSSAALVCSAAIAIMAALGLNFTKKEVAQFTCKCER-HIGTQSGGMDQAISIMAQQGVAKLIDFNPVRATD 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 211 VPLSdPGLVILISNS--NVKHSLTGSE-YPSRRRQCEEAAAIL--------EKASLRDATLKDLED-------------- 265
Cdd:PLN02521 235 VQLP-AGGTFVIANSlaESNKAVTAATnYNNRVVECRLAAIVLavklgmsaEEAISKVKTLSDVEGlcvsfagshgssdp 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 266 ---AKSRLDDETY------------------------------------RRARHVIEEIERTAQAAEALKKG-----AYK 301
Cdd:PLN02521 314 avaVKELLHEGPYtaeeieeilgesltsifknsptslavlkaakhfklhQRAVHVYSEAKRVHAFRDTVSSSlseeeKLK 393

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 929273847 302 EFGKLMVESHNSLRDLYEVSCKELDELVSAAVEvEGVFGSRMTGGGFGGCTVTLLQAEAIDRTMQNM 368
Cdd:PLN02521 394 KLGDLMNESHYSCSVLYECSCPELEELVKVCRD-NGALGARLTGAGWGGCAVALVKEAIVPQFILAL 459
BTB_POZ_KCTD21 cd18395
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 396-492 1.94e-48

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 21 (KCTD21); KCTD21, also calledz KCTD containing, Cullin3 adaptor, suppressor of Hedgehog 2 (KCASH2), is a BTB/POZ domain-containing protein that functions as a substrate-specific adaptor of cullin-3, promoting the ubiquitination and degradation of histone deacetylase HDAC1, thereby inhibiting the deacetylation-mediated transcriptional activation of the Hedgehog effectors Gli1 and Gli2. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349703 [Multi-domain]  Cd Length: 98  Bit Score: 165.12  E-value: 1.94e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 396 DPVSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRR 475
Cdd:cd18395    1 DPITLNVGGKLYTTSLATLTRYPDSMLGAMFSGKFPTKKDSQGNCFIDRDGKIFRYILNFLRTSHLDLPEDFQEMGLLKR 80

                         90
                 ....*....|....*..
gi 929273847 476 EADFFQIRPLLDEIRRR 492
Cdd:cd18395   81 EADFYQIQPLIEALQEK 97
BTB_POZ_KCTD6 cd18394
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 396-486 5.50e-44

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 6 (KCTD6); KCTD6, also called KCTD containing, Cullin3 adaptor, suppressor of Hedgehog 3 (KCASH3), is a BTB/POZ domain-containing protein that functions as a substrate-specific adaptor of cullin-3, regulating protein levels of the muscle small ankyrin-1 isoform 5 (sAnk1.5) as well as suppressing histone deacetylase and Hedgehog activity in medulloblastoma. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349702 [Multi-domain]  Cd Length: 104  Bit Score: 153.19  E-value: 5.50e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 396 DPVSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRR 475
Cdd:cd18394    3 DPVTLNVGGHLYTTSLSTLTRYPDSMLGAMFRGDFPTARDSQGNYFIDRDGPLFRYILNFLRTSELTLPVDFKEFDLLRK 82

                         90
                 ....*....|.
gi 929273847 476 EADFFQIRPLL 486
Cdd:cd18394   83 EADFYQIEPLI 93
PLN02865 PLN02865
galactokinase
 2-359 9.06e-43

galactokinase


Pssm-ID: 215466 [Multi-domain]  Cd Length: 423  Bit Score: 159.97  E-value: 9.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847   2 ASPVPSVSELvAEARRVYEQSFGGDGPQV-AVCAPGRVNLIGEHIDYNQGFVLPMALPMvTVVVGSRTSGQSASIITAAK 80
Cdd:PLN02865   3 LGSWPSANEL-DEIRERVAAMSGRNSGEVrVVVSPYRICPLGAHIDHQGGTVSAMTINK-GILLGFVPSGDPEVLLRSAQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  81 DVEEPR-RVDFDLPNDKALLSPGKPS--WANYVKGVVQHYRAPPV---PGFRAVIASSVPL-GGGLSSSASLEVAMYTFL 153
Cdd:PLN02865  81 FEGEVRfRVDEIQHPIANVSSDSKEEsnWGDYARGAVYALQSRGHalsQGITGYISGSEGLdSSGLSSSAAVGVAYLLAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 154 QQ-----LKPDDGDKVAKAVacqkaEHTHAGVPCGIMDQFVSVLGREAHALLIDCRSLEATPVPLSDPG------LVILI 222
Cdd:PLN02865 161 ENannltVSPEDNIELDRLI-----ENEYLGLRNGILDQSAILLSRYGCLTFMDCKTLDHKLVSLQFQQpggekpFKILL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 223 SNSNVKHSLTGSE-YPSRRRQCEEAAAILEKASLRD---ATLKDLEDA-----KSRLDDETYRRARHVIEEIERTAQAAE 293
Cdd:PLN02865 236 AFSGLRHALTNKPgYNLRVSECQEAARFLLEASGNDelePLLCNVEPEvyeahKCKLEAVLARRAEHYFSENMRVIKGVE 315

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 929273847 294 ALKKGAYKEFGKLMVESHNSLRDLYEVSCKELDELVSAAVEVEGVFGSRMTGGGFGGCTVTLLQAE 359
Cdd:PLN02865 316 AWASGNLEEFGKLISASGLSSIENYECGCEPLIQLYEILLKAPGVYGARFSGAGFRGCCVAFVDAE 381
PTZ00290 PTZ00290
galactokinase; Provisional
 34-370 9.17e-40

galactokinase; Provisional


Pssm-ID: 240347 [Multi-domain]  Cd Length: 468  Bit Score: 152.28  E-value: 9.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  34 APGRVNLIGEHIDYNQGFVLPMALPMVT-VVVGSRTSGQSASIITAAKDVEEprrvdFDLPNdkalLSPGK--PSWANYV 110
Cdd:PTZ00290  42 APGRVNFIGEHVDYMGGYVCPAAVLEGChILVGRVKHFCDHKLRFATETDEH-----FVLDH----LGGAKhnKAWTTFV 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 111 KGVVQ--------HYRAPPVPGFRAVIASSVPLGGGLSSSASLEVAM----------------------YTFLQQLKPDD 160
Cdd:PTZ00290 113 RGAATlrlnrlgvAIDAPSLQGVCMVVHGTLPMGAGMSASASFGVALlnaintvvtrrykgcptspgrrYSILPPMSKEE 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 161 GDKVAKAVacQKAEHTHAGVPCGIMDQFVSVLGREAHALLIDCRSLEATPVPLS----DPGLVILIsNSNVKHSLTGSE- 235
Cdd:PTZ00290 193 LIELAKQA--RRIETEFCGVNVGIMDQFISAFAEEDKFMFLDCKSLTFESHDMTpllgDGACFLLI-DSMIKHDLLGGTa 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 236 --YPSRRRQCEEAAAILEKASLRDA--TLKDL-----------------EDAKSRLDDETYRRARHVIEEIERTAQ---- 290
Cdd:PTZ00290 270 gmYNTVRSDQEGAQKKIGKHRYRGKpfTFSDLvrnpkkytfdgdvvafmESCKPLMTPGEFERGTYNIMEQIRTLEfikl 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 291 --AAEAL-KKGAYKEFGKLMVESHNSLRDLYEVSCKELDELVSAAVEVEGVFGSRMTGGGFGGCTVTLLQAEAIDRTMQN 367
Cdd:PTZ00290 350 ndPELPLsREERFRKAGEILNAGHQGMRDLMKITTPELDFIHELINEEKGVAGGRMMGGGFGGCIILLLKKNAVDRVVAH 429


                 ...
gi 929273847 368 MQR 370
Cdd:PTZ00290 430 VRE 432
BTB_POZ_KCTD4 cd18364
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-482 1.20e-35

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 4 (KCTD4); KCTD4 is a BTB/POZ domain-containing protein with an unknown biological function. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349673 [Multi-domain]  Cd Length: 86  Bit Score: 129.03  E-value: 1.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRREA 477
Cdd:cd18364    2 VTLNVGGYLYITQRQTLTKYPDSFLEGMVNGKIQCTVDADGNYFIDRDGLLFRHVLNFLRNGELLLPEGFQENQLLALEA 81


                 ....*
gi 929273847 478 DFFQI 482
Cdd:cd18364   82 DFYQL 86
BTB_POZ_KCTD-like cd18316
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-480 2.45e-35

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins; The potassium channel tetramerization domain (KCTD) family proteins contain the BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. Some others show Cullin-independent functions including binding and regulation of GABA (gamma-aminobutyric acid) receptors (KCTD8, KCTD12 and KCTD16) and inhibition of AP-2 function (KCTD15). KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349625  Cd Length: 83  Bit Score: 128.06  E-value: 2.45e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRREA 477
Cdd:cd18316    1 VKLNVGGTLFTTSRSTLLKDPDSLLAALFSGRWPLPRDEDGSIFIDRDPELFRHILNFLRTGKLPLPSDFVELEELLAEA 80


                 ...
gi 929273847 478 DFF 480
Cdd:cd18316   81 EFY 83
BTB_POZ_KCTD8-like cd18367
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-491 5.92e-34

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins, KCTD8, KCTD12, KCTD16 and similar proteins; This subfamily of KCTD proteins includes KCTD8, KCTD12 (also called predominantly fetal expressed T1 domain/Pfetin), and KCTD16. They act as auxiliary subunits of GABAB receptors associated with mood disorders. KCTD8 interacts as a tetramer with GABRB1 and GABRB2. KCTD12 regulates agonist potency and kinetics of GABAB receptor signaling. It promotes tumorigenesis by facilitating CDC25B/CDK1/Aurora A-dependent G2/M transition. KCTD16 interacts with amyloid beta precursor protein (APP), a type I transmembrane protein involved in a variety of cellular processes such as cell adhesion, and axon guidance. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349676  Cd Length: 100  Bit Score: 125.10  E-value: 5.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQI--STLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRR 475
Cdd:cd18367    5 VELNVGGQVYTTSLSTLIKDPDSLLGRMFSGKNrqELARDSKGRYFLDRDGVLFRYILDYLRNQKLVLPENFPERERLKR 84

                         90
                 ....*....|....*.
gi 929273847 476 EADFFQIRPLLDEIRR 491
Cdd:cd18367   85 EAEYFQLPELVKALRA 100
BTB_POZ_KCTD11 cd18370
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-481 2.17e-32

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein KCTD11; KCTD11 may function as an antagonist of the Hedgehog pathway of cell proliferation and differentiation by affecting the nuclear transfer of transcription factor GLI1, thus maintaining cerebellar granule cells in the undifferentiated state. It is a probable substrate-specific adapter for a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex towards HDAC1. It contains a BTB/POZ domain; in some cases the domain may be truncated. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. Variants of the human/mouse KCTD11 appear to contain truncated BTB/POZ domains.


Pssm-ID: 349679  Cd Length: 88  Bit Score: 120.10  E-value: 2.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTG----QISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLL 473
Cdd:cd18370    1 VTLNVGGTLYSTTLETLTRFPDSMLGAMFRAgtpiPPNLNMQGGGHYFIDRDGKAFRHILNFLRLGRLDLPRGYGETALL 80


                 ....*...
gi 929273847 474 RREADFFQ 481
Cdd:cd18370   81 RAEADFYQ 88
BTB_POZ_FIP2-like cd18376
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-485 7.61e-32

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Arabidopsis thaliana FH protein interacting protein FIP2 and similar proteins; FIP2 may act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It contains a BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization.


Pssm-ID: 349685  Cd Length: 89  Bit Score: 118.50  E-value: 7.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSL-DLPEGFSEMRLLRRE 476
Cdd:cd18376    1 VKLNVGGQKFTTTLDTLTKDPDSMLAAMFSGRHSLKKDEDGSYFIDRDGTHFRHILNYLRDGEVkIPTEDRSVLKELLEE 80


                 ....*....
gi 929273847 477 ADFFQIRPL 485
Cdd:cd18376   81 AEYYQLRGL 89
BTB_POZ_KCTD1-like cd18361
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-489 2.32e-31

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins, KCTD1 and KCTD15; This subfamily of KCTD proteins includes KCTD1 and KCTD15. KCTD1 is a nuclear BTB/POZ domain-containing protein that acts as a transcriptional repressor and mediates protein-protein interactions through a BTB domain. It represses the transcriptional activity of AP-2 family members, including TFAP2A, TFAP2B and TFAP2C. It also functions as a novel inhibitor of the Wnt signaling pathway. Mutations in KCTD1 cause scalp-ear-nipple (SEN) syndrome. KCTD15 is a BTB/POZ domain-containing protein that plays a role in the regulation of neural crest (NC) formation and other steps in embryonic development. It inhibits AP2 transcriptional activity by interaction with its activation domain. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD1 BTB domains form pentamers.


Pssm-ID: 349670  Cd Length: 94  Bit Score: 117.48  E-value: 2.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDK-RGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRRE 476
Cdd:cd18361    1 VHIDVGGHIYTSSLETLTKYPESRLGKLFNGSIPIVLDSlKQHYFIDRDGKMFRHILNFLRTSKLLLPDDFTEFDLLYEE 80

                         90
                 ....*....|...
gi 929273847 477 ADFFQIRPLLDEI 489
Cdd:cd18361   81 ARYYELQPMVKQL 93
BTB_POZ_KCTD7 cd18366
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-487 3.76e-28

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 7 (KCTD7); KCTD7 is a BTB/POZ domain-containing protein that has an impact on K+ fluxes, neurotransmitter synthesis, and neuronal function. It functions as a regulator of potassium conductance in neurons, and is involved in the control of excitability of cortical neurons. Mutations in KCTD7 may cause progressive myoclonus epilepsy (PME). The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349675  Cd Length: 92  Bit Score: 108.16  E-value: 3.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEgfsEMRLLRREA 477
Cdd:cd18366    6 VPLNVGGMHFTTRLSTLRKYEDSMLAAMFSGRHHIPKDSEGRYFIDRDGSYFGYILNFLRDGDLPPRE---RARAVYKEA 82

                         90
                 ....*....|
gi 929273847 478 DFFQIRPLLD 487
Cdd:cd18366   83 QYYGIGPLIE 92
BTB_POZ_KCTD15 cd18388
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 397-491 3.36e-26

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 15 (KCTD15); KCTD15 is a BTB/POZ domain-containing protein that plays a role in the regulation of neural crest (NC) formation and other steps in embryonic development. It inhibits AP2 transcriptional activity by interaction with its activation domain. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD1 BTB domains, closely related to KCTD15, form pentamers.


Pssm-ID: 349696  Cd Length: 99  Bit Score: 103.15  E-value: 3.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 397 PVSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDK-RGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRR 475
Cdd:cd18388    3 PVHIDVGGHMYTSSLATLTKYPDSRISRLFNGTEPIVLDSlKQHYFIDRDGEIFRYILSFLRTSKLLLPEDFKDFNLLYE 82

                         90
                 ....*....|....*.
gi 929273847 476 EADFFQIRPLLDEIRR 491
Cdd:cd18388   83 EAKYYQLQPMVKELER 98
KCTD11_21_C pfam19329
BTB/POZ domain-containing protein KCTD11/21 C-terminus; This family represents the C-terminal ...
 505-674 8.66e-26

BTB/POZ domain-containing protein KCTD11/21 C-terminus; This family represents the C-terminal region of BTB/POZ domain-containing protein KCTD11 (known as REN: EGF-, NGF- and retinoic acid-responsive gene) and one homolog, a member of KCTD containing, Cullin3 adaptor, suppressor of Hedgehog (KCASH) family, KCASH2-KCTD21 protein. They share high similarity and a BTB domain responsible for oligomerization and formation of a Cullin3 ubiquitin ligase complex, specific expression in brain and cerebellum where they have a role in neuronal differentiation, and suppressor activity on acetylation-dependent Hedgehog/Gli signalling through ubiquitination and degradation of histone deacetylase 1. These proteins have been described as tumor suppressors that inhibit medulloblastoma growth by antagonizing Hedgehog signalling.


Pssm-ID: 466043  Cd Length: 154  Bit Score: 103.87  E-value: 8.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  505 RGAMLLVDVDCQVRVLHFNLRRAPENYELRTCSVRILTAEIFCTWRAFLVLLCERFSYrTTQGPTSPLPSD-QRHNRLKL 583
Cdd:pfam19329   2 KNAMLNISLDQKMQTVHFTVREAPQIYSLSSSTMEVFNANIFCTSGLFLKLLGSQLCY-FFNGNLSPICSElEDQNHLTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  584 EWVPRPDELPQDQYEKQQYRGLvvsdsWATQTHSgdlcdvimprcspcEVKDTRGFVEELLTVSLAEGFRVDSVTPDPMD 663
Cdd:pfam19329  81 QWVAAVEGLPEEEYTLQNLKRL-----WVFPANK--------------QINSFQAFVEEVLKIAMNDGFCMDSSHPSSLD 141

                         170
                  ....*....|.
gi 929273847  664 ILNCRTLQLVR 674
Cdd:pfam19329 142 FMNNKIIRLIR 152
BTB_POZ_KCNRG cd18375
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-487 1.06e-25

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel regulatory protein (KCNRG); KCNRG, also called potassium channel regulator or protein CLLD4, is an endoplasmic reticulum (ER)-associated tumor suppressor that regulates Kv1 family potassium channel proteins by retaining a fraction of the channels in endomembranes. It contains a BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization.


Pssm-ID: 349684  Cd Length: 97  Bit Score: 101.34  E-value: 1.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRREA 477
Cdd:cd18375    3 VTLNVGGKKFTTRPSTLRRFPDSRLARMLDGKDQDFKVVNGQFFVDRDGSLFSYILDYLRTGQLTLPTEFSDYNRLAREA 82

                         90
                 ....*....|
gi 929273847 478 DFFQIRPLLD 487
Cdd:cd18375   83 EFYGLYSLAD 92
BTB_POZ_KCTD10-like_BACURD cd18369
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-488 4.70e-25

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins, KCTD10 (BACURD3), KCTD13 (BACURD1), and TNFAIP1 (BACURD2); This subfamily of KCTD proteins, also called the BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein (BACURD) subfamily, includes KCTD10 (BACURD3), KCTD13 (BACURD1), and TNFAIP1 (BACURD2). KCTD10 is a BTB/POZ domain-containing protein that interacts with proliferating cell nuclear antigen (PCNA) and polymerase delta, and participates in DNA repair, DNA replication, and cell-cycle control. Its down-regulation could inhibit cell proliferation. KCTD10 also plays crucial roles in embryonic angiogenesis and heart development in mammals by negatively regulating the Notch signaling pathway. KCTD13 is a BTB/POZ domain-containing protein that may function as a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of RhoA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. TNFAIP1, also called protein B12, is a BTB/POZ domain-containing protein that is involved in DNA replication, DNA damage repair, cell apoptosis, and is implicated in human diseases including cancer, Alzheimer's disease (AD) and type 2 diabetic nephropathy. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. KCTD10 and KCTD13 BTB domains form a novel two-fold symmetric tetramer that is distinct from the tetramer formed by voltage-gated potassium (Kv) channels.


Pssm-ID: 349678 [Multi-domain]  Cd Length: 91  Bit Score: 99.39  E-value: 4.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRyQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRREA 477
Cdd:cd18369    1 VKLNVGGSLHYTTIGTLTK-QDTMLRAMFSGRMEVLTDSEGWILIDRCGKHFGTILNYLRDGSVPLPESRRELAELLAEA 79

                         90
                 ....*....|.
gi 929273847 478 DFFQIRPLLDE 488
Cdd:cd18369   80 KYYLVQGLVEQ 90
BTB_POZ_KCTD1 cd18387
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 397-491 8.22e-24

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 1 (KCTD1); KCTD1 is a nuclear BTB/POZ domain-containing protein that acts as a transcriptional repressor and mediates protein-protein interactions through a BTB domain. It represses the transcriptional activity of AP-2 family members, including TFAP2A, TFAP2B and TFAP2C to various extent. It also functions as a novel inhibitor of the Wnt signaling pathway. Mutations in KCTD1 cause scalp-ear-nipple (SEN) syndrome. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD1 BTB domains form pentamers.


Pssm-ID: 349695  Cd Length: 105  Bit Score: 96.22  E-value: 8.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 397 PVSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDK-RGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRR 475
Cdd:cd18387    4 PVHIDVGGHMYTSSLATLTKYPESRIGRLFDGTEPIVLDSlKQHYFIDRDGQMFRYILNFLRTSKLLIPDDFKDYSLLYE 83

                         90
                 ....*....|....*.
gi 929273847 476 EADFFQIRPLLDEIRR 491
Cdd:cd18387   84 EAKYFQLQPMLLELER 99
BTB_POZ_KCTD3-like cd18363
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 396-482 1.86e-23

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 3 (KCTD3) and SH3KBP1-binding protein 1 (SHKBP1); The group of KCTD proteins includes KCTD3 and SHKBP1. KCTD3, also called renal carcinoma antigen NY-REN-45, is a BTB/POZ domain-containing protein that is an accessory subunit of potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3 (HCN3), upregulating its cell-surface expression and current density without affecting its voltage dependence and kinetics. SHKBP1, also called SETA-binding protein 1, interacts with cathepsin B and participates in tumor necrosis factor (TNF)-induced apoptosis in ovarian cancer cells. It can promote epidermal growth factor receptor (EGFR) signaling by interrupting c-Cbl-CIN85 complex and inhibiting EGFR degradation. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349672  Cd Length: 86  Bit Score: 94.74  E-value: 1.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 396 DPVSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEgfSEMRLLRR 475
Cdd:cd18363    2 DIINLNVGGKRFSTSRQTLTWIPDSFFTSLLSGRISSLKDETGAIFIDRDPKLFSIILNYLRTKEIDLRN--VDISSLRH 79


                 ....*..
gi 929273847 476 EADFFQI 482
Cdd:cd18363   80 EAEFYGI 86
ERG12 COG1577
Mevalonate kinase [Lipid transport and metabolism]; Mevalonate kinase is part of the Pathway ...
 34-355 1.10e-22

Mevalonate kinase [Lipid transport and metabolism]; Mevalonate kinase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 441185 [Multi-domain]  Cd Length: 277  Bit Score: 98.38  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  34 APGRVNLIGEHID-YNQGfVLPMALPMVTVVVGSRTSGQSASIITAakdvEEPRRVDFDLPNDKALlspgkpswaNYVKG 112
Cdd:COG1577    1 APGKLILFGEHAVvYGQP-AIAVAVDRRATVTVEPSDDDKLRIESP----DLGGTLDLDPLADAAL---------RYIKA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 113 VVQ---HYRAPPVPGFRAVIASSVPLGGGLSSSASLEVAM---YTFLQQLKPDDgDKVAKAVacQKAEHTHAGVPCGiMD 186
Cdd:COG1577   67 AIEaalEYLGLPLKGFDIEIDSEIPRKRGLGSSAAVAVAViraLAAFYGVELSK-EELFKLA--LEAEKIVHGNPSG-LD 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 187 QFVSVLGreaHALLIDcRSLEATPVPLSDPgLVILISNSNVKHSlTGseypsrrrqceeaaailekaslrdATLKDLEDA 266
Cdd:COG1577  143 TAASTYG---GPIYYQ-RGDRAEPLELPKN-LPLVVGDTGVPAS-TK------------------------ELVAKVRKL 192

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 267 KSRLDDetyrRARHVIEEIER-TAQAAEALKKGAYKEFGKLMVESHNSLRDLYeVSCKELDELVSAAVEvEGVFGSRMTG 345
Cdd:COG1577  193 KERNPE----LYEAFLEEIGDlVEEAIEALEEGDLEALGELMNENHGLLRALG-VSTPELDRLVEAARK-AGALGAKLTG 266

                        330
                 ....*....|
gi 929273847 346 GGFGGCTVTL 355
Cdd:COG1577  267 AGGGGCVIAL 276
BTB_POZ_KCTD14 cd18371
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-489 2.14e-22

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 14 (KCTD14); KCTD14 is a BTB/POZ domain-containing protein with unknown biological function. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349680  Cd Length: 99  Bit Score: 92.12  E-value: 2.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRssSLDLPEGFseMRLLRREA 477
Cdd:cd18371    4 VSLNVGGHIYTTTLSTLRKFPGSKLAELFNGQPKLRTDSEGRYFIDRDGTYFRYILEYLR--TNQVPTQH--IQEVYKEA 79

                         90
                 ....*....|..
gi 929273847 478 DFFQIRPLLDEI 489
Cdd:cd18371   80 LFYDIEPLVKLL 91
BTB_POZ_KCTD8 cd18396
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-486 7.27e-22

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein KCTD8; KCTD8, a BTB/POZ domain-containing protein, is an auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. It interacts as a tetramer with GABRB1 and GABRB2. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349704 [Multi-domain]  Cd Length: 103  Bit Score: 90.63  E-value: 7.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTL--RDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRR 475
Cdd:cd18396    6 VELNVGGQVYVTKHSTLLSVPDSTLASMFSRRAARElpRDNRGRFFIDRDGFLFRYVLDYLRDKQLALPDHFPEKERLLR 85

                         90
                 ....*....|.
gi 929273847 476 EADFFQIRPLL 486
Cdd:cd18396   86 EAEYFQLGDLV 96
BTB_POZ_TNFAIP1_BACURD2 cd18401
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-487 7.53e-22

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in tumor necrosis factor, alpha-induced protein 1, endothelial (TNFAIP1); TNFAIP1, also called BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2 (BACURD2), or protein B12, is a BTB/POZ domain-containing protein that is involved in DNA replication, DNA damage repair and cell apoptosis, and is implicated in human diseases including cancer, Alzheimer's disease (AD) and type 2 diabetic nephropathy. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The BTB domains of other BACURD subfamily members, KCTD10 and KCTD13, form a novel two-fold symmetric tetramer that is distinct from the tetramer formed by voltage-gated potassium (Kv) channels.


Pssm-ID: 349709  Cd Length: 104  Bit Score: 90.71  E-value: 7.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRyQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRREA 477
Cdd:cd18401    5 VRLNVGGSLYYTTVQVLTR-HDTMLKAMFSGRMEVLTDKEGWILIDRCGKHFGTILNYLRDDTVALPKSRQEIKELMAEA 83

                         90
                 ....*....|
gi 929273847 478 DFFQIRPLLD 487
Cdd:cd18401   84 KYYLIQGLVD 93
BTB_POZ_KCTD12_Pfetin cd18397
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 396-485 8.29e-22

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 12 (KCTD12); KCTD12, also called predominantly fetal expressed T1 domain (Pfetin), is a BTB/POZ domain-containing protein that is an auxiliary subunit of GABAB receptors associated with mood disorders. It regulates agonist potency and kinetics of GABAB receptor signaling. It promotes tumorigenesis by facilitating CDC25B/CDK1/Aurora A-dependent G2/M transition. It also regulates colorectal cancer cell stemness through the ERK pathway. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349705 [Multi-domain]  Cd Length: 100  Bit Score: 90.33  E-value: 8.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 396 DPVSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQI--STLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLL 473
Cdd:cd18397    3 EIVELNVGGQVYVTRHTTLVSVPDSLLWHMFSQQKpgELARDSKGRFFLDRDGFLFRYILDYLRDLQLVLPDYFPERSRL 82

                         90
                 ....*....|..
gi 929273847 474 RREADFFQIRPL 485
Cdd:cd18397   83 QREAEFFQLPEL 94
BTB_POZ_KCTD16 cd18398
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 396-486 7.37e-21

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 16 (KCTD16); KCTD16 is a BTB/POZ domain-containing protein that is an auxiliary subunit of GABAB receptors associated with mood disorders. It interacts with amyloid beta precursor protein (APP), a type I transmembrane protein involved in a variety of cellular processes such as cell adhesion and axon guidance. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349706 [Multi-domain]  Cd Length: 103  Bit Score: 88.05  E-value: 7.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 396 DPVSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTL----RDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMR 471
Cdd:cd18398    3 EVVELNVGGQVYFTRHATLVSIPHSLLWKMFSPKRDTAndlaKDSKGRFFIDRDGFLFRYILDYLRDRQVVLPDHFPEKG 82

                         90
                 ....*....|....*
gi 929273847 472 LLRREADFFQIRPLL 486
Cdd:cd18398   83 RLKREAEYFQLPDLV 97
BTB_POZ_KCTD9 cd18368
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 396-493 1.08e-20

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 9 (KCTD9); KCTD9 is a BTB/POZ domain-containing protein that contributes to liver injury through NK cell activation during hepatitis B virus-induced acute-on-chronic liver failure. It functions as a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of target proteins, leading to their degradation by the proteasome. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD9 BTB domain forms a pentameric structure.


Pssm-ID: 349677 [Multi-domain]  Cd Length: 100  Bit Score: 87.32  E-value: 1.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 396 DPVSLNVGGEIYTTTLDTLTRYQ-DSMLGAMFT--GQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRL 472
Cdd:cd18368    1 DWIKLNVGGRIFTTTRSTLVKKEpDSMLARMFSddSTWPSSRDENGAYLIDRSPEYFEPILNYLRHGQLILNDGLNPLGV 80

                         90       100
                 ....*....|....*....|.
gi 929273847 473 LrREADFFQIRPLLDEIRRRV 493
Cdd:cd18368   81 L-EEAKFFGIQSLIEILEQLI 100
BTB_2 pfam02214
BTB/POZ domain; In voltage-gated K+ channels this domain is responsible for subfamily-specific ...
 398-486 2.05e-20

BTB/POZ domain; In voltage-gated K+ channels this domain is responsible for subfamily-specific assembly of alpha-subunits into functional tetrameric channels. In KCTD1 this domain functions as a transcriptional repressor. It also mediates homomultimerization of KCTD1 and interaction of KCTD1 with the transcription factor AP-2-alpha.


Pssm-ID: 426665 [Multi-domain]  Cd Length: 93  Bit Score: 86.11  E-value: 2.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRsSSLDLPEGFS-EMRLLRRE 476
Cdd:pfam02214   1 VKLNVGGTRFETLKSTLTRFPDTRLGRLLELECDDYDDDTNEYFFDRSPKHFETILNFYR-TGGKLHRPEEvCLDEFLEE 79

                          90
                  ....*....|
gi 929273847  477 ADFFQIRPLL 486
Cdd:pfam02214  80 AEFYGLDELA 89
GalKase_gal_bdg pfam10509
Galactokinase galactose-binding signature; This is the highly conserved galactokinase ...
 19-67 3.00e-20

Galactokinase galactose-binding signature; This is the highly conserved galactokinase signature sequence which appears to be present in all galactokinases irrespective of how many other ATP binding sites, etc that they carry. The function of this domain appears to be to bind galactose, and the domain is normally at the N-terminus of the enzymes, EC:2.7.1.6. This domain is associated with the families GHMP_kinases_C, pfam08544 and GHMP_kinases_N, pfam00288.


Pssm-ID: 463125 [Multi-domain]  Cd Length: 50  Bit Score: 84.43  E-value: 3.00e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 929273847   19 YEQSFGGDgPQVAVCAPGRVNLIGEHIDYNQGFVLPMALPMVTVVVGSR 67
Cdd:pfam10509   3 FEELFGKE-PVGVASAPGRVNLIGEHTDYNGGFVLPAAINLDTYVAVSP 50
BTB_POZ_KCTD13_BACURD1 cd18400
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-488 4.39e-20

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 13 (KCTD13); KCTD13, also called BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1 (BACURD1), or TNFAIP1-like protein, is a BTB/POZ domain-containing protein that may function as a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of RhoA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD13 BTB domain forms a novel two-fold symmetric tetramer that is distinct from the tetramer formed by voltage-gated potassium (Kv) channels.


Pssm-ID: 349708  Cd Length: 103  Bit Score: 85.76  E-value: 4.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRyQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRREA 477
Cdd:cd18400    4 VKLNVGGSLHYTTVQTLTK-QDTMLKAMFSGRVEVLTDSEGWVLIDRSGRHFGTILNYLRDGSVPLPESTRELEELLGEA 82

                         90
                 ....*....|.
gi 929273847 478 DFFQIRPLLDE 488
Cdd:cd18400   83 RYYLVQGLVED 93
BTB_POZ_SHKBP1 cd18393
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 396-494 2.92e-19

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in SH3KBP1-binding protein 1 (SHKBP1); SHKBP1, also called SETA-binding protein 1, interacts with cathepsin B and participates in tumor necrosis factor (TNF)-induced apoptosis in ovarian cancer cells. It can promote epidermal growth factor receptor (EGFR) signaling by interrupting c-Cbl-CIN85 complex and inhibiting EGFR degradation. It contains a BTB/POZ domain, also known as tetramerization (T1) domain, a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349701  Cd Length: 103  Bit Score: 83.45  E-value: 2.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 396 DPVSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDlPEGFsEMRLLRR 475
Cdd:cd18393    2 EVIHLNVGGKRFSTSRQTLTWIPDSFFSSLLSGRISTLKDETGAIFIDRDPTVFAPILNFLRTKELD-PRGI-HVSLLLH 79

                         90
                 ....*....|....*....
gi 929273847 476 EADFFQIRPLLDEIRRRVE 494
Cdd:cd18393   80 EAQFYGITPLVRRLQLCEE 98
BTB_POZ_KCTD3 cd18392
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 396-484 3.53e-19

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 3 (KCTD3); KCTD3, also called renal carcinoma antigen NY-REN-45, is a BTB/POZ domain-containing protein that is an accessory subunit of potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3 (HCN3), upregulating its cell-surface expression and current density without affecting its voltage dependence and kinetics. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349700  Cd Length: 88  Bit Score: 82.61  E-value: 3.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 396 DPVSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLpEGFSeMRLLRR 475
Cdd:cd18392    2 EIIQLNVGGTRFSTSRQTLMWIPDSFFSSLLSGRISSLKDETGAIFIDRDPTAFVPILNFLRTKELDL-RGVN-INVLRH 79


                 ....*....
gi 929273847 476 EADFFQIRP 484
Cdd:cd18392   80 EAEFYGITP 88
BTB_POZ_KCTD10_BACURD3 cd18399
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-488 9.53e-19

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 10 (KCTD10); KCTD10, also called BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3 (BACURD3), is a BTB/POZ domain-containing protein that interacts with proliferating cell nuclear antigen (PCNA) and polymerase delta, and participates in DNA repair, DNA replication, and cell-cycle control. Its down-regulation could inhibit cell proliferation. KCTD10 also plays crucial roles in embryonic angiogenesis and heart development in mammals by negatively regulating the Notch signaling pathway. Furthermore, KCTD10 may function as a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of target proteins, leading to their degradation by the proteasome. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD10 BTB domain forms a novel two-fold symmetric tetramer that is distinct from the tetramer formed by voltage-gated potassium (Kv) channels.


Pssm-ID: 349707  Cd Length: 110  Bit Score: 82.04  E-value: 9.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRyQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRREA 477
Cdd:cd18399    9 VKLNVGGALYYTTMQTLTK-QDTMLKAMFSGRMEVLTDSEGWILIDRCGKHFGTILNYLRDGAVPLPESRREIEELLAEA 87

                         90
                 ....*....|.
gi 929273847 478 DFFQIRPLLDE 488
Cdd:cd18399   88 KYYLVQGLVEE 98
mevalon_kin TIGR00549
mevalonate kinase; This model represents mevalonate kinase, the third step in the mevalonate ...
 34-355 1.13e-18

mevalonate kinase; This model represents mevalonate kinase, the third step in the mevalonate pathway of isopentanyl pyrophosphate (IPP) biosynthesis. IPP is a common intermediate for a number of pathways including cholesterol biosynthesis. This model covers enzymes from eukaryotes, archaea and bacteria. The related enzyme from the same pathway, phosphmevalonate kinase, serves as an outgroup for this clade. Paracoccus exhibits two genes within the phosphomevalonate/mevalonate kinase family, one of which falls between trusted and noise cutoffs of this model. The degree of divergence is high, but if the trees created from this model are correct, the proper names of these genes have been swapped. [Central intermediary metabolism, Other]


Pssm-ID: 273130 [Multi-domain]  Cd Length: 273  Bit Score: 86.58  E-value: 1.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847   34 APGRVNLIGEH-IDYNQGfVLPMALPMVTVVVgSRTSGQSASIITaakDVEEPRRVDFDLPNDKALLSPGKpswanyvkg 112
Cdd:TIGR00549   1 APGKIILFGEHaVVYGEP-AIAAPIPLRTTVT-VIESSDGSFIES---DLGRGSLDDAPDELDGLKYVLAE--------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  113 VVQHYRAPPVPGFRAVIASSVPLGGGLSSSASLEVAMYTFLQQLKPDDGDKVAKAVACQKAEHTHAGVPCGImDQFVSVL 192
Cdd:TIGR00549  67 FLSRFSELNPPPLEITIESEIPPGRGLGSSAAVAVALIRALADYFGSELSKEELAELANEAEKIAHGKPSGI-DTATSTS 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  193 GreaHALLIDCRSLEATPvpLSDPGLVILISNSNVKHSlTGseypsrrrqceEAAAILEKaslrdatlkdLEDAKSRLDD 272
Cdd:TIGR00549 146 G---GPVYFEKGEGEFTK--LISLDGYFVIADTGVSGS-TK-----------EAVARVRQ----------LLERFPELID 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  273 ETYRRarhvIEEIerTAQAAEALKKGAYKEFGKLMVESHNSLRDLyEVSCKELDELVSAAVEvEGVFGSRMTGGGFGGCT 352
Cdd:TIGR00549 199 SIMDA----IGEL--TLEAKAALQDGDVESLGELMNINQGLLKAL-GVSHPKLDQLVEIARK-AGALGAKLTGAGGGGCM 270


                  ...
gi 929273847  353 VTL 355
Cdd:TIGR00549 271 IAL 273
BTB_POZ_KCTD18 cd18372
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 396-482 6.10e-17

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 18 (KCTD18); KCTD18 is a BTB/POZ domain-containing protein with with unknown biological function. A duplication of the KCTD18 gene has been found in a patient with epilepsy, developmental delay, and autistic behavior, which may contribute to the phenotype. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349681  Cd Length: 101  Bit Score: 76.77  E-value: 6.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 396 DPVSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRsSSLDLPEGFSEMRLLRR 475
Cdd:cd18372    1 DVLRLNVGGCIYTARRESLCRFKDSMLSSMFSGRFPLKLDESGACVIDRDGRLFKYLLDYLH-GELQIPEDEQTRLALQE 79


                 ....*..
gi 929273847 476 EADFFQI 482
Cdd:cd18372   80 EADYFGI 86
BTB_POZ_Kv_KCTD cd18187
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-480 2.66e-16

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in voltage-gated potassium (Kv) channels and potassium channel tetramerization domain-containing (KCTD) proteins; This family includes two protein groups: voltage-gated potassium (Kv) channels and potassium channel tetramerization domain-containing (KCTD) proteins. Kv channels are membrane proteins with fundamental physiological roles. They are responsible for a variety of electrical phenomena, such as the repolarization of the action potential, spike frequency adaptation, synaptic repolarization, and smooth muscle contraction. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels, and others. All family members contain the BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization.


Pssm-ID: 349498  Cd Length: 83  Bit Score: 74.05  E-value: 2.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFT-GQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEmRLLRRE 476
Cdd:cd18187    1 VVLNVSGTRFVTNRQTLTRHPDTLLGRMFKpGREFTFPNETGEYFIDRDPTVFRTILNYYRTGKLNCPDGISI-PDLREE 79


                 ....
gi 929273847 477 ADFF 480
Cdd:cd18187   80 CDFY 83
BTB_POZ_KCTD17 cd18391
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-494 1.34e-14

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 17 (KCTD17); KCTD17 is a BTB/POZ domain-containing protein that functions as a substrate-adaptor for cullin3-RING ubiquitin ligases that polyubiquitylates trichoplein, a protein involved in ciliogenesis down-regulation. It is a positive regulator of ciliogenesis, playing a crucial role in the initial steps of axoneme extension. A missense mutation in KCTD17 causes autosomal dominant myoclonus-dystonia (M-D). The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD17 BTB domains form pentamers.


Pssm-ID: 349699  Cd Length: 101  Bit Score: 70.02  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQ-ISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLrRE 476
Cdd:cd18391    3 VRLNVGGTVFLTTRQTLCREQKSFLSRLCQGEeLQSDRDETGAYLIDRDPTYFGPILNFLRHGKLVLDKDMAEEGVL-EE 81

                         90
                 ....*....|....*...
gi 929273847 477 ADFFQIRPLLDEIRRRVE 494
Cdd:cd18391   82 AEFYNIGPLIRIIKDRME 99
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
 398-487 5.42e-12

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


Pssm-ID: 197585 [Multi-domain]  Cd Length: 97  Bit Score: 62.32  E-value: 5.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847   398 VSLNVGGEIYTTTLDTLTRYqDSMLGAMFTGQIStLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEgfSEMRLLRREA 477
Cdd:smart00225   2 VTLVVGGKKFHAHKAVLAAH-SPYFKALFSSDFK-ESDKSEIYLDDVSPEDFRALLNFLYTGKLDLPE--ENVEELLELA 77

                           90
                   ....*....|
gi 929273847   478 DFFQIRPLLD 487
Cdd:smart00225  78 DYLQIPGLVE 87
PRK03926 PRK03926
mevalonate kinase; Provisional
 34-362 8.06e-12

mevalonate kinase; Provisional


Pssm-ID: 179677 [Multi-domain]  Cd Length: 302  Bit Score: 66.62  E-value: 8.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847  34 APGRVNLIGEHidynqgfvlpmalpmvTVVVGSRTsgqsasiITAAKDVEEprRVDFDLPNDKALLSP--GKPSWAN-YV 110
Cdd:PRK03926   6 APGKIYLFGEH----------------AVVYGKPA-------IACAIDLRT--YVRAEFNDDSIYIESdyGKTGEKHpYV 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 111 KGVVQHYR-APPVPGFRAVIASSVPLGGGLSSSASLEVAMYTFLQQLKPDDGDKVAKAVACQKAEHTHAGVPCGImDQFV 189
Cdd:PRK03926  61 SAAIEKMReEADKDGVTVSITSQIPVGSGLGSSAAVTVATIGALNRLLGLGLSLEEIAKLGHKVELLVQGAASPT-DTYV 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 190 SVLGreaHALLIDCRSleatpvPLSDPGLVILISNSNVKHSLtgSEYPSRRRQceeaaailekaslrdatlkdledaksr 269
Cdd:PRK03926 140 STMG---GFVTIPDRK------KLPFPECGIVVGYTGSSGST--KELVANVRK--------------------------- 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 270 lddeTYRRARHVIEEI-----ERTAQAAEALKKGAYKEFGKLMVESHnSLRDLYEVSCKELDELVSAAvEVEGVFGSRMT 344
Cdd:PRK03926 182 ----LKEEYPELIEPIlssigKISEKGEELILSGDYVSLGELMNINQ-GLLDALGVSTKELSELIYAA-RTAGALGAKIT 255

                        330
                 ....*....|....*...
gi 929273847 345 GGGFGGCTVTLLQAEAID 362
Cdd:PRK03926 256 GAGGGGCMVALAAPEKQS 273
BTB2_POZ_KCTD19 cd18374
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
 398-490 1.21e-11

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 19 (KCTD19); KCTD19 is a BTB/POZ domain-containing protein with unclear biological function. It may be a host factor involved in Nef-induced downregulation of MHC-I. Nef is a HIV-1-encoded protein that plays a key role in the development of AIDS. KCTD19 contains two BTB domains. This model corresponds to the second domain. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349683  Cd Length: 99  Bit Score: 61.36  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLRdkrgNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLRREA 477
Cdd:cd18374    3 VKVYVGSHWYATYLKTLLKYPELLSNSKKVRWITYGQ----TLLISGDGQMFRHILNFLRLGKLLLPSEFKEWPLLCQEV 78

                         90
                 ....*....|...
gi 929273847 478 DFFQIRPLLDEIR 490
Cdd:cd18374   79 EEYQIPALSEALR 91
BTB_POZ_Kv cd18317
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-479 1.94e-11

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in voltage-gated potassium (Kv) channels; Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. This family includes several groups of alpha subunits such as KCNA/Kv1 family of Shaker-type Kv channels, KCNB/Kv2 family of Shab-type Kv channels, KCNC/Kv3 family of Shaw-type Kv channels, KCND/Kv4 family of Shal-type Kv channels, KCNF/Kv5 subfamily of Kv channels, KCNG/Kv6 subfamily of Kv channels, KCNV/Kv8 subfamily of Kv channels, and KCNS/Kv9 subfamily of Kv channels. Kv alpha subunits form functional homo- or hetero-tetrameric channels (typically with other alpha subunits from the same subfamily) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif. KCNQ/Kv7 channels are not included in this family, since they do not contain a BTB/POZ domain.


Pssm-ID: 349626  Cd Length: 82  Bit Score: 60.31  E-value: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMfTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRlLRREA 477
Cdd:cd18317    1 VVLNVGGTRFELSRSTLLRFPDTRLGKL-AKESHAYDESTNEYFFDRNPEVFEAILDYYRTGELHLPSNVCPAS-FKEEL 78


                 ..
gi 929273847 478 DF 479
Cdd:cd18317   79 EF 80
BTB_POZ_Kv4_KCND cd18380
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-484 2.90e-11

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCND/Kv4 subfamily of Shal-type voltage-dependent potassium channels; Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv4, also known as subfamily D, contains three alpha subunit members, Kv4.1 (KCND1), Kv4.2 (KCND2), and Kv4.3 (KCND3), which are orthologs of the Shal gene in Drosophila. They are A-type potassium channels that mediate the native, fast inactivating (A-type) K+ current (IA) described both in the nervous system (A currents) and the heart (transient outward current). Kv4/KCND subfamily alpha subunits form functional homo- or hetero-tetrameric channels through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif. They are modulated by cytoplasmic KChIPs/KCNIPs (Kv-channel interacting proteins), which are small calcium binding proteins with EF-hand-like domains.


Pssm-ID: 349689 [Multi-domain]  Cd Length: 102  Bit Score: 60.46  E-value: 2.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGamftgqiSTLR-----DKRGNVFIDRDGKVFRYILNFLRSSSLDLP-----EGF 467
Cdd:cd18380    2 IVINVSGRRFETWKNTLEKYPDTLLG-------STEKeffydDDTKEYFFDRDPEIFRHILNFYRTGKLHYPrheciSAY 74

                         90
                 ....*....|....*..
gi 929273847 468 SEmrllrrEADFFQIRP 484
Cdd:cd18380   75 DD------ELAFFGILP 85
GHMP_kinases_N pfam00288
GHMP kinases N terminal domain; This family includes homoserine kinases, galactokinases and ...
 128-194 6.03e-11

GHMP kinases N terminal domain; This family includes homoserine kinases, galactokinases and mevalonate kinases.


Pssm-ID: 395225 [Multi-domain]  Cd Length: 64  Bit Score: 58.33  E-value: 6.03e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 929273847  128 VIASSVPLGGGLSSSASLEVAMYTFLQQLKpddGDKVAKavACQKAEHTHAGVPCGIMDQFVSVLGR 194
Cdd:pfam00288   3 EIESNIPLGAGLGSSAALAVALLLALNELF---GLPLAK--LALEAEELAGGGRGGGMDVAASLYGG 64
BTB_POZ_KCTD2-like cd18362
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-480 4.57e-10

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins KCTD2, KCTD5, and KCTD17, and similar proteins; This subfamily includes potassium channel tetramerization domain-containing proteins KCTD2, KCTD5, and KCTD17, all of which function as adaptors of Cullin3 based ubiquitin E3 ubiquitin ligases. KCTD2 suppresses gliomagenesis by destabilizing c-Myc. KCTD5 is a negative regulator of the AKT pathway, a key signaling cascade frequently deregulated in cancer. KCTD5 does not impact the operation of Kv4.2, Kv3.4, Kv2.1, or Kv1.2 channels. KCTD17 polyubiquitylates trichoplein, a protein involved in ciliogenesis down-regulation. It is a positive regulator of ciliogenesis, playing a crucial role in the initial steps of axoneme extension. A missense mutation in KCTD17 causes autosomal dominant myoclonus-dystonia (M-D). The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. KCTD5 and KCTD17 BTB domains form pentamer structures.


Pssm-ID: 349671 [Multi-domain]  Cd Length: 85  Bit Score: 56.61  E-value: 4.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQ--ISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLrR 475
Cdd:cd18362    2 VKLNVGGTYFLTTRTTLCRDPKSFLCRLCQEDpdLPSDKDETGAYLIDRDPTYFGPILNYLRHGKLIIDKDLAEEGVL-E 80


                 ....*
gi 929273847 476 EADFF 480
Cdd:cd18362   81 EAEFY 85
BTB1_POZ_KCTD19 cd18373
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
 399-489 1.06e-09

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 19 (KCTD19); KCTD19 is a BTB/POZ domain-containing protein with unclear biological function. It may be a host factor involved in Nef-induced downregulation of MHC-I. Nef is a HIV-1-encoded protein that plays a key role in the development of AIDS. KCTD19 contains two BTB domains. This model corresponds to the first domain. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349682  Cd Length: 98  Bit Score: 55.94  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 399 SLNVGGEIYTTTLDTLTRYQDSMLgamFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLpEGFSEMRLLRREAD 478
Cdd:cd18373    2 YFNVGGWIFSVPKSKLAQFPDSLL---WKEASSLSESENTRLFIDRDGFTFRHVHYYLQTSKLSS-SSCSELNLLYEQAA 77

                         90
                 ....*....|.
gi 929273847 479 FFQIRPLLDEI 489
Cdd:cd18373   78 GLQLTSLLQAL 88
BTB_POZ_KCND2 cd18418
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-464 1.13e-09

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily D member 2 (KCND2); KCND2, also called voltage-gated potassium channel subunit Kv4.2, is a major pore-forming subunit in somatodendritic subthreshold A-type potassium current I(SA) channels. It mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCND2 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv4/KCND alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif. It is modulated by cytoplasmic KChIPs/KCNIPs (Kv-channel interacting proteins), which are small calcium binding proteins with EF-hand-like domains.


Pssm-ID: 349725 [Multi-domain]  Cd Length: 103  Bit Score: 56.12  E-value: 1.13e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGamftgqiSTLRD-----KRGNVFIDRDGKVFRYILNFLRSSSLDLP 464
Cdd:cd18418    2 IVLNVSGTRFQTWRNTLERYPDTLLG-------SSERDffyheETQEYFFDRDPDIFRHILNFYRTGKLHYP 66
BTB_POZ_KCTD2 cd18389
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-493 7.19e-09

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 2 (KCTD2); KCTD2 is a BTB/POZ domain-containing protein that functions as an adaptor of Cullin3 E3 ubiquitin ligase. It suppresses gliomagenesis by destabilizing c-Myc. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. KCTD5 and KCTD17 BTB domain, highly similar to KCTD2, form pentamer structures.


Pssm-ID: 349697 [Multi-domain]  Cd Length: 105  Bit Score: 53.84  E-value: 7.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTG--QISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLrR 475
Cdd:cd18389    3 VRLNVGGTYFVSTKQTLCRDPKSFLYRLCQEdpDLDSDKDETGAYLIDRDPTYFGPILNYLRHGKLIINKELAEEGVL-E 81

                         90
                 ....*....|....*...
gi 929273847 476 EADFFQIRPLLDEIRRRV 493
Cdd:cd18389   82 EAEFYNIASLVRLVKERI 99
GHMP_kinases_C pfam08544
GHMP kinases C terminal; This family includes homoserine kinases, galactokinases and ...
 291-355 7.30e-09

GHMP kinases C terminal; This family includes homoserine kinases, galactokinases and mevalonate kinases.


Pssm-ID: 430063 [Multi-domain]  Cd Length: 85  Bit Score: 53.24  E-value: 7.30e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 929273847  291 AAEALKKGAYKEFGKLMVESHNSL--RDLYEVSCKELDELVSAAVEVegVFGSRMTGGGFGGCTVTL 355
Cdd:pfam08544   1 LLEALLRGDLEELGKLLTESAESLepLLVVGILPPELDELLEALLEL--GLGAKLSGSGGGPTVFAL 65
BTB_POZ_KCTD5 cd18390
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-492 2.10e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 5 (KCTD5); KCTD5 is a BTB/POZ domain-containing protein that functions as a substrate adaptor for cullin3 based ubiquitin E3 ligases. It is a negative regulator of the AKT pathway, a key signaling cascade frequently deregulated in cancer. KCTD5 does not impact the operation of Kv4.2, Kv3.4, Kv2.1, or Kv1.2 channels. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. KCTD5 forms pentamers mediated by its BTB domain.


Pssm-ID: 349698 [Multi-domain]  Cd Length: 112  Bit Score: 52.69  E-value: 2.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQ--ISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEGFSEMRLLrR 475
Cdd:cd18390    7 VRLNVGGTYFLTTRQTLCRDPKSFLYRLCQADpdLDSDKDETGAYLIDRDPTYFGPVLNYLRHGKLVINKDLAEEGVL-E 85

                         90       100
                 ....*....|....*....|.
gi 929273847 476 EADFFQIRPLL----DEIRRR 492
Cdd:cd18390   86 EAEFYNITSLIklvkDKIRER 106
BTB_POZ_KCND3 cd18419
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 400-484 4.84e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily D member 3 (KCND3); KCND3, also called voltage-gated potassium channel subunit Kv4.3, is a pore-forming subunit of voltage-gated rapidly inactivating A-type potassium channels. Mutations in KCND3 cause spinocerebellar ataxia. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCND3 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv4/KCND alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif. It is modulated by cytoplasmic KChIPs/KCNIPs (Kv-channel interacting proteins), which are small calcium binding proteins with EF-hand-like domains.


Pssm-ID: 349726 [Multi-domain]  Cd Length: 138  Bit Score: 52.28  E-value: 4.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 400 LNVGGEIYTTTLDTLTRYQDSMLGAmfTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLPEgFSEMRLLRREADF 479
Cdd:cd18419   39 LNVSGRRFQTWRTTLERYPDTLLGS--TEKEFFFNEDTKEYFFDRDPEVFRCVLNFYRTGKLHYPR-YECISAYDEELAF 115


                 ....*
gi 929273847 480 FQIRP 484
Cdd:cd18419  116 YGILP 120
BTB_POZ_KCND1 cd18417
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 400-492 1.75e-07

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily D member 1 (KCND1); KCND1, also called voltage-gated potassium channel subunit Kv4.1, is a pore-forming subunit of voltage-gated rapidly inactivating A-type potassium channels. It may contribute to I (To) current in heart and I (Sa) current in neurons. Its properties are modulated by interactions with other alpha subunits and with regulatory subunits. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCND1 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv4/KCND alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif. It is modulated by cytoplasmic KChIPs/KCNIPs (Kv-channel interacting proteins), which are small calcium binding proteins with EF-hand-like domains.


Pssm-ID: 349724 [Multi-domain]  Cd Length: 138  Bit Score: 50.72  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 400 LNVGGEIYTTTLDTLTRYQDSMLGAmfTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLP-----EGFSEmrllr 474
Cdd:cd18417   39 VNVSGRRFQTWKNTLDRYPDTLLGS--SEKEFFYNEDTQEYFFDRDPEMFRHILNFYRTGRLHYPrheciQAFDE----- 111

                         90       100
                 ....*....|....*....|....
gi 929273847 475 rEADFFQIRP------LLDEIRRR 492
Cdd:cd18417  112 -ELSFYGIIPeiigdcCLEEYRDR 134
PTZ00298 PTZ00298
mevalonate kinase; Provisional
 290-360 4.12e-06

mevalonate kinase; Provisional


Pssm-ID: 240351 [Multi-domain]  Cd Length: 328  Bit Score: 49.47  E-value: 4.12e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 929273847 290 QAAEALKKGAYKEFGKLMVESHNSLRDLyEVSCKELDELVSAAVEVeGVFGSRMTGGGFGGCTVTLLQAEA 360
Cdd:PTZ00298 229 EAKEALQKGNLFRVGELMNANHDLCQKL-TVSCRELDSIVQTCRTY-GALGAKMSGTGRGGLVVALAASED 297
BTB_POZ_Shal-like cd18420
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-484 1.77e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster potassium voltage-gated channel protein Shal and similar proteins; Drosophila melanogaster Shal, also called Shaker cognate l or Shal2, is a transient potassium current (I(A)) channel, which is required for maintaining excitability during repetitive firing and normal locomotion in Drosophila. It may play a role in the nervous system and in the regulation of beating frequency in pacemaker cells. Shal mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. Shal is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.


Pssm-ID: 349727 [Multi-domain]  Cd Length: 139  Bit Score: 44.84  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGamftgqiSTLRD-----KRGNVFIDRDGKVFRYILNFLRSSSLDLPEgfSE-MR 471
Cdd:cd18420   38 LIINVSGRRFETWRNTLEKYPDTLLG-------SNEREffydeETKEYFFDRDPDIFRHILNYYRTGKLHYPK--HEcLT 108

                         90
                 ....*....|...
gi 929273847 472 LLRREADFFQIRP 484
Cdd:cd18420  109 AYDEELAFFGIMP 121
BTB_KCNC2_4 cd18415
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 396-464 7.82e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily C members KCNC2 and KCNC4; KCNC2, also called Shaw-like potassium channel or voltage-gated potassium channel Kv3.2, is a delayed rectifier voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. It contributes to the regulation of the fast action potential repolarization and in sustained high-frequency firing in neurons of the central nervous system. KCNC4, also called KSHIIIC or voltage-gated potassium channel subunit Kv3.4, is a novel high-voltage-activating, tetraethylammonium (TEA)-sensitive, type-A potassium channel that mediates the voltage-dependent potassium ion permeability of excitable membranes. It plays a pivotal role in oxidative stress-related neural cell damage as an oxidation-sensitive channel. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNC2 and KCNC4 are alpha subunit that form functional homo- or hetero-tetrameric channels (with other alpha subunits) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.


Pssm-ID: 349722 [Multi-domain]  Cd Length: 124  Bit Score: 39.76  E-value: 7.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 396 DPVSLNVGG---EIYTTTLDTL--TRY--------QDSMLGAMFTGQISTLRDKRGN-VFIDRDGKVFRYILNFLRSSSL 461
Cdd:cd18415    2 ERIILNVGGtrhETYRSTLKTLpgTRLallassdpQGDCLTQCSQVGGSDGSPGGGNeFFFDRHPGVFAYVLNYYRTGKL 81


                 ...
gi 929273847 462 DLP 464
Cdd:cd18415   82 HCP 84
BTB_POZ_Kv2_KCNB cd18378
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-465 1.57e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCNB/Kv2 subfamily of Shab-type voltage-dependent potassium channels; Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv3, also known as subfamily C, contains two alpha subunit members, Kv2.1 (KCNB1) and Kv2.2 (KCNB2), which are orthologs of the Shab gene in Drosophila. They are delayed-rectifier potassium currents in various neurons, although their physiological roles often remain elusive. Kv2/KCNB subfamily alpha subunits form functional homo- or hetero-tetrameric channels (with other alpha subunits) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.


Pssm-ID: 349687 [Multi-domain]  Cd Length: 109  Bit Score: 38.53  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGamftgqisTLRD----------------KRGNVFIDRDGKVFRYILNFLRSSSL 461
Cdd:cd18378    4 VLLNVGGVRHEVLWRTLDRLPRTRLG--------RLREcnthesllelcddydlEDNEYFFDRHPGAFTSILNFYRTGKL 75


                 ....
gi 929273847 462 DLPE 465
Cdd:cd18378   76 HMPE 79
BTB_POZ_Kv3_KCNC cd18379
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 398-464 1.96e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCNC/Kv3 subfamily of Shaw-type voltage-dependent potassium channels; Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv3, also known as subfamily C, contains four alpha subunit members, Kv3.1 (KCNC1), Kv3.2 (KCNC2), Kv3.3 (KCNC3), and Kv3.4 (KCNC4), which are orthologs of the Shaw gene in Drosophila. Unlike other Kv subfamilies, Kv3 channels typically open only at positive potentials and both, activation and deactivation, in response to changes in voltage are very rapid. They are uniquely associated with the ability of certain neurons to fire action potentials and to release neurotransmitter at high rates of up to 1,000 Hz. Kv3/KCNC subfamily alpha subunits form functional homo- or hetero-tetrameric channels (with other alpha subunits) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.


Pssm-ID: 349688 [Multi-domain]  Cd Length: 109  Bit Score: 38.53  E-value: 1.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 929273847 398 VSLNVGGEIYTTTLDTLTRYQDSMLGAMFTGQISTLR-DKRGN-VFIDRDGKVFRYILNFLRSSSLDLP 464
Cdd:cd18379    1 IVINVGGVRHETYKSTLRNLPDTRLAWLTETEASAFDyDPVTGeFFFDRHPGVFAQILNYYRTGKLHCP 69
BTB_POZ_KCNV2 cd18425
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 400-461 2.58e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily V member 2 (KCNV2); KCNV2, also called voltage-gated potassium channel subunit Kv8.2, is a modulatory voltage-gated potassium channel alpha subunit that modulates channel activity by shifting the threshold and the half-maximal activation to more negative values. KCNV2 is essential for visual function and cone survival. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNV2 is a regulatory alpha subunit that cannot form a functional homo-tetrameric channel. It forms hetero-tetrameric channels (with other functional alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.


Pssm-ID: 349732  Cd Length: 108  Bit Score: 37.82  E-value: 2.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929273847 400 LNVGGEIYTTTLDTLTRYQDSMLGAMFTG-----QISTLRD---KRGNVFIDRDGKVFRYILNFLRSSSL 461
Cdd:cd18425    3 INVGGTSYQISYRVAASYPKTRIGRLATYtdrsrKLDLCDDynvQNDEYFFDRDPAVFHHIYNFYRTGVL 72
BTB_KCNC1_3 cd18414
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 396-464 5.51e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily C members KCNC1 and KCNC3; KCNC1 (also called NGK2, voltage-gated potassium channel subunit Kv3.1, or voltage-gated potassium channel subunit Kv4) and KCNC3 (also called KSHIIID or voltage-gated potassium channel subunit Kv3.3) play important roles in the rapid repolarization of fast-firing brain neurons. Assuming opened or closed conformations in response to the voltage difference across the membrane, the proteins form tetrameric potassium-selective channels through which potassium ions may pass in accordance with their electrochemical gradient. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNC1 and KCNC3 are alpha subunit that form functional homo- or hetero-tetrameric channels (with other alpha subunits) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.


Pssm-ID: 349721 [Multi-domain]  Cd Length: 117  Bit Score: 37.24  E-value: 5.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 929273847 396 DPVSLNVGG---EIYTTTLDTLTRYQDSMLGAMFTGQISTLRDKRGNVFIDRDGKVFRYILNFLRSSSLDLP 464
Cdd:cd18414    3 DRIVINVGGtrhETYRSTLRTLPGTRLAWLAEPDAHSNFDYDPRADEFFFDRHPGVFAHILNYYRTGKLHCP 74
BTB_POZ_KCTD20-like cd18318
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 414-482 7.83e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 20 (KCTD20) and BTB/POZ domain-containing protein 10 (BTBD10); KCTD20, also termed potassium channel tetramerization domain containing 20, is a positive regulator of Akt signaling. It may play an important role in regulating the death and growth of some non-nervous and nervous cells. BTBD10, also termed glucose metabolism-related protein 1 (GMRP1), plays a major role as an activator of AKT family members. It binds to Akt and protein phosphatase 2A (PP2A) and inhibits the PP2A-mediated dephosphorylation of Akt, thereby keeping Akt activated. It also plays a role in preventing motor neuronal death and accelerating the growth of pancreatic beta cells.


Pssm-ID: 349627  Cd Length: 92  Bit Score: 36.14  E-value: 7.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 929273847 414 LTRYQDSMLGAMFT---GQISTLRDKRGNVFIdRDG---KVFRYILNFLRSSSLDLPEGFSEMRLlrREA-DFFQI 482
Cdd:cd18318   19 FTAHPDTMLGRMFGsglENNFTRPNERGEYEV-ADGisaTVFRAILDYYKTGIIRCPPSVSVAEL--REAcDYLLI 91
 
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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