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Conserved domains on  [gi|1939208951|gb|KAF9676154|]
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hypothetical protein SADUNF_Sadunf09G0108800 [Salix dunnii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA_26S_proteasome_subunit cd01452
26S proteasome plays a major role in eukaryotic protein breakdown, especially for ...
 631-816 1.54e-104

26S proteasome plays a major role in eukaryotic protein breakdown, especially for ubiquitin-tagged proteins. It is an ATP-dependent protease responsible for the bulk of non-lysosomal proteolysis in eukaryotes, often using covalent modification of proteins by ubiquitylation. It consists of a 20S proteolytic core particle (CP) and a 19S regulatory particle (RP). The CP is an ATP independent peptidase consisting of hydrolyzing activities. One or both ends of CP carry the RP that confers both ubiquitin and ATP dependence to the 26S proteosome. The RP's proposed functions include recognition of substrates and translocation of these to CP for proteolysis. The RP can dissociate into a stable lid and base subcomplexes. The base is composed of three non-ATPase subunits (Rpn 1, 2 and 10). A single residue in the vWA domain of Rpn10 has been implicated to be responsible for stabilizing the lid-base association.


:

Pssm-ID: 238729  Cd Length: 187  Bit Score: 328.17  E-value: 1.54e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  631 LEATMICIDNSEWMRNGDYSPSRFQAQADAVNLLCGAKTQSNPENTVGILTMAGKQVRVLTTLTSDLGKILSCMHGLEVG 710
Cdd:cd01452      3 LEATMICIDNSEYMRNGDYPPTRFQAQADAVNLICQAKTRSNPENNVGLMTMAGNSPEVLVTLTNDQGKILSKLHDVQPK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  711 GEMNLSAGIQVAQLALKHRQNKNQQQRIIVFAGSPIKYDKKMLETIGKKLKKNNVSLDIVDFGEEEDGkPEKLEALFAAV 790
Cdd:cd01452     83 GKANFITGIQIAQLALKHRQNKNQKQRIVAFVGSPIEEDEKDLVKLAKRLKKNNVSVDIINFGEIDDN-TEKLTAFIDAV 161

                          170       180
                   ....*....|....*....|....*.
gi 1939208951  791 NSNDSSHIVHIPPGGTAISDALMNTP 816
Cdd:cd01452    162 NGKDGSHLVSVPPGENLLSDALLSSP 187
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 1130-1265 6.51e-97

actin depolymerizing factor; Provisional


:

Pssm-ID: 178755  Cd Length: 141  Bit Score: 305.31  E-value: 6.51e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951 1130 ATTGMWVTDECKNSFHQMKWKKVHKYIVFKIDEKSRLVTVDKVGGPGESYDDLAASLPGDDCRYAVFDFDFVTVDNCRKS 1209
Cdd:PLN03216     6 ATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKS 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1939208951 1210 KIFFIAWAPAASRIRAKMLYATSKAGLRRVLEGIHYELQATDPTEMGFDLIRDRAK 1265
Cdd:PLN03216    86 KIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRAK 141
Choline_transpo pfam04515
Plasma-membrane choline transporter; This family represents a high-affinity plasma-membrane ...
 206-529 2.23e-72

Plasma-membrane choline transporter; This family represents a high-affinity plasma-membrane choline transporter in C.elegans which is thought to be rate-limiting for ACh synthesis in cholinergic nerve terminals.


:

Pssm-ID: 461337  Cd Length: 325  Bit Score: 244.41  E-value: 2.23e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  206 VFVFLIIGIIVWIFVANWQRVELTVKIIGVASDALSKNLGLCVVIPLLTLGLVVYYTPIVVFLVFARLNGKIVSK----- 280
Cdd:pfam04515    1 IVFLIIAVILLLLLIFLRKRIPLAIALLKEASKAIKSNPSLLLVPLLTFLILLAFSAYWIVVAVALYLASSGGPPykvnd 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  281 -ESKGEYTCVWKQDSWVPAYYTLAILTMLWSLTIMVEAQVYVISGTIAQWYFTKEDAK-PRRSIRSSLRwsvatysssvt 358
Cdd:pfam04515   81 gNSSGGGGVEFESDSKVIYLLLYHLFGLLWTSEFILAVQQMTIAGAVASWYFAKKDPGtPKFPVLGSFK----------- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  359 litNAFGPSSGTVCLSGLLICIIRLVRAAVDSASQE------NVPGMVNLVLRCCVRVFLSAVDFLNKFTINFVAITGEA 432
Cdd:pfam04515  150 ---RALTYHLGSIAFGSLILAIVQILRLILEYLDRKlkkaenKIARCLLCCLQCCLWCLEKFLKYLNKNAYIMIAIYGKS 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  433 YCTSARMTYELLKRNLLSAVFVETVSTRLLAGITFVLSAIYAIVVCAILKGASNIGVYSY--VVAVLAWALLIIVLGFFV 510
Cdd:pfam04515  227 FCTSAKDAFELLKRNGLRVAVNDCLGDFVLFLGKLFVALLTGLIAYLYLRFTTNPASLNSpvVPLLVAFLIGYLIASIFM 306

                          330
                   ....*....|....*....
gi 1939208951  511 HVLDNVIETVYVCYAIDRD 529
Cdd:pfam04515  307 SVYESGVDTIFLCFAEDPE 325
PSMD4_RAZUL cd22297
RAZUL (Rpn10 AZUL-binding) domain of 26S proteasome non-ATPase regulatory subunit 4 (PSMD4) ...
 968-1015 1.42e-15

RAZUL (Rpn10 AZUL-binding) domain of 26S proteasome non-ATPase regulatory subunit 4 (PSMD4) and similar proteins; PSMD4 is also called 26S proteasome regulatory subunit RPN10, 26S proteasome regulatory subunit S5A, antisecretory factor 1, AF, ASF, or multiubiquitin chain-binding protein (MCB1). It acts as a ubiquitin receptor subunit through ubiquitin-interacting motifs and selects ubiquitin-conjugates for destruction. It displays a preferred selectivity for longer polyubiquitin chains. PSMD4 is a component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. The proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. The model corresponds to the C-terminal Rpn10 AZUL-binding domain (RAZUL) of PSMD4, which is responsible for binding the AZUL domain of E6AP/UBE3A. AZUL stands for amino-terminal zinc-binding domain of ubiquitin E3a ligase.


:

Pssm-ID: 412092  Cd Length: 48  Bit Score: 71.83  E-value: 1.42e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1939208951  968 SSQSDMSKALEDQSFVSSVLASLPGVDPNDPSVKELLASFQGQASQSE 1015
Cdd:cd22297      1 SEEEDMSDVMQDPEFLQSVLGSLPGVDPNDEAVQNALGSLAKQDEKKK 48
Voltage_CLC super family cl28978
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 120-219 4.32e-04

Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane helices. Each protein forms a single pore. It has been shown that some members of this family form homodimers. In terms of primary structure, they are unrelated to known cation channels or other types of anion channels. Three ClC subfamilies are found in animals. ClC-1 is involved in setting and restoring the resting membrane potential of skeletal muscle, while other channels play important parts in solute concentration mechanisms in the kidney. These proteins contain two pfam00571 domains.


The actual alignment was detected with superfamily member pfam00654:

Pssm-ID: 425802 [Multi-domain]  Cd Length: 344  Bit Score: 44.08  E-value: 4.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  120 FYSLSSSGSVFLKSLISTLVVTLILSVPVCFLLllslkHYTKQIVYVSLPLFVVIPFFFNV--YWFVACTV-SSSCSDAF 196
Cdd:pfam00654  119 SFSLRALIPVLLASVVAALVSRLIFGNSPLFSV-----GEPGSLSLLELPLFILLGILCGLlgALFNRLLLkVQRLFRKL 193

                           90       100
                   ....*....|....*....|...
gi 1939208951  197 PLVYRILVLVFVFLIIGIIVWIF 219
Cdd:pfam00654  194 LKIPPVLRPALGGLLVGLLGLLF 216
 
Name Accession Description Interval E-value
VWA_26S_proteasome_subunit cd01452
26S proteasome plays a major role in eukaryotic protein breakdown, especially for ...
 631-816 1.54e-104

26S proteasome plays a major role in eukaryotic protein breakdown, especially for ubiquitin-tagged proteins. It is an ATP-dependent protease responsible for the bulk of non-lysosomal proteolysis in eukaryotes, often using covalent modification of proteins by ubiquitylation. It consists of a 20S proteolytic core particle (CP) and a 19S regulatory particle (RP). The CP is an ATP independent peptidase consisting of hydrolyzing activities. One or both ends of CP carry the RP that confers both ubiquitin and ATP dependence to the 26S proteosome. The RP's proposed functions include recognition of substrates and translocation of these to CP for proteolysis. The RP can dissociate into a stable lid and base subcomplexes. The base is composed of three non-ATPase subunits (Rpn 1, 2 and 10). A single residue in the vWA domain of Rpn10 has been implicated to be responsible for stabilizing the lid-base association.


Pssm-ID: 238729  Cd Length: 187  Bit Score: 328.17  E-value: 1.54e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  631 LEATMICIDNSEWMRNGDYSPSRFQAQADAVNLLCGAKTQSNPENTVGILTMAGKQVRVLTTLTSDLGKILSCMHGLEVG 710
Cdd:cd01452      3 LEATMICIDNSEYMRNGDYPPTRFQAQADAVNLICQAKTRSNPENNVGLMTMAGNSPEVLVTLTNDQGKILSKLHDVQPK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  711 GEMNLSAGIQVAQLALKHRQNKNQQQRIIVFAGSPIKYDKKMLETIGKKLKKNNVSLDIVDFGEEEDGkPEKLEALFAAV 790
Cdd:cd01452     83 GKANFITGIQIAQLALKHRQNKNQKQRIVAFVGSPIEEDEKDLVKLAKRLKKNNVSVDIINFGEIDDN-TEKLTAFIDAV 161

                          170       180
                   ....*....|....*....|....*.
gi 1939208951  791 NSNDSSHIVHIPPGGTAISDALMNTP 816
Cdd:cd01452    162 NGKDGSHLVSVPPGENLLSDALLSSP 187
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 1130-1265 6.51e-97

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 305.31  E-value: 6.51e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951 1130 ATTGMWVTDECKNSFHQMKWKKVHKYIVFKIDEKSRLVTVDKVGGPGESYDDLAASLPGDDCRYAVFDFDFVTVDNCRKS 1209
Cdd:PLN03216     6 ATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKS 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1939208951 1210 KIFFIAWAPAASRIRAKMLYATSKAGLRRVLEGIHYELQATDPTEMGFDLIRDRAK 1265
Cdd:PLN03216    86 KIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRAK 141
Choline_transpo pfam04515
Plasma-membrane choline transporter; This family represents a high-affinity plasma-membrane ...
 206-529 2.23e-72

Plasma-membrane choline transporter; This family represents a high-affinity plasma-membrane choline transporter in C.elegans which is thought to be rate-limiting for ACh synthesis in cholinergic nerve terminals.


Pssm-ID: 461337  Cd Length: 325  Bit Score: 244.41  E-value: 2.23e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  206 VFVFLIIGIIVWIFVANWQRVELTVKIIGVASDALSKNLGLCVVIPLLTLGLVVYYTPIVVFLVFARLNGKIVSK----- 280
Cdd:pfam04515    1 IVFLIIAVILLLLLIFLRKRIPLAIALLKEASKAIKSNPSLLLVPLLTFLILLAFSAYWIVVAVALYLASSGGPPykvnd 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  281 -ESKGEYTCVWKQDSWVPAYYTLAILTMLWSLTIMVEAQVYVISGTIAQWYFTKEDAK-PRRSIRSSLRwsvatysssvt 358
Cdd:pfam04515   81 gNSSGGGGVEFESDSKVIYLLLYHLFGLLWTSEFILAVQQMTIAGAVASWYFAKKDPGtPKFPVLGSFK----------- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  359 litNAFGPSSGTVCLSGLLICIIRLVRAAVDSASQE------NVPGMVNLVLRCCVRVFLSAVDFLNKFTINFVAITGEA 432
Cdd:pfam04515  150 ---RALTYHLGSIAFGSLILAIVQILRLILEYLDRKlkkaenKIARCLLCCLQCCLWCLEKFLKYLNKNAYIMIAIYGKS 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  433 YCTSARMTYELLKRNLLSAVFVETVSTRLLAGITFVLSAIYAIVVCAILKGASNIGVYSY--VVAVLAWALLIIVLGFFV 510
Cdd:pfam04515  227 FCTSAKDAFELLKRNGLRVAVNDCLGDFVLFLGKLFVALLTGLIAYLYLRFTTNPASLNSpvVPLLVAFLIGYLIASIFM 306

                          330
                   ....*....|....*....
gi 1939208951  511 HVLDNVIETVYVCYAIDRD 529
Cdd:pfam04515  307 SVYESGVDTIFLCFAEDPE 325
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 1132-1264 4.22e-56

Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. These proteins enhance the turnover rate of actin, and interact with actin monomers (G-actin) as well as actin filaments (F-actin), typically with a preference for ADP-G-actin subunits. The basic function of cofilin is to promote disassembly of aged actin filaments. Vertebrates have three isoforms of cofilin: cofilin-1 (Cfl1, non-muscle cofilin), cofilin-2 (muscle cofilin), and ADF (destrin). When bound to actin monomers, cofilins inhibit their spontaneous exchange of nucleotides. The cooperative binding to (aged) ADP-F-actin induces a local change in the actin filament structure and further promotes aging.


Pssm-ID: 200442  Cd Length: 133  Bit Score: 190.46  E-value: 4.22e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951 1132 TGMWVTDECKNSFHQMKWKKVHKYIVFKIDEKSRLVTVDKVGGPGESYDDLAASLPGDDCRYAVFDFDFVTVDNCRKSKI 1211
Cdd:cd11286      1 SGVKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1939208951 1212 FFIAWAPAASRIRAKMLYATSKAGLRRVLEGIHYELQATDPTEMGFDLIRDRA 1264
Cdd:cd11286     81 VFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 1138-1265 1.12e-45

Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers.


Pssm-ID: 214516  Cd Length: 127  Bit Score: 160.53  E-value: 1.12e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  1138 DECKNSFHQMKWKKVHKYIVFKIDEKSRLVTVDKVGGPGESYDDLAASLPGDDCRYAVFDFDFVTvDNCRKSKIFFIAWA 1217
Cdd:smart00102    1 EDCKEAFNELKKKRKHSAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKFTT-EESKKSKIVFIFWS 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1939208951  1218 PAASRIRAKMLYATSKAGLRRVLEGIHYELQATDPTEMGFDLIRDRAK 1265
Cdd:smart00102   80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 1140-1262 2.04e-41

Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin monomers.


Pssm-ID: 459727  Cd Length: 123  Bit Score: 148.11  E-value: 2.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951 1140 CKNSFHQMKWKKVHKYIVFKIDEKSRLVTVDKVGGPGESYDDLAASLPGDDCRYAVFDFDFVTVDNCRKSKIFFIAWAPA 1219
Cdd:pfam00241    1 CKEAYQELRSDKKTNWIIFKIDDDKEEIVVEETGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITWCPD 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1939208951 1220 ASRIRAKMLYATSKAGLRRVLEGIHYELQATDPTEMGFDLIRD 1262
Cdd:pfam00241   81 GAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
VWA_2 pfam13519
von Willebrand factor type A domain;
634-741 5.33e-29

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 112.00  E-value: 5.33e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  634 TMICIDNSEWMRNGDYSPSRFQAQADAVNLLCgaktQSNPENTVGILTMAGkQVRVLTTLTSDLGKILSCMHGLEV-GGE 712
Cdd:pfam13519    1 LVFVLDTSGSMRNGDYGPTRLEAAKDAVLALL----KSLPGDRVGLVTFGD-GPEVLIPLTKDRAKILRALRRLEPkGGG 75

                           90       100
                   ....*....|....*....|....*....
gi 1939208951  713 MNLSAGIQVAQLALKHRQnKNQQQRIIVF 741
Cdd:pfam13519   76 TNLAAALQLARAALKHRR-KNQPRRIVLI 103
PSMD4_RAZUL cd22297
RAZUL (Rpn10 AZUL-binding) domain of 26S proteasome non-ATPase regulatory subunit 4 (PSMD4) ...
 968-1015 1.42e-15

RAZUL (Rpn10 AZUL-binding) domain of 26S proteasome non-ATPase regulatory subunit 4 (PSMD4) and similar proteins; PSMD4 is also called 26S proteasome regulatory subunit RPN10, 26S proteasome regulatory subunit S5A, antisecretory factor 1, AF, ASF, or multiubiquitin chain-binding protein (MCB1). It acts as a ubiquitin receptor subunit through ubiquitin-interacting motifs and selects ubiquitin-conjugates for destruction. It displays a preferred selectivity for longer polyubiquitin chains. PSMD4 is a component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. The proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. The model corresponds to the C-terminal Rpn10 AZUL-binding domain (RAZUL) of PSMD4, which is responsible for binding the AZUL domain of E6AP/UBE3A. AZUL stands for amino-terminal zinc-binding domain of ubiquitin E3a ligase.


Pssm-ID: 412092  Cd Length: 48  Bit Score: 71.83  E-value: 1.42e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1939208951  968 SSQSDMSKALEDQSFVSSVLASLPGVDPNDPSVKELLASFQGQASQSE 1015
Cdd:cd22297      1 SEEEDMSDVMQDPEFLQSVLGSLPGVDPNDEAVQNALGSLAKQDEKKK 48
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 635-802 5.29e-15

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 74.41  E-value: 5.29e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951   635 MICIDNSEWMRngdysPSRFQAQADAVNLLCGAKTQSNPENTVGILTMAGKqVRVLTTL--TSDLGKILSCMHGLEV--G 710
Cdd:smart00327    3 VFLLDGSGSMG-----GNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDD-ARVLFPLndSRSKDALLEALASLSYklG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951   711 GEMNLSAGIQVAQLALKHRQNKNQ---QQRIIVFAGSPIKYDKKMLETIGKKLKKNNVSLDIVDFGEEEDgkPEKLEAL- 786
Cdd:smart00327   77 GGTNLGAALQYALENLFSKSAGSRrgaPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVD--EEELKKLa 154

                           170       180
                    ....*....|....*....|.
gi 1939208951   787 -----FAAVNSNDSSHIVHIP 802
Cdd:smart00327  155 sapggVYVFLPELLDLLIDLL 175
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 635-776 6.04e-07

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 52.25  E-value: 6.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  635 MICIDNSEWMRngdySPSRFQAQADAV-NLLcgakTQSNPENTVGILTMAGkQVRVLTTLTSDLGKILSCMHGLEVGGEM 713
Cdd:COG1240     96 VLVVDASGSMA----AENRLEAAKGALlDFL----DDYRPRDRVGLVAFGG-EAEVLLPLTRDREALKRALDELPPGGGT 166

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939208951  714 NLSAGIQVAQLALKhRQNKNQQQRIIVF------AGSPikydkkMLETIGKKLKKNNVSLDIVDFGEEE 776
Cdd:COG1240    167 PLGDALALALELLK-RADPARRKVIVLLtdgrdnAGRI------DPLEAAELAAAAGIRIYTIGVGTEA 228
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 120-219 4.32e-04

Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane helices. Each protein forms a single pore. It has been shown that some members of this family form homodimers. In terms of primary structure, they are unrelated to known cation channels or other types of anion channels. Three ClC subfamilies are found in animals. ClC-1 is involved in setting and restoring the resting membrane potential of skeletal muscle, while other channels play important parts in solute concentration mechanisms in the kidney. These proteins contain two pfam00571 domains.


Pssm-ID: 425802 [Multi-domain]  Cd Length: 344  Bit Score: 44.08  E-value: 4.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  120 FYSLSSSGSVFLKSLISTLVVTLILSVPVCFLLllslkHYTKQIVYVSLPLFVVIPFFFNV--YWFVACTV-SSSCSDAF 196
Cdd:pfam00654  119 SFSLRALIPVLLASVVAALVSRLIFGNSPLFSV-----GEPGSLSLLELPLFILLGILCGLlgALFNRLLLkVQRLFRKL 193

                           90       100
                   ....*....|....*....|...
gi 1939208951  197 PLVYRILVLVFVFLIIGIIVWIF 219
Cdd:pfam00654  194 LKIPPVLRPALGGLLVGLLGLLF 216
7tmA_EDG-like cd14972
endothelial differentiation gene family, member of the class A family of seven-transmembrane G ...
 118-269 6.07e-03

endothelial differentiation gene family, member of the class A family of seven-transmembrane G protein-coupled receptors; This group represents the endothelial differentiation gene (Edg) family of G-protein coupled receptors, melanocortin/ACTH receptors, and cannabinoid receptors as well as their closely related receptors. The Edg GPCRs bind blood borne lysophospholipids including sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA), which are involved in the regulation of cell proliferation, survival, migration, invasion, endothelial cell shape change and cytoskeletal remodeling. The Edg receptors are classified into two subfamilies: the lysophosphatidic acid subfamily that includes LPA1 (Edg2), LPA2 (Edg4), and LPA3 (Edg7); and the S1P subfamily that includes S1P1 (Edg1), S1P2 (Edg5), S1P3 (Edg3), S1P4 (Edg6), and S1P5 (Edg8). Melanocortin receptors bind a group of pituitary peptide hormones known as melanocortins, which include adrenocorticotropic hormone (ACTH) and the different isoforms of melanocyte-stimulating hormones. Two types of cannabinoid receptors, CB1 and CB2, are activated by naturally occurring endocannabinoids, cannabis plant-derived cannabinoids such as tetrahydrocannabinol, or synthetic cannabinoids. The CB receptors are involved in the various physiological processes such as appetite, mood, memory, and pain sensation. CB1 receptor is expressed predominantly in central and peripheral neurons, while CB2 receptor is found mainly in the immune system.


Pssm-ID: 341317 [Multi-domain]  Cd Length: 275  Bit Score: 39.97  E-value: 6.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  118 FDFYSLSSSGSVFLKSLIST-LVVTLILSVpvCFLLLLSLKHY-------------TKQIVYVSL----PLFVVIPFFFN 179
Cdd:cd14972     56 LSVLLVSLTPSPATWLLRKGsLVLSLLASA--YSLLAIAVDRYisivhgltyvnnvTNKRVKVLIalvwVWSVLLALLPV 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  180 VYWFVACTVSSSCSDAFPLV---YRILVLVFVFLIIGIIVW----IFVANWQRVELTVKIIGVASDA-LSKNLGLCVVIP 251
Cdd:cd14972    134 LGWNCVLCDQESCSPLGPGLpksYLVLILVFFFIALVIIVFlyvrIFWCLWRHANAIAARQEAAVPAqPSTSRKLAKTVV 213

                          170
                   ....*....|....*...
gi 1939208951  252 LLTLGLVVYYTPIVVFLV 269
Cdd:cd14972    214 IVLGVFLVCWLPLLILLV 231
 
Name Accession Description Interval E-value
VWA_26S_proteasome_subunit cd01452
26S proteasome plays a major role in eukaryotic protein breakdown, especially for ...
 631-816 1.54e-104

26S proteasome plays a major role in eukaryotic protein breakdown, especially for ubiquitin-tagged proteins. It is an ATP-dependent protease responsible for the bulk of non-lysosomal proteolysis in eukaryotes, often using covalent modification of proteins by ubiquitylation. It consists of a 20S proteolytic core particle (CP) and a 19S regulatory particle (RP). The CP is an ATP independent peptidase consisting of hydrolyzing activities. One or both ends of CP carry the RP that confers both ubiquitin and ATP dependence to the 26S proteosome. The RP's proposed functions include recognition of substrates and translocation of these to CP for proteolysis. The RP can dissociate into a stable lid and base subcomplexes. The base is composed of three non-ATPase subunits (Rpn 1, 2 and 10). A single residue in the vWA domain of Rpn10 has been implicated to be responsible for stabilizing the lid-base association.


Pssm-ID: 238729  Cd Length: 187  Bit Score: 328.17  E-value: 1.54e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  631 LEATMICIDNSEWMRNGDYSPSRFQAQADAVNLLCGAKTQSNPENTVGILTMAGKQVRVLTTLTSDLGKILSCMHGLEVG 710
Cdd:cd01452      3 LEATMICIDNSEYMRNGDYPPTRFQAQADAVNLICQAKTRSNPENNVGLMTMAGNSPEVLVTLTNDQGKILSKLHDVQPK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  711 GEMNLSAGIQVAQLALKHRQNKNQQQRIIVFAGSPIKYDKKMLETIGKKLKKNNVSLDIVDFGEEEDGkPEKLEALFAAV 790
Cdd:cd01452     83 GKANFITGIQIAQLALKHRQNKNQKQRIVAFVGSPIEEDEKDLVKLAKRLKKNNVSVDIINFGEIDDN-TEKLTAFIDAV 161

                          170       180
                   ....*....|....*....|....*.
gi 1939208951  791 NSNDSSHIVHIPPGGTAISDALMNTP 816
Cdd:cd01452    162 NGKDGSHLVSVPPGENLLSDALLSSP 187
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 1130-1265 6.51e-97

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 305.31  E-value: 6.51e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951 1130 ATTGMWVTDECKNSFHQMKWKKVHKYIVFKIDEKSRLVTVDKVGGPGESYDDLAASLPGDDCRYAVFDFDFVTVDNCRKS 1209
Cdd:PLN03216     6 ATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKS 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1939208951 1210 KIFFIAWAPAASRIRAKMLYATSKAGLRRVLEGIHYELQATDPTEMGFDLIRDRAK 1265
Cdd:PLN03216    86 KIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRAK 141
Choline_transpo pfam04515
Plasma-membrane choline transporter; This family represents a high-affinity plasma-membrane ...
 206-529 2.23e-72

Plasma-membrane choline transporter; This family represents a high-affinity plasma-membrane choline transporter in C.elegans which is thought to be rate-limiting for ACh synthesis in cholinergic nerve terminals.


Pssm-ID: 461337  Cd Length: 325  Bit Score: 244.41  E-value: 2.23e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  206 VFVFLIIGIIVWIFVANWQRVELTVKIIGVASDALSKNLGLCVVIPLLTLGLVVYYTPIVVFLVFARLNGKIVSK----- 280
Cdd:pfam04515    1 IVFLIIAVILLLLLIFLRKRIPLAIALLKEASKAIKSNPSLLLVPLLTFLILLAFSAYWIVVAVALYLASSGGPPykvnd 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  281 -ESKGEYTCVWKQDSWVPAYYTLAILTMLWSLTIMVEAQVYVISGTIAQWYFTKEDAK-PRRSIRSSLRwsvatysssvt 358
Cdd:pfam04515   81 gNSSGGGGVEFESDSKVIYLLLYHLFGLLWTSEFILAVQQMTIAGAVASWYFAKKDPGtPKFPVLGSFK----------- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  359 litNAFGPSSGTVCLSGLLICIIRLVRAAVDSASQE------NVPGMVNLVLRCCVRVFLSAVDFLNKFTINFVAITGEA 432
Cdd:pfam04515  150 ---RALTYHLGSIAFGSLILAIVQILRLILEYLDRKlkkaenKIARCLLCCLQCCLWCLEKFLKYLNKNAYIMIAIYGKS 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  433 YCTSARMTYELLKRNLLSAVFVETVSTRLLAGITFVLSAIYAIVVCAILKGASNIGVYSY--VVAVLAWALLIIVLGFFV 510
Cdd:pfam04515  227 FCTSAKDAFELLKRNGLRVAVNDCLGDFVLFLGKLFVALLTGLIAYLYLRFTTNPASLNSpvVPLLVAFLIGYLIASIFM 306

                          330
                   ....*....|....*....
gi 1939208951  511 HVLDNVIETVYVCYAIDRD 529
Cdd:pfam04515  307 SVYESGVDTIFLCFAEDPE 325
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 1132-1264 4.22e-56

Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. These proteins enhance the turnover rate of actin, and interact with actin monomers (G-actin) as well as actin filaments (F-actin), typically with a preference for ADP-G-actin subunits. The basic function of cofilin is to promote disassembly of aged actin filaments. Vertebrates have three isoforms of cofilin: cofilin-1 (Cfl1, non-muscle cofilin), cofilin-2 (muscle cofilin), and ADF (destrin). When bound to actin monomers, cofilins inhibit their spontaneous exchange of nucleotides. The cooperative binding to (aged) ADP-F-actin induces a local change in the actin filament structure and further promotes aging.


Pssm-ID: 200442  Cd Length: 133  Bit Score: 190.46  E-value: 4.22e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951 1132 TGMWVTDECKNSFHQMKWKKVHKYIVFKIDEKSRLVTVDKVGGPGESYDDLAASLPGDDCRYAVFDFDFVTVDNCRKSKI 1211
Cdd:cd11286      1 SGVKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1939208951 1212 FFIAWAPAASRIRAKMLYATSKAGLRRVLEGIHYELQATDPTEMGFDLIRDRA 1264
Cdd:cd11286     81 VFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 1138-1265 1.12e-45

Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers.


Pssm-ID: 214516  Cd Length: 127  Bit Score: 160.53  E-value: 1.12e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  1138 DECKNSFHQMKWKKVHKYIVFKIDEKSRLVTVDKVGGPGESYDDLAASLPGDDCRYAVFDFDFVTvDNCRKSKIFFIAWA 1217
Cdd:smart00102    1 EDCKEAFNELKKKRKHSAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKFTT-EESKKSKIVFIFWS 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1939208951  1218 PAASRIRAKMLYATSKAGLRRVLEGIHYELQATDPTEMGFDLIRDRAK 1265
Cdd:smart00102   80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 1140-1262 2.04e-41

Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin monomers.


Pssm-ID: 459727  Cd Length: 123  Bit Score: 148.11  E-value: 2.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951 1140 CKNSFHQMKWKKVHKYIVFKIDEKSRLVTVDKVGGPGESYDDLAASLPGDDCRYAVFDFDFVTVDNCRKSKIFFIAWAPA 1219
Cdd:pfam00241    1 CKEAYQELRSDKKTNWIIFKIDDDKEEIVVEETGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITWCPD 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1939208951 1220 ASRIRAKMLYATSKAGLRRVLEGIHYELQATDPTEMGFDLIRD 1262
Cdd:pfam00241   81 GAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
VWA_2 pfam13519
von Willebrand factor type A domain;
634-741 5.33e-29

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 112.00  E-value: 5.33e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  634 TMICIDNSEWMRNGDYSPSRFQAQADAVNLLCgaktQSNPENTVGILTMAGkQVRVLTTLTSDLGKILSCMHGLEV-GGE 712
Cdd:pfam13519    1 LVFVLDTSGSMRNGDYGPTRLEAAKDAVLALL----KSLPGDRVGLVTFGD-GPEVLIPLTKDRAKILRALRRLEPkGGG 75

                           90       100
                   ....*....|....*....|....*....
gi 1939208951  713 MNLSAGIQVAQLALKHRQnKNQQQRIIVF 741
Cdd:pfam13519   76 TNLAAALQLARAALKHRR-KNQPRRIVLI 103
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 1154-1251 1.57e-19

Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization factor/cofilin-like domains are present in a family of essential eukaryotic actin regulatory proteins; these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments.


Pssm-ID: 200435  Cd Length: 97  Bit Score: 84.82  E-value: 1.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951 1154 KYIVFKIDEKSRLVtvdKVGGPGESY-DDLAASLPGDDCRYAVFDFDFVTVDNCRkSKIFFIAWAPAASRIRAKMLYATS 1232
Cdd:cd00013      1 DWVLFKVDAKKEEI---VVGSTGAGFlDEFLEELPEDDPRYAFYRFKYPHSDDKR-SKFVFISWIPDGVSIKQKMVYATN 76

                           90
                   ....*....|....*....
gi 1939208951 1233 KAGLRRVLEGIHYELQATD 1251
Cdd:cd00013     77 KQTLKEALFGLAVPVQIRD 95
PSMD4_RAZUL cd22297
RAZUL (Rpn10 AZUL-binding) domain of 26S proteasome non-ATPase regulatory subunit 4 (PSMD4) ...
 968-1015 1.42e-15

RAZUL (Rpn10 AZUL-binding) domain of 26S proteasome non-ATPase regulatory subunit 4 (PSMD4) and similar proteins; PSMD4 is also called 26S proteasome regulatory subunit RPN10, 26S proteasome regulatory subunit S5A, antisecretory factor 1, AF, ASF, or multiubiquitin chain-binding protein (MCB1). It acts as a ubiquitin receptor subunit through ubiquitin-interacting motifs and selects ubiquitin-conjugates for destruction. It displays a preferred selectivity for longer polyubiquitin chains. PSMD4 is a component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. The proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. The model corresponds to the C-terminal Rpn10 AZUL-binding domain (RAZUL) of PSMD4, which is responsible for binding the AZUL domain of E6AP/UBE3A. AZUL stands for amino-terminal zinc-binding domain of ubiquitin E3a ligase.


Pssm-ID: 412092  Cd Length: 48  Bit Score: 71.83  E-value: 1.42e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1939208951  968 SSQSDMSKALEDQSFVSSVLASLPGVDPNDPSVKELLASFQGQASQSE 1015
Cdd:cd22297      1 SEEEDMSDVMQDPEFLQSVLGSLPGVDPNDEAVQNALGSLAKQDEKKK 48
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 635-802 5.29e-15

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 74.41  E-value: 5.29e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951   635 MICIDNSEWMRngdysPSRFQAQADAVNLLCGAKTQSNPENTVGILTMAGKqVRVLTTL--TSDLGKILSCMHGLEV--G 710
Cdd:smart00327    3 VFLLDGSGSMG-----GNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDD-ARVLFPLndSRSKDALLEALASLSYklG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951   711 GEMNLSAGIQVAQLALKHRQNKNQ---QQRIIVFAGSPIKYDKKMLETIGKKLKKNNVSLDIVDFGEEEDgkPEKLEAL- 786
Cdd:smart00327   77 GGTNLGAALQYALENLFSKSAGSRrgaPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVD--EEELKKLa 154

                           170       180
                    ....*....|....*....|.
gi 1939208951   787 -----FAAVNSNDSSHIVHIP 802
Cdd:smart00327  155 sapggVYVFLPELLDLLIDLL 175
PTZ00152 PTZ00152
cofilin/actin-depolymerizing factor 1-like protein; Provisional
 1132-1243 1.81e-14

cofilin/actin-depolymerizing factor 1-like protein; Provisional


Pssm-ID: 173441  Cd Length: 122  Bit Score: 71.14  E-value: 1.81e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951 1132 TGMWVTDECKNSFHQMKWKKVHKYIVFKIDEKSRLVTVDkvgGPGESYDDLAASLPGDD---CRYAVFDfdfvtvdncRK 1208
Cdd:PTZ00152     3 SGIRVNDNCVTEFNNMKIRKTCRWIIFVIENCEIIIHSK---GATTTLTELVGSIDKNDkiqCAYVVFD---------AV 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1939208951 1209 SKIFFIAWAPAASRIRAKMLYATSKAGLRRVLEGI 1243
Cdd:PTZ00152    71 NKIHFFMYARESSNSRDRMTYASSKQALLKKIEGV 105
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 1136-1262 4.23e-11

C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Twinfilin contains two ADF domains, and inhibits the assembly of actin filaments by strongly interacting with monomeric ADP-actin (ADP-G-actin) in a 1:1 stochiometry (with it's C-terminal ADF domain, Twf-C) and inhibiting the actin monomer's nucleotide exchange. Mammalian twinfilin may also cap the barbed ends of F-actin filaments and prevent further assembly (or disassembly), in a process which requires both ADF domains. The N-terminal ADF domain (Twf-N) binds G-actin with a lower affinity than Twf-C; Twf-C can also bind F-actin. During capping, Twf-N may interact with the terminal actin subunit, and Twf-C may bind between two adjacent subunits at the side of the filament.


Pssm-ID: 200440  Cd Length: 132  Bit Score: 61.86  E-value: 4.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951 1136 VTDECKNSFHQMKwKKVHKYIVFKID---EKSRLVTVDKVGGPgesyDDLAASLPGDDCRYAVFDFDfvtvdNCRKSKIF 1212
Cdd:cd11284      7 VSEEAKDALSELA-SGGVNLVQLSIDlenETIELVSSSSISIP----DDLSSLIPSDHPRYHFYRYP-----HTYLSSVV 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1939208951 1213 FIAWAPAASRIRAKMLYATSKAGLRRVLEG-----IHYELQATDPTEMGFDLIRD 1262
Cdd:cd11284     77 FIYSCPSGSKVKERMLYASSKSGLLNHAEDegkieIDKKIEIGDPDELTESFLSD 131
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 1136-1241 2.69e-10

ADF-homology domain of glia maturation factor beta and related proteins; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Most of these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. The glia maturation factor (GMF), however, does not bind actin but interacts with the Arp2/3 complex (which contains actin-related proteins, amongst others) and suppresses Arp2/3 activity, inducing the dissociation of branched daughter filaments from their mother filaments. This family includes both mammalian GMF isoforms, GMF-beta and GMF-gamma. GMF-beta regulates cellular growth, fission, differentiation and apoptosis. GMF-gamma is important in myeloid cell development and is an important regulator for cell migration and polarity in neutrophils.


Pssm-ID: 200439 [Multi-domain]  Cd Length: 122  Bit Score: 59.17  E-value: 2.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951 1136 VTDECKNSFHQMKWKK--VHKYIVFKIDEKSRLVTVDKVGgPGESYDDLAASLPGDDCRYAVFDFDFVTVDNcRKS-KIF 1212
Cdd:cd11283      2 ISDEVKEALKKFRFRKskANAALILKIDKEKQEIVVDEEL-EDISIEELAEELPEHSPRFVLYSYKMKHDDG-RISyPLV 79

                           90       100
                   ....*....|....*....|....*....
gi 1939208951 1213 FIAWAPAASRIRAKMLYATSKAGLRRVLE 1241
Cdd:cd11283     80 LIYWSPQGCSPELQMLYAGAKELLVKEAE 108
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 1132-1255 2.98e-07

N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Twinfilin contains two ADF domains, and inhibits the assembly of actin filaments by strongly interacting with monomeric ADP-actin (ADP-G-actin) in a 1:1 stochiometry (with it's C-terminal ADF domain, Twf-C) and inhibiting the actin monomer's nucleotide exchange. Mammalian twinfilin may also cap the barbed ends of F-actin filaments and prevent further assembly (or disassembly), in a process which requires both ADF domains. The N-terminal ADF domain (Twf-N) binds G-actin with a lower affinity than Twf-C; Twf-C can also bind F-actin. During capping, Twf-N may interact with the terminal actin subunit, and Twf-C may bind between two adjacent subunits at the side of the filament.


Pssm-ID: 200441  Cd Length: 139  Bit Score: 51.09  E-value: 2.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951 1132 TGMWVTDECKNSFHQMKWKKVHKYIVFKIDEKSrLVTVDKVGGPGESYDDLAA----SLPGDDCRYAVFDFDfvtvDNCR 1207
Cdd:cd11285      2 SGITASEELLDAFKSAKSSGSVRAIKITIENEE-LVPDATIETTGSWEQDFDLlvlpLLEEKEPCYILYRLD----SKSA 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1939208951 1208 KSKIFFIAWAPAASRIRAKMLYATSKAGLRRVL--EGIHYELQATDPTEM 1255
Cdd:cd11285     77 GYEWVFISFVPDSAPVRQKMLYASTRATLKRELgsNHIKDELFATELEEL 126
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 635-776 6.04e-07

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 52.25  E-value: 6.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  635 MICIDNSEWMRngdySPSRFQAQADAV-NLLcgakTQSNPENTVGILTMAGkQVRVLTTLTSDLGKILSCMHGLEVGGEM 713
Cdd:COG1240     96 VLVVDASGSMA----AENRLEAAKGALlDFL----DDYRPRDRVGLVAFGG-EAEVLLPLTRDREALKRALDELPPGGGT 166

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939208951  714 NLSAGIQVAQLALKhRQNKNQQQRIIVF------AGSPikydkkMLETIGKKLKKNNVSLDIVDFGEEE 776
Cdd:COG1240    167 PLGDALALALELLK-RADPARRKVIVLLtdgrdnAGRI------DPLEAAELAAAAGIRIYTIGVGTEA 228
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 635-786 1.60e-06

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 49.49  E-value: 1.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  635 MICIDNSEWMrngdySPSRFQAQADAVNLLCGAKTQSNPENTVGILTMAGKQVRVLT-TLTSDLGKILSCMHGLE--VGG 711
Cdd:cd00198      4 VFLLDVSGSM-----GGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPlTTDTDKADLLEAIDALKkgLGG 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939208951  712 EMNLSAGIQVAQLALKHRQNKNQQQRIIVFAGSPIKYDKKMLETIGKKLKKNNVSLDIVDFGeeEDGKPEKLEAL 786
Cdd:cd00198     79 GTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIG--DDANEDELKEI 151
vWA_transcription_factor_IIH_type cd01453
Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five ...
 635-765 1.12e-05

Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five general transcription factors that binds RNA polymerase II holoenzyme. Orthologues of these genes are found in all completed eukaryotic genomes and all these proteins contain a VWA domain. The p44 subunit of TFIIH functions as a DNA helicase in RNA polymerase II transcription initiation and DNA repair, and its transcriptional activity is dependent on its C-terminal Zn-binding domains. The function of the vWA domain is unclear, but may be involved in complex assembly. The MIDAS motif is not conserved in this sub-group.


Pssm-ID: 238730  Cd Length: 183  Bit Score: 47.33  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  635 MICIDNSEWMRNGDYSPSRFQAQADAVNLLCGAKTQSNPENTVGILTMAGKQVRVLTTLTSDLGK-ILSCMHGLEVGGEM 713
Cdd:cd01453      7 IIVIDCSRSMEEQDLKPSRLAVVLKLLELFIEEFFDQNPISQLGIISIKNGRAEKLTDLTGNPRKhIQALKTARECSGEP 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1939208951  714 NLSAGIQVAQLALKHRQNKNQQQRIIVFaGSPIKYDKK-MLETIgKKLKKNNV 765
Cdd:cd01453     87 SLQNGLEMALESLKHMPSHGSREVLIIF-SSLSTCDPGnIYETI-DKLKKENI 137
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 672-793 2.36e-05

VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 46.11  E-value: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  672 NPENTVGILTMAGK-QVRVLTTLTSDLGKILSCMHGLEVGGEMNLSAGIQVAQLALKHRQNKNQQQRIIVF----AGSPI 746
Cdd:cd01465     33 RPDDRLAIVTYDGAaETVLPATPVRDKAAILAAIDRLTAGGSTAGGAGIQLGYQEAQKHFVPGGVNRILLAtdgdFNVGE 112

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1939208951  747 KYDKKMLETIGKKLKKnNVSLDIVDFGEEEdgKPEKLEALFAAVNSN 793
Cdd:cd01465    113 TDPDELARLVAQKRES-GITLSTLGFGDNY--NEDLMEAIADAGNGN 156
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 120-219 4.32e-04

Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane helices. Each protein forms a single pore. It has been shown that some members of this family form homodimers. In terms of primary structure, they are unrelated to known cation channels or other types of anion channels. Three ClC subfamilies are found in animals. ClC-1 is involved in setting and restoring the resting membrane potential of skeletal muscle, while other channels play important parts in solute concentration mechanisms in the kidney. These proteins contain two pfam00571 domains.


Pssm-ID: 425802 [Multi-domain]  Cd Length: 344  Bit Score: 44.08  E-value: 4.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  120 FYSLSSSGSVFLKSLISTLVVTLILSVPVCFLLllslkHYTKQIVYVSLPLFVVIPFFFNV--YWFVACTV-SSSCSDAF 196
Cdd:pfam00654  119 SFSLRALIPVLLASVVAALVSRLIFGNSPLFSV-----GEPGSLSLLELPLFILLGILCGLlgALFNRLLLkVQRLFRKL 193

                           90       100
                   ....*....|....*....|...
gi 1939208951  197 PLVYRILVLVFVFLIIGIIVWIF 219
Cdd:pfam00654  194 LKIPPVLRPALGGLLVGLLGLLF 216
7tmA_EDG-like cd14972
endothelial differentiation gene family, member of the class A family of seven-transmembrane G ...
 118-269 6.07e-03

endothelial differentiation gene family, member of the class A family of seven-transmembrane G protein-coupled receptors; This group represents the endothelial differentiation gene (Edg) family of G-protein coupled receptors, melanocortin/ACTH receptors, and cannabinoid receptors as well as their closely related receptors. The Edg GPCRs bind blood borne lysophospholipids including sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA), which are involved in the regulation of cell proliferation, survival, migration, invasion, endothelial cell shape change and cytoskeletal remodeling. The Edg receptors are classified into two subfamilies: the lysophosphatidic acid subfamily that includes LPA1 (Edg2), LPA2 (Edg4), and LPA3 (Edg7); and the S1P subfamily that includes S1P1 (Edg1), S1P2 (Edg5), S1P3 (Edg3), S1P4 (Edg6), and S1P5 (Edg8). Melanocortin receptors bind a group of pituitary peptide hormones known as melanocortins, which include adrenocorticotropic hormone (ACTH) and the different isoforms of melanocyte-stimulating hormones. Two types of cannabinoid receptors, CB1 and CB2, are activated by naturally occurring endocannabinoids, cannabis plant-derived cannabinoids such as tetrahydrocannabinol, or synthetic cannabinoids. The CB receptors are involved in the various physiological processes such as appetite, mood, memory, and pain sensation. CB1 receptor is expressed predominantly in central and peripheral neurons, while CB2 receptor is found mainly in the immune system.


Pssm-ID: 341317 [Multi-domain]  Cd Length: 275  Bit Score: 39.97  E-value: 6.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  118 FDFYSLSSSGSVFLKSLIST-LVVTLILSVpvCFLLLLSLKHY-------------TKQIVYVSL----PLFVVIPFFFN 179
Cdd:cd14972     56 LSVLLVSLTPSPATWLLRKGsLVLSLLASA--YSLLAIAVDRYisivhgltyvnnvTNKRVKVLIalvwVWSVLLALLPV 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939208951  180 VYWFVACTVSSSCSDAFPLV---YRILVLVFVFLIIGIIVW----IFVANWQRVELTVKIIGVASDA-LSKNLGLCVVIP 251
Cdd:cd14972    134 LGWNCVLCDQESCSPLGPGLpksYLVLILVFFFIALVIIVFlyvrIFWCLWRHANAIAARQEAAVPAqPSTSRKLAKTVV 213

                          170
                   ....*....|....*...
gi 1939208951  252 LLTLGLVVYYTPIVVFLV 269
Cdd:cd14972    214 IVLGVFLVCWLPLLILLV 231
 
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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