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Conserved domains on  [gi|1057503203|ref|NP_001317203|]
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WD repeat, SAM and U-box domain-containing protein 1 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
3-311 2.92e-76

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 242.89  E-value: 2.92e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203   3 KLIHTLADHGDDVNCCAFSF--SLLATCSLDKTIRLYSLRDFTELphSPLKFHTYAVHCCCFSPSGHILASCSTDGTTVL 80
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRL 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203  81 WNTENGQMLAVMEQPSGsPVRVCQFSPDSTCLASGAADGTVVLWNAQSYKLYRCGSVKDGSLAACAFSPNGSFFVTGSSC 160
Cdd:COG2319   189 WDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSAD 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203 161 GDLTVWD-DKMRCLHSEKAHDLGITCCDFSSqpvsDGEqglqffRLASCGQDCQVKIWIVSFTHILGfelkyksTLSGHC 239
Cdd:COG2319   268 GTVRLWDlATGELLRTLTGHSGGVNSVAFSP----DGK------LLASGSDDGTVRLWDLATGKLLR-------TLTGHT 330

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057503203 240 APVLACAFSHDGQMLVSGSVDKSVIVYDTNTENILHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWQFD 311
Cdd:COG2319   331 GAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
SAM_superfamily super family cl15755
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 328-377 1.18e-23

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


The actual alignment was detected with superfamily member cd09505:

Pssm-ID: 472832  Cd Length: 72  Bit Score: 93.54  E-value: 1.18e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1057503203 328 FTEDWSEEDVSTWLCAQDLKDLVGIFKMNNIDGKELLNLTKESLADDLKI 377
Cdd:cd09505     1 SLQDWSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKI 50
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 378-429 1.88e-14

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member pfam04564:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 73  Bit Score: 68.11  E-value: 1.88e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1057503203 378 DGYSYEKEAMENWISKKKRTSPMTNLVLPSAVLTPNRTLKMAINRWLETHQK 429
Cdd:pfam04564  22 SGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKRW 73
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
3-311 2.92e-76

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 242.89  E-value: 2.92e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203   3 KLIHTLADHGDDVNCCAFSF--SLLATCSLDKTIRLYSLRDFTELphSPLKFHTYAVHCCCFSPSGHILASCSTDGTTVL 80
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRL 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203  81 WNTENGQMLAVMEQPSGsPVRVCQFSPDSTCLASGAADGTVVLWNAQSYKLYRCGSVKDGSLAACAFSPNGSFFVTGSSC 160
Cdd:COG2319   189 WDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSAD 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203 161 GDLTVWD-DKMRCLHSEKAHDLGITCCDFSSqpvsDGEqglqffRLASCGQDCQVKIWIVSFTHILGfelkyksTLSGHC 239
Cdd:COG2319   268 GTVRLWDlATGELLRTLTGHSGGVNSVAFSP----DGK------LLASGSDDGTVRLWDLATGKLLR-------TLTGHT 330

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057503203 240 APVLACAFSHDGQMLVSGSVDKSVIVYDTNTENILHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWQFD 311
Cdd:COG2319   331 GAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 4-309 2.93e-59

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 195.25  E-value: 2.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203   4 LIHTLADHGDDVNCCAFS--FSLLATCSLDKTIRLYSLrdFTELPHSPLKFHTYAVHCCCFSPSGHILASCSTDGTTVLW 81
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSpdGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203  82 NTENGQMLAVMEQpSGSPVRVCQFSPDSTCLASGAADGTVVLWNAQSYKLYRCGSVKDGSLAACAFSPNGSFFVTGSSCG 161
Cdd:cd00200    79 DLETGECVRTLTG-HTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203 162 DLTVWD-DKMRCLHSEKAHDLGITCCDFSSqpvsDGEqglqffRLASCGQDCQVKIWIVSFTHILGfelkyksTLSGHCA 240
Cdd:cd00200   158 TIKLWDlRTGKCVATLTGHTGEVNSVAFSP----DGE------KLLSSSSDGTIKLWDLSTGKCLG-------TLRGHEN 220

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057503203 241 PVLACAFSHDGQMLVSGSVDKSVIVYDTNTENILHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWQ 309
Cdd:cd00200   221 GVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 328-377 1.18e-23

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.


Pssm-ID: 188904  Cd Length: 72  Bit Score: 93.54  E-value: 1.18e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1057503203 328 FTEDWSEEDVSTWLCAQDLKDLVGIFKMNNIDGKELLNLTKESLADDLKI 377
Cdd:cd09505     1 SLQDWSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKI 50
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 378-429 1.88e-14

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 68.11  E-value: 1.88e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1057503203 378 DGYSYEKEAMENWISKKKRTSPMTNLVLPSAVLTPNRTLKMAINRWLETHQK 429
Cdd:pfam04564  22 SGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKRW 73
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 378-413 3.85e-13

U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis.


Pssm-ID: 438317 [Multi-domain]  Cd Length: 55  Bit Score: 63.68  E-value: 3.85e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1057503203 378 DGYSYEKEAMENWIsKKKRTSPMTNLVLPSAVLTPN 413
Cdd:cd16655    21 DGHTYERSAIEEWL-ETHNTSPMTRLPLSSTDLVPN 55
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 378-423 1.54e-08

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 50.70  E-value: 1.54e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1057503203  378 DGYSYEKEAMENWIsKKKRTSPMTNLVLPSAVLTPNRTLKMAINRW 423
Cdd:smart00504  19 SGQTYERSAIEKWL-LSHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 230-267 1.59e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 47.31  E-value: 1.59e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1057503203  230 KYKSTLSGHCAPVLACAFSHDGQMLVSGSVDKSVIVYD 267
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
230-267 8.13e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 8.13e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1057503203 230 KYKSTLSGHCAPVLACAFSHDGQMLVSGSVDKSVIVYD 267
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 332-377 2.68e-06

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 44.59  E-value: 2.68e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1057503203  332 WSEEDVSTWLCAQDLKDLVGIFKMNNIDGKELLNLTKESLADDLKI 377
Cdd:smart00454   4 WSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGI 49
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 332-377 6.33e-06

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 43.41  E-value: 6.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1057503203 332 WSEEDVSTWLCAQDLKDLVGIFKMNNIDGKELLNLTKESLaDDLKI 377
Cdd:pfam00536   3 WSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDL-LKLGV 47
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 11-152 5.21e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 42.38  E-value: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203  11 HGDDVN----CCAFSF----SLLATCSLDKTIRLYS----LRDFTELpHSP---LKFHTYAVHCCCFSPSGHILASCSTD 75
Cdd:PLN00181  476 QGDLLNssnlVCAIGFdrdgEFFATAGVNKKIKIFEcesiIKDGRDI-HYPvveLASRSKLSGICWNSYIKSQVASSNFE 554

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1057503203  76 GTTVLWNTENGQMLAVMEQPSGSPVRVCQFSPDSTCLASGAADGTVVLWNAQsyKLYRCGSVKDGSLAACAFSPNGS 152
Cdd:PLN00181  555 GVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSIN--QGVSIGTIKTKANICCVQFPSES 629
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
3-311 2.92e-76

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 242.89  E-value: 2.92e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203   3 KLIHTLADHGDDVNCCAFSF--SLLATCSLDKTIRLYSLRDFTELphSPLKFHTYAVHCCCFSPSGHILASCSTDGTTVL 80
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRL 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203  81 WNTENGQMLAVMEQPSGsPVRVCQFSPDSTCLASGAADGTVVLWNAQSYKLYRCGSVKDGSLAACAFSPNGSFFVTGSSC 160
Cdd:COG2319   189 WDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSAD 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203 161 GDLTVWD-DKMRCLHSEKAHDLGITCCDFSSqpvsDGEqglqffRLASCGQDCQVKIWIVSFTHILGfelkyksTLSGHC 239
Cdd:COG2319   268 GTVRLWDlATGELLRTLTGHSGGVNSVAFSP----DGK------LLASGSDDGTVRLWDLATGKLLR-------TLTGHT 330

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057503203 240 APVLACAFSHDGQMLVSGSVDKSVIVYDTNTENILHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWQFD 311
Cdd:COG2319   331 GAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
4-314 8.58e-62

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 205.53  E-value: 8.58e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203   4 LIHTLADHGDDVNCCAFSFSLLATCSLDKTIRLYSLRDFTELPHSPLKFHTYAVHCCCFSPSGHILASCSTDGTTVLWNT 83
Cdd:COG2319    28 LLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203  84 ENGQMLAVMEQPSGsPVRVCQFSPDSTCLASGAADGTVVLWNAQSYKLYRCGSVKDGSLAACAFSPNGSFFVTGSSCGDL 163
Cdd:COG2319   108 ATGLLLRTLTGHTG-AVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTV 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203 164 TVWD-DKMRCLHSEKAHDLGITCCDFSsqpvSDGEqglqffRLASCGQDCQVKIWivsftHILGFELKYksTLSGHCAPV 242
Cdd:COG2319   187 RLWDlATGKLLRTLTGHTGAVRSVAFS----PDGK------LLASGSADGTVRLW-----DLATGKLLR--TLTGHSGSV 249

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057503203 243 LACAFSHDGQMLVSGSVDKSVIVYDTNTENILHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWqfDLET 314
Cdd:COG2319   250 RSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW--DLAT 319
WD40 COG2319
WD40 repeat [General function prediction only];
3-270 5.78e-61

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 203.22  E-value: 5.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203   3 KLIHTLADHGDDVNCCAFSF--SLLATCSLDKTIRLYSLRDFTELphSPLKFHTYAVHCCCFSPSGHILASCSTDGTTVL 80
Cdd:COG2319   153 KLLRTLTGHSGAVTSVAFSPdgKLLASGSDDGTVRLWDLATGKLL--RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRL 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203  81 WNTENGQMLAVMEQPSGSpVRVCQFSPDSTCLASGAADGTVVLWNAQSYKLYRCGSVKDGSLAACAFSPNGSFFVTGSSC 160
Cdd:COG2319   231 WDLATGKLLRTLTGHSGS-VRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDD 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203 161 GDLTVWD-DKMRCLHSEKAHDLGITCCDFSSqpvsDGEqglqffRLASCGQDCQVKIWIVSFTHILGfelkyksTLSGHC 239
Cdd:COG2319   310 GTVRLWDlATGKLLRTLTGHTGAVRSVAFSP----DGK------TLASGSDDGTVRLWDLATGELLR-------TLTGHT 372

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1057503203 240 APVLACAFSHDGQMLVSGSVDKSVIVYDTNT 270
Cdd:COG2319   373 GAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 4-309 2.93e-59

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 195.25  E-value: 2.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203   4 LIHTLADHGDDVNCCAFS--FSLLATCSLDKTIRLYSLrdFTELPHSPLKFHTYAVHCCCFSPSGHILASCSTDGTTVLW 81
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSpdGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203  82 NTENGQMLAVMEQpSGSPVRVCQFSPDSTCLASGAADGTVVLWNAQSYKLYRCGSVKDGSLAACAFSPNGSFFVTGSSCG 161
Cdd:cd00200    79 DLETGECVRTLTG-HTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203 162 DLTVWD-DKMRCLHSEKAHDLGITCCDFSSqpvsDGEqglqffRLASCGQDCQVKIWIVSFTHILGfelkyksTLSGHCA 240
Cdd:cd00200   158 TIKLWDlRTGKCVATLTGHTGEVNSVAFSP----DGE------KLLSSSSDGTIKLWDLSTGKCLG-------TLRGHEN 220

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057503203 241 PVLACAFSHDGQMLVSGSVDKSVIVYDTNTENILHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWQ 309
Cdd:cd00200   221 GVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 50-317 2.59e-51

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 174.45  E-value: 2.59e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203  50 LKFHTYAVHCCCFSPSGHILASCSTDGTTVLWNTENGQMLAVMEQPSGsPVRVCQFSPDSTCLASGAADGTVVLWNAQSY 129
Cdd:cd00200     5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTG-PVRDVAASADGTYLASGSSDKTIRLWDLETG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203 130 KLYRCGSVKDGSLAACAFSPNGSFFVTGSSCGDLTVWD-DKMRCLHSEKAHDLGITCCDFSSQPvsdgeqglQFfrLASC 208
Cdd:cd00200    84 ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDvETGKCLTTLRGHTDWVNSVAFSPDG--------TF--VASS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203 209 GQDCQVKIWIVSfthilgfELKYKSTLSGHCAPVLACAFSHDGQMLVSGSVDKSVIVYDTNTENILHTLTQHTRYVTTCA 288
Cdd:cd00200   154 SQDGTIKLWDLR-------TGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVA 226

                         250       260
                  ....*....|....*....|....*....
gi 1057503203 289 FAPNTLLLATGSMDKTVNIWQFDLETLCQ 317
Cdd:cd00200   227 FSPDGYLLASGSEDGTIRVWDLRTGECVQ 255
WD40 COG2319
WD40 repeat [General function prediction only];
19-314 5.78e-49

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 171.63  E-value: 5.78e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203  19 AFSFSLLATCSLDKTIRLYSLRDFTELPHSPLKFHTYAVHCCCFSPSGHILASCSTDGTTVLWNTENGQMLAVMEQPSGs 98
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203  99 PVRVCQFSPDSTCLASGAADGTVVLWNAQSYKLYRCGSVKDGSLAACAFSPNGSFFVTGSSCGDLTVWD-DKMRCLHSEK 177
Cdd:COG2319    80 AVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDlATGKLLRTLT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203 178 AHDLGITCCDFSsqpvSDGEqglqffRLASCGQDCQVKIWIVSfthilgfELKYKSTLSGHCAPVLACAFSHDGQMLVSG 257
Cdd:COG2319   160 GHSGAVTSVAFS----PDGK------LLASGSDDGTVRLWDLA-------TGKLLRTLTGHTGAVRSVAFSPDGKLLASG 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1057503203 258 SVDKSVIVYDTNTENILHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWqfDLET 314
Cdd:COG2319   223 SADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW--DLAT 277
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3-217 9.18e-40

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 144.01  E-value: 9.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203   3 KLIHTLADHGDDVNCCAFS--FSLLATCSLDKTIRLYSLRDFTELphSPLKFHTYAVHCCCFSPSGHILASCSTDGTTVL 80
Cdd:cd00200    84 ECVRTLTGHTSYVSSVAFSpdGRILSSSSRDKTIKVWDVETGKCL--TTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203  81 WNTENGQMLAVMEQPSGsPVRVCQFSPDSTCLASGAADGTVVLWNAQSYKLYRCGSVKDGSLAACAFSPNGSFFVTGSSC 160
Cdd:cd00200   162 WDLRTGKCVATLTGHTG-EVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSED 240

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1057503203 161 GDLTVWD-DKMRCLHSEKAHDLGITCCDFSsqpvSDGeqglqfFRLASCGQDCQVKIW 217
Cdd:cd00200   241 GTIRVWDlRTGECVQTLSGHTNSVTSLAWS----PDG------KRLASGSADGTIRIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 140-324 1.24e-34

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 130.15  E-value: 1.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203 140 GSLAACAFSPNGSFFVTGSSCGDLTVWD-DKMRCLHSEKAHDLGITCCDFSSqpvsDGEQglqffrLASCGQDCQVKIWI 218
Cdd:cd00200    10 GGVTCVAFSPDGKLLATGSGDGTIKVWDlETGELLRTLKGHTGPVRDVAASA----DGTY------LASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203 219 VSFTHILgfelkykSTLSGHCAPVLACAFSHDGQMLVSGSVDKSVIVYDTNTENILHTLTQHTRYVTTCAFAPNTLLLAT 298
Cdd:cd00200    80 LETGECV-------RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVAS 152

                         170       180
                  ....*....|....*....|....*..
gi 1057503203 299 GSMDKTVNIWqfDLETL-CQARRTEHQ 324
Cdd:cd00200   153 SSQDGTIKLW--DLRTGkCVATLTGHT 177
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 328-377 1.18e-23

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.


Pssm-ID: 188904  Cd Length: 72  Bit Score: 93.54  E-value: 1.18e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1057503203 328 FTEDWSEEDVSTWLCAQDLKDLVGIFKMNNIDGKELLNLTKESLADDLKI 377
Cdd:cd09505     1 SLQDWSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKI 50
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 378-429 1.88e-14

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 68.11  E-value: 1.88e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1057503203 378 DGYSYEKEAMENWISKKKRTSPMTNLVLPSAVLTPNRTLKMAINRWLETHQK 429
Cdd:pfam04564  22 SGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKRW 73
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 378-413 3.85e-13

U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis.


Pssm-ID: 438317 [Multi-domain]  Cd Length: 55  Bit Score: 63.68  E-value: 3.85e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1057503203 378 DGYSYEKEAMENWIsKKKRTSPMTNLVLPSAVLTPN 413
Cdd:cd16655    21 DGHTYERSAIEEWL-ETHNTSPMTRLPLSSTDLVPN 55
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 378-423 1.54e-08

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 50.70  E-value: 1.54e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1057503203  378 DGYSYEKEAMENWIsKKKRTSPMTNLVLPSAVLTPNRTLKMAINRW 423
Cdd:smart00504  19 SGQTYERSAIEKWL-LSHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 230-267 1.59e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 47.31  E-value: 1.59e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1057503203  230 KYKSTLSGHCAPVLACAFSHDGQMLVSGSVDKSVIVYD 267
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 270-308 4.19e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 46.15  E-value: 4.19e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1057503203  270 TENILHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIW 308
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 46-82 4.58e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 46.15  E-value: 4.58e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1057503203   46 PHSPLKFHTYAVHCCCFSPSGHILASCSTDGTTVLWN 82
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
230-267 8.13e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 8.13e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1057503203 230 KYKSTLSGHCAPVLACAFSHDGQMLVSGSVDKSVIVYD 267
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
272-308 1.93e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.26  E-value: 1.93e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1057503203 272 NILHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIW 308
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 336-374 2.05e-06

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 44.54  E-value: 2.05e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1057503203 336 DVSTWLCAQDLKDLVGIFKMNNIDGKELLNLTKESLADD 374
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKEL 39
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 332-377 2.68e-06

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 44.59  E-value: 2.68e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1057503203  332 WSEEDVSTWLCAQDLKDLVGIFKMNNIDGKELLNLTKESLADDLKI 377
Cdd:smart00454   4 WSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGI 49
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 332-377 6.33e-06

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 43.41  E-value: 6.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1057503203 332 WSEEDVSTWLCAQDLKDLVGIFKMNNIDGKELLNLTKESLaDDLKI 377
Cdd:pfam00536   3 WSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDL-LKLGV 47
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 332-373 1.26e-05

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 42.78  E-value: 1.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1057503203 332 WSEEDVSTWLCAQDLKDLVGIFKMNNIDGKELLNLTKESLAD 373
Cdd:cd09507     5 WTTEEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLKD 46
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3-38 1.27e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.91  E-value: 1.27e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1057503203    3 KLIHTLADHGDDVNCCAFS--FSLLATCSLDKTIRLYS 38
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSpdGKYLASGSDDGTIKLWD 40
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 329-379 1.49e-05

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 42.64  E-value: 1.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1057503203 329 TEDWSEEDVSTWLCAQDLKDLVGIFKMNNIDGKELLNLTKeslaDDLKIDG 379
Cdd:cd09512     4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGQQLLQLDS----SKLKALG 50
WD40 pfam00400
WD domain, G-beta repeat;
50-82 1.67e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.56  E-value: 1.67e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1057503203  50 LKFHTYAVHCCCFSPSGHILASCSTDGTTVLWN 82
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 332-377 2.30e-05

SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a protein-protein interaction domain. The Polycomb group includes transcriptional repressors which are involved in the regulation of some key regulatory genes during development in many organisms. They are best known for silencing Hox (Homeobox) genes. Polycomb proteins work together in large multimeric and chromatin-associated complexes. They organize chromatin of the target genes and maintain repressed states during many cell divisions. Polycomb proteins are classified based on their common function, but not on conserved domains and/or motifs; however many Polycomb proteins (members of PRC1 class complex) contain SAM domains which are more similar to each other inside of the Polycomb group than to SAM domains outside of it. Most information about structure and function of Polycomb SAM domains comes from studies of Ph (Polyhomeotic) and Scm (Sex comb on midleg) proteins. Polycomb SAM domains usually can be found at the C-terminus of the proteins. Some members of this group contain, in addition to the SAM domain, MTB repeats, Zn finger, and/or DUF3588 domains. Polycomb SAM domains can form homo- and/or heterooligomers through ML and EH surfaces. SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Polycomb proteins are known to be highly expressed in some cells years before their cancer pathology; thus they are attractive markers for early cancer therapy.


Pssm-ID: 188908  Cd Length: 64  Bit Score: 42.08  E-value: 2.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1057503203 332 WSEEDVSTWLC-AQDLKDLVGIFKMNNIDGKELLNLTKESLADDLKI 377
Cdd:cd09509     4 WSVDDVAQFIKsLDGCAEYAEVFREQEIDGQALLLLTEDDLLKGMGL 50
WD40 pfam00400
WD domain, G-beta repeat;
3-38 3.52e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.79  E-value: 3.52e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1057503203   3 KLIHTLADHGDDVNCCAFSF--SLLATCSLDKTIRLYS 38
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPdgKLLASGSDDGTVKVWD 39
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 332-371 6.83e-05

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.


Pssm-ID: 188933  Cd Length: 62  Bit Score: 40.66  E-value: 6.83e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1057503203 332 WSEEDVSTWL----CAQDLKdlvgIFKMNNIDGKELLNLTKESL 371
Cdd:cd09534     1 WDEEFVEEWLnelnCGQYLD----IFEKNLITGDLLLELDKEAL 40
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 332-395 1.01e-04

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 40.36  E-value: 1.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1057503203 332 WSEEDVSTWLCAQDLKDLVGIFKMNNIDGKELLNLTKESLADDLkidgysyekeAMENWISKKK 395
Cdd:cd09501     4 WSVADVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDL----------GMSSGLLRKR 57
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 274-325 1.58e-04

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 43.48  E-value: 1.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1057503203 274 LHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWqfDLET-LCQARRTEHQL 325
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVW--DLETgELLRTLKGHTG 52
RING-Ubox_LubX-like_rpt2 cd23150
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein ...
 378-424 1.67e-04

second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the second one.


Pssm-ID: 438512 [Multi-domain]  Cd Length: 69  Bit Score: 39.76  E-value: 1.67e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1057503203 378 DGYSYEKEAMENWISKKKrTSPMTNLVLPSAVLTPNRTLKMAINRWL 424
Cdd:cd23150    21 QGKVYDQEALSNFLIATG-NKDETGKKLSIDDVVVFDELYQQIKVYN 66
SAM_Scm-like-4MBT cd09580
SAM domain of Scm-like-4MBT proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 332-373 1.84e-04

SAM domain of Scm-like-4MBT proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-4MBT (Sex comb on midleg like, Malignant Brain Tumor) subfamily proteins of the polycomb group is a putative protein-protein interaction domain. Additionally to the SAM domain, most of the proteins of this subfamily have 4 MBT repeats. In Drosophila SAM-Scm-like-4MBT protein (known as dSfmbt) is a member of Pho repressive complex (PhoRC). Additionally to dSfmbt, the PhoRC complex includes Pho or Pho-like proteins. This complex is responsible for HOX (Homeobox) gene silencing: Pho or Pho-like proteins bind DNA and dSmbt binds methylated histones. dSmbt can interact with mono- and di-methylated histones H3 and H4 (however this activity has been shown for the MBT repeats, while exact function of the SAM domain is unclear). Besides interaction with histones, dSmbt can interact with Scm (a member of PRC complex), but this interaction also seems to be SAM domain independent.


Pssm-ID: 188979  Cd Length: 67  Bit Score: 39.66  E-value: 1.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1057503203 332 WSEEDVSTWLCAQDLKDLVGIFKMNNIDGKELLNLTKESLAD 373
Cdd:cd09580     4 WGVKDVSQFLRENDCGAYCECFCRQNIDGKRLLSLTKEQIMT 45
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 332-373 2.20e-04

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.


Pssm-ID: 188914  Cd Length: 70  Bit Score: 39.16  E-value: 2.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1057503203 332 WSEEDVSTWLCAQDLKDLVGIFKMNN-IDGKELLNLTKESLAD 373
Cdd:cd09515     4 WTCEDVAKWLKKEGFSKYVDLLCNKHrIDGKVLLSLTEEDLRS 46
SAM_MLTK cd09529
SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a ...
 332-373 2.21e-04

SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a protein-protein interaction domain. Besides SAM domain, these proteins have N-terminal protein tyrosine kinase domain and leucine-zipper motif. Proteins of this group act as mitogen-activated protein triple kinase in a number of MAPK cascades. They can be activated by autophosphorylation in response to stress signals. MLTK-alpha is known to phosphorylate histone H3. In mammals, MLTKs participate in the activation of the JNK/SAPK, p38, ERK5 pathways, the transcriptional factor NF-kB, in the regulation of the cell cycle checkpoint, and in the induction of apoptosis in a hepatoma cell line. Some members of this subfamily are proto-oncogenes, thus MLTK-alpha is involved in neoplasmic cell transformation and/or skin cancer development in athymic nude mice. Based on in vivo coprecipitation experiments in mammalian cells, it has been demonstrated that MLTK proteins might form homodimers/oligomers via their SAM domains.


Pssm-ID: 188928  Cd Length: 71  Bit Score: 39.41  E-value: 2.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1057503203 332 WSEEDVSTW--------LCAQDLKDLVGIFKMNNIDGKELLNLTKESLAD 373
Cdd:cd09529     2 WTEEDVHFWmqqlvrkgGHPSELSQYADLFKENHITGKRLLLLTEEDLRD 51
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 98-125 4.39e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 37.68  E-value: 4.39e-04
                           10        20
                   ....*....|....*....|....*...
gi 1057503203   98 SPVRVCQFSPDSTCLASGAADGTVVLWN 125
Cdd:smart00320  13 GPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 11-152 5.21e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 42.38  E-value: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503203  11 HGDDVN----CCAFSF----SLLATCSLDKTIRLYS----LRDFTELpHSP---LKFHTYAVHCCCFSPSGHILASCSTD 75
Cdd:PLN00181  476 QGDLLNssnlVCAIGFdrdgEFFATAGVNKKIKIFEcesiIKDGRDI-HYPvveLASRSKLSGICWNSYIKSQVASSNFE 554

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1057503203  76 GTTVLWNTENGQMLAVMEQPSGSPVRVCQFSPDSTCLASGAADGTVVLWNAQsyKLYRCGSVKDGSLAACAFSPNGS 152
Cdd:PLN00181  555 GVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSIN--QGVSIGTIKTKANICCVQFPSES 629
SAM_PNT-Tel_Yan cd08535
Sterile alpha motif (SAM)/Pointed domain of Tel/Yan protein; SAM Pointed domain of Tel ...
 332-373 9.93e-04

Sterile alpha motif (SAM)/Pointed domain of Tel/Yan protein; SAM Pointed domain of Tel (Translocation, Ets, Leukemia)/Yan subfamily of ETS transcriptional repressors is a protein-protein interaction domain. SAM Pointed domains of this type of regulators can interact with each other, forming head-to-tail homodimers or homooligomers, and/or interact with SAM Pointed domains of another subfamily of ETS factors forming heterodimers. The oligomeric form is able to block transcription of target genes and is involved in MAPK signaling. They participate in regulation of different processes during embryoniv development including hematopoietic differentiation and eye development. Tel/Yan transcriptional factors are frequent targets of chromosomal translocations resulting in fusions of SAM domain with new neighboring genes. Such chimeric proteins were found in different tumors. Members of this subfamily are potential targets for cancer therapy.


Pssm-ID: 176085  Cd Length: 68  Bit Score: 37.37  E-value: 9.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1057503203 332 WSEEDVSTWL-CAQDLKDLVGI----FKMNnidGKELLNLTKESLAD 373
Cdd:cd08535     6 WSREDVLQWLrWAENEFSLPPIdsntFEMN---GKALCLLTKEDFRY 49
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
 378-427 9.95e-04

U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins; CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins, thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (or apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase.


Pssm-ID: 438316 [Multi-domain]  Cd Length: 71  Bit Score: 37.56  E-value: 9.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1057503203 378 DGYSYEKEAMENWISKKKRTSPMTNLVLPSAVLTPNRTLKMAINRWLETH 427
Cdd:cd16654    22 SGITYERKDIEEHLQRVGHFDPITREPLTQDQLIPNLALKEAIEAFLEEN 71
SAM_PNT pfam02198
Sterile alpha motif (SAM)/Pointed domain;
320-369 1.69e-03

Sterile alpha motif (SAM)/Pointed domain;


Pssm-ID: 460486  Cd Length: 83  Bit Score: 37.27  E-value: 1.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1057503203 320 RTEHQLKQFTED---WSEEDVSTWLC-AQDLKDLVGI-FKMNNIDGKELLNLTKE 369
Cdd:pfam02198   5 EKEQLRLWIPADprlWTKDHVLEWLEwAVDEFDLSKIdFSQFDMNGKALCSLGKE 59
WD40 pfam00400
WD domain, G-beta repeat;
98-125 2.05e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 2.05e-03
                          10        20
                  ....*....|....*....|....*...
gi 1057503203  98 SPVRVCQFSPDSTCLASGAADGTVVLWN 125
Cdd:pfam00400  12 GSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 332-373 4.34e-03

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 35.76  E-value: 4.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1057503203 332 WSEEDVSTWLCAQDLKDLVGIFKMNNIDGKELLNLTKESLAD 373
Cdd:cd09506     5 WTVDDVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTE 46
SAM_PNT smart00251
SAM / Pointed domain; A subfamily of the SAM domain
 316-369 6.00e-03

SAM / Pointed domain; A subfamily of the SAM domain


Pssm-ID: 128547  Cd Length: 82  Bit Score: 35.70  E-value: 6.00e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1057503203  316 CQARRTEHQLKQFTED---WSEEDVSTWLC-AQDLKDLVGI-FKMNNIDGKELLNLTKE 369
Cdd:smart00251   1 PPNFEKEQKRLGIPADpqlWTEDHVLEWLEwAVKEFSLSPIdFSKFDMSGKELCSMSKE 59
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 169-217 6.52e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 34.21  E-value: 6.52e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1057503203  169 KMRCLHSEKAHDLGITCCDFSSqpvsDGEqglqffRLASCGQDCQVKIW 217
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSP----DGK------YLASGSDDGTIKLW 39
SAM_HD cd09508
SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily ...
 332-373 8.23e-03

SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily proteins is a putative protein-protein interaction domain. Proteins of this group, additionally to the SAM domain, contain a HD hydrolase domain. Human SAM-HD1 is a nuclear protein involved in innate immune response and may act as a negative regulator of the cell-intrinsic antiviral response. Mutations in this gene lead to Aicardi-Goutieres syndrome (symptoms include cerebral atrophy, leukoencephalopathy, hepatosplenomegaly, and increased production of alpha-interferon).


Pssm-ID: 188907  Cd Length: 70  Bit Score: 34.98  E-value: 8.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1057503203 332 WSEEDVSTWLCAQDLKD--LVGIFKMNNIDGKELLNLTKESLAD 373
Cdd:cd09508     5 WDPEDVCQFLRGNGFGEpeLLEIFRENEITGAHLPDLTESRLEK 48
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 378-405 8.27e-03

U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.


Pssm-ID: 438117 [Multi-domain]  Cd Length: 44  Bit Score: 34.07  E-value: 8.27e-03
                          10        20
                  ....*....|....*....|....*...
gi 1057503203 378 DGYSYEKEAMENWIsKKKRTSPMTNLVL 405
Cdd:cd16453    18 SGITYDRSAIERWL-LSDNTDPFTREPL 44
 
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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