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Conserved domains on  [gi|227452250|ref|NP_001153108|]
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WD repeat, SAM and U-box domain-containing protein 1 isoform 2 [Mus musculus]

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];
3-310 2.84e-71

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 229.80  E-value: 2.84e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250   3 RLIHTLADHGDDVSCCAFSA--ALLATCSLDKTIRLYSLSDFAELpySPLKFHTYAVHCCCFSPSGHVLASCSTDGTTVL 80
Cdd:COG2319  111 LLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRL 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250  81 WSSHSGHTLTVLEQPGGsPVRVCCFSPDSAYLASGAADGSIALWNAQTYKLYRCGSVKDSSLVACAFSPDGGLFVTGSSG 160
Cdd:COG2319  189 WDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSAD 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 161 GDLTVWD-DRMRCLHSEKAHDLGITCCSFSSQplsgGEglqsyQLASCGQDCEIKLWAVTITRVLGfelkyksTLSGHCA 239
Cdd:COG2319  268 GTVRLWDlATGELLRTLTGHSGGVNSVAFSPD----GK-----LLASGSDDGTVRLWDLATGKLLR-------TLTGHTG 331

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227452250 240 PVLACAFSHDGKMLASGSVDKSVIIHGIGPQSVLHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWQFD 310
Cdd:COG2319  332 AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 326-397 2.19e-36

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: 127.82  E-value: 2.19e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227452250 326 FTEEWSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAGDLKIESLGLRSKVLRSIEELRAKMDS 397
Cdd:cd09505    1 SLQDWSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEELKMKSDS 72
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 403-422 8.04e-09

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 cd16655:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 55  Bit Score: 51.35  E-value: 8.04e-09
                         10        20
                 ....*....|....*....|
gi 227452250 403 PDEFICPITRELMKDPVIAS 422
Cdd:cd16655    1 PDEFLCPITQELMRDPVVAA 20
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
3-310 2.84e-71

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 229.80  E-value: 2.84e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250   3 RLIHTLADHGDDVSCCAFSA--ALLATCSLDKTIRLYSLSDFAELpySPLKFHTYAVHCCCFSPSGHVLASCSTDGTTVL 80
Cdd:COG2319  111 LLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRL 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250  81 WSSHSGHTLTVLEQPGGsPVRVCCFSPDSAYLASGAADGSIALWNAQTYKLYRCGSVKDSSLVACAFSPDGGLFVTGSSG 160
Cdd:COG2319  189 WDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSAD 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 161 GDLTVWD-DRMRCLHSEKAHDLGITCCSFSSQplsgGEglqsyQLASCGQDCEIKLWAVTITRVLGfelkyksTLSGHCA 239
Cdd:COG2319  268 GTVRLWDlATGELLRTLTGHSGGVNSVAFSPD----GK-----LLASGSDDGTVRLWDLATGKLLR-------TLTGHTG 331

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227452250 240 PVLACAFSHDGKMLASGSVDKSVIIHGIGPQSVLHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWQFD 310
Cdd:COG2319  332 AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 4-308 1.77e-55

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: 185.23  E-value: 1.77e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250   4 LIHTLADHGDDVSCCAFSAA--LLATCSLDKTIRLYSLSDfAELPYSpLKFHTYAVHCCCFSPSGHVLASCSTDGTTVLW 81
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLET-GELLRT-LKGHTGPVRDVAASADGTYLASGSSDKTIRLW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250  82 SSHSGHTLTVLEqpgG--SPVRVCCFSPDSAYLASGAADGSIALWNAQTYKLYRCGSVKDSSLVACAFSPDGGLFVTGSS 159
Cdd:cd00200   79 DLETGECVRTLT---GhtSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 160 GGDLTVWDDR-MRCLHSEKAHDLGITCCSFSSQplsggeglqSYQLASCGQDCEIKLWAVTITRVLGfelkyksTLSGHC 238
Cdd:cd00200  156 DGTIKLWDLRtGKCVATLTGHTGEVNSVAFSPD---------GEKLLSSSSDGTIKLWDLSTGKCLG-------TLRGHE 219

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 239 APVLACAFSHDGKMLASGSVDKSVIIHGIGPQSVLHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWQ 308
Cdd:cd00200  220 NGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 326-397 2.19e-36

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: 127.82  E-value: 2.19e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227452250 326 FTEEWSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAGDLKIESLGLRSKVLRSIEELRAKMDS 397
Cdd:cd09505    1 SLQDWSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEELKMKSDS 72
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 328-393 1.80e-15

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: 70.79  E-value: 1.80e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227452250   328 EEWSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAGDLKIESLGLRSKVLRSIEELRA 393
Cdd:smart00454   2 SQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 328-392 3.02e-12

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: 61.52  E-value: 3.02e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227452250  328 EEWSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLaGDLKIESLGLRSKVLRSIEELR 392
Cdd:pfam00536   1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRLK 64
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 403-422 8.04e-09

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: 51.35  E-value: 8.04e-09
                         10        20
                 ....*....|....*....|
gi 227452250 403 PDEFICPITRELMKDPVIAS 422
Cdd:cd16655    1 PDEFLCPITQELMRDPVVAA 20
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 402-422 2.14e-07

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: 48.08  E-value: 2.14e-07
                          10        20
                  ....*....|....*....|.
gi 227452250  402 IPDEFICPITRELMKDPVIAS 422
Cdd:pfam04564   1 IPDEFLDPITFELMTDPVILP 21
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 269-307 6.00e-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: 45.77  E-value: 6.00e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 227452250   269 PQSVLHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIW 307
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
271-307 2.20e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.26  E-value: 2.20e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 227452250  271 SVLHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIW 307
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 405-422 3.24e-05

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: 41.45  E-value: 3.24e-05
                           10
                   ....*....|....*...
gi 227452250   405 EFICPITRELMKDPVIAS 422
Cdd:smart00504   1 EFLCPISLEVMKDPVILP 18
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
3-310 2.84e-71

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 229.80  E-value: 2.84e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250   3 RLIHTLADHGDDVSCCAFSA--ALLATCSLDKTIRLYSLSDFAELpySPLKFHTYAVHCCCFSPSGHVLASCSTDGTTVL 80
Cdd:COG2319  111 LLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRL 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250  81 WSSHSGHTLTVLEQPGGsPVRVCCFSPDSAYLASGAADGSIALWNAQTYKLYRCGSVKDSSLVACAFSPDGGLFVTGSSG 160
Cdd:COG2319  189 WDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSAD 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 161 GDLTVWD-DRMRCLHSEKAHDLGITCCSFSSQplsgGEglqsyQLASCGQDCEIKLWAVTITRVLGfelkyksTLSGHCA 239
Cdd:COG2319  268 GTVRLWDlATGELLRTLTGHSGGVNSVAFSPD----GK-----LLASGSDDGTVRLWDLATGKLLR-------TLTGHTG 331

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227452250 240 PVLACAFSHDGKMLASGSVDKSVIIHGIGPQSVLHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWQFD 310
Cdd:COG2319  332 AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
3-314 2.07e-57

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 193.59  E-value: 2.07e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250   3 RLIHTLADHGDDVSCCAFS--AALLATCSLDKTIRLYSLSDFAELPysPLKFHTYAVHCCCFSPSGHVLASCSTDGTTVL 80
Cdd:COG2319   27 ALLLLLLGLAAAVASLAASpdGARLAAGAGDLTLLLLDAAAGALLA--TLLGHTAAVLSVAFSPDGRLLASASADGTVRL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250  81 WSSHSGHTLTVLEQPGGsPVRVCCFSPDSAYLASGAADGSIALWNAQTYKLYRCGSVKDSSLVACAFSPDGGLFVTGSSG 160
Cdd:COG2319  105 WDLATGLLLRTLTGHTG-AVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDD 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 161 GDLTVWD-DRMRCLHSEKAHDLGITCCSFSSQplsgGEglqsyQLASCGQDCEIKLWAVTITRVLGfelkyksTLSGHCA 239
Cdd:COG2319  184 GTVRLWDlATGKLLRTLTGHTGAVRSVAFSPD----GK-----LLASGSADGTVRLWDLATGKLLR-------TLTGHSG 247

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227452250 240 PVLACAFSHDGKMLASGSVDKSVIIHGIGPQSVLHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWqfDLETP 314
Cdd:COG2319  248 SVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW--DLATG 320
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 4-308 1.77e-55

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: 185.23  E-value: 1.77e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250   4 LIHTLADHGDDVSCCAFSAA--LLATCSLDKTIRLYSLSDfAELPYSpLKFHTYAVHCCCFSPSGHVLASCSTDGTTVLW 81
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLET-GELLRT-LKGHTGPVRDVAASADGTYLASGSSDKTIRLW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250  82 SSHSGHTLTVLEqpgG--SPVRVCCFSPDSAYLASGAADGSIALWNAQTYKLYRCGSVKDSSLVACAFSPDGGLFVTGSS 159
Cdd:cd00200   79 DLETGECVRTLT---GhtSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 160 GGDLTVWDDR-MRCLHSEKAHDLGITCCSFSSQplsggeglqSYQLASCGQDCEIKLWAVTITRVLGfelkyksTLSGHC 238
Cdd:cd00200  156 DGTIKLWDLRtGKCVATLTGHTGEVNSVAFSPD---------GEKLLSSSSDGTIKLWDLSTGKCLG-------TLRGHE 219

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 239 APVLACAFSHDGKMLASGSVDKSVIIHGIGPQSVLHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWQ 308
Cdd:cd00200  220 NGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 50-316 1.20e-46

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: 162.12  E-value: 1.20e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250  50 LKFHTYAVHCCCFSPSGHVLASCSTDGTTVLWSSHSGHTLTVLEQPGGsPVRVCCFSPDSAYLASGAADGSIALWNAQTY 129
Cdd:cd00200    5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTG-PVRDVAASADGTYLASGSSDKTIRLWDLETG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 130 KLYRCGSVKDSSLVACAFSPDGGLFVTGSSGGDLTVWD-DRMRCLHSEKAHDLGITCCSFSSQPLSggeglqsyqLASCG 208
Cdd:cd00200   84 ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDvETGKCLTTLRGHTDWVNSVAFSPDGTF---------VASSS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 209 QDCEIKLWAVTITRVLGfelkyksTLSGHCAPVLACAFSHDGKMLASGSVDKSVIIHGIGPQSVLHTLTQHTRYVTTCAF 288
Cdd:cd00200  155 QDGTIKLWDLRTGKCVA-------TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAF 227

                        250       260
                 ....*....|....*....|....*...
gi 227452250 289 APNTLLLATGSMDKTVNIWQFDLETPCQ 316
Cdd:cd00200  228 SPDGYLLASGSEDGTIRVWDLRTGECVQ 255
WD40 COG2319
WD40 repeat [General function prediction only];
19-313 1.20e-45

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 162.39  E-value: 1.20e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250  19 AFSAALLATCSLDKTIRLYSLSDFAELPysPLKFHTYAVHCCCFSPSGHVLASCSTDGTTVLWSSHSGHTLTVLeQPGGS 98
Cdd:COG2319    3 SADGAALAAASADLALALLAAALGALLL--LLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATL-LGHTA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250  99 PVRVCCFSPDSAYLASGAADGSIALWNAQTYKLYRCGSVKDSSLVACAFSPDGGLFVTGSSGGDLTVWD-DRMRCLHSEK 177
Cdd:COG2319   80 AVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDlATGKLLRTLT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 178 AHDLGITCCSFSSqplsggeglQSYQLASCGQDCEIKLWAVTITRVLGfelkyksTLSGHCAPVLACAFSHDGKMLASGS 257
Cdd:COG2319  160 GHSGAVTSVAFSP---------DGKLLASGSDDGTVRLWDLATGKLLR-------TLTGHTGAVRSVAFSPDGKLLASGS 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 227452250 258 VDKSVIIHGIGPQSVLHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWqfDLET 313
Cdd:COG2319  224 ADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW--DLAT 277
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3-217 5.76e-39

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: 141.70  E-value: 5.76e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250   3 RLIHTLADHGDDVSCCAFSAA--LLATCSLDKTIRLYSLSDFAELpySPLKFHTYAVHCCCFSPSGHVLASCSTDGTTVL 80
Cdd:cd00200   84 ECVRTLTGHTSYVSSVAFSPDgrILSSSSRDKTIKVWDVETGKCL--TTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250  81 WSSHSGHTLTVLEQPGGsPVRVCCFSPDSAYLASGAADGSIALWNAQTYKLYRCGSVKDSSLVACAFSPDGGLFVTGSSG 160
Cdd:cd00200  162 WDLRTGKCVATLTGHTG-EVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSED 240

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 227452250 161 GDLTVWDDRM-RCLHSEKAHDLGITCCSFSSqplSGGeglqsyQLASCGQDCEIKLWA 217
Cdd:cd00200  241 GTIRVWDLRTgECVQTLSGHTNSVTSLAWSP---DGK------RLASGSADGTIRIWD 289
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 326-397 2.19e-36

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: 127.82  E-value: 2.19e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227452250 326 FTEEWSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAGDLKIESLGLRSKVLRSIEELRAKMDS 397
Cdd:cd09505    1 SLQDWSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEELKMKSDS 72
WD40 COG2319
WD40 repeat [General function prediction only];
3-128 2.33e-27

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 112.31  E-value: 2.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250   3 RLIHTLADHGDDVSCCAFSA--ALLATCSLDKTIRLYSLSDFAELpySPLKFHTYAVHCCCFSPSGHVLASCSTDGTTVL 80
Cdd:COG2319  279 ELLRTLTGHSGGVNSVAFSPdgKLLASGSDDGTVRLWDLATGKLL--RTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 227452250  81 WSSHSGHTLTVLEQPGGsPVRVCCFSPDSAYLASGAADGSIALWNAQT 128
Cdd:COG2319  357 WDLATGELLRTLTGHTG-AVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 328-393 1.80e-15

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: 70.79  E-value: 1.80e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227452250   328 EEWSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAGDLKIESLGLRSKVLRSIEELRA 393
Cdd:smart00454   2 SQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
WD40 COG2319
WD40 repeat [General function prediction only];
146-313 9.96e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 69.17  E-value: 9.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 146 AFSPDGGLFVTGSSGGDLTVWD-DRMRCLHSEKAHDLGITCCSFSSQPLsggeglqsyQLASCGQDCEIKLWAVTITRVL 224
Cdd:COG2319    1 ALSADGAALAAASADLALALLAaALGALLLLLLGLAAAVASLAASPDGA---------RLAAGAGDLTLLLLDAAAGALL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 225 GfelkyksTLSGHCAPVLACAFSHDGKMLASGSVDKSVIIHGIGPQSVLHTLTQHTRYVTTCAFAPNTLLLATGSMDKTV 304
Cdd:COG2319   72 A-------TLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTV 144


                 ....*....
gi 227452250 305 NIWqfDLET 313
Cdd:COG2319  145 RLW--DLAT 151
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 328-392 3.02e-12

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: 61.52  E-value: 3.02e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227452250  328 EEWSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLaGDLKIESLGLRSKVLRSIEELR 392
Cdd:pfam00536   1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRLK 64
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 334-390 4.63e-12

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: 60.72  E-value: 4.63e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 227452250 334 DVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAgDLKIESLGLRSKVLRSIEE 390
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
328-392 6.37e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 60.36  E-value: 6.37e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227452250  328 EEWSEEDVSVWLRAQGLEDLVGIFRANNIDGKE-LLHLTKESLAgDLKIESLGLRSKVLRSIEELR 392
Cdd:pfam07647   2 ESWSLESVADWLRSIGLEQYTDNFRDQGITGAElLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
SAM_HD cd09508
SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily ...
 329-392 2.66e-11

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: 58.87  E-value: 2.66e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227452250 329 EWSEEDVSVWLRAQGLED--LVGIFRANNIDGKELLHLTKESLAgDLKIESLGLRSKVLRSIEELR 392
Cdd:cd09508    4 SWDPEDVCQFLRGNGFGEpeLLEIFRENEITGAHLPDLTESRLE-KLGVSSLGERLKLLKCLQKLS 68
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 329-393 3.86e-10

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: 55.77  E-value: 3.86e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227452250 329 EWSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAGDLKIESLGLRSKVLRSIEELRA 393
Cdd:cd09501    3 LWSVADVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRFLRELVELKT 67
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 330-392 1.14e-09

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: 54.14  E-value: 1.14e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227452250 330 WSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAgDLKIESLGLRSKVLRSIEELR 392
Cdd:cd09534    1 WDEEFVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALK-ELGITKVGDRIRLLRAIKSLR 62
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 327-394 1.96e-09

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: 53.43  E-value: 1.96e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227452250 327 TEEWSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKEslagDLKIesLGL-----RSKVLRSIEELRAK 394
Cdd:cd09512    4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGQQLLQLDSS----KLKA--LGItsssdRSLLKKKLKELKAQ 70
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 328-392 4.93e-09

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: 52.64  E-value: 4.93e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227452250 328 EEWSEEDVSVWLRAQGLEDLVGIFRANN-IDGKELLHLTKESLAG-DLKIESLGLRSKVLRSIEELR 392
Cdd:cd09515    2 HEWTCEDVAKWLKKEGFSKYVDLLCNKHrIDGKVLLSLTEEDLRSpPLEIKVLGDIKRLWLAIRKLQ 68
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 403-422 8.04e-09

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: 51.35  E-value: 8.04e-09
                         10        20
                 ....*....|....*....|
gi 227452250 403 PDEFICPITRELMKDPVIAS 422
Cdd:cd16655    1 PDEFLCPITQELMRDPVVAA 20
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 330-391 1.06e-08

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: 51.26  E-value: 1.06e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227452250 330 WSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAgDLKIESLGLRSKVLRSIEEL 391
Cdd:cd09507    5 WTTEEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLK-DLGITKVGHVKRILQAIKDL 65
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 328-392 1.69e-08

SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal subfamily is a potential protein-protein interaction domain. Proteins of this subfamily are apparently scaffold proteins, since most contain SH3 and PH domains, which are also protein-protein interaction domains, in addition to SAM domain. BOI-like proteins participate in cell cycle regulation. In particular BOI1 and BOI2 proteins of budding yeast S.cerevisiae are involved in bud formation, and POB1 protein of fission yeast S.pombe plays a role in cell elongation and separation. Among binding partners of BOI-like fungal subfamily members are such proteins as Bem1 and Cdc42 (they are known to be involved in cell polarization and bud formation).


Pssm-ID: 188934  Cd Length: 65  Bit Score: 50.63  E-value: 1.69e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227452250 328 EEWSEEDVSVWLRAQGLED-LVGIFRANNIDGKELLHLTKESLAgDLKIESLGLRSKVLRSIEELR 392
Cdd:cd09535    1 RSWSPEQVAEWLLSAGFDDsVCEKFRENEITGDILLELDLEDLK-ELDIGSFGKRFKLWNEIKSLR 65
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
 403-423 1.43e-07

U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain.


Pssm-ID: 438326 [Multi-domain]  Cd Length: 53  Bit Score: 47.94  E-value: 1.43e-07
                         10        20
                 ....*....|....*....|..
gi 227452250 403 PDEFICPITRELMKDPVI-ASG 423
Cdd:cd16664    1 PEEFICPISLELMKDPVIlATG 22
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 402-422 2.14e-07

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: 48.08  E-value: 2.14e-07
                          10        20
                  ....*....|....*....|.
gi 227452250  402 IPDEFICPITRELMKDPVIAS 422
Cdd:pfam04564   1 IPDEFLDPITFELMTDPVILP 21
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 269-307 6.00e-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: 45.77  E-value: 6.00e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 227452250   269 PQSVLHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIW 307
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
SAM_DGK-eta cd09576
SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily ...
 328-391 1.06e-06

SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases. The SAM domain is located at the C-terminus of two out of three isoforms of DGK-eta protein. DGK-eta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DCK-eta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-delta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it is responsible for sustained endosomal localization of the protein and resulted in negative regulation of DCK-eta catalytic activity.


Pssm-ID: 188975  Cd Length: 65  Bit Score: 45.73  E-value: 1.06e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227452250 328 EEWSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAgDLKIESLGLRSKVLRSIEEL 391
Cdd:cd09576    3 QKWGTDEVAAWLDLLSLGEYKEIFIRHDIRGSELLHLERRDLK-DLGIPKVGHMKRILQGIKEL 65
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 50-82 1.19e-06

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: 45.00  E-value: 1.19e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 227452250    50 LKFHTYAVHCCCFSPSGHVLASCSTDGTTVLWS 82
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
SAM_MLTK cd09529
SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a ...
 329-391 1.31e-06

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: 45.57  E-value: 1.31e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227452250 329 EWSEEDVSVWLR--------AQGLEDLVGIFRANNIDGKELLHLTKESLAgDLKIESLGLRSKVLRSIEEL 391
Cdd:cd09529    1 AWTEEDVHFWMQqlvrkgghPSELSQYADLFKENHITGKRLLLLTEEDLR-DMGIGSKGHIIHLKSAIEKL 70
WD40 pfam00400
WD domain, G-beta repeat;
271-307 2.20e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.26  E-value: 2.20e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 227452250  271 SVLHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIW 307
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 229-265 2.42e-06

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: 43.84  E-value: 2.42e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 227452250   229 KYKSTLSGHCAPVLACAFSHDGKMLASGSVDKSVIIH 265
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 330-381 5.00e-06

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: 43.62  E-value: 5.00e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 227452250 330 WSEEDVSVWLR-AQGLEDLVGIFRANNIDGKELLHLTKESLagdlkIESLGLR 381
Cdd:cd09509    4 WSVDDVAQFIKsLDGCAEYAEVFREQEIDGQALLLLTEDDL-----LKGMGLK 51
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 330-391 7.53e-06

SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-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-delta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. In particular DGK-delta is involved in the regulation of clathrin-dependent endocytosis. The SAM domain of DGK-delta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-eta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it inhibits the translocation of the protein to the plasma membrane from the cytoplasm. The SAM domain also can bind Zn at multiple (not conserved) sites driving the formation of highly ordered large sheets of polymers, thus suggesting that Zn may play important role in the function of DCK-delta.


Pssm-ID: 188974  Cd Length: 65  Bit Score: 43.40  E-value: 7.53e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227452250 330 WSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAgDLKIESLGLRSKVLRSIEEL 391
Cdd:cd09575    5 WGTEEVAAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDLK-DLGVTKVGHMKRILCGIKEL 65
SAM_Scm-like-4MBT cd09580
SAM domain of Scm-like-4MBT proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 328-394 8.49e-06

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: 43.13  E-value: 8.49e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227452250 328 EEWSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLagdlkIESLGLRS----KVLRSIEELRAK 394
Cdd:cd09580    2 STWGVKDVSQFLRENDCGAYCECFCRQNIDGKRLLSLTKEQI-----MTLTGMKVgpslKIYDLIQQLKCK 67
WD40 pfam00400
WD domain, G-beta repeat;
229-264 1.49e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.56  E-value: 1.49e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 227452250  229 KYKSTLSGHCAPVLACAFSHDGKMLASGSVDKSVII 264
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 329-391 1.59e-05

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: 42.31  E-value: 1.59e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227452250 329 EWSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAgDLKIESLGLRSKVLRSIEEL 391
Cdd:cd09506    4 EWTVDDVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLT-ELGVTRVGHRMNIERALKKL 65
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 405-422 3.24e-05

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: 41.45  E-value: 3.24e-05
                           10
                   ....*....|....*...
gi 227452250   405 EFICPITRELMKDPVIAS 422
Cdd:smart00504   1 EFLCPISLEVMKDPVILP 18
WD40 pfam00400
WD domain, G-beta repeat;
50-82 4.23e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 4.23e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 227452250   50 LKFHTYAVHCCCFSPSGHVLASCSTDGTTVLWS 82
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 334-392 4.39e-05

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity.


Pssm-ID: 188932  Cd Length: 58  Bit Score: 40.76  E-value: 4.39e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 227452250 334 DVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAgDLKIESLGLRSKVLRSIEELR 392
Cdd:cd09533    1 DVADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLK-EMGITSVGHRLTILKAVYELK 58
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
 402-423 7.93e-05

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: 40.64  E-value: 7.93e-05
                         10        20
                 ....*....|....*....|...
gi 227452250 402 IPDEFICPITRELMKDPVIA-SG 423
Cdd:cd16654    1 VPDYLCCKISFELMRDPVITpSG 23
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3-38 9.99e-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: 39.60  E-value: 9.99e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 227452250     3 RLIHTLADHGDDVSCCAFSAA--LLATCSLDKTIRLYS 38
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDgkYLASGSDDGTIKLWD 40
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 406-422 1.06e-04

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: 39.46  E-value: 1.06e-04
                         10
                 ....*....|....*..
gi 227452250 406 FICPITRELMKDPVIAS 422
Cdd:cd16453    1 FLCPISGELMKDPVITP 17
SAM_USH1G_HARP cd09517
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ...
 337-396 1.51e-04

SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher syndrome type-1G/ Harmonin-interacting Ankyrin Repeat-containing protein) family is a protein-protein interaction domain. Members of this family have an N-terminal ankyrin repeat region and a C-terminal SAM domain. In mammals these proteins can interact via the SAM domain with the PDZ domain of harmonin to form a scaffolding complex that facilitates signal transduction in epithelial and inner ear sensory cells. It was suggested that USH1G and HARP can be tissue specific partners of harmonin. Mutations in ush1g genes lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.


Pssm-ID: 188916  Cd Length: 66  Bit Score: 39.63  E-value: 1.51e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 337 VWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAgDLKIEsLGLRSKVLRSIEELRAKMD 396
Cdd:cd09517    7 RFLTSNHLEEYLPVFEREKIDLEALMLLTDEDLQ-SLKLP-LGPRRKLLNAIAKRKQALE 64
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 328-393 2.00e-04

SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK (connector enhancer of kinase suppressor of ras (Ksr)) subfamily is a protein-protein interaction domain. CNK proteins are multidomain scaffold proteins containing a few protein-protein interaction domains and are required for connecting Rho and Ras signaling pathways. In Drosophila, the SAM domain of CNK is known to interact with the SAM domain of the aveugle protein, forming a heterodimer. Mutation of the SAM domain in human CNK1 abolishes the ability to cooperate with the Ras effector, supporting the idea that this interaction is necessary for proper Ras signal transduction.


Pssm-ID: 188910  Cd Length: 69  Bit Score: 39.58  E-value: 2.00e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 328 EEWSEEDVSVWLRaqGLEDLVGI----FRANNIDGKELLHLTKESLAgDLKIESLGLRSKVLRSIEELRA 393
Cdd:cd09511    2 AKWSPKQVTDWLK--GLDDCLQQyiytFEREKVTGEQLLNLSPQDLE-NLGVTKIGHQELILEAVELLCA 68
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 330-392 2.88e-04

SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain of Ph (polyhomeotic) proteins of Polycomb group is a protein-protein interaction domain. Ph1,2,3 proteins are members of PRC1 complex. This complex is involved in transcriptional repression of Hox (Homeobox) cluster genes. It is recruited through methylated H3Lys27 and supports the repression state by mediating monoubiquitination of histone H2A. Proteins of the Ph1,2,3 subfamily contribute to anterior-posterior neural tissue specification during embryogenesis. Additionally, the P2 protein of zebrafish is known to be involved in epiboly and tailbud formation. SAM domains of Ph proteins may interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with the SAM domain of Scm (sex comb on midleg) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome.


Pssm-ID: 188976  Cd Length: 69  Bit Score: 38.92  E-value: 2.88e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227452250 330 WSEEDVSVWLRA-QGLEDLVGIFRANNIDGKELLHLTKESLAGDLKIEsLGLRSKVLRSIEELR 392
Cdd:cd09577    6 WSVEDVYEFIRSlPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIK-LGPALKICAKINSLK 68
SAM_SGMS1 cd09514
SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 ...
 330-392 3.16e-04

SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. Sphingomyelin synthase 1 is a transmembrane protein with a SAM domain at the N-terminus and a catalytic domain at the C-terminus. Sphingomyelin synthase 1 is a Golgi-associated enzyme, and depending on the concentration of diacylglycerol and ceramide, can catalyze synthesis phosphocholine or sphingomyelin, respectively. It plays a central role in sphingolipid and glycerophospholipid metabolism.


Pssm-ID: 188913  Cd Length: 72  Bit Score: 39.00  E-value: 3.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227452250 330 WSEEDVSVWLRAQGLEDLVGIFRanNIDGKELLHLTKEslagDLKIESLGLRS-----KVLRSIEELR 392
Cdd:cd09514    7 WSPKEVSDWLSEEGMQEYSEALR--SFDGQALLNLTEE----DFKKTPLSLVSsdsgrQLLEMIETLK 68
WD40 pfam00400
WD domain, G-beta repeat;
3-38 3.40e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.10  E-value: 3.40e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 227452250    3 RLIHTLADHGDDVSCCAFSA--ALLATCSLDKTIRLYS 38
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPdgKLLASGSDDGTVKVWD 39
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 334-391 4.65e-04

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


Pssm-ID: 188920  Cd Length: 64  Bit Score: 38.42  E-value: 4.65e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 227452250 334 DVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAgDLKIESLGLRSKVLRSIEEL 391
Cdd:cd09521    7 DLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLE-KIGITQPGDQKKILDAIKEV 63
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 98-125 5.98e-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: 37.29  E-value: 5.98e-04
                           10        20
                   ....*....|....*....|....*...
gi 227452250    98 SPVRVCCFSPDSAYLASGAADGSIALWN 125
Cdd:smart00320  13 GPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Ge1_WD40 pfam16529
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ...
 139-216 6.99e-04

WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of Ge-1 or enhancer of mRNA-decapping proteins. WD40-repeat regions are involved in protein-protein interactions.


Pssm-ID: 465162 [Multi-domain]  Cd Length: 328  Bit Score: 41.29  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250  139 DSSLVACAFSPDGGLFVTGSSGGDLTVW------DDRMRCLHSEKAHDLGITCCSFSSQPLSGGEGLQSYQLA--SCGQD 210
Cdd:pfam16529 186 HSLLVDAAFSPDGTALATASLDGEVKFFqiylfdNRNPRCLHEWKPHDGKPLSSLFFLDNHKKPPEVQFWRFAitGADNN 265


                  ....*.
gi 227452250  211 CEIKLW 216
Cdd:pfam16529 266 SELKLW 271
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 273-313 1.00e-03

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: 40.78  E-value: 1.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 227452250 273 LHTLTQHTRYVTTCAFAPNTLLLATGSMDKTVNIWqfDLET 313
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVW--DLET 40
SAM_GAREM cd09525
SAM domain of GAREM subfamily; SAM (sterile alpha motif) domain of GAREM (Grb2-associated and ...
 331-378 1.18e-03

SAM domain of GAREM subfamily; SAM (sterile alpha motif) domain of GAREM (Grb2-associated and regulator of Erk/MARK) protein subfamily (also known as FAM59A) is a putative protein-protein interaction domain. SAM domain is a widespread domain in signaling proteins. Proteins of this group have SAM at the C-terminus. Human GAREM protein is known to play a role in regulation of the EGF (Epidermal Growth Factor) receptor and of Gab or insulin preceptor substrate-1 family proteins. Grb2 (Growth factor receptor-bound) protein was identified as a binding partner of human GAREM. Proline-rich motifs and phosphorylation of two conserved tyrosines in GAREM are important for the interaction with the SH3 domains of Grb2 protein; however these motifs and residues do not belong to the SAM domain.


Pssm-ID: 188924  Cd Length: 67  Bit Score: 37.13  E-value: 1.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 227452250 331 SEEDVSVWLRAQGL-EDLVGIFRANNIDGKELLHLTKESLAGDLKIESL 378
Cdd:cd09525    5 SIEEVSKSLRFIGLsEDVVSFFVTEKIDGNLLVQLTEEILSEDFKLSKL 53
SAM_PNT-Tel_Yan cd08535
Sterile alpha motif (SAM)/Pointed domain of Tel/Yan protein; SAM Pointed domain of Tel ...
 330-378 1.24e-03

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: 36.98  E-value: 1.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 330 WSEEDVSVWLR-AQGLEDLVGI----FRANnidGKELLHLTKESL------AGDLKIESL 378
Cdd:cd08535    6 WSREDVLQWLRwAENEFSLPPIdsntFEMN---GKALCLLTKEDFryrcphAGDVLYNLL 62
SAM_aveugle-like cd09510
SAM domain of aveugle-like subfamily; SAM (sterile alpha motif) domain of SAM_aveugle-like ...
 330-396 1.33e-03

SAM domain of aveugle-like subfamily; SAM (sterile alpha motif) domain of SAM_aveugle-like subfamily is a protein-protein interaction domain. In Drosophila, the aveugle (AVE) protein (also known as HYP (Hyphen)) is involved in normal photoreceptor differentiation, and required for epidermal growth factor receptor (EGFR) signaling between ras and raf genes during eye development and wing vein formation. SAM domain of the HYP(AVE) protein interacts with SAM domain of CNK, the multidomain scaffold protein connector enhancer of kinase suppressor of ras. CNK/HYP(AVE) complex interacts with KSR (kinase suppressor of Ras) protein. This interaction leads to stimulation of Ras-dependent Raf activation. This subfamily also includes vertebrate AVE homologs - Samd10 and Samd12 proteins. Their exact function is unknown, but they may play a role in signal transduction during embryogenesis.


Pssm-ID: 188909  Cd Length: 75  Bit Score: 37.28  E-value: 1.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250 330 WSEEDVSVWLRAQGLED---LVGIFRANNIDGKELLHLTKESLAgDLKIESLGLRSKVLRSIEELRAKMD 396
Cdd:cd09510    6 WSVQDVCKWLKRHCPDYyllYAELFLQHDITGRALLRLNDNKLE-RMGITDEDHRQDILREILKLRLKTE 74
SAM_Atherin-like cd09583
SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin ...
 330-379 1.66e-03

SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin and Atherin-like subfamily proteins is a putative protein-protein and/or protein-lipid interaction domain. In addition to the C-terminal SAM domain, the majority of proteins belonging to this group also have PHD (or Zn finger) domain. As potential members of the polycomb group, these proteins may be involved in regulation of some key regulatory genes during development. Atherin can be recruited by Ruk/CIN85 kinase-binding proteins via its SH3 domains thus participating in the signal transferring kinase cascades. Also, atherin was found associated with low density lipids (LDL) in atherosclerotic lesions in human. It was suggested that atherin plays an essential role in atherogenesis via immobilization of LDL in the arterial wall. SAM domains of atherins are predicted to form polymers. Inhibition of polymer formation could be a potential antiatherosclerotic therapy.


Pssm-ID: 188982  Cd Length: 69  Bit Score: 36.86  E-value: 1.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 227452250 330 WSEEDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAGDLKIEsLG 379
Cdd:cd09583    4 WSVEDVVQYFKTAGFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLK-LG 52
SAM_Ste50_fungal cd09536
SAM domain of Ste50 fungal subfamily; SAM (sterile alpha motif) domain of Ste50 fungal ...
 325-385 2.06e-03

SAM domain of Ste50 fungal subfamily; SAM (sterile alpha motif) domain of Ste50 fungal subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and Ras-associated UBQ superfamily domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response, and contribute to cell wall integrity in vegetative cells. Ste50 of S.cerevisiae acts as an adaptor protein between G protein and MAP triple kinase Ste11. Ste50 proteins are able to form homooligomers, binding each other via their SAM domains, as well as heterodimers and heterogeneous complexes with SAM domain or SAM homodimers of MAPKKK Ste11 protein kinase.


Pssm-ID: 188935  Cd Length: 74  Bit Score: 36.64  E-value: 2.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227452250 325 HFTEEWSEEDVSVWLRAQ-GLED---LVGIFRANNIDGKELLHLT----KESLAGDLkieSLGLRSKVL 385
Cdd:cd09536    1 EEFNEWSTDEVVKWCISSlGLDDgdpLCDRLRENNITGSLLSELTledcKELCDNDL---SLAIRLKLL 66
WD40 pfam00400
WD domain, G-beta repeat;
98-125 2.16e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 2.16e-03
                          10        20
                  ....*....|....*....|....*...
gi 227452250   98 SPVRVCCFSPDSAYLASGAADGSIALWN 125
Cdd:pfam00400  12 GSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
 333-394 4.73e-03

SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates.


Pssm-ID: 188919  Cd Length: 65  Bit Score: 35.35  E-value: 4.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227452250 333 EDVSVWLRAQGLEDLVGIFRANNIDGKELLHLTKESLAgDLKIESLGLRSKVLRSIEELRAK 394
Cdd:cd09520    5 SDLPELLAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLK-ELGITAFGARRKMLLAISELNKR 65
SAM_PNT smart00251
SAM / Pointed domain; A subfamily of the SAM domain
 320-367 6.08e-03

SAM / Pointed domain; A subfamily of the SAM domain


Pssm-ID: 128547  Cd Length: 82  Bit Score: 35.70  E-value: 6.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 227452250   320 NDPlkhftEEWSEEDVSVWLRAQGLE-DLVGI-FRANNIDGKELLHLTKE 367
Cdd:smart00251  15 ADP-----QLWTEDHVLEWLEWAVKEfSLSPIdFSKFDMSGKELCSMSKE 59
Frtz pfam11768
WD repeat-containing and planar cell polarity effector protein Fritz; Fritz is a probable ...
 87-167 6.56e-03

WD repeat-containing and planar cell polarity effector protein Fritz; Fritz is a probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements. In Drosophila melanogaster, fritz regulates both the location and the number of wing cell prehair initiation sites.


Pssm-ID: 432059  Cd Length: 544  Bit Score: 38.72  E-value: 6.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250   87 HTLTVLEQPGGSPVRVCCFSPDSAYLASGAADGSIALWNAQTYKLYRCGSVKDSSLVACafSPDGGLFVTGSSGGDLTVW 166
Cdd:pfam11768 249 ECVSVTRIPLRSPVISCARNHAEDKLLLGCEDSSLILYEGHRKITLLAQAAVTPHLIRW--HPAGAIILVCSAQGELQIF 326


                  .
gi 227452250  167 D 167
Cdd:pfam11768 327 D 327
SAM_PNT-ERG_FLI-1 cd08531
Sterile alpha motif (SAM)/Pointed domain of ERG (Ets related gene) and FLI-1 (Friend leukemia ...
 330-367 6.87e-03

Sterile alpha motif (SAM)/Pointed domain of ERG (Ets related gene) and FLI-1 (Friend leukemia integration 1) transcription factors; SAM Pointed domain of ERG/FLI-1 subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. The ERG and FLI regulators are involved in endothelial cell differentiation, bone morphogenesis and neural crest development. They are proto-oncogenes implicated in cancer development such as myeloid leukemia, Ewing's sarcoma and erythroleukemia. Members of this subfamily are potential targets for cancer therapy.


Pssm-ID: 188877  Cd Length: 75  Bit Score: 35.46  E-value: 6.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 227452250 330 WSEEDVSVWL----RAQGLEDlVGIFRANNIDGKELLHLTKE 367
Cdd:cd08531    8 WTREHVRQWVewaiKEYSLKD-VDVSRFDNIDGKELCRMTRD 48
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
 105-171 7.07e-03

Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation initiation factors.


Pssm-ID: 462552 [Multi-domain]  Cd Length: 194  Bit Score: 37.64  E-value: 7.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227452250  105 FSPDSAYLAS---GAADGSIALWNAQTYKLYrcGSVKDSSLVACAFSPDGGLFVTGSsggdlTVWddRMR 171
Cdd:pfam08662 108 WSPFGRLVLLagfGNLAGDIEFWDVVNKKKI--ATAEASNATLCEWSPDGRYFLTAT-----TAP--RLR 168
 
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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