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Conserved domains on  [gi|685260289|ref|XP_009139264|]
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zinc finger CCCH domain-containing protein 48 [Brassica rapa]

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];
123-419 7.55e-34

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 130.80  E-value: 7.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 123 WSQGDSFSLLTQLDGHQKVVTGIALPSGSDKLYTASKDETLRIWDCASGQCTGVLNP-GGEVGCM-IS-EGPWLLVG-MP 198
Cdd:COG2319   62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGhTGAVRSVaFSpDGKTLASGsAD 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 199 NLVKAWNIQTNVDL-SLTGPVGQVYSLVVGTD--LLFAGTQDGSILVWRYNTATncfdPAASLTGHTLAVVSLYVGAN-- 273
Cdd:COG2319  142 GTVRLWDLATGKLLrTLTGHSGAVTSVAFSPDgkLLASGSDDGTVRLWDLATGK----LLRTLTGHTGAVRSVAFSPDgk 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 274 RLYSGSMDNSIKVWSLDNLQCVQTLTEHTSVVMSlICW---DQFLLSCSLDNTVKIWAAtQGGNLEVTYTHkEEYGVLAL 350
Cdd:COG2319  218 LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS-VAFspdGRLLASGSADGTVRLWDL-ATGELLRTLTG-HSGGVNSV 294
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685260289 351 CGVHDAEakpVLLCSCNDNSLHLYDLPSFTERGKILAKQE-IRSIQIGP-GGIFFTGDGTGQVKVWKWSTQ 419
Cdd:COG2319  295 AFSPDGK---LLASGSDDGTVRLWDLATGKLLRTLTGHTGaVRSVAFSPdGKTLASGSDDGTVRLWDLATG 362
ZnF_C3H1 smart00356
zinc finger;
100-122 2.07e-06

zinc finger;


:

Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 43.77  E-value: 2.07e-06
                           10        20
                   ....*....|....*....|...
gi 685260289   100 EKLCKFWADGNCPYGDKCKYLHC 122
Cdd:smart00356   4 TELCKFFKRGYCPRGDRCKFAHP 26
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
123-419 7.55e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 130.80  E-value: 7.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 123 WSQGDSFSLLTQLDGHQKVVTGIALPSGSDKLYTASKDETLRIWDCASGQCTGVLNP-GGEVGCM-IS-EGPWLLVG-MP 198
Cdd:COG2319   62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGhTGAVRSVaFSpDGKTLASGsAD 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 199 NLVKAWNIQTNVDL-SLTGPVGQVYSLVVGTD--LLFAGTQDGSILVWRYNTATncfdPAASLTGHTLAVVSLYVGAN-- 273
Cdd:COG2319  142 GTVRLWDLATGKLLrTLTGHSGAVTSVAFSPDgkLLASGSDDGTVRLWDLATGK----LLRTLTGHTGAVRSVAFSPDgk 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 274 RLYSGSMDNSIKVWSLDNLQCVQTLTEHTSVVMSlICW---DQFLLSCSLDNTVKIWAAtQGGNLEVTYTHkEEYGVLAL 350
Cdd:COG2319  218 LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS-VAFspdGRLLASGSADGTVRLWDL-ATGELLRTLTG-HSGGVNSV 294
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685260289 351 CGVHDAEakpVLLCSCNDNSLHLYDLPSFTERGKILAKQE-IRSIQIGP-GGIFFTGDGTGQVKVWKWSTQ 419
Cdd:COG2319  295 AFSPDGK---LLASGSDDGTVRLWDLATGKLLRTLTGHTGaVRSVAFSPdGKTLASGSDDGTVRLWDLATG 362
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
131-415 2.48e-33

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: 126.68  E-value: 2.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 131 LLTQLDGHQKVVTGIALPSGSDKLYTASKDETLRIWDCASGQC--TGVLNPGGEVGCM-ISEGPWLL-VGMPNLVKAWNI 206
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELlrTLKGHTGPVRDVAaSADGTYLAsGSSDKTIRLWDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 207 QTNVDLS-LTGPVGQVYSLVVGTD--LLFAGTQDGSILVWRYNTATNCFdpaaSLTGHTLAVVSL-YVGANR-LYSGSMD 281
Cdd:cd00200   81 ETGECVRtLTGHTSYVSSVAFSPDgrILSSSSRDKTIKVWDVETGKCLT----TLRGHTDWVNSVaFSPDGTfVASSSQD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 282 NSIKVWSLDNLQCVQTLTEHTSVVMSlICWD---QFLLSCSLDNTVKIWaATQGGNLEVTYT-HkeEYGVLALCgVHDae 357
Cdd:cd00200  157 GTIKLWDLRTGKCVATLTGHTGEVNS-VAFSpdgEKLLSSSSDGTIKLW-DLSTGKCLGTLRgH--ENGVNSVA-FSP-- 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685260289 358 aKPVLLCSCN-DNSLHLYDLPSFTERGKILAKQE-IRSIQIGP-GGIFFTGDGTGQVKVWK 415
Cdd:cd00200  230 -DGYLLASGSeDGTIRVWDLRTGECVQTLSGHTNsVTSLAWSPdGKRLASGSADGTIRIWD 289
ZnF_C3H1 smart00356
zinc finger;
100-122 2.07e-06

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 43.77  E-value: 2.07e-06
                           10        20
                   ....*....|....*....|...
gi 685260289   100 EKLCKFWADGNCPYGDKCKYLHC 122
Cdd:smart00356   4 TELCKFFKRGYCPRGDRCKFAHP 26
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
103-121 3.88e-06

Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.


Pssm-ID: 465719 [Multi-domain]  Cd Length: 19  Bit Score: 43.17  E-value: 3.88e-06
                          10
                  ....*....|....*....
gi 685260289  103 CKFWADGNCPYGDKCKYLH 121
Cdd:pfam18345   1 CKFFLKGRCRYGDKCRFAH 19
PTZ00421 PTZ00421
coronin; Provisional
231-326 6.46e-06

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 48.35  E-value: 6.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 231 LFAGTQDGSILVWRYNT---ATNCFDPAASLTGHT--LAVVSLYVGA-NRLYSGSMDNSIKVWSLDNLQCVQTLTEHTSV 304
Cdd:PTZ00421  91 LFTASEDGTIMGWGIPEeglTQNISDPIVHLQGHTkkVGIVSFHPSAmNVLASAGADMVVNVWDVERGKAVEVIKCHSDQ 170
                         90       100
                 ....*....|....*....|....*
gi 685260289 305 VMSLIcWD---QFLLSCSLDNTVKI 326
Cdd:PTZ00421 171 ITSLE-WNldgSLLCTTSKDKKLNI 194
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
291-327 8.66e-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: 8.66e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 685260289   291 NLQCVQTLTEHTSVVMSlICWD---QFLLSCSLDNTVKIW 327
Cdd:smart00320   1 SGELLKTLKGHTGPVTS-VAFSpdgKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
129-167 1.57e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 1.57e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 685260289  129 FSLLTQLDGHQKVVTGIALPSGSDKLYTASKDETLRIWD 167
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
123-419 7.55e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 130.80  E-value: 7.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 123 WSQGDSFSLLTQLDGHQKVVTGIALPSGSDKLYTASKDETLRIWDCASGQCTGVLNP-GGEVGCM-IS-EGPWLLVG-MP 198
Cdd:COG2319   62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGhTGAVRSVaFSpDGKTLASGsAD 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 199 NLVKAWNIQTNVDL-SLTGPVGQVYSLVVGTD--LLFAGTQDGSILVWRYNTATncfdPAASLTGHTLAVVSLYVGAN-- 273
Cdd:COG2319  142 GTVRLWDLATGKLLrTLTGHSGAVTSVAFSPDgkLLASGSDDGTVRLWDLATGK----LLRTLTGHTGAVRSVAFSPDgk 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 274 RLYSGSMDNSIKVWSLDNLQCVQTLTEHTSVVMSlICW---DQFLLSCSLDNTVKIWAAtQGGNLEVTYTHkEEYGVLAL 350
Cdd:COG2319  218 LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS-VAFspdGRLLASGSADGTVRLWDL-ATGELLRTLTG-HSGGVNSV 294
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685260289 351 CGVHDAEakpVLLCSCNDNSLHLYDLPSFTERGKILAKQE-IRSIQIGP-GGIFFTGDGTGQVKVWKWSTQ 419
Cdd:COG2319  295 AFSPDGK---LLASGSDDGTVRLWDLATGKLLRTLTGHTGaVRSVAFSPdGKTLASGSDDGTVRLWDLATG 362
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
131-415 2.48e-33

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: 126.68  E-value: 2.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 131 LLTQLDGHQKVVTGIALPSGSDKLYTASKDETLRIWDCASGQC--TGVLNPGGEVGCM-ISEGPWLL-VGMPNLVKAWNI 206
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELlrTLKGHTGPVRDVAaSADGTYLAsGSSDKTIRLWDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 207 QTNVDLS-LTGPVGQVYSLVVGTD--LLFAGTQDGSILVWRYNTATNCFdpaaSLTGHTLAVVSL-YVGANR-LYSGSMD 281
Cdd:cd00200   81 ETGECVRtLTGHTSYVSSVAFSPDgrILSSSSRDKTIKVWDVETGKCLT----TLRGHTDWVNSVaFSPDGTfVASSSQD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 282 NSIKVWSLDNLQCVQTLTEHTSVVMSlICWD---QFLLSCSLDNTVKIWaATQGGNLEVTYT-HkeEYGVLALCgVHDae 357
Cdd:cd00200  157 GTIKLWDLRTGKCVATLTGHTGEVNS-VAFSpdgEKLLSSSSDGTIKLW-DLSTGKCLGTLRgH--ENGVNSVA-FSP-- 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685260289 358 aKPVLLCSCN-DNSLHLYDLPSFTERGKILAKQE-IRSIQIGP-GGIFFTGDGTGQVKVWK 415
Cdd:cd00200  230 -DGYLLASGSeDGTIRVWDLRTGECVQTLSGHTNsVTSLAWSPdGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
131-418 4.25e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 125.79  E-value: 4.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 131 LLTQLDGHQKVVTGIAL-PSGSdKLYTASKDETLRIWDCASGQCTGVLN-PGGEVGCM-IS-EGPWLLVGMP-NLVKAWN 205
Cdd:COG2319  112 LLRTLTGHTGAVRSVAFsPDGK-TLASGSADGTVRLWDLATGKLLRTLTgHSGAVTSVaFSpDGKLLASGSDdGTVRLWD 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 206 IQTNVDL-SLTGPVGQVYSLVVGTD--LLFAGTQDGSILVWRYNTATncfdPAASLTGHTLAVVSLYVGAN--RLYSGSM 280
Cdd:COG2319  191 LATGKLLrTLTGHTGAVRSVAFSPDgkLLASGSADGTVRLWDLATGK----LLRTLTGHSGSVRSVAFSPDgrLLASGSA 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 281 DNSIKVWSLDNLQCVQTLTEHTSVVMSlICW---DQFLLSCSLDNTVKIWAATQGgnlEVTYTHK-EEYGVLALCGVHDA 356
Cdd:COG2319  267 DGTVRLWDLATGELLRTLTGHSGGVNS-VAFspdGKLLASGSDDGTVRLWDLATG---KLLRTLTgHTGAVRSVAFSPDG 342
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685260289 357 EakpVLLCSCNDNSLHLYDLPSFTERGKILA-KQEIRSIQIGP-GGIFFTGDGTGQVKVWKWST 418
Cdd:COG2319  343 K---TLASGSDDGTVRLWDLATGELLRTLTGhTGAVTSVAFSPdGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
127-327 1.15e-29

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 118.86  E-value: 1.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 127 DSFSLLTQLDGHQKVVTGIALPSGSDKLYTASKDETLRIWDCASGQCTGVLN-PGGEVGCM-IS-EGPWLLVGMP-NLVK 202
Cdd:COG2319  192 ATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTgHSGSVRSVaFSpDGRLLASGSAdGTVR 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 203 AWNIQTNVDL-SLTGPVGQVYSLVVGTD--LLFAGTQDGSILVWRYNTATncfdPAASLTGHTLAVVSLYVGAN--RLYS 277
Cdd:COG2319  272 LWDLATGELLrTLTGHSGGVNSVAFSPDgkLLASGSDDGTVRLWDLATGK----LLRTLTGHTGAVRSVAFSPDgkTLAS 347
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 685260289 278 GSMDNSIKVWSLDNLQCVQTLTEHTSVVMSlICW---DQFLLSCSLDNTVKIW 327
Cdd:COG2319  348 GSDDGTVRLWDLATGELLRTLTGHTGAVTS-VAFspdGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
130-327 4.16e-26

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: 106.65  E-value: 4.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 130 SLLTQLDGHQKVVTGIALPSGSDKLYTASKDETLRIWDCASGQCTGVLN--PGGEVGCMIS-EGPWLLVGMPNL-VKAWN 205
Cdd:cd00200   42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTghTSYVSSVAFSpDGRILSSSSRDKtIKVWD 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 206 IQTNVDL-SLTGPVGQVYSLVVGTD--LLFAGTQDGSILVWRYNTATncfdPAASLTGHTLAVVSLYV--GANRLYSGSM 280
Cdd:cd00200  122 VETGKCLtTLRGHTDWVNSVAFSPDgtFVASSSQDGTIKLWDLRTGK----CVATLTGHTGEVNSVAFspDGEKLLSSSS 197
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 685260289 281 DNSIKVWSLDNLQCVQTLTEHTSVVMSLiCWDQ---FLLSCSLDNTVKIW 327
Cdd:cd00200  198 DGTIKLWDLSTGKCLGTLRGHENGVNSV-AFSPdgyLLASGSEDGTIRVW 246
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
127-328 1.78e-23

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: 99.33  E-value: 1.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 127 DSFSLLTQLDGHQKVVTGIALPSGSDKLYTASKDETLRIWDCASGQCtgvlnpggevgcmisegpwllvgmpnlvkawnI 206
Cdd:cd00200  123 ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC--------------------------------V 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 207 QTnvdlsLTGPVGQVYSLVVGTD--LLFAGTQDGSILVWRYNTatncFDPAASLTGHTLAVVSLYVGANRLY--SGSMDN 282
Cdd:cd00200  171 AT-----LTGHTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLST----GKCLGTLRGHENGVNSVAFSPDGYLlaSGSEDG 241
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 685260289 283 SIKVWSLDNLQCVQTLTEHTSVVMSLiCWD---QFLLSCSLDNTVKIWA 328
Cdd:cd00200  242 TIRVWDLRTGECVQTLSGHTNSVTSL-AWSpdgKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
118-288 1.54e-15

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: 76.60  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 118 KYLHCWSqGDSFSLLTQLDGHQKVVTGIALPSGSDKLYTASKDETLRIWDCASGQCTGVlnpggevgcmisegpwllvgm 197
Cdd:cd00200  157 GTIKLWD-LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT--------------------- 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 198 pnlvkawniqtnvdlsLTGPVGQVYSLVVGTD--LLFAGTQDGSILVWRYNTatncFDPAASLTGHTLAVVSLYV--GAN 273
Cdd:cd00200  215 ----------------LRGHENGVNSVAFSPDgyLLASGSEDGTIRVWDLRT----GECVQTLSGHTNSVTSLAWspDGK 274
                        170
                 ....*....|....*
gi 685260289 274 RLYSGSMDNSIKVWS 288
Cdd:cd00200  275 RLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
203-419 8.27e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 72.64  E-value: 8.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 203 AWNIQTNVDLSLTGPVGQVYSLVVGTDLLFAGTQDGSILVWRYNTATNcfDPAASLTGHTLAVVSLYV--GANRLYSGSM 280
Cdd:COG2319   21 LAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAG--ALLATLLGHTAAVLSVAFspDGRLLASASA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 281 DNSIKVWSLDNLQCVQTLTEHTSVVMSlICWD---QFLLSCSLDNTVKIWAATQGGNLEVTYTHKEeyGVLALCGVHDAE 357
Cdd:COG2319   99 DGTVRLWDLATGLLLRTLTGHTGAVRS-VAFSpdgKTLASGSADGTVRLWDLATGKLLRTLTGHSG--AVTSVAFSPDGK 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685260289 358 akpVLLCSCNDNSLHLYDLPSFTERGKILA-KQEIRSIQIGPGG-IFFTGDGTGQVKVWKWSTQ 419
Cdd:COG2319  176 ---LLASGSDDGTVRLWDLATGKLLRTLTGhTGAVRSVAFSPDGkLLASGSADGTVRLWDLATG 236
ZnF_C3H1 smart00356
zinc finger;
100-122 2.07e-06

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 43.77  E-value: 2.07e-06
                           10        20
                   ....*....|....*....|...
gi 685260289   100 EKLCKFWADGNCPYGDKCKYLHC 122
Cdd:smart00356   4 TELCKFFKRGYCPRGDRCKFAHP 26
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
103-121 3.88e-06

Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.


Pssm-ID: 465719 [Multi-domain]  Cd Length: 19  Bit Score: 43.17  E-value: 3.88e-06
                          10
                  ....*....|....*....
gi 685260289  103 CKFWADGNCPYGDKCKYLH 121
Cdd:pfam18345   1 CKFFLKGRCRYGDKCRFAH 19
PTZ00421 PTZ00421
coronin; Provisional
231-326 6.46e-06

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 48.35  E-value: 6.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685260289 231 LFAGTQDGSILVWRYNT---ATNCFDPAASLTGHT--LAVVSLYVGA-NRLYSGSMDNSIKVWSLDNLQCVQTLTEHTSV 304
Cdd:PTZ00421  91 LFTASEDGTIMGWGIPEeglTQNISDPIVHLQGHTkkVGIVSFHPSAmNVLASAGADMVVNVWDVERGKAVEVIKCHSDQ 170
                         90       100
                 ....*....|....*....|....*
gi 685260289 305 VMSLIcWD---QFLLSCSLDNTVKI 326
Cdd:PTZ00421 171 ITSLE-WNldgSLLCTTSKDKKLNI 194
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
291-327 8.66e-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: 8.66e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 685260289   291 NLQCVQTLTEHTSVVMSlICWD---QFLLSCSLDNTVKIW 327
Cdd:smart00320   1 SGELLKTLKGHTGPVTS-VAFSpdgKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
129-167 1.57e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 1.57e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 685260289  129 FSLLTQLDGHQKVVTGIALPSGSDKLYTASKDETLRIWD 167
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
128-167 1.59e-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: 38.83  E-value: 1.59e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 685260289   128 SFSLLTQLDGHQKVVTGIALPSGSDKLYTASKDETLRIWD 167
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
293-327 1.97e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.48  E-value: 1.97e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 685260289  293 QCVQTLTEHTSVVMSLiCWD---QFLLSCSLDNTVKIW 327
Cdd:pfam00400   2 KLLKTLEGHTGSVTSL-AFSpdgKLLASGSDDGTVKVW 38
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
98-121 2.80e-04

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 37.94  E-value: 2.80e-04
                          10        20
                  ....*....|....*....|....*
gi 685260289   98 KTEkLCKFWA-DGNCPYGDKCKYLH 121
Cdd:pfam00642   2 KTE-LCRFFLrTGYCKYGDRCKFAH 25
zf-CCCH_4 pfam18044
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and ...
101-121 3.96e-04

CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and one histidine to coordinate the zinc ion. This domain is found in a wide variety of proteins such as E3 ligases.


Pssm-ID: 465626  Cd Length: 22  Bit Score: 37.57  E-value: 3.96e-04
                          10        20
                  ....*....|....*....|.
gi 685260289  101 KLCKFWADGNCPYGDKCKYLH 121
Cdd:pfam18044   1 RLCRYFQKGGCRYGDNCRFSH 21
WD40 COG2319
WD40 repeat [General function prediction only];
127-170 1.56e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 40.66  E-value: 1.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 685260289 127 DSFSLLTQLDGHQKVVTGIALPSGSDKLYTASKDETLRIWDCAS 170
Cdd:COG2319  360 ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
zf-CCCH_2 pfam14608
RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented ...
102-121 3.97e-03

RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented by fingers 5-7 of Nab2. Nab2 ZnF5-7 are zinc-fingers of the type C-x8-C-x5-C-x3-H. Nab2 ZnFs function in the generation of export-competent mRNPs. Mab2 is a conserved polyadenosine-RNA-binding Zn finger protein required for both mRNA export and polyadenylation regulation and becomes attached to the mRNP after splicing and during or immediately after polyadenylation. The three ZnFs, 5-7, have almost identical folds and, most unusually, associate with one another to form a single coherent structural unit. ZnF5-7 bind to eight consecutive adenines, and chemical shift perturbations identify residues on each finger that interact with RNA.


Pssm-ID: 464217  Cd Length: 19  Bit Score: 34.41  E-value: 3.97e-03
                          10        20
                  ....*....|....*....|
gi 685260289  102 LCKFWadGNCPYGDKCKYLH 121
Cdd:pfam14608   1 PCRFG--GNCTFGPKCPFSH 18
 
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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