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Conserved domains on  [gi|511772961|ref|NP_001265442|]
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cullin-4A isoform 2 [Homo sapiens]

Protein Classification

cullin( domain architecture ID 12011724)

cullin is a core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cullin pfam00888
Cullin family;
2-560 0e+00

Cullin family;


:

Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 759.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961    2 LYKQLRQACEDHVQAQILPFREDSLDSVLFLKKINTCWQDHCRQMIMIRSIFLFLDRTYVlqnSTLPSIWDMGLELFRTH 81
Cdd:pfam00888  40 LYDKLKEYLEEHLKKLVKPLIKEASSGEEFLKAYVKEWEDHTISMKMIRDIFMYLDRVYV---KRLPSIYDLGLELFRDH 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961   82 IISDKmVQSKTIDGILLLIERERSGEAVDRSLLRSLLGMLSDL-------QVYKDSFELKFLEETNCLYAAEGQRLMQER 154
Cdd:pfam00888 117 VFRIP-LKDKLIDALLDLIEKERNGEVIDRSLIKSVIDMLVSLgedekkdNVYEEDFEPPFLEATEEYYRAESQELLAEN 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  155 EVPEYLNHVSKRLEEEGDRVITYLDHSTQKPLIACVEKQLLGEHLTAILQKGLDHLLDENRVPDLAQMYQLFSRVRGGQQ 234
Cdd:pfam00888 196 VAPEYLKKAERRLEEEEERVRHYLHSSTKKKLLDVLEEVLISDHLEELLEEELQNLLDDNKTEDLKRLYRLLSRVPDGLE 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  235 ALLQHWSEYIKTFGTAIVIN----PEKDKDMVQDLLDFKDKVDHVIEVCFQKNERFVNLMKESFETFINK--RPNKPAEL 308
Cdd:pfam00888 276 PLRKAFEEYIKKEGKAIVKDakeqTTDAKKYVEDLLELKDKFDKIVKDAFSNDELFVKALDEAFEEFINKntSNSKSPEL 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  309 IAKHVDSKLRAGNKEATDEELERTLDKIMILFRFIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFT 388
Cdd:pfam00888 356 LAKYIDDLLKKGLKGKSEEELEEKLDKVITLFRYIQDKDVFEAFYKKHLAKRLLLGKSASDDAERSMISKLKEECGSEFT 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  389 SKLEGMFKDMELSKDIMVHFKQHMQN-QSDSGPIDLTVNILTMGYWPTYTPMEVHLTPEMIKLQEVFKAFYLGKHSGRKL 467
Cdd:pfam00888 436 SKLEGMFKDMELSKDLMKEFKEHLSEnKSSKKGIDLSVNVLTSGAWPTYLTSDFILPPELEKAIERFEKFYLSKHSGRKL 515
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  468 QWQTTLGHAVLKAEFKEGKK-EFQVSLFQTLVLLMFN-EGDGFSFEEIKMATGIEDSELRRTLQSLACGKARVLIKSPKG 545
Cdd:pfam00888 516 TWLHSLGTAELKATFPKGKKhELNVSTYQMAILLLFNdDGDSLSYEEIQEATGLPDEELKRTLQSLACAKAKVLLKEPMS 595
                         570
                  ....*....|....*
gi 511772961  546 KEVEDGDKFIFNGEF 560
Cdd:pfam00888 596 KDINPTDTFSFNEDF 610
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
588-653 3.56e-26

Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a family of structurally related proteins containing an evolutionarily conserved cullin domain. With the exception of APC2, each member of the cullin family is modified by Nedd8 and several cullins function in Ubiquitin-dependent proteolysis, a process in which the 26S proteasome recognises and subsequently degrades a target protein tagged with K48-linked poly-ubiquitin chains. Cullins are molecular scaffolds responsible for assembling the ROC1/Rbx1 RING-based E3 ubiquitin ligases, of which several play a direct role in tumorigenesis. Nedd8/Rub1 is a small ubiquitin-like protein, which was originally found to be conjugated to Cdc53, a cullin component of the SCF (Skp1-Cdc53/CUL1-F-box protein) E3 Ub ligase complex in Saccharomyces cerevisiae, and Nedd8 modification has now emerged as a regulatory pathway of fundamental importance for cell cycle control and for embryogenesis in metazoans. The only identified Nedd8 substrates are cullins. Neddylation results in covalent conjugation of a Nedd8 moiety onto a conserved cullin lysine residue.


:

Pssm-ID: 214883 [Multi-domain]  Cd Length: 68  Bit Score: 101.85  E-value: 3.56e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511772961   588 VFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLK--FPVKPGDLKKRIESLIDRDYMERDKDNPN 653
Cdd:smart00884   1 VEEDRKLEIQAAIVRIMKSRKTLSHSELVSEVIEQLKkrFKPSVSDIKKRIESLIEREYLERDEDDPN 68
 
Name Accession Description Interval E-value
Cullin pfam00888
Cullin family;
2-560 0e+00

Cullin family;


Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 759.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961    2 LYKQLRQACEDHVQAQILPFREDSLDSVLFLKKINTCWQDHCRQMIMIRSIFLFLDRTYVlqnSTLPSIWDMGLELFRTH 81
Cdd:pfam00888  40 LYDKLKEYLEEHLKKLVKPLIKEASSGEEFLKAYVKEWEDHTISMKMIRDIFMYLDRVYV---KRLPSIYDLGLELFRDH 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961   82 IISDKmVQSKTIDGILLLIERERSGEAVDRSLLRSLLGMLSDL-------QVYKDSFELKFLEETNCLYAAEGQRLMQER 154
Cdd:pfam00888 117 VFRIP-LKDKLIDALLDLIEKERNGEVIDRSLIKSVIDMLVSLgedekkdNVYEEDFEPPFLEATEEYYRAESQELLAEN 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  155 EVPEYLNHVSKRLEEEGDRVITYLDHSTQKPLIACVEKQLLGEHLTAILQKGLDHLLDENRVPDLAQMYQLFSRVRGGQQ 234
Cdd:pfam00888 196 VAPEYLKKAERRLEEEEERVRHYLHSSTKKKLLDVLEEVLISDHLEELLEEELQNLLDDNKTEDLKRLYRLLSRVPDGLE 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  235 ALLQHWSEYIKTFGTAIVIN----PEKDKDMVQDLLDFKDKVDHVIEVCFQKNERFVNLMKESFETFINK--RPNKPAEL 308
Cdd:pfam00888 276 PLRKAFEEYIKKEGKAIVKDakeqTTDAKKYVEDLLELKDKFDKIVKDAFSNDELFVKALDEAFEEFINKntSNSKSPEL 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  309 IAKHVDSKLRAGNKEATDEELERTLDKIMILFRFIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFT 388
Cdd:pfam00888 356 LAKYIDDLLKKGLKGKSEEELEEKLDKVITLFRYIQDKDVFEAFYKKHLAKRLLLGKSASDDAERSMISKLKEECGSEFT 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  389 SKLEGMFKDMELSKDIMVHFKQHMQN-QSDSGPIDLTVNILTMGYWPTYTPMEVHLTPEMIKLQEVFKAFYLGKHSGRKL 467
Cdd:pfam00888 436 SKLEGMFKDMELSKDLMKEFKEHLSEnKSSKKGIDLSVNVLTSGAWPTYLTSDFILPPELEKAIERFEKFYLSKHSGRKL 515
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  468 QWQTTLGHAVLKAEFKEGKK-EFQVSLFQTLVLLMFN-EGDGFSFEEIKMATGIEDSELRRTLQSLACGKARVLIKSPKG 545
Cdd:pfam00888 516 TWLHSLGTAELKATFPKGKKhELNVSTYQMAILLLFNdDGDSLSYEEIQEATGLPDEELKRTLQSLACAKAKVLLKEPMS 595
                         570
                  ....*....|....*
gi 511772961  546 KEVEDGDKFIFNGEF 560
Cdd:pfam00888 596 KDINPTDTFSFNEDF 610
COG5647 COG5647
Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
28-659 4.92e-146

Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227934 [Multi-domain]  Cd Length: 773  Bit Score: 443.09  E-value: 4.92e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  28 SVLFLKKINTCWQDHCRQMIMIRSIFLFLDRTYVLQNS--TLPSIWDMGLELFRTHIISDKMVQSKTIDGILLLIERERS 105
Cdd:COG5647  106 MEEFLDELVKFWNRFTKGATMINHLFLYMDRVYLKKARydKTLVFEVYSLCLVKEKIESFRLIVDSLINPLLYYVERYRA 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961 106 GEAVDRSLL---RSLLGMLS--------DLQVYKDSFELKFLEETNCLYAAEGQRLMQEREVPEYLNHVSKRLEEEGDRV 174
Cdd:COG5647  186 LQSIDRKYIedaKDMLESLErpsdykkeNLSYYKSVFEPIFLEETWEFYEMESSEVIELLSVTEYLEKAHKILEREEELV 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961 175 ITYLDHSTQKPLIACVEKQLLGEHLTAILQKGLD--HLLDENRVPDLAQMYQLFSRVRGGQQALLQHWSEYIKTFGTAIV 252
Cdd:COG5647  266 EIYLKVSTKKPLLEVLEDVLITRHLDDLEEQGSGfrEALDASNLEKLQVLYRLLSETKYGVQPLQEVFERYVKDEGVLIN 345
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961 253 I-----------------NPEKDKDMVQDLLDFKDKVDHVIEVCFQKNERFVNLMKESFETFINK---RPNKPAELIAKH 312
Cdd:COG5647  346 IetnyifhckvdvgflgsRECLPKLYVQKLLSCHDLFPSLVNESFEGDGSIVKALGNAFKTFINGnesADSGPSEYLAKY 425
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961 313 VDSKLRAGNKEATDEELERTLDKIMILFRFIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLE 392
Cdd:COG5647  426 IDGLLKKDGKQSFIGKIKDLLQDIITLFRYVEEKDVFEKYYKKLLAKRLLNGRSASAQAELKMISMLKKVCGQEFTSKLE 505
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961 393 GMFKDMELSKDIMVHFKQhmQNQSDSGPIDLTVNILTMGYWPT-YTPMEVHLTPEMIKLQEVFKAFYLGKHSGRKLQWQT 471
Cdd:COG5647  506 GMFRDISLSSEFTEAFQH--SPQSYNKYLDLFVWVLTQAYWPLsPEEVSIRLPKELVPILEGFKKFYSSKHNGRKLKWYW 583
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961 472 TLGHAVLKAEFKEGKKE---FQVSLFQTLVLLMFNEGDGFSFEEIKMATGIEDSELRRTLQSLACGKARVLIKspKGKEV 548
Cdd:COG5647  584 HLGSGEVKARFNEGQKYleiSTFSVYQLLVFLLFNDHEELTFEEILELTKLSTDDLKRVLQSLSCAKLVVLLK--DDKLV 661
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961 549 EDGDKFIFNGEFKHKLFRIKINQIQMKETVEEQVSTTERVFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLK--FP 626
Cdd:COG5647  662 SPNTKFYVNENFSSKLERIKINYIAESECMQDNLDTHETVEEDRQAELQACIVRIMKARKKLKHGDLVKEVIAQHKsrFE 741
                        650       660       670
                 ....*....|....*....|....*....|...
gi 511772961 627 VKPGDLKKRIESLIDRDYMERDKDNpNQYHYVA 659
Cdd:COG5647  742 PKVSMVKRAIETLIEKEYLERQADD-EIYVYLA 773
CULLIN smart00182
Cullin;
342-482 1.29e-54

Cullin;


Pssm-ID: 214545 [Multi-domain]  Cd Length: 143  Bit Score: 182.90  E-value: 1.29e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961   342 FIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQHMQNQ-SDSGP 420
Cdd:smart00182   1 YIQDKDVFEKYYKKHLAKRLILNRSASDDAEENMITKLKQECGYEFTSKLERMFRDISLSKDLNQSFKDMLENNpSAKPI 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511772961   421 IDLTVNILTMGYWPTY-TPMEVHLTPEMIKLQEVFKAFYLGKHSGRKLQWQTTLGHAVLKAEF 482
Cdd:smart00182  81 IDLNVRVLTSGYWPTSsTEVEINLPQELEDALEEFEEFYLAKHSGRKLTWLHSLGRGEVKANF 143
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
588-653 3.56e-26

Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a family of structurally related proteins containing an evolutionarily conserved cullin domain. With the exception of APC2, each member of the cullin family is modified by Nedd8 and several cullins function in Ubiquitin-dependent proteolysis, a process in which the 26S proteasome recognises and subsequently degrades a target protein tagged with K48-linked poly-ubiquitin chains. Cullins are molecular scaffolds responsible for assembling the ROC1/Rbx1 RING-based E3 ubiquitin ligases, of which several play a direct role in tumorigenesis. Nedd8/Rub1 is a small ubiquitin-like protein, which was originally found to be conjugated to Cdc53, a cullin component of the SCF (Skp1-Cdc53/CUL1-F-box protein) E3 Ub ligase complex in Saccharomyces cerevisiae, and Nedd8 modification has now emerged as a regulatory pathway of fundamental importance for cell cycle control and for embryogenesis in metazoans. The only identified Nedd8 substrates are cullins. Neddylation results in covalent conjugation of a Nedd8 moiety onto a conserved cullin lysine residue.


Pssm-ID: 214883 [Multi-domain]  Cd Length: 68  Bit Score: 101.85  E-value: 3.56e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511772961   588 VFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLK--FPVKPGDLKKRIESLIDRDYMERDKDNPN 653
Cdd:smart00884   1 VEEDRKLEIQAAIVRIMKSRKTLSHSELVSEVIEQLKkrFKPSVSDIKKRIESLIEREYLERDEDDPN 68
Cullin_Nedd8 pfam10557
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
591-651 5.55e-26

Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a family of structurally related proteins containing an evolutionarily conserved cullin domain. With the exception of APC2, each member of the cullin family is modified by Nedd8 and several cullins function in Ubiquitin-dependent proteolysis, a process in which the 26S proteasome recognizes and subsequently degrades a target protein tagged with K48-linked poly-ubiquitin chains. Cullins are molecular scaffolds responsible for assembling the ROC1/Rbx1 RING-based E3 ubiquitin ligases, of which several play a direct role in tumorigenesis. Nedd8/Rub1 is a small ubiquitin-like protein, which was originally found to be conjugated to Cdc53, a cullin component of the SCF (Skp1-Cdc53/CUL1-F-box protein) E3 Ub ligase complex in Saccharomyces cerevisiae, and Nedd8 modification has now emerged as a regulatory pathway of fundamental importance for cell cycle control and for embryogenesis in metazoans. The only identified Nedd8 substrates are cullins. Neddylation results in covalent conjugation of a Nedd8 moiety onto a conserved cullin lysine residue.


Pssm-ID: 463146  Cd Length: 63  Bit Score: 100.99  E-value: 5.55e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511772961  591 DRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLK--FPVKPGDLKKRIESLIDRDYMERDKDN 651
Cdd:pfam10557   1 DRKHEIQAAIVRIMKSRKTLSHNELVNEVIEQLKsrFKPSVSDIKKRIESLIEKEYLERDEDD 63
 
Name Accession Description Interval E-value
Cullin pfam00888
Cullin family;
2-560 0e+00

Cullin family;


Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 759.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961    2 LYKQLRQACEDHVQAQILPFREDSLDSVLFLKKINTCWQDHCRQMIMIRSIFLFLDRTYVlqnSTLPSIWDMGLELFRTH 81
Cdd:pfam00888  40 LYDKLKEYLEEHLKKLVKPLIKEASSGEEFLKAYVKEWEDHTISMKMIRDIFMYLDRVYV---KRLPSIYDLGLELFRDH 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961   82 IISDKmVQSKTIDGILLLIERERSGEAVDRSLLRSLLGMLSDL-------QVYKDSFELKFLEETNCLYAAEGQRLMQER 154
Cdd:pfam00888 117 VFRIP-LKDKLIDALLDLIEKERNGEVIDRSLIKSVIDMLVSLgedekkdNVYEEDFEPPFLEATEEYYRAESQELLAEN 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  155 EVPEYLNHVSKRLEEEGDRVITYLDHSTQKPLIACVEKQLLGEHLTAILQKGLDHLLDENRVPDLAQMYQLFSRVRGGQQ 234
Cdd:pfam00888 196 VAPEYLKKAERRLEEEEERVRHYLHSSTKKKLLDVLEEVLISDHLEELLEEELQNLLDDNKTEDLKRLYRLLSRVPDGLE 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  235 ALLQHWSEYIKTFGTAIVIN----PEKDKDMVQDLLDFKDKVDHVIEVCFQKNERFVNLMKESFETFINK--RPNKPAEL 308
Cdd:pfam00888 276 PLRKAFEEYIKKEGKAIVKDakeqTTDAKKYVEDLLELKDKFDKIVKDAFSNDELFVKALDEAFEEFINKntSNSKSPEL 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  309 IAKHVDSKLRAGNKEATDEELERTLDKIMILFRFIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFT 388
Cdd:pfam00888 356 LAKYIDDLLKKGLKGKSEEELEEKLDKVITLFRYIQDKDVFEAFYKKHLAKRLLLGKSASDDAERSMISKLKEECGSEFT 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  389 SKLEGMFKDMELSKDIMVHFKQHMQN-QSDSGPIDLTVNILTMGYWPTYTPMEVHLTPEMIKLQEVFKAFYLGKHSGRKL 467
Cdd:pfam00888 436 SKLEGMFKDMELSKDLMKEFKEHLSEnKSSKKGIDLSVNVLTSGAWPTYLTSDFILPPELEKAIERFEKFYLSKHSGRKL 515
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  468 QWQTTLGHAVLKAEFKEGKK-EFQVSLFQTLVLLMFN-EGDGFSFEEIKMATGIEDSELRRTLQSLACGKARVLIKSPKG 545
Cdd:pfam00888 516 TWLHSLGTAELKATFPKGKKhELNVSTYQMAILLLFNdDGDSLSYEEIQEATGLPDEELKRTLQSLACAKAKVLLKEPMS 595
                         570
                  ....*....|....*
gi 511772961  546 KEVEDGDKFIFNGEF 560
Cdd:pfam00888 596 KDINPTDTFSFNEDF 610
COG5647 COG5647
Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
28-659 4.92e-146

Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227934 [Multi-domain]  Cd Length: 773  Bit Score: 443.09  E-value: 4.92e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961  28 SVLFLKKINTCWQDHCRQMIMIRSIFLFLDRTYVLQNS--TLPSIWDMGLELFRTHIISDKMVQSKTIDGILLLIERERS 105
Cdd:COG5647  106 MEEFLDELVKFWNRFTKGATMINHLFLYMDRVYLKKARydKTLVFEVYSLCLVKEKIESFRLIVDSLINPLLYYVERYRA 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961 106 GEAVDRSLL---RSLLGMLS--------DLQVYKDSFELKFLEETNCLYAAEGQRLMQEREVPEYLNHVSKRLEEEGDRV 174
Cdd:COG5647  186 LQSIDRKYIedaKDMLESLErpsdykkeNLSYYKSVFEPIFLEETWEFYEMESSEVIELLSVTEYLEKAHKILEREEELV 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961 175 ITYLDHSTQKPLIACVEKQLLGEHLTAILQKGLD--HLLDENRVPDLAQMYQLFSRVRGGQQALLQHWSEYIKTFGTAIV 252
Cdd:COG5647  266 EIYLKVSTKKPLLEVLEDVLITRHLDDLEEQGSGfrEALDASNLEKLQVLYRLLSETKYGVQPLQEVFERYVKDEGVLIN 345
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961 253 I-----------------NPEKDKDMVQDLLDFKDKVDHVIEVCFQKNERFVNLMKESFETFINK---RPNKPAELIAKH 312
Cdd:COG5647  346 IetnyifhckvdvgflgsRECLPKLYVQKLLSCHDLFPSLVNESFEGDGSIVKALGNAFKTFINGnesADSGPSEYLAKY 425
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961 313 VDSKLRAGNKEATDEELERTLDKIMILFRFIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLE 392
Cdd:COG5647  426 IDGLLKKDGKQSFIGKIKDLLQDIITLFRYVEEKDVFEKYYKKLLAKRLLNGRSASAQAELKMISMLKKVCGQEFTSKLE 505
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961 393 GMFKDMELSKDIMVHFKQhmQNQSDSGPIDLTVNILTMGYWPT-YTPMEVHLTPEMIKLQEVFKAFYLGKHSGRKLQWQT 471
Cdd:COG5647  506 GMFRDISLSSEFTEAFQH--SPQSYNKYLDLFVWVLTQAYWPLsPEEVSIRLPKELVPILEGFKKFYSSKHNGRKLKWYW 583
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961 472 TLGHAVLKAEFKEGKKE---FQVSLFQTLVLLMFNEGDGFSFEEIKMATGIEDSELRRTLQSLACGKARVLIKspKGKEV 548
Cdd:COG5647  584 HLGSGEVKARFNEGQKYleiSTFSVYQLLVFLLFNDHEELTFEEILELTKLSTDDLKRVLQSLSCAKLVVLLK--DDKLV 661
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961 549 EDGDKFIFNGEFKHKLFRIKINQIQMKETVEEQVSTTERVFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLK--FP 626
Cdd:COG5647  662 SPNTKFYVNENFSSKLERIKINYIAESECMQDNLDTHETVEEDRQAELQACIVRIMKARKKLKHGDLVKEVIAQHKsrFE 741
                        650       660       670
                 ....*....|....*....|....*....|...
gi 511772961 627 VKPGDLKKRIESLIDRDYMERDKDNpNQYHYVA 659
Cdd:COG5647  742 PKVSMVKRAIETLIEKEYLERQADD-EIYVYLA 773
CULLIN smart00182
Cullin;
342-482 1.29e-54

Cullin;


Pssm-ID: 214545 [Multi-domain]  Cd Length: 143  Bit Score: 182.90  E-value: 1.29e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772961   342 FIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQHMQNQ-SDSGP 420
Cdd:smart00182   1 YIQDKDVFEKYYKKHLAKRLILNRSASDDAEENMITKLKQECGYEFTSKLERMFRDISLSKDLNQSFKDMLENNpSAKPI 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511772961   421 IDLTVNILTMGYWPTY-TPMEVHLTPEMIKLQEVFKAFYLGKHSGRKLQWQTTLGHAVLKAEF 482
Cdd:smart00182  81 IDLNVRVLTSGYWPTSsTEVEINLPQELEDALEEFEEFYLAKHSGRKLTWLHSLGRGEVKANF 143
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
588-653 3.56e-26

Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a family of structurally related proteins containing an evolutionarily conserved cullin domain. With the exception of APC2, each member of the cullin family is modified by Nedd8 and several cullins function in Ubiquitin-dependent proteolysis, a process in which the 26S proteasome recognises and subsequently degrades a target protein tagged with K48-linked poly-ubiquitin chains. Cullins are molecular scaffolds responsible for assembling the ROC1/Rbx1 RING-based E3 ubiquitin ligases, of which several play a direct role in tumorigenesis. Nedd8/Rub1 is a small ubiquitin-like protein, which was originally found to be conjugated to Cdc53, a cullin component of the SCF (Skp1-Cdc53/CUL1-F-box protein) E3 Ub ligase complex in Saccharomyces cerevisiae, and Nedd8 modification has now emerged as a regulatory pathway of fundamental importance for cell cycle control and for embryogenesis in metazoans. The only identified Nedd8 substrates are cullins. Neddylation results in covalent conjugation of a Nedd8 moiety onto a conserved cullin lysine residue.


Pssm-ID: 214883 [Multi-domain]  Cd Length: 68  Bit Score: 101.85  E-value: 3.56e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511772961   588 VFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLK--FPVKPGDLKKRIESLIDRDYMERDKDNPN 653
Cdd:smart00884   1 VEEDRKLEIQAAIVRIMKSRKTLSHSELVSEVIEQLKkrFKPSVSDIKKRIESLIEREYLERDEDDPN 68
Cullin_Nedd8 pfam10557
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
591-651 5.55e-26

Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a family of structurally related proteins containing an evolutionarily conserved cullin domain. With the exception of APC2, each member of the cullin family is modified by Nedd8 and several cullins function in Ubiquitin-dependent proteolysis, a process in which the 26S proteasome recognizes and subsequently degrades a target protein tagged with K48-linked poly-ubiquitin chains. Cullins are molecular scaffolds responsible for assembling the ROC1/Rbx1 RING-based E3 ubiquitin ligases, of which several play a direct role in tumorigenesis. Nedd8/Rub1 is a small ubiquitin-like protein, which was originally found to be conjugated to Cdc53, a cullin component of the SCF (Skp1-Cdc53/CUL1-F-box protein) E3 Ub ligase complex in Saccharomyces cerevisiae, and Nedd8 modification has now emerged as a regulatory pathway of fundamental importance for cell cycle control and for embryogenesis in metazoans. The only identified Nedd8 substrates are cullins. Neddylation results in covalent conjugation of a Nedd8 moiety onto a conserved cullin lysine residue.


Pssm-ID: 463146  Cd Length: 63  Bit Score: 100.99  E-value: 5.55e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511772961  591 DRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLK--FPVKPGDLKKRIESLIDRDYMERDKDN 651
Cdd:pfam10557   1 DRKHEIQAAIVRIMKSRKTLSHNELVNEVIEQLKsrFKPSVSDIKKRIESLIEKEYLERDEDD 63
 
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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