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Conserved domains on  [gi|121114302|ref|NP_001073341|]
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cullin-4B 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;
199-796 0e+00

Cullin family;


:

Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 779.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  199 WQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSYKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNH 278
Cdd:pfam00888   1 WAKLEDAIDEILNKNVSSLSYEELYRAVYNLCLHKQGEKLYDKLKEYLEEHLKKLVKPLIKEASSGEEFLKAYVKEWEDH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  279 CRQMIMIRSIFLFLDRTYVlqnSMLPSIWDMGLELFRAHIIsDQKVQNKTIDGILLLIERERNGEAIDRSLL-------R 351
Cdd:pfam00888  81 TISMKMIRDIFMYLDRVYV---KRLPSIYDLGLELFRDHVF-RIPLKDKLIDALLDLIEKERNGEVIDRSLIksvidmlV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  352 SLLSMLSDLQIYQDSFEQRFLEETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIATVEKQLL 431
Cdd:pfam00888 157 SLGEDEKKDNVYEEDFEPPFLEATEEYYRAESQELLAENVAPEYLKKAERRLEEEEERVRHYLHSSTKKKLLDVLEEVLI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  432 GEHLTAILQKGLNNLLDENRIQDLSLLYQLFSRVRGGVQVLLQQWIEYIKAFGSTIVIN----PEKDKTMVQELLDFKDK 507
Cdd:pfam00888 237 SDHLEELLEEELQNLLDDNKTEDLKRLYRLLSRVPDGLEPLRKAFEEYIKKEGKAIVKDakeqTTDAKKYVEDLLELKDK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  508 VDHIIDICFLKNEKFINAMKEAFETFINK--RPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVF 585
Cdd:pfam00888 317 FDKIVKDAFSNDELFVKALDEAFEEFINKntSNSKSPELLAKYIDDLLKKGLKGKSEEELEEKLDKVITLFRYIQDKDVF 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  586 EAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVPG-NIELTVNIL 664
Cdd:pfam00888 397 EAFYKKHLAKRLLLGKSASDDAERSMISKLKEECGSEFTSKLEGMFKDMELSKDLMKEFKEHLSENKSSKkGIDLSVNVL 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  665 TMGYWPTYVPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKK-ELQVSLFQTLVLLMFN-EGE 742
Cdd:pfam00888 477 TSGAWPTYLTSDFILPPELEKAIERFEKFYLSKHSGRKLTWLHSLGTAELKATFPKGKKhELNVSTYQMAILLLFNdDGD 556
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 121114302  743 EFSLEEIKQATGIEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDF 796
Cdd:pfam00888 557 SLSYEEIQEATGLPDEELKRTLQSLACAKAKVLLKEPMSKDINPTDTFSFNEDF 610
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
824-889 1.69e-27

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: 105.70  E-value: 1.69e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 121114302   824 VFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLK--FPVKPADLKKRIESLIDRDYMERDKENPN 889
Cdd:smart00884   1 VEEDRKLEIQAAIVRIMKSRKTLSHSELVSEVIEQLKkrFKPSVSDIKKRIESLIEREYLERDEDDPN 68
 
Name Accession Description Interval E-value
Cullin pfam00888
Cullin family;
199-796 0e+00

Cullin family;


Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 779.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  199 WQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSYKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNH 278
Cdd:pfam00888   1 WAKLEDAIDEILNKNVSSLSYEELYRAVYNLCLHKQGEKLYDKLKEYLEEHLKKLVKPLIKEASSGEEFLKAYVKEWEDH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  279 CRQMIMIRSIFLFLDRTYVlqnSMLPSIWDMGLELFRAHIIsDQKVQNKTIDGILLLIERERNGEAIDRSLL-------R 351
Cdd:pfam00888  81 TISMKMIRDIFMYLDRVYV---KRLPSIYDLGLELFRDHVF-RIPLKDKLIDALLDLIEKERNGEVIDRSLIksvidmlV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  352 SLLSMLSDLQIYQDSFEQRFLEETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIATVEKQLL 431
Cdd:pfam00888 157 SLGEDEKKDNVYEEDFEPPFLEATEEYYRAESQELLAENVAPEYLKKAERRLEEEEERVRHYLHSSTKKKLLDVLEEVLI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  432 GEHLTAILQKGLNNLLDENRIQDLSLLYQLFSRVRGGVQVLLQQWIEYIKAFGSTIVIN----PEKDKTMVQELLDFKDK 507
Cdd:pfam00888 237 SDHLEELLEEELQNLLDDNKTEDLKRLYRLLSRVPDGLEPLRKAFEEYIKKEGKAIVKDakeqTTDAKKYVEDLLELKDK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  508 VDHIIDICFLKNEKFINAMKEAFETFINK--RPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVF 585
Cdd:pfam00888 317 FDKIVKDAFSNDELFVKALDEAFEEFINKntSNSKSPELLAKYIDDLLKKGLKGKSEEELEEKLDKVITLFRYIQDKDVF 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  586 EAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVPG-NIELTVNIL 664
Cdd:pfam00888 397 EAFYKKHLAKRLLLGKSASDDAERSMISKLKEECGSEFTSKLEGMFKDMELSKDLMKEFKEHLSENKSSKkGIDLSVNVL 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  665 TMGYWPTYVPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKK-ELQVSLFQTLVLLMFN-EGE 742
Cdd:pfam00888 477 TSGAWPTYLTSDFILPPELEKAIERFEKFYLSKHSGRKLTWLHSLGTAELKATFPKGKKhELNVSTYQMAILLLFNdDGD 556
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 121114302  743 EFSLEEIKQATGIEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDF 796
Cdd:pfam00888 557 SLSYEEIQEATGLPDEELKRTLQSLACAKAKVLLKEPMSKDINPTDTFSFNEDF 610
COG5647 COG5647
Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
173-895 6.15e-150

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


Pssm-ID: 227934 [Multi-domain]  Cd Length: 773  Bit Score: 460.81  E-value: 6.15e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 173 PGSAKKLVIKNFKdkpkLPENYTDETWQKLKEAV----EAIQNSTSIkYNLEELYQAVENLCSYKISANLYKQLRQICED 248
Cdd:COG5647    2 ITNAIKIDVPRKT----LSEEDFESTWEFIERAIgqifERLYDSMAI-LSLMEVYTKIYNYCTNKTRSLESDLRWKIDFI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 249 HIKAQIHQFREDSLDSVL--------------FLKKIDRCWQNHCRQMIMIRSIFLFLDRTYVLQNSMLPS-IWDMG-LE 312
Cdd:COG5647   77 YLGSRLIQKLVDYAKNYIeeynrgrsqenmeeFLDELVKFWNRFTKGATMINHLFLYMDRVYLKKARYDKTlVFEVYsLC 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 313 LFRAHIISDQKVQNKTIDGILLLIERERNGEAIDRSLLRSLLSMLSDLQIYQDS-----------FEQRFLEETNRLYAA 381
Cdd:COG5647  157 LVKEKIESFRLIVDSLINPLLYYVERYRALQSIDRKYIEDAKDMLESLERPSDYkkenlsyyksvFEPIFLEETWEFYEM 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 382 EGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIATVEKQLLGEHLTAIL--QKGLNNLLDENRIQDLSLLY 459
Cdd:COG5647  237 ESSEVIELLSVTEYLEKAHKILEREEELVEIYLKVSTKKPLLEVLEDVLITRHLDDLEeqGSGFREALDASNLEKLQVLY 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 460 QLFSRVRGGVQVLLQQWIEYIKAFGSTIVI-----------------NPEKDKTMVQELLDFKDKVDHIIDICFLKNEKF 522
Cdd:COG5647  317 RLLSETKYGVQPLQEVFERYVKDEGVLINIetnyifhckvdvgflgsRECLPKLYVQKLLSCHDLFPSLVNESFEGDGSI 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 523 INAMKEAFETFINK---RPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVFEAFYKKDLAKRLLV 599
Cdd:COG5647  397 VKALGNAFKTFINGnesADSGPSEYLAKYIDGLLKKDGKQSFIGKIKDLLQDIITLFRYVEEKDVFEKYYKKLLAKRLLN 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 600 GKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNvpGNIELTVNILTMGYWPT-YVPMEVH 678
Cdd:COG5647  477 GRSASAQAELKMISMLKKVCGQEFTSKLEGMFRDISLSSEFTEAFQHSPQSYN--KYLDLFVWVLTQAYWPLsPEEVSIR 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 679 LPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKKELQVSLFQT---LVLLMFNEGEEFSLEEIKQATGI 755
Cdd:COG5647  555 LPKELVPILEGFKKFYSSKHNGRKLKWYWHLGSGEVKARFNEGQKYLEISTFSVyqlLVFLLFNDHEELTFEEILELTKL 634
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 756 EDGELRRTLQSLACGKARVLAKNpkGKDIEDGDKFICNDDFKHKLFRIKINQIQMKETVEEQASTTERVFQDRQYQIDAA 835
Cdd:COG5647  635 STDDLKRVLQSLSCAKLVVLLKD--DKLVSPNTKFYVNENFSSKLERIKINYIAESECMQDNLDTHETVEEDRQAELQAC 712
                        730       740       750       760       770       780
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 121114302 836 IVRIMKMRKTLSHNLLVSEVYNQLK--FPVKPADLKKRIESLIDRDYMERdKENPNQYNYIA 895
Cdd:COG5647  713 IVRIMKARKKLKHGDLVKEVIAQHKsrFEPKVSMVKRAIETLIEKEYLER-QADDEIYVYLA 773
CULLIN smart00182
Cullin;
578-718 1.10e-53

Cullin;


Pssm-ID: 214545 [Multi-domain]  Cd Length: 143  Bit Score: 182.90  E-value: 1.10e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302   578 FIYGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVP-GN 656
Cdd:smart00182   1 YIQDKDVFEKYYKKHLAKRLILNRSASDDAEENMITKLKQECGYEFTSKLERMFRDISLSKDLNQSFKDMLENNPSAkPI 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 121114302   657 IELTVNILTMGYWPTY-VPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEF 718
Cdd:smart00182  81 IDLNVRVLTSGYWPTSsTEVEINLPQELEDALEEFEEFYLAKHSGRKLTWLHSLGRGEVKANF 143
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
824-889 1.69e-27

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: 105.70  E-value: 1.69e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 121114302   824 VFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLK--FPVKPADLKKRIESLIDRDYMERDKENPN 889
Cdd:smart00884   1 VEEDRKLEIQAAIVRIMKSRKTLSHSELVSEVIEQLKkrFKPSVSDIKKRIESLIEREYLERDEDDPN 68
Cullin_Nedd8 pfam10557
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
827-887 2.01e-27

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: 105.61  E-value: 2.01e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 121114302  827 DRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLK--FPVKPADLKKRIESLIDRDYMERDKEN 887
Cdd:pfam10557   1 DRKHEIQAAIVRIMKSRKTLSHNELVNEVIEQLKsrFKPSVSDIKKRIESLIEKEYLERDEDD 63
 
Name Accession Description Interval E-value
Cullin pfam00888
Cullin family;
199-796 0e+00

Cullin family;


Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 779.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  199 WQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSYKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNH 278
Cdd:pfam00888   1 WAKLEDAIDEILNKNVSSLSYEELYRAVYNLCLHKQGEKLYDKLKEYLEEHLKKLVKPLIKEASSGEEFLKAYVKEWEDH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  279 CRQMIMIRSIFLFLDRTYVlqnSMLPSIWDMGLELFRAHIIsDQKVQNKTIDGILLLIERERNGEAIDRSLL-------R 351
Cdd:pfam00888  81 TISMKMIRDIFMYLDRVYV---KRLPSIYDLGLELFRDHVF-RIPLKDKLIDALLDLIEKERNGEVIDRSLIksvidmlV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  352 SLLSMLSDLQIYQDSFEQRFLEETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIATVEKQLL 431
Cdd:pfam00888 157 SLGEDEKKDNVYEEDFEPPFLEATEEYYRAESQELLAENVAPEYLKKAERRLEEEEERVRHYLHSSTKKKLLDVLEEVLI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  432 GEHLTAILQKGLNNLLDENRIQDLSLLYQLFSRVRGGVQVLLQQWIEYIKAFGSTIVIN----PEKDKTMVQELLDFKDK 507
Cdd:pfam00888 237 SDHLEELLEEELQNLLDDNKTEDLKRLYRLLSRVPDGLEPLRKAFEEYIKKEGKAIVKDakeqTTDAKKYVEDLLELKDK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  508 VDHIIDICFLKNEKFINAMKEAFETFINK--RPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVF 585
Cdd:pfam00888 317 FDKIVKDAFSNDELFVKALDEAFEEFINKntSNSKSPELLAKYIDDLLKKGLKGKSEEELEEKLDKVITLFRYIQDKDVF 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  586 EAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVPG-NIELTVNIL 664
Cdd:pfam00888 397 EAFYKKHLAKRLLLGKSASDDAERSMISKLKEECGSEFTSKLEGMFKDMELSKDLMKEFKEHLSENKSSKkGIDLSVNVL 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302  665 TMGYWPTYVPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKK-ELQVSLFQTLVLLMFN-EGE 742
Cdd:pfam00888 477 TSGAWPTYLTSDFILPPELEKAIERFEKFYLSKHSGRKLTWLHSLGTAELKATFPKGKKhELNVSTYQMAILLLFNdDGD 556
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 121114302  743 EFSLEEIKQATGIEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDF 796
Cdd:pfam00888 557 SLSYEEIQEATGLPDEELKRTLQSLACAKAKVLLKEPMSKDINPTDTFSFNEDF 610
COG5647 COG5647
Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
173-895 6.15e-150

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


Pssm-ID: 227934 [Multi-domain]  Cd Length: 773  Bit Score: 460.81  E-value: 6.15e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 173 PGSAKKLVIKNFKdkpkLPENYTDETWQKLKEAV----EAIQNSTSIkYNLEELYQAVENLCSYKISANLYKQLRQICED 248
Cdd:COG5647    2 ITNAIKIDVPRKT----LSEEDFESTWEFIERAIgqifERLYDSMAI-LSLMEVYTKIYNYCTNKTRSLESDLRWKIDFI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 249 HIKAQIHQFREDSLDSVL--------------FLKKIDRCWQNHCRQMIMIRSIFLFLDRTYVLQNSMLPS-IWDMG-LE 312
Cdd:COG5647   77 YLGSRLIQKLVDYAKNYIeeynrgrsqenmeeFLDELVKFWNRFTKGATMINHLFLYMDRVYLKKARYDKTlVFEVYsLC 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 313 LFRAHIISDQKVQNKTIDGILLLIERERNGEAIDRSLLRSLLSMLSDLQIYQDS-----------FEQRFLEETNRLYAA 381
Cdd:COG5647  157 LVKEKIESFRLIVDSLINPLLYYVERYRALQSIDRKYIEDAKDMLESLERPSDYkkenlsyyksvFEPIFLEETWEFYEM 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 382 EGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIATVEKQLLGEHLTAIL--QKGLNNLLDENRIQDLSLLY 459
Cdd:COG5647  237 ESSEVIELLSVTEYLEKAHKILEREEELVEIYLKVSTKKPLLEVLEDVLITRHLDDLEeqGSGFREALDASNLEKLQVLY 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 460 QLFSRVRGGVQVLLQQWIEYIKAFGSTIVI-----------------NPEKDKTMVQELLDFKDKVDHIIDICFLKNEKF 522
Cdd:COG5647  317 RLLSETKYGVQPLQEVFERYVKDEGVLINIetnyifhckvdvgflgsRECLPKLYVQKLLSCHDLFPSLVNESFEGDGSI 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 523 INAMKEAFETFINK---RPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVFEAFYKKDLAKRLLV 599
Cdd:COG5647  397 VKALGNAFKTFINGnesADSGPSEYLAKYIDGLLKKDGKQSFIGKIKDLLQDIITLFRYVEEKDVFEKYYKKLLAKRLLN 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 600 GKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNvpGNIELTVNILTMGYWPT-YVPMEVH 678
Cdd:COG5647  477 GRSASAQAELKMISMLKKVCGQEFTSKLEGMFRDISLSSEFTEAFQHSPQSYN--KYLDLFVWVLTQAYWPLsPEEVSIR 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 679 LPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKKELQVSLFQT---LVLLMFNEGEEFSLEEIKQATGI 755
Cdd:COG5647  555 LPKELVPILEGFKKFYSSKHNGRKLKWYWHLGSGEVKARFNEGQKYLEISTFSVyqlLVFLLFNDHEELTFEEILELTKL 634
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302 756 EDGELRRTLQSLACGKARVLAKNpkGKDIEDGDKFICNDDFKHKLFRIKINQIQMKETVEEQASTTERVFQDRQYQIDAA 835
Cdd:COG5647  635 STDDLKRVLQSLSCAKLVVLLKD--DKLVSPNTKFYVNENFSSKLERIKINYIAESECMQDNLDTHETVEEDRQAELQAC 712
                        730       740       750       760       770       780
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 121114302 836 IVRIMKMRKTLSHNLLVSEVYNQLK--FPVKPADLKKRIESLIDRDYMERdKENPNQYNYIA 895
Cdd:COG5647  713 IVRIMKARKKLKHGDLVKEVIAQHKsrFEPKVSMVKRAIETLIEKEYLER-QADDEIYVYLA 773
CULLIN smart00182
Cullin;
578-718 1.10e-53

Cullin;


Pssm-ID: 214545 [Multi-domain]  Cd Length: 143  Bit Score: 182.90  E-value: 1.10e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121114302   578 FIYGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVP-GN 656
Cdd:smart00182   1 YIQDKDVFEKYYKKHLAKRLILNRSASDDAEENMITKLKQECGYEFTSKLERMFRDISLSKDLNQSFKDMLENNPSAkPI 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 121114302   657 IELTVNILTMGYWPTY-VPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEF 718
Cdd:smart00182  81 IDLNVRVLTSGYWPTSsTEVEINLPQELEDALEEFEEFYLAKHSGRKLTWLHSLGRGEVKANF 143
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
824-889 1.69e-27

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: 105.70  E-value: 1.69e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 121114302   824 VFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLK--FPVKPADLKKRIESLIDRDYMERDKENPN 889
Cdd:smart00884   1 VEEDRKLEIQAAIVRIMKSRKTLSHSELVSEVIEQLKkrFKPSVSDIKKRIESLIEREYLERDEDDPN 68
Cullin_Nedd8 pfam10557
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
827-887 2.01e-27

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: 105.61  E-value: 2.01e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 121114302  827 DRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLK--FPVKPADLKKRIESLIDRDYMERDKEN 887
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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