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Conserved domains on  [gi|1390157516|ref|NP_001350379|]
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cullin-4A isoform 3 [Mus musculus]

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;
1-515 0e+00

Cullin family;


:

Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 693.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516   1 MIMIRSIFLFLDRTYVlqnSMLPSIWDMGLELFRNHIISDRmVQSKTIDGILLLIGRERSGEAVDRSLL-------RSLL 73
Cdd:pfam00888  84 MKMIRDIFMYLDRVYV---KRLPSIYDLGLELFRDHVFRIP-LKDKLIDALLDLIEKERNGEVIDRSLIksvidmlVSLG 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516  74 SMLSDLQVYKDSFELKFLEETNCLYAAEGQRLMQDREVPEYLNHVSKRLEEEADRVITYLDHSTQKPLIACVEKQLLGEH 153
Cdd:pfam00888 160 EDEKKDNVYEEDFEPPFLEATEEYYRAESQELLAENVAPEYLKKAERRLEEEEERVRHYLHSSTKKKLLDVLEEVLISDH 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 154 LTAILQKGLEHLLDENRVPDLTQMYQLFSRVKGGQHALLQHWSEYIKTFGTTIVIN----PEKDKDMVQDLLDFKDKVDH 229
Cdd:pfam00888 240 LEELLEEELQNLLDDNKTEDLKRLYRLLSRVPDGLEPLRKAFEEYIKKEGKAIVKDakeqTTDAKKYVEDLLELKDKFDK 319
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 230 VVEVCFQRNERFINLMKESFETFINK--RPNKPAELIAKHVDSKLRAGNKEATDEELERILDKIMILFRFIHGKDVFEAF 307
Cdd:pfam00888 320 IVKDAFSNDELFVKALDEAFEEFINKntSNSKSPELLAKYIDDLLKKGLKGKSEEELEEKLDKVITLFRYIQDKDVFEAF 399
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 308 YKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQHMQNQSAPG-PIDLTVNILTMG 386
Cdd:pfam00888 400 YKKHLAKRLLLGKSASDDAERSMISKLKEECGSEFTSKLEGMFKDMELSKDLMKEFKEHLSENKSSKkGIDLSVNVLTSG 479
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 387 YWPTYTPMEVHLPPEMVRLQEVFKTFYLGKHSGRKLQWQTTLGHAVLKADFKEGKK-EFQVSLFQTLVLLMFN-EGDGFS 464
Cdd:pfam00888 480 AWPTYLTSDFILPPELEKAIERFEKFYLSKHSGRKLTWLHSLGTAELKATFPKGKKhELNVSTYQMAILLLFNdDGDSLS 559
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1390157516 465 FEEIKMATGIEDSELRRTLQSLACGKARVLIKSPKGKEVEDGDKFIFNADF 515
Cdd:pfam00888 560 YEEIQEATGLPDEELKRTLQSLACAKAKVLLKEPMSKDINPTDTFSFNEDF 610
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
543-608 8.92e-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: 100.31  E-value: 8.92e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390157516  543 VFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLK--FPVKPGDLKKRIESLIDRDYMERDKDSPN 608
Cdd:smart00884   1 VEEDRKLEIQAAIVRIMKSRKTLSHSELVSEVIEQLKkrFKPSVSDIKKRIESLIEREYLERDEDDPN 68
 
Name Accession Description Interval E-value
Cullin pfam00888
Cullin family;
1-515 0e+00

Cullin family;


Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 693.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516   1 MIMIRSIFLFLDRTYVlqnSMLPSIWDMGLELFRNHIISDRmVQSKTIDGILLLIGRERSGEAVDRSLL-------RSLL 73
Cdd:pfam00888  84 MKMIRDIFMYLDRVYV---KRLPSIYDLGLELFRDHVFRIP-LKDKLIDALLDLIEKERNGEVIDRSLIksvidmlVSLG 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516  74 SMLSDLQVYKDSFELKFLEETNCLYAAEGQRLMQDREVPEYLNHVSKRLEEEADRVITYLDHSTQKPLIACVEKQLLGEH 153
Cdd:pfam00888 160 EDEKKDNVYEEDFEPPFLEATEEYYRAESQELLAENVAPEYLKKAERRLEEEEERVRHYLHSSTKKKLLDVLEEVLISDH 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 154 LTAILQKGLEHLLDENRVPDLTQMYQLFSRVKGGQHALLQHWSEYIKTFGTTIVIN----PEKDKDMVQDLLDFKDKVDH 229
Cdd:pfam00888 240 LEELLEEELQNLLDDNKTEDLKRLYRLLSRVPDGLEPLRKAFEEYIKKEGKAIVKDakeqTTDAKKYVEDLLELKDKFDK 319
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 230 VVEVCFQRNERFINLMKESFETFINK--RPNKPAELIAKHVDSKLRAGNKEATDEELERILDKIMILFRFIHGKDVFEAF 307
Cdd:pfam00888 320 IVKDAFSNDELFVKALDEAFEEFINKntSNSKSPELLAKYIDDLLKKGLKGKSEEELEEKLDKVITLFRYIQDKDVFEAF 399
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 308 YKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQHMQNQSAPG-PIDLTVNILTMG 386
Cdd:pfam00888 400 YKKHLAKRLLLGKSASDDAERSMISKLKEECGSEFTSKLEGMFKDMELSKDLMKEFKEHLSENKSSKkGIDLSVNVLTSG 479
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 387 YWPTYTPMEVHLPPEMVRLQEVFKTFYLGKHSGRKLQWQTTLGHAVLKADFKEGKK-EFQVSLFQTLVLLMFN-EGDGFS 464
Cdd:pfam00888 480 AWPTYLTSDFILPPELEKAIERFEKFYLSKHSGRKLTWLHSLGTAELKATFPKGKKhELNVSTYQMAILLLFNdDGDSLS 559
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1390157516 465 FEEIKMATGIEDSELRRTLQSLACGKARVLIKSPKGKEVEDGDKFIFNADF 515
Cdd:pfam00888 560 YEEIQEATGLPDEELKRTLQSLACAKAKVLLKEPMSKDINPTDTFSFNEDF 610
COG5647 COG5647
Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
1-614 6.50e-138

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


Pssm-ID: 227934 [Multi-domain]  Cd Length: 773  Bit Score: 420.36  E-value: 6.50e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516   1 MIMIRSIFLFLDRTYVLQNSMLPS-IWDMG-LELFRNHIISDRMVQSKTIDGILLLIGRERSGEAVD-----------RS 67
Cdd:COG5647   124 ATMINHLFLYMDRVYLKKARYDKTlVFEVYsLCLVKEKIESFRLIVDSLINPLLYYVERYRALQSIDrkyiedakdmlES 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516  68 LLRSLLSMLSDLQVYKDSFELKFLEETNCLYAAEGQRLMQDREVPEYLNHVSKRLEEEADRVITYLDHSTQKPLIACVEK 147
Cdd:COG5647   204 LERPSDYKKENLSYYKSVFEPIFLEETWEFYEMESSEVIELLSVTEYLEKAHKILEREEELVEIYLKVSTKKPLLEVLED 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 148 QLLGEHLTAILQKGLE--HLLDENRVPDLTQMYQLFSRVKGGQHALLQHWSEYIKTFGTTIVI----------------- 208
Cdd:COG5647   284 VLITRHLDDLEEQGSGfrEALDASNLEKLQVLYRLLSETKYGVQPLQEVFERYVKDEGVLINIetnyifhckvdvgflgs 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 209 NPEKDKDMVQDLLDFKDKVDHVVEVCFQRNERFINLMKESFETFINK---RPNKPAELIAKHVDSKLRAGNKEATDEELE 285
Cdd:COG5647   364 RECLPKLYVQKLLSCHDLFPSLVNESFEGDGSIVKALGNAFKTFINGnesADSGPSEYLAKYIDGLLKKDGKQSFIGKIK 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 286 RILDKIMILFRFIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQ 365
Cdd:COG5647   444 DLLQDIITLFRYVEEKDVFEKYYKKLLAKRLLNGRSASAQAELKMISMLKKVCGQEFTSKLEGMFRDISLSSEFTEAFQH 523
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 366 hmQNQSAPGPIDLTVNILTMGYWPT-YTPMEVHLPPEMVRLQEVFKTFYLGKHSGRKLQWQTTLGHAVLKADFKEGKKE- 443
Cdd:COG5647   524 --SPQSYNKYLDLFVWVLTQAYWPLsPEEVSIRLPKELVPILEGFKKFYSSKHNGRKLKWYWHLGSGEVKARFNEGQKYl 601
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 444 --FQVSLFQTLVLLMFNEGDGFSFEEIKMATGIEDSELRRTLQSLACGKARVLIKspKGKEVEDGDKFIFNADFKHKLFR 521
Cdd:COG5647   602 eiSTFSVYQLLVFLLFNDHEELTFEEILELTKLSTDDLKRVLQSLSCAKLVVLLK--DDKLVSPNTKFYVNENFSSKLER 679
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 522 IKINQIQMKETVEEQVSTTERVFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLK--FPVKPGDLKKRIESLIDRDY 599
Cdd:COG5647   680 IKINYIAESECMQDNLDTHETVEEDRQAELQACIVRIMKARKKLKHGDLVKEVIAQHKsrFEPKVSMVKRAIETLIEKEY 759
                         650
                  ....*....|....*
gi 1390157516 600 MERDKDSpNQYHYVA 614
Cdd:COG5647   760 LERQADD-EIYVYLA 773
CULLIN smart00182
Cullin;
297-437 4.00e-57

Cullin;


Pssm-ID: 214545 [Multi-domain]  Cd Length: 143  Bit Score: 189.07  E-value: 4.00e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516  297 FIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQHMQNQ-SAPGP 375
Cdd:smart00182   1 YIQDKDVFEKYYKKHLAKRLILNRSASDDAEENMITKLKQECGYEFTSKLERMFRDISLSKDLNQSFKDMLENNpSAKPI 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390157516  376 IDLTVNILTMGYWPTY-TPMEVHLPPEMVRLQEVFKTFYLGKHSGRKLQWQTTLGHAVLKADF 437
Cdd:smart00182  81 IDLNVRVLTSGYWPTSsTEVEINLPQELEDALEEFEEFYLAKHSGRKLTWLHSLGRGEVKANF 143
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
543-608 8.92e-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: 100.31  E-value: 8.92e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390157516  543 VFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLK--FPVKPGDLKKRIESLIDRDYMERDKDSPN 608
Cdd:smart00884   1 VEEDRKLEIQAAIVRIMKSRKTLSHSELVSEVIEQLKkrFKPSVSDIKKRIESLIEREYLERDEDDPN 68
Cullin_Nedd8 pfam10557
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
546-606 1.71e-25

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: 99.45  E-value: 1.71e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390157516 546 DRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLK--FPVKPGDLKKRIESLIDRDYMERDKDS 606
Cdd:pfam10557   1 DRKHEIQAAIVRIMKSRKTLSHNELVNEVIEQLKsrFKPSVSDIKKRIESLIEKEYLERDEDD 63
 
Name Accession Description Interval E-value
Cullin pfam00888
Cullin family;
1-515 0e+00

Cullin family;


Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 693.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516   1 MIMIRSIFLFLDRTYVlqnSMLPSIWDMGLELFRNHIISDRmVQSKTIDGILLLIGRERSGEAVDRSLL-------RSLL 73
Cdd:pfam00888  84 MKMIRDIFMYLDRVYV---KRLPSIYDLGLELFRDHVFRIP-LKDKLIDALLDLIEKERNGEVIDRSLIksvidmlVSLG 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516  74 SMLSDLQVYKDSFELKFLEETNCLYAAEGQRLMQDREVPEYLNHVSKRLEEEADRVITYLDHSTQKPLIACVEKQLLGEH 153
Cdd:pfam00888 160 EDEKKDNVYEEDFEPPFLEATEEYYRAESQELLAENVAPEYLKKAERRLEEEEERVRHYLHSSTKKKLLDVLEEVLISDH 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 154 LTAILQKGLEHLLDENRVPDLTQMYQLFSRVKGGQHALLQHWSEYIKTFGTTIVIN----PEKDKDMVQDLLDFKDKVDH 229
Cdd:pfam00888 240 LEELLEEELQNLLDDNKTEDLKRLYRLLSRVPDGLEPLRKAFEEYIKKEGKAIVKDakeqTTDAKKYVEDLLELKDKFDK 319
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 230 VVEVCFQRNERFINLMKESFETFINK--RPNKPAELIAKHVDSKLRAGNKEATDEELERILDKIMILFRFIHGKDVFEAF 307
Cdd:pfam00888 320 IVKDAFSNDELFVKALDEAFEEFINKntSNSKSPELLAKYIDDLLKKGLKGKSEEELEEKLDKVITLFRYIQDKDVFEAF 399
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 308 YKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQHMQNQSAPG-PIDLTVNILTMG 386
Cdd:pfam00888 400 YKKHLAKRLLLGKSASDDAERSMISKLKEECGSEFTSKLEGMFKDMELSKDLMKEFKEHLSENKSSKkGIDLSVNVLTSG 479
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 387 YWPTYTPMEVHLPPEMVRLQEVFKTFYLGKHSGRKLQWQTTLGHAVLKADFKEGKK-EFQVSLFQTLVLLMFN-EGDGFS 464
Cdd:pfam00888 480 AWPTYLTSDFILPPELEKAIERFEKFYLSKHSGRKLTWLHSLGTAELKATFPKGKKhELNVSTYQMAILLLFNdDGDSLS 559
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1390157516 465 FEEIKMATGIEDSELRRTLQSLACGKARVLIKSPKGKEVEDGDKFIFNADF 515
Cdd:pfam00888 560 YEEIQEATGLPDEELKRTLQSLACAKAKVLLKEPMSKDINPTDTFSFNEDF 610
COG5647 COG5647
Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
1-614 6.50e-138

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


Pssm-ID: 227934 [Multi-domain]  Cd Length: 773  Bit Score: 420.36  E-value: 6.50e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516   1 MIMIRSIFLFLDRTYVLQNSMLPS-IWDMG-LELFRNHIISDRMVQSKTIDGILLLIGRERSGEAVD-----------RS 67
Cdd:COG5647   124 ATMINHLFLYMDRVYLKKARYDKTlVFEVYsLCLVKEKIESFRLIVDSLINPLLYYVERYRALQSIDrkyiedakdmlES 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516  68 LLRSLLSMLSDLQVYKDSFELKFLEETNCLYAAEGQRLMQDREVPEYLNHVSKRLEEEADRVITYLDHSTQKPLIACVEK 147
Cdd:COG5647   204 LERPSDYKKENLSYYKSVFEPIFLEETWEFYEMESSEVIELLSVTEYLEKAHKILEREEELVEIYLKVSTKKPLLEVLED 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 148 QLLGEHLTAILQKGLE--HLLDENRVPDLTQMYQLFSRVKGGQHALLQHWSEYIKTFGTTIVI----------------- 208
Cdd:COG5647   284 VLITRHLDDLEEQGSGfrEALDASNLEKLQVLYRLLSETKYGVQPLQEVFERYVKDEGVLINIetnyifhckvdvgflgs 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 209 NPEKDKDMVQDLLDFKDKVDHVVEVCFQRNERFINLMKESFETFINK---RPNKPAELIAKHVDSKLRAGNKEATDEELE 285
Cdd:COG5647   364 RECLPKLYVQKLLSCHDLFPSLVNESFEGDGSIVKALGNAFKTFINGnesADSGPSEYLAKYIDGLLKKDGKQSFIGKIK 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 286 RILDKIMILFRFIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQ 365
Cdd:COG5647   444 DLLQDIITLFRYVEEKDVFEKYYKKLLAKRLLNGRSASAQAELKMISMLKKVCGQEFTSKLEGMFRDISLSSEFTEAFQH 523
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 366 hmQNQSAPGPIDLTVNILTMGYWPT-YTPMEVHLPPEMVRLQEVFKTFYLGKHSGRKLQWQTTLGHAVLKADFKEGKKE- 443
Cdd:COG5647   524 --SPQSYNKYLDLFVWVLTQAYWPLsPEEVSIRLPKELVPILEGFKKFYSSKHNGRKLKWYWHLGSGEVKARFNEGQKYl 601
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 444 --FQVSLFQTLVLLMFNEGDGFSFEEIKMATGIEDSELRRTLQSLACGKARVLIKspKGKEVEDGDKFIFNADFKHKLFR 521
Cdd:COG5647   602 eiSTFSVYQLLVFLLFNDHEELTFEEILELTKLSTDDLKRVLQSLSCAKLVVLLK--DDKLVSPNTKFYVNENFSSKLER 679
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516 522 IKINQIQMKETVEEQVSTTERVFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLK--FPVKPGDLKKRIESLIDRDY 599
Cdd:COG5647   680 IKINYIAESECMQDNLDTHETVEEDRQAELQACIVRIMKARKKLKHGDLVKEVIAQHKsrFEPKVSMVKRAIETLIEKEY 759
                         650
                  ....*....|....*
gi 1390157516 600 MERDKDSpNQYHYVA 614
Cdd:COG5647   760 LERQADD-EIYVYLA 773
CULLIN smart00182
Cullin;
297-437 4.00e-57

Cullin;


Pssm-ID: 214545 [Multi-domain]  Cd Length: 143  Bit Score: 189.07  E-value: 4.00e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157516  297 FIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQHMQNQ-SAPGP 375
Cdd:smart00182   1 YIQDKDVFEKYYKKHLAKRLILNRSASDDAEENMITKLKQECGYEFTSKLERMFRDISLSKDLNQSFKDMLENNpSAKPI 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390157516  376 IDLTVNILTMGYWPTY-TPMEVHLPPEMVRLQEVFKTFYLGKHSGRKLQWQTTLGHAVLKADF 437
Cdd:smart00182  81 IDLNVRVLTSGYWPTSsTEVEINLPQELEDALEEFEEFYLAKHSGRKLTWLHSLGRGEVKANF 143
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
543-608 8.92e-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: 100.31  E-value: 8.92e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390157516  543 VFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLK--FPVKPGDLKKRIESLIDRDYMERDKDSPN 608
Cdd:smart00884   1 VEEDRKLEIQAAIVRIMKSRKTLSHSELVSEVIEQLKkrFKPSVSDIKKRIESLIEREYLERDEDDPN 68
Cullin_Nedd8 pfam10557
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
546-606 1.71e-25

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: 99.45  E-value: 1.71e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390157516 546 DRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLK--FPVKPGDLKKRIESLIDRDYMERDKDS 606
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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