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Conserved domains on  [gi|459369447|gb|EMG47832|]
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Cullin-family protein, putative [Candida maltosa Xu316]

Protein Classification

cullin( domain architecture ID 12011692)

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;
84-703 9.15e-49

Cullin family;


:

Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 182.37  E-value: 9.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447   84 STIDTILDGNLPPHSLGYLnlqFT---KLCKYKHieQSKLSDIINDKISSDFTTNIKPKIIDIFQQDDLqtcvLNFL-EL 159
Cdd:pfam00888   6 DAIDEILNKNVSSLSYEEL---YRavyNLCLHKQ--GEKLYDKLKEYLEEHLKKLVKPLIKEASSGEEF----LKAYvKE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  160 FDTWFDKLVLLHNAFIYLDTMYLKNhsvRPTILKFSMSLFIEQVF--ENDKELTRTIFSryeqLLRLWRENAQIrDDNHV 237
Cdd:pfam00888  77 WEDHTISMKMIRDIFMYLDRVYVKR---LPSIYDLGLELFRDHVFriPLKDKLIDALLD----LIEKERNGEVI-DRSLI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  238 ED--SQLYDLSIRLTKllSQFYEEisslEFETILITSTINLYRVLGDKWLQNNESINYIQQVFKAINENLKFFTNSMKNT 315
Cdd:pfam00888 149 KSviDMLVSLGEDEKK--DNVYEE----DFEPPFLEATEEYYRAESQELLAENVAPEYLKKAERRLEEEEERVRHYLHSS 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  316 SfIKKLFDKLRWQLIFIDFNNLLPRILPFLLDNPK--ELSIIYNYCVHTEDqyGLDSIAILVYQWglfTKKVFEDVIANN 393
Cdd:pfam00888 223 T-KKKLLDVLEEVLISDHLEELLEEELQNLLDDNKteDLKRLYRLLSRVPD--GLEPLRKAFEEY---IKKEGKAIVKDA 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  394 KQKKTV-NLIIGELVDKFKHFKRLIDTNFSSDR-FEFELRNSLIKTINGQTNNNS---LLiyqlCKYCDNF----YKKKS 464
Cdd:pfam00888 297 KEQTTDaKKYVEDLLELKDKFDKIVKDAFSNDElFVKALDEAFEEFINKNTSNSKspeLL----AKYIDDLlkkgLKGKS 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  465 DISITDFEDNVLIIFKAINNKQDFINFYKKDLSKRLFFNVKFNFDGEQKLASKLNEVIGS--TDeaiSINTMFQDLTISK 542
Cdd:pfam00888 373 EEELEEKLDKVITLFRYIQDKDVFEAFYKKHLAKRLLLGKSASDDAERSMISKLKEECGSefTS---KLEGMFKDMELSK 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  543 EI---YKPLMAKNSVSSDllsrSFEFNPLILDKRQWPEIPNnedlSELKIPPMLQSLLDQMSNEYKQldpKYKSRQLDWt 619
Cdd:pfam00888 450 DLmkeFKEHLSENKSSKK----GIDLSVNVLTSGAWPTYLT----SDFILPPELEKAIERFEKFYLS---KHSGRKLTW- 517
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  620 NYKLHQITISASFQQGTK-EITGNLLQIMVILLFDDNDCGFNVDELVEKTGINENFLLKILNSISTDKYNIIVSHQGK-- 696
Cdd:pfam00888 518 LHSLGTAELKATFPKGKKhELNVSTYQMAILLLFNDDGDSLSYEEIQEATGLPDEELKRTLQSLACAKAKVLLKEPMSkd 597
                         650
                  ....*....|...
gi 459369447  697 ------YYFNNEF 703
Cdd:pfam00888 598 inptdtFSFNEDF 610
Cullin_Nedd8 pfam10557
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
739-801 4.66e-13

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: 64.39  E-value: 4.66e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 459369447  739 NRDEEFKSCVIKIMKQERELNIVNLLNQSIAMLERRQPVNITNLKTIVENLIQMEFLKRDDNN 801
Cdd:pfam10557   1 DRKHEIQAAIVRIMKSRKTLSHNELVNEVIEQLKSRFKPSVSDIKKRIESLIEKEYLERDEDD 63
 
Name Accession Description Interval E-value
Cullin pfam00888
Cullin family;
84-703 9.15e-49

Cullin family;


Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 182.37  E-value: 9.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447   84 STIDTILDGNLPPHSLGYLnlqFT---KLCKYKHieQSKLSDIINDKISSDFTTNIKPKIIDIFQQDDLqtcvLNFL-EL 159
Cdd:pfam00888   6 DAIDEILNKNVSSLSYEEL---YRavyNLCLHKQ--GEKLYDKLKEYLEEHLKKLVKPLIKEASSGEEF----LKAYvKE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  160 FDTWFDKLVLLHNAFIYLDTMYLKNhsvRPTILKFSMSLFIEQVF--ENDKELTRTIFSryeqLLRLWRENAQIrDDNHV 237
Cdd:pfam00888  77 WEDHTISMKMIRDIFMYLDRVYVKR---LPSIYDLGLELFRDHVFriPLKDKLIDALLD----LIEKERNGEVI-DRSLI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  238 ED--SQLYDLSIRLTKllSQFYEEisslEFETILITSTINLYRVLGDKWLQNNESINYIQQVFKAINENLKFFTNSMKNT 315
Cdd:pfam00888 149 KSviDMLVSLGEDEKK--DNVYEE----DFEPPFLEATEEYYRAESQELLAENVAPEYLKKAERRLEEEEERVRHYLHSS 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  316 SfIKKLFDKLRWQLIFIDFNNLLPRILPFLLDNPK--ELSIIYNYCVHTEDqyGLDSIAILVYQWglfTKKVFEDVIANN 393
Cdd:pfam00888 223 T-KKKLLDVLEEVLISDHLEELLEEELQNLLDDNKteDLKRLYRLLSRVPD--GLEPLRKAFEEY---IKKEGKAIVKDA 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  394 KQKKTV-NLIIGELVDKFKHFKRLIDTNFSSDR-FEFELRNSLIKTINGQTNNNS---LLiyqlCKYCDNF----YKKKS 464
Cdd:pfam00888 297 KEQTTDaKKYVEDLLELKDKFDKIVKDAFSNDElFVKALDEAFEEFINKNTSNSKspeLL----AKYIDDLlkkgLKGKS 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  465 DISITDFEDNVLIIFKAINNKQDFINFYKKDLSKRLFFNVKFNFDGEQKLASKLNEVIGS--TDeaiSINTMFQDLTISK 542
Cdd:pfam00888 373 EEELEEKLDKVITLFRYIQDKDVFEAFYKKHLAKRLLLGKSASDDAERSMISKLKEECGSefTS---KLEGMFKDMELSK 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  543 EI---YKPLMAKNSVSSDllsrSFEFNPLILDKRQWPEIPNnedlSELKIPPMLQSLLDQMSNEYKQldpKYKSRQLDWt 619
Cdd:pfam00888 450 DLmkeFKEHLSENKSSKK----GIDLSVNVLTSGAWPTYLT----SDFILPPELEKAIERFEKFYLS---KHSGRKLTW- 517
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  620 NYKLHQITISASFQQGTK-EITGNLLQIMVILLFDDNDCGFNVDELVEKTGINENFLLKILNSISTDKYNIIVSHQGK-- 696
Cdd:pfam00888 518 LHSLGTAELKATFPKGKKhELNVSTYQMAILLLFNDDGDSLSYEEIQEATGLPDEELKRTLQSLACAKAKVLLKEPMSkd 597
                         650
                  ....*....|...
gi 459369447  697 ------YYFNNEF 703
Cdd:pfam00888 598 inptdtFSFNEDF 610
COG5647 COG5647
Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
169-808 2.65e-42

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


Pssm-ID: 227934 [Multi-domain]  Cd Length: 773  Bit Score: 165.36  E-value: 2.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 169 LLHNAFIYLDTMYLKN--HSVRPTILKFSMSLF---IEQVFENDKELTRTIFSRYEQLlrlwrENAQIRDDNHVED--SQ 241
Cdd:COG5647  126 MINHLFLYMDRVYLKKarYDKTLVFEVYSLCLVkekIESFRLIVDSLINPLLYYVERY-----RALQSIDRKYIEDakDM 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 242 LYDLSIR--LTKLLSQFYEEIssleFETILITSTINLYRVLGDKWLQNNESINYIQQVFKAINENLKFFTNSMkNTSFIK 319
Cdd:COG5647  201 LESLERPsdYKKENLSYYKSV----FEPIFLEETWEFYEMESSEVIELLSVTEYLEKAHKILEREEELVEIYL-KVSTKK 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 320 KLFDKLRWQLIFIDFNNLLPRILPF--LLD--NPKELSIIYNYcvHTEDQYGldsIAILVYQWGLFTKK--VFEDVIANN 393
Cdd:COG5647  276 PLLEVLEDVLITRHLDDLEEQGSGFreALDasNLEKLQVLYRL--LSETKYG---VQPLQEVFERYVKDegVLINIETNY 350
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 394 KQKKTVNLIIG---ELVDK---------FKHFKRLIDTNFSSDR-FEFELRNSLIKTINGQTNNNSLLIYQLCKYCDNFY 460
Cdd:COG5647  351 IFHCKVDVGFLgsrECLPKlyvqkllscHDLFPSLVNESFEGDGsIVKALGNAFKTFINGNESADSGPSEYLAKYIDGLL 430
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 461 K---KKSDI-SITDFEDNVLIIFKAINNKQDFINFYKKDLSKRLFFNVKFNFDGEQKLASKLNEVIGsTDEAISINTMFQ 536
Cdd:COG5647  431 KkdgKQSFIgKIKDLLQDIITLFRYVEEKDVFEKYYKKLLAKRLLNGRSASAQAELKMISMLKKVCG-QEFTSKLEGMFR 509
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 537 DLTISKEIYKPLmaKNSVSSDLLSRSfeFNPLILDKRQWPEIPNNEdlsELKIPPMLQSLLDQMSNEYkqlDPKYKSRQL 616
Cdd:COG5647  510 DISLSSEFTEAF--QHSPQSYNKYLD--LFVWVLTQAYWPLSPEEV---SIRLPKELVPILEGFKKFY---SSKHNGRKL 579
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 617 DWTnYKLHQITISASFQQGTKEI---TGNLLQIMVILLFDDNDCgFNVDELVEKTGINENFLLKILNSISTDKYNIIV-- 691
Cdd:COG5647  580 KWY-WHLGSGEVKARFNEGQKYLeisTFSVYQLLVFLLFNDHEE-LTFEEILELTKLSTDDLKRVLQSLSCAKLVVLLkd 657
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 692 ----SHQGKYYFNNEFTDKSTKIKLPMIKESSVRVDS--NQKEQDEltsniqtNRDEEFKSCVIKIMKQERELNIVNLLN 765
Cdd:COG5647  658 dklvSPNTKFYVNENFSSKLERIKINYIAESECMQDNldTHETVEE-------DRQAELQACIVRIMKARKKLKHGDLVK 730
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|...
gi 459369447 766 QSIAMLERRQPVNITNLKTIVENLIQMEFLKRDDNNKdviIYI 808
Cdd:COG5647  731 EVIAQHKSRFEPKVSMVKRAIETLIEKEYLERQADDE---IYV 770
Cullin_Nedd8 pfam10557
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
739-801 4.66e-13

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: 64.39  E-value: 4.66e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 459369447  739 NRDEEFKSCVIKIMKQERELNIVNLLNQSIAMLERRQPVNITNLKTIVENLIQMEFLKRDDNN 801
Cdd:pfam10557   1 DRKHEIQAAIVRIMKSRKTLSHNELVNEVIEQLKSRFKPSVSDIKKRIESLIEKEYLERDEDD 63
CULLIN smart00182
Cullin;
482-632 1.60e-12

Cullin;


Pssm-ID: 214545 [Multi-domain]  Cd Length: 143  Bit Score: 65.42  E-value: 1.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447   482 INNKQDFINFYKKDLSKRLFFNVKFNFDGEQKLASKLNEVIGStDEAISINTMFQDLTISKEIYKpLMAKNSVSSDLLSR 561
Cdd:smart00182   2 IQDKDVFEKYYKKHLAKRLILNRSASDDAEENMITKLKQECGY-EFTSKLERMFRDISLSKDLNQ-SFKDMLENNPSAKP 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 459369447   562 SFEFNPLILDKRQWPEIPNNedlSELKIPPMLQSLLDQMSNEYKQldpKYKSRQLDWTnYKLHQITISASF 632
Cdd:smart00182  80 IIDLNVRVLTSGYWPTSSTE---VEINLPQELEDALEEFEEFYLA---KHSGRKLTWL-HSLGRGEVKANF 143
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
736-803 3.24e-09

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: 53.70  E-value: 3.24e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 459369447   736 IQTNRDEEFKSCVIKIMKQERELNIVNLLNQSIAMLERRQPVNITNLKTIVENLIQMEFLKRDDNNKD 803
Cdd:smart00884   1 VEEDRKLEIQAAIVRIMKSRKTLSHSELVSEVIEQLKKRFKPSVSDIKKRIESLIEREYLERDEDDPN 68
 
Name Accession Description Interval E-value
Cullin pfam00888
Cullin family;
84-703 9.15e-49

Cullin family;


Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 182.37  E-value: 9.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447   84 STIDTILDGNLPPHSLGYLnlqFT---KLCKYKHieQSKLSDIINDKISSDFTTNIKPKIIDIFQQDDLqtcvLNFL-EL 159
Cdd:pfam00888   6 DAIDEILNKNVSSLSYEEL---YRavyNLCLHKQ--GEKLYDKLKEYLEEHLKKLVKPLIKEASSGEEF----LKAYvKE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  160 FDTWFDKLVLLHNAFIYLDTMYLKNhsvRPTILKFSMSLFIEQVF--ENDKELTRTIFSryeqLLRLWRENAQIrDDNHV 237
Cdd:pfam00888  77 WEDHTISMKMIRDIFMYLDRVYVKR---LPSIYDLGLELFRDHVFriPLKDKLIDALLD----LIEKERNGEVI-DRSLI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  238 ED--SQLYDLSIRLTKllSQFYEEisslEFETILITSTINLYRVLGDKWLQNNESINYIQQVFKAINENLKFFTNSMKNT 315
Cdd:pfam00888 149 KSviDMLVSLGEDEKK--DNVYEE----DFEPPFLEATEEYYRAESQELLAENVAPEYLKKAERRLEEEEERVRHYLHSS 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  316 SfIKKLFDKLRWQLIFIDFNNLLPRILPFLLDNPK--ELSIIYNYCVHTEDqyGLDSIAILVYQWglfTKKVFEDVIANN 393
Cdd:pfam00888 223 T-KKKLLDVLEEVLISDHLEELLEEELQNLLDDNKteDLKRLYRLLSRVPD--GLEPLRKAFEEY---IKKEGKAIVKDA 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  394 KQKKTV-NLIIGELVDKFKHFKRLIDTNFSSDR-FEFELRNSLIKTINGQTNNNS---LLiyqlCKYCDNF----YKKKS 464
Cdd:pfam00888 297 KEQTTDaKKYVEDLLELKDKFDKIVKDAFSNDElFVKALDEAFEEFINKNTSNSKspeLL----AKYIDDLlkkgLKGKS 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  465 DISITDFEDNVLIIFKAINNKQDFINFYKKDLSKRLFFNVKFNFDGEQKLASKLNEVIGS--TDeaiSINTMFQDLTISK 542
Cdd:pfam00888 373 EEELEEKLDKVITLFRYIQDKDVFEAFYKKHLAKRLLLGKSASDDAERSMISKLKEECGSefTS---KLEGMFKDMELSK 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  543 EI---YKPLMAKNSVSSDllsrSFEFNPLILDKRQWPEIPNnedlSELKIPPMLQSLLDQMSNEYKQldpKYKSRQLDWt 619
Cdd:pfam00888 450 DLmkeFKEHLSENKSSKK----GIDLSVNVLTSGAWPTYLT----SDFILPPELEKAIERFEKFYLS---KHSGRKLTW- 517
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447  620 NYKLHQITISASFQQGTK-EITGNLLQIMVILLFDDNDCGFNVDELVEKTGINENFLLKILNSISTDKYNIIVSHQGK-- 696
Cdd:pfam00888 518 LHSLGTAELKATFPKGKKhELNVSTYQMAILLLFNDDGDSLSYEEIQEATGLPDEELKRTLQSLACAKAKVLLKEPMSkd 597
                         650
                  ....*....|...
gi 459369447  697 ------YYFNNEF 703
Cdd:pfam00888 598 inptdtFSFNEDF 610
COG5647 COG5647
Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
169-808 2.65e-42

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


Pssm-ID: 227934 [Multi-domain]  Cd Length: 773  Bit Score: 165.36  E-value: 2.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 169 LLHNAFIYLDTMYLKN--HSVRPTILKFSMSLF---IEQVFENDKELTRTIFSRYEQLlrlwrENAQIRDDNHVED--SQ 241
Cdd:COG5647  126 MINHLFLYMDRVYLKKarYDKTLVFEVYSLCLVkekIESFRLIVDSLINPLLYYVERY-----RALQSIDRKYIEDakDM 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 242 LYDLSIR--LTKLLSQFYEEIssleFETILITSTINLYRVLGDKWLQNNESINYIQQVFKAINENLKFFTNSMkNTSFIK 319
Cdd:COG5647  201 LESLERPsdYKKENLSYYKSV----FEPIFLEETWEFYEMESSEVIELLSVTEYLEKAHKILEREEELVEIYL-KVSTKK 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 320 KLFDKLRWQLIFIDFNNLLPRILPF--LLD--NPKELSIIYNYcvHTEDQYGldsIAILVYQWGLFTKK--VFEDVIANN 393
Cdd:COG5647  276 PLLEVLEDVLITRHLDDLEEQGSGFreALDasNLEKLQVLYRL--LSETKYG---VQPLQEVFERYVKDegVLINIETNY 350
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 394 KQKKTVNLIIG---ELVDK---------FKHFKRLIDTNFSSDR-FEFELRNSLIKTINGQTNNNSLLIYQLCKYCDNFY 460
Cdd:COG5647  351 IFHCKVDVGFLgsrECLPKlyvqkllscHDLFPSLVNESFEGDGsIVKALGNAFKTFINGNESADSGPSEYLAKYIDGLL 430
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 461 K---KKSDI-SITDFEDNVLIIFKAINNKQDFINFYKKDLSKRLFFNVKFNFDGEQKLASKLNEVIGsTDEAISINTMFQ 536
Cdd:COG5647  431 KkdgKQSFIgKIKDLLQDIITLFRYVEEKDVFEKYYKKLLAKRLLNGRSASAQAELKMISMLKKVCG-QEFTSKLEGMFR 509
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 537 DLTISKEIYKPLmaKNSVSSDLLSRSfeFNPLILDKRQWPEIPNNEdlsELKIPPMLQSLLDQMSNEYkqlDPKYKSRQL 616
Cdd:COG5647  510 DISLSSEFTEAF--QHSPQSYNKYLD--LFVWVLTQAYWPLSPEEV---SIRLPKELVPILEGFKKFY---SSKHNGRKL 579
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 617 DWTnYKLHQITISASFQQGTKEI---TGNLLQIMVILLFDDNDCgFNVDELVEKTGINENFLLKILNSISTDKYNIIV-- 691
Cdd:COG5647  580 KWY-WHLGSGEVKARFNEGQKYLeisTFSVYQLLVFLLFNDHEE-LTFEEILELTKLSTDDLKRVLQSLSCAKLVVLLkd 657
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447 692 ----SHQGKYYFNNEFTDKSTKIKLPMIKESSVRVDS--NQKEQDEltsniqtNRDEEFKSCVIKIMKQERELNIVNLLN 765
Cdd:COG5647  658 dklvSPNTKFYVNENFSSKLERIKINYIAESECMQDNldTHETVEE-------DRQAELQACIVRIMKARKKLKHGDLVK 730
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|...
gi 459369447 766 QSIAMLERRQPVNITNLKTIVENLIQMEFLKRDDNNKdviIYI 808
Cdd:COG5647  731 EVIAQHKSRFEPKVSMVKRAIETLIEKEYLERQADDE---IYV 770
Cullin_Nedd8 pfam10557
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
739-801 4.66e-13

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: 64.39  E-value: 4.66e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 459369447  739 NRDEEFKSCVIKIMKQERELNIVNLLNQSIAMLERRQPVNITNLKTIVENLIQMEFLKRDDNN 801
Cdd:pfam10557   1 DRKHEIQAAIVRIMKSRKTLSHNELVNEVIEQLKSRFKPSVSDIKKRIESLIEKEYLERDEDD 63
CULLIN smart00182
Cullin;
482-632 1.60e-12

Cullin;


Pssm-ID: 214545 [Multi-domain]  Cd Length: 143  Bit Score: 65.42  E-value: 1.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459369447   482 INNKQDFINFYKKDLSKRLFFNVKFNFDGEQKLASKLNEVIGStDEAISINTMFQDLTISKEIYKpLMAKNSVSSDLLSR 561
Cdd:smart00182   2 IQDKDVFEKYYKKHLAKRLILNRSASDDAEENMITKLKQECGY-EFTSKLERMFRDISLSKDLNQ-SFKDMLENNPSAKP 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 459369447   562 SFEFNPLILDKRQWPEIPNNedlSELKIPPMLQSLLDQMSNEYKQldpKYKSRQLDWTnYKLHQITISASF 632
Cdd:smart00182  80 IIDLNVRVLTSGYWPTSSTE---VEINLPQELEDALEEFEEFYLA---KHSGRKLTWL-HSLGRGEVKANF 143
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
736-803 3.24e-09

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: 53.70  E-value: 3.24e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 459369447   736 IQTNRDEEFKSCVIKIMKQERELNIVNLLNQSIAMLERRQPVNITNLKTIVENLIQMEFLKRDDNNKD 803
Cdd:smart00884   1 VEEDRKLEIQAAIVRIMKSRKTLSHSELVSEVIEQLKKRFKPSVSDIKKRIESLIEREYLERDEDDPN 68
 
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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