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Conserved domains on  [gi|1831604145|ref|XP_033295753|]
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cullin-1-like [Orcinus orca]

Protein Classification

cullin family protein( domain architecture ID 12011692)

cullin family protein, similar to cullins that are core components 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;
21-630 0e+00

Cullin family;


:

Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 612.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145  21 WDDLRAGIQQVYTRQsMVKSRYMELYTHVYNCCTsvhqsnqaqeagvppsksrkgetlegvQLVGLELYKQLKEFLKNYL 100
Cdd:pfam00888   1 WAKLEDAIDEILNKN-VSSLSYEELYRAVYNLCL---------------------------HKQGEKLYDKLKEYLEEHL 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 101 TNLLKD--GEGLLDESVLKFYTQQWEDYRFSSKVLNGICAYLSRYWVlckyyggrKAIYQIYSLALVTWRDCLFR-PLNK 177
Cdd:pfam00888  53 KKLVKPliKEASSGEEFLKAYVKEWEDHTISMKMIRDIFMYLDRVYV--------KRLPSIYDLGLELFRDHVFRiPLKD 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 178 QVTHAVLKLIEKERNGETINTRLMGGIVQSYVELGLNEDDafamgprLKVYKESFESRFLADTERFYTRESTKFLQQNPV 257
Cdd:pfam00888 125 KLIDALLDLIEKERNGEVIDRSLIKSVIDMLVSLGEDEKK-------DNVYEEDFEPPFLEATEEYYRAESQELLAENVA 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 258 TEYMKKAETRLLEEQRRGQ-YLHENTQEELARKCRQVLIEKHLEIFH-GEFQNLLDADKSEDLGRMYNLVSRIQDGLGEL 335
Cdd:pfam00888 198 PEYLKKAERRLEEEEERVRhYLHSSTKKKLLDVLEEVLISDHLEELLeEELQNLLDDNKTEDLKRLYRLLSRVPDGLEPL 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 336 KTLLETHIHNQCiAAIEKCGEAALNDPKMYIQTVLDVHKKYNALVMLAFNNNAGFVAVLDKACGRFINNNavtkmaQSSS 415
Cdd:pfam00888 278 RKAFEEYIKKEG-KAIVKDAKEQTTDAKKYVEDLLELKDKFDKIVKDAFSNDELFVKALDEAFEEFINKN------TSNS 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 416 KSSELLAGYCDSLLKKRSKNPEEAELEDTLNQVIAVFKYIEDRDVFQKFYAKMLAKSLVHQNSASDDAEASMIAKLKQAC 495
Cdd:pfam00888 351 KSPELLAKYIDDLLKKGLKGKSEEELEEKLDKVITLFRYIQDKDVFEAFYKKHLAKRLLLGKSASDDAERSMISKLKEEC 430
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 496 GFEYTSKLQQMFQDIGTSKYLNEWFKKHP--TNSEPLGLDFSIQVLSSGSRPSQQSGTFALPSELERSYQRLTAFYASRH 573
Cdd:pfam00888 431 GSEFTSKLEGMFKDMELSKDLMKEFKEHLseNKSSKKGIDLSVNVLTSGAWPTYLTSDFILPPELEKAIERFEKFYLSKH 510
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831604145 574 SGRKLTWLYQLSEGELVTNCFKNR-YTLQASTFQMAILLRYNTE-DAYAVQQLMDGTQI 630
Cdd:pfam00888 511 SGRKLTWLHSLGTAELKATFPKGKkHELNVSTYQMAILLLFNDDgDSLSYEEIQEATGL 569
Cullin_Nedd8 pfam10557
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
705-767 5.24e-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: 98.29  E-value: 5.24e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831604145 705 DRKLLIQAALVIIMKMRKVLKHQQLLGEVLTQLSSIFKPRIPVIKKCIDVLIAKEYLERVDGE 767
Cdd:pfam10557   1 DRKHEIQAAIVRIMKSRKTLSHNELVNEVIEQLKSRFKPSVSDIKKRIESLIEKEYLERDEDD 63
 
Name Accession Description Interval E-value
Cullin pfam00888
Cullin family;
21-630 0e+00

Cullin family;


Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 612.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145  21 WDDLRAGIQQVYTRQsMVKSRYMELYTHVYNCCTsvhqsnqaqeagvppsksrkgetlegvQLVGLELYKQLKEFLKNYL 100
Cdd:pfam00888   1 WAKLEDAIDEILNKN-VSSLSYEELYRAVYNLCL---------------------------HKQGEKLYDKLKEYLEEHL 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 101 TNLLKD--GEGLLDESVLKFYTQQWEDYRFSSKVLNGICAYLSRYWVlckyyggrKAIYQIYSLALVTWRDCLFR-PLNK 177
Cdd:pfam00888  53 KKLVKPliKEASSGEEFLKAYVKEWEDHTISMKMIRDIFMYLDRVYV--------KRLPSIYDLGLELFRDHVFRiPLKD 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 178 QVTHAVLKLIEKERNGETINTRLMGGIVQSYVELGLNEDDafamgprLKVYKESFESRFLADTERFYTRESTKFLQQNPV 257
Cdd:pfam00888 125 KLIDALLDLIEKERNGEVIDRSLIKSVIDMLVSLGEDEKK-------DNVYEEDFEPPFLEATEEYYRAESQELLAENVA 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 258 TEYMKKAETRLLEEQRRGQ-YLHENTQEELARKCRQVLIEKHLEIFH-GEFQNLLDADKSEDLGRMYNLVSRIQDGLGEL 335
Cdd:pfam00888 198 PEYLKKAERRLEEEEERVRhYLHSSTKKKLLDVLEEVLISDHLEELLeEELQNLLDDNKTEDLKRLYRLLSRVPDGLEPL 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 336 KTLLETHIHNQCiAAIEKCGEAALNDPKMYIQTVLDVHKKYNALVMLAFNNNAGFVAVLDKACGRFINNNavtkmaQSSS 415
Cdd:pfam00888 278 RKAFEEYIKKEG-KAIVKDAKEQTTDAKKYVEDLLELKDKFDKIVKDAFSNDELFVKALDEAFEEFINKN------TSNS 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 416 KSSELLAGYCDSLLKKRSKNPEEAELEDTLNQVIAVFKYIEDRDVFQKFYAKMLAKSLVHQNSASDDAEASMIAKLKQAC 495
Cdd:pfam00888 351 KSPELLAKYIDDLLKKGLKGKSEEELEEKLDKVITLFRYIQDKDVFEAFYKKHLAKRLLLGKSASDDAERSMISKLKEEC 430
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 496 GFEYTSKLQQMFQDIGTSKYLNEWFKKHP--TNSEPLGLDFSIQVLSSGSRPSQQSGTFALPSELERSYQRLTAFYASRH 573
Cdd:pfam00888 431 GSEFTSKLEGMFKDMELSKDLMKEFKEHLseNKSSKKGIDLSVNVLTSGAWPTYLTSDFILPPELEKAIERFEKFYLSKH 510
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831604145 574 SGRKLTWLYQLSEGELVTNCFKNR-YTLQASTFQMAILLRYNTE-DAYAVQQLMDGTQI 630
Cdd:pfam00888 511 SGRKLTWLHSLGTAELKATFPKGKkHELNVSTYQMAILLLFNDDgDSLSYEEIQEATGL 569
COG5647 COG5647
Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
20-773 5.28e-135

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


Pssm-ID: 227934 [Multi-domain]  Cd Length: 773  Bit Score: 418.82  E-value: 5.28e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145  20 TWDDLRAGIQQVYTR--QSMVKSRYMELYTHVYNCCTSVHQSNQaqeagvppSKSRKGETLegvQLVGLELYKQLKEFLK 97
Cdd:COG5647    23 TWEFIERAIGQIFERlyDSMAILSLMEVYTKIYNYCTNKTRSLE--------SDLRWKIDF---IYLGSRLIQKLVDYAK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145  98 NYLTNLLKDGEGLLDESVLKFYTQQWEDYRFSSKVLNGICAYLSRYWVLCKYYGGRKaIYQIYSLALVTWRDCLFRPLNK 177
Cdd:COG5647    92 NYIEEYNRGRSQENMEEFLDELVKFWNRFTKGATMINHLFLYMDRVYLKKARYDKTL-VFEVYSLCLVKEKIESFRLIVD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 178 QVTHAVLKLIEKERNGETINTRLMGGIVQSYVELGLNEDDAfamGPRLKVYKESFESRFLADTERFYTRESTKFLQQNPV 257
Cdd:COG5647   171 SLINPLLYYVERYRALQSIDRKYIEDAKDMLESLERPSDYK---KENLSYYKSVFEPIFLEETWEFYEMESSEVIELLSV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 258 TEYMKKAETRLLEEQRRGQ-YLHENTQEELARKCRQVLIEKHLEIFH---GEFQNLLDADKSEDLGRMYNLVSRIQDGLG 333
Cdd:COG5647   248 TEYLEKAHKILEREEELVEiYLKVSTKKPLLEVLEDVLITRHLDDLEeqgSGFREALDASNLEKLQVLYRLLSETKYGVQ 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 334 ELKTLLE-------------THIHNQCIAAIEKCGEAALnDPKMYIQTVLDVHKKYNALVMLAFNNNAGFVAVLDKACGR 400
Cdd:COG5647   328 PLQEVFEryvkdegvlinieTNYIFHCKVDVGFLGSREC-LPKLYVQKLLSCHDLFPSLVNESFEGDGSIVKALGNAFKT 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 401 FINNNAvtkmaQSSSKSSELLAGYCDSLLKKRSKNPEEAELEDTLNQVIAVFKYIEDRDVFQKFYAKMLAKSLVHQNSAS 480
Cdd:COG5647   407 FINGNE-----SADSGPSEYLAKYIDGLLKKDGKQSFIGKIKDLLQDIITLFRYVEEKDVFEKYYKKLLAKRLLNGRSAS 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 481 DDAEASMIAKLKQACGFEYTSKLQQMFQDIGTSKYLNEWFKKHPTNSEPlGLDFSIQVLSSGSRP-SQQSGTFALPSELE 559
Cdd:COG5647   482 AQAELKMISMLKKVCGQEFTSKLEGMFRDISLSSEFTEAFQHSPQSYNK-YLDLFVWVLTQAYWPlSPEEVSIRLPKELV 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 560 RSYQRLTAFYASRHSGRKLTWLYQLSEGELVTNCFKNRYTLQASTF---QMAILLRYNTEDAYAVQQLMDGTQIKTDIFA 636
Cdd:COG5647   561 PILEGFKKFYSSKHNGRKLKWYWHLGSGEVKARFNEGQKYLEISTFsvyQLLVFLLFNDHEELTFEEILELTKLSTDDLK 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 637 QVLQILLKLKLLVLEDentpvDEMELKQDTLIKLYLGYRNKKLRVNINVPMKMEQKQEQETTHRNIEADRKLLIQAALVI 716
Cdd:COG5647   641 RVLQSLSCAKLVVLLK-----DDKLVSPNTKFYVNENFSSKLERIKINYIAESECMQDNLDTHETVEEDRQAELQACIVR 715
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831604145 717 IMKMRKVLKHQQLLGEVLTQLSSIFKPRIPVIKKCIDVLIAKEYLERVDGEQdTYSY 773
Cdd:COG5647   716 IMKARKKLKHGDLVKEVIAQHKSRFEPKVSMVKRAIETLIEKEYLERQADDE-IYVY 771
CULLIN smart00182
Cullin;
454-589 6.19e-50

Cullin;


Pssm-ID: 214545 [Multi-domain]  Cd Length: 143  Bit Score: 171.73  E-value: 6.19e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145  454 YIEDRDVFQKFYAKMLAKSLVHQNSASDDAEASMIAKLKQACGFEYTSKLQQMFQDIGTSKYLNEWFKKHPTNSEP--LG 531
Cdd:smart00182   1 YIQDKDVFEKYYKKHLAKRLILNRSASDDAEENMITKLKQECGYEFTSKLERMFRDISLSKDLNQSFKDMLENNPSakPI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831604145  532 LDFSIQVLSSGSRPSQQSGT-FALPSELERSYQRLTAFYASRHSGRKLTWLYQLSEGEL 589
Cdd:smart00182  81 IDLNVRVLTSGYWPTSSTEVeINLPQELEDALEEFEEFYLAKHSGRKLTWLHSLGRGEV 139
Cullin_Nedd8 pfam10557
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
705-767 5.24e-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: 98.29  E-value: 5.24e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831604145 705 DRKLLIQAALVIIMKMRKVLKHQQLLGEVLTQLSSIFKPRIPVIKKCIDVLIAKEYLERVDGE 767
Cdd:pfam10557   1 DRKHEIQAAIVRIMKSRKTLSHNELVNEVIEQLKSRFKPSVSDIKKRIESLIEKEYLERDEDD 63
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
702-769 2.74e-23

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: 93.76  E-value: 2.74e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831604145  702 IEADRKLLIQAALVIIMKMRKVLKHQQLLGEVLTQLSSIFKPRIPVIKKCIDVLIAKEYLERVDGEQD 769
Cdd:smart00884   1 VEEDRKLEIQAAIVRIMKSRKTLSHSELVSEVIEQLKKRFKPSVSDIKKRIESLIEREYLERDEDDPN 68
 
Name Accession Description Interval E-value
Cullin pfam00888
Cullin family;
21-630 0e+00

Cullin family;


Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 612.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145  21 WDDLRAGIQQVYTRQsMVKSRYMELYTHVYNCCTsvhqsnqaqeagvppsksrkgetlegvQLVGLELYKQLKEFLKNYL 100
Cdd:pfam00888   1 WAKLEDAIDEILNKN-VSSLSYEELYRAVYNLCL---------------------------HKQGEKLYDKLKEYLEEHL 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 101 TNLLKD--GEGLLDESVLKFYTQQWEDYRFSSKVLNGICAYLSRYWVlckyyggrKAIYQIYSLALVTWRDCLFR-PLNK 177
Cdd:pfam00888  53 KKLVKPliKEASSGEEFLKAYVKEWEDHTISMKMIRDIFMYLDRVYV--------KRLPSIYDLGLELFRDHVFRiPLKD 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 178 QVTHAVLKLIEKERNGETINTRLMGGIVQSYVELGLNEDDafamgprLKVYKESFESRFLADTERFYTRESTKFLQQNPV 257
Cdd:pfam00888 125 KLIDALLDLIEKERNGEVIDRSLIKSVIDMLVSLGEDEKK-------DNVYEEDFEPPFLEATEEYYRAESQELLAENVA 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 258 TEYMKKAETRLLEEQRRGQ-YLHENTQEELARKCRQVLIEKHLEIFH-GEFQNLLDADKSEDLGRMYNLVSRIQDGLGEL 335
Cdd:pfam00888 198 PEYLKKAERRLEEEEERVRhYLHSSTKKKLLDVLEEVLISDHLEELLeEELQNLLDDNKTEDLKRLYRLLSRVPDGLEPL 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 336 KTLLETHIHNQCiAAIEKCGEAALNDPKMYIQTVLDVHKKYNALVMLAFNNNAGFVAVLDKACGRFINNNavtkmaQSSS 415
Cdd:pfam00888 278 RKAFEEYIKKEG-KAIVKDAKEQTTDAKKYVEDLLELKDKFDKIVKDAFSNDELFVKALDEAFEEFINKN------TSNS 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 416 KSSELLAGYCDSLLKKRSKNPEEAELEDTLNQVIAVFKYIEDRDVFQKFYAKMLAKSLVHQNSASDDAEASMIAKLKQAC 495
Cdd:pfam00888 351 KSPELLAKYIDDLLKKGLKGKSEEELEEKLDKVITLFRYIQDKDVFEAFYKKHLAKRLLLGKSASDDAERSMISKLKEEC 430
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 496 GFEYTSKLQQMFQDIGTSKYLNEWFKKHP--TNSEPLGLDFSIQVLSSGSRPSQQSGTFALPSELERSYQRLTAFYASRH 573
Cdd:pfam00888 431 GSEFTSKLEGMFKDMELSKDLMKEFKEHLseNKSSKKGIDLSVNVLTSGAWPTYLTSDFILPPELEKAIERFEKFYLSKH 510
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831604145 574 SGRKLTWLYQLSEGELVTNCFKNR-YTLQASTFQMAILLRYNTE-DAYAVQQLMDGTQI 630
Cdd:pfam00888 511 SGRKLTWLHSLGTAELKATFPKGKkHELNVSTYQMAILLLFNDDgDSLSYEEIQEATGL 569
COG5647 COG5647
Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
20-773 5.28e-135

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


Pssm-ID: 227934 [Multi-domain]  Cd Length: 773  Bit Score: 418.82  E-value: 5.28e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145  20 TWDDLRAGIQQVYTR--QSMVKSRYMELYTHVYNCCTSVHQSNQaqeagvppSKSRKGETLegvQLVGLELYKQLKEFLK 97
Cdd:COG5647    23 TWEFIERAIGQIFERlyDSMAILSLMEVYTKIYNYCTNKTRSLE--------SDLRWKIDF---IYLGSRLIQKLVDYAK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145  98 NYLTNLLKDGEGLLDESVLKFYTQQWEDYRFSSKVLNGICAYLSRYWVLCKYYGGRKaIYQIYSLALVTWRDCLFRPLNK 177
Cdd:COG5647    92 NYIEEYNRGRSQENMEEFLDELVKFWNRFTKGATMINHLFLYMDRVYLKKARYDKTL-VFEVYSLCLVKEKIESFRLIVD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 178 QVTHAVLKLIEKERNGETINTRLMGGIVQSYVELGLNEDDAfamGPRLKVYKESFESRFLADTERFYTRESTKFLQQNPV 257
Cdd:COG5647   171 SLINPLLYYVERYRALQSIDRKYIEDAKDMLESLERPSDYK---KENLSYYKSVFEPIFLEETWEFYEMESSEVIELLSV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 258 TEYMKKAETRLLEEQRRGQ-YLHENTQEELARKCRQVLIEKHLEIFH---GEFQNLLDADKSEDLGRMYNLVSRIQDGLG 333
Cdd:COG5647   248 TEYLEKAHKILEREEELVEiYLKVSTKKPLLEVLEDVLITRHLDDLEeqgSGFREALDASNLEKLQVLYRLLSETKYGVQ 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 334 ELKTLLE-------------THIHNQCIAAIEKCGEAALnDPKMYIQTVLDVHKKYNALVMLAFNNNAGFVAVLDKACGR 400
Cdd:COG5647   328 PLQEVFEryvkdegvlinieTNYIFHCKVDVGFLGSREC-LPKLYVQKLLSCHDLFPSLVNESFEGDGSIVKALGNAFKT 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 401 FINNNAvtkmaQSSSKSSELLAGYCDSLLKKRSKNPEEAELEDTLNQVIAVFKYIEDRDVFQKFYAKMLAKSLVHQNSAS 480
Cdd:COG5647   407 FINGNE-----SADSGPSEYLAKYIDGLLKKDGKQSFIGKIKDLLQDIITLFRYVEEKDVFEKYYKKLLAKRLLNGRSAS 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 481 DDAEASMIAKLKQACGFEYTSKLQQMFQDIGTSKYLNEWFKKHPTNSEPlGLDFSIQVLSSGSRP-SQQSGTFALPSELE 559
Cdd:COG5647   482 AQAELKMISMLKKVCGQEFTSKLEGMFRDISLSSEFTEAFQHSPQSYNK-YLDLFVWVLTQAYWPlSPEEVSIRLPKELV 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 560 RSYQRLTAFYASRHSGRKLTWLYQLSEGELVTNCFKNRYTLQASTF---QMAILLRYNTEDAYAVQQLMDGTQIKTDIFA 636
Cdd:COG5647   561 PILEGFKKFYSSKHNGRKLKWYWHLGSGEVKARFNEGQKYLEISTFsvyQLLVFLLFNDHEELTFEEILELTKLSTDDLK 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145 637 QVLQILLKLKLLVLEDentpvDEMELKQDTLIKLYLGYRNKKLRVNINVPMKMEQKQEQETTHRNIEADRKLLIQAALVI 716
Cdd:COG5647   641 RVLQSLSCAKLVVLLK-----DDKLVSPNTKFYVNENFSSKLERIKINYIAESECMQDNLDTHETVEEDRQAELQACIVR 715
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831604145 717 IMKMRKVLKHQQLLGEVLTQLSSIFKPRIPVIKKCIDVLIAKEYLERVDGEQdTYSY 773
Cdd:COG5647   716 IMKARKKLKHGDLVKEVIAQHKSRFEPKVSMVKRAIETLIEKEYLERQADDE-IYVY 771
CULLIN smart00182
Cullin;
454-589 6.19e-50

Cullin;


Pssm-ID: 214545 [Multi-domain]  Cd Length: 143  Bit Score: 171.73  E-value: 6.19e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831604145  454 YIEDRDVFQKFYAKMLAKSLVHQNSASDDAEASMIAKLKQACGFEYTSKLQQMFQDIGTSKYLNEWFKKHPTNSEP--LG 531
Cdd:smart00182   1 YIQDKDVFEKYYKKHLAKRLILNRSASDDAEENMITKLKQECGYEFTSKLERMFRDISLSKDLNQSFKDMLENNPSakPI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831604145  532 LDFSIQVLSSGSRPSQQSGT-FALPSELERSYQRLTAFYASRHSGRKLTWLYQLSEGEL 589
Cdd:smart00182  81 IDLNVRVLTSGYWPTSSTEVeINLPQELEDALEEFEEFYLAKHSGRKLTWLHSLGRGEV 139
Cullin_Nedd8 pfam10557
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
705-767 5.24e-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: 98.29  E-value: 5.24e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831604145 705 DRKLLIQAALVIIMKMRKVLKHQQLLGEVLTQLSSIFKPRIPVIKKCIDVLIAKEYLERVDGE 767
Cdd:pfam10557   1 DRKHEIQAAIVRIMKSRKTLSHNELVNEVIEQLKSRFKPSVSDIKKRIESLIEKEYLERDEDD 63
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
702-769 2.74e-23

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: 93.76  E-value: 2.74e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831604145  702 IEADRKLLIQAALVIIMKMRKVLKHQQLLGEVLTQLSSIFKPRIPVIKKCIDVLIAKEYLERVDGEQD 769
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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