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Conserved domains on  [gi|21707140|gb|AAH33647|]
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Cullin 7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APC10-CUL7 cd08665
APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that ...
 838-968 1.46e-91

APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that mediates substrate ubiquitination; This model represents the APC10/DOC1 domain present in CUL7, a subunit of the SCF-ROC1-like E3 Ubiquitin (Ub) ligase complex, which mediates substrate ubiquitination (or ubiquitylation), and is a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling the SCF-ROC1-like E3 Ub ligase complex consisting of the adapter protein Skp1, CUL7, the WD40 repeat-containing F-box Fbw8 (also known as Fbx29), and ROC1 (RING-box protein 1). CUL7 is a large protein with a C-terminal cullin domain that binds ROC1 and additional domains, including an APC10/DOC1 domain. While the Fbw8 protein is responsible for substrate protein recognition, the ROC1 RING domain recruits an Ub-charged E2 Ub-conjugating enzyme for substrate ubiquitination. It remains to be determined how CUL7 binds to the Skp1-Fbw8 heterodimer. The CUL7 E3 Ub ligase has been implicated in the proteasomal degradation of the cellular proteins, cyclin D1, an important regulator of the G1 to S-phase cell cycle progression, and insulin receptor substrate 1, a critical component of the signaling pathways downstream of the insulin and insulin-like growth factor 1 receptor. CUL7 appears to be an important regulator of placental development. Germ line mutations of CUL7 are linked to 3-M syndrome and Yakuts short stature syndrome.


:

Pssm-ID: 176486  Cd Length: 131  Bit Score: 292.21  E-value: 1.46e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140  838 DKCWEKVEVSSNPHRASKLTDHNPKTYWESNGSAGSHYITLHMRRGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLH 917
Cdd:cd08665    1 DKCWEKVEVSSNPHRANKLTDGNPKTYWESNGSTGSHYINIHMHRGVVIRQLYMLVASEDSSYMPARVVVLGGDSPSCIT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 21707140  918 TELNSVNVMPSASRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLEILG 968
Cdd:cd08665   81 TELNAVNVSPTASRVVLLENMTRFWPIIQIRIKRCQQGGIDTRVRGLEILG 131
Cul7 pfam11515
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ...
 362-434 3.22e-41

Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family member, Cul7, is required for normal mouse development and cellular proliferation. Cul7 has a CPH domain which is a p53 interaction domain. The CPH domain interaction surface of P53 is present in the tetramerization domain.


:

Pssm-ID: 463286  Cd Length: 78  Bit Score: 146.34  E-value: 3.22e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21707140    362 EFASGNTYALYVRDTLQPGMRVRMLDDYEEISAGDEGEFRQSNNGV---PPVQVFWESTGRTYWVHWHMLEILGFE 434
Cdd:pfam11515    3 DFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGlhdLNVQVDWQSKGRTYWVHWHHVEILGFP 78
Cullin super family cl38017
Cullin family;
1217-1506 2.89e-09

Cullin family;


The actual alignment was detected with superfamily member pfam00888:

Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 61.81  E-value: 2.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140   1217 SEQFARHIDQQI-QGSRIGGAQEMERlaQLQQCLqavLIFSGLEIATTFEHYYQHYMADRLLG--VVSSWLEGAVL---- 1289
Cdd:pfam00888  353 PELLAKYIDDLLkKGLKGKSEEELEE--KLDKVI---TLFRYIQDKDVFEAFYKKHLAKRLLLgkSASDDAERSMIsklk 427

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140   1290 EQIGPCFPNRLpQQMLQSLSTSKELQRQFHVYQLqqldqellklEDTEKKIQVglgasgkehksekeeeagaaavvdvae 1369
Cdd:pfam00888  428 EECGSEFTSKL-EGMFKDMELSKDLMKEFKEHLS----------ENKSSKKGI--------------------------- 469

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140   1370 geeeeeenedlyyegampEVSVLVLSRHSWPVasichTLNPRTCLPSYLRGTLNRYSNFYNKSQSHpalergsqRRLQWT 1449
Cdd:pfam00888  470 ------------------DLSVNVLTSGAWPT-----YLTSDFILPPELEKAIERFEKFYLSKHSG--------RKLTWL 518

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21707140   1450 W-LGWAEL--QFGNQT---LHVSTVQMW-LLLYLNDLKAVSVESLLAFSGLSADMLNQAIGPLT 1506
Cdd:pfam00888  519 HsLGTAELkaTFPKGKkheLNVSTYQMAiLLLFNDDGDSLSYEEIQEATGLPDEELKRTLQSLA 582
Cullin_Nedd8 super family cl47051
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
 1561-1639 1.07e-06

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.


The actual alignment was detected with superfamily member smart00884:

Pssm-ID: 214883 [Multi-domain]  Cd Length: 68  Bit Score: 47.54  E-value: 1.07e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21707140    1561 EKRRNLLNCLIVRILKAHGDegLHIDQLVCLVLEAWQKgpcppRGLVsslgkgsacSSTDVLSCILHLLGKGTLRRHDD 1639
Cdd:smart00884    3 EDRKLEIQAAIVRIMKSRKT--LSHSELVSEVIEQLKK-----RFKP---------SVSDIKKRIESLIEREYLERDED 65
 
Name Accession Description Interval E-value
APC10-CUL7 cd08665
APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that ...
 838-968 1.46e-91

APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that mediates substrate ubiquitination; This model represents the APC10/DOC1 domain present in CUL7, a subunit of the SCF-ROC1-like E3 Ubiquitin (Ub) ligase complex, which mediates substrate ubiquitination (or ubiquitylation), and is a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling the SCF-ROC1-like E3 Ub ligase complex consisting of the adapter protein Skp1, CUL7, the WD40 repeat-containing F-box Fbw8 (also known as Fbx29), and ROC1 (RING-box protein 1). CUL7 is a large protein with a C-terminal cullin domain that binds ROC1 and additional domains, including an APC10/DOC1 domain. While the Fbw8 protein is responsible for substrate protein recognition, the ROC1 RING domain recruits an Ub-charged E2 Ub-conjugating enzyme for substrate ubiquitination. It remains to be determined how CUL7 binds to the Skp1-Fbw8 heterodimer. The CUL7 E3 Ub ligase has been implicated in the proteasomal degradation of the cellular proteins, cyclin D1, an important regulator of the G1 to S-phase cell cycle progression, and insulin receptor substrate 1, a critical component of the signaling pathways downstream of the insulin and insulin-like growth factor 1 receptor. CUL7 appears to be an important regulator of placental development. Germ line mutations of CUL7 are linked to 3-M syndrome and Yakuts short stature syndrome.


Pssm-ID: 176486  Cd Length: 131  Bit Score: 292.21  E-value: 1.46e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140  838 DKCWEKVEVSSNPHRASKLTDHNPKTYWESNGSAGSHYITLHMRRGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLH 917
Cdd:cd08665    1 DKCWEKVEVSSNPHRANKLTDGNPKTYWESNGSTGSHYINIHMHRGVVIRQLYMLVASEDSSYMPARVVVLGGDSPSCIT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 21707140  918 TELNSVNVMPSASRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLEILG 968
Cdd:cd08665   81 TELNAVNVSPTASRVVLLENMTRFWPIIQIRIKRCQQGGIDTRVRGLEILG 131
Cul7 pfam11515
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ...
 362-434 3.22e-41

Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family member, Cul7, is required for normal mouse development and cellular proliferation. Cul7 has a CPH domain which is a p53 interaction domain. The CPH domain interaction surface of P53 is present in the tetramerization domain.


Pssm-ID: 463286  Cd Length: 78  Bit Score: 146.34  E-value: 3.22e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21707140    362 EFASGNTYALYVRDTLQPGMRVRMLDDYEEISAGDEGEFRQSNNGV---PPVQVFWESTGRTYWVHWHMLEILGFE 434
Cdd:pfam11515    3 DFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGlhdLNVQVDWQSKGRTYWVHWHHVEILGFP 78
Cullin pfam00888
Cullin family;
1217-1506 2.89e-09

Cullin family;


Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 61.81  E-value: 2.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140   1217 SEQFARHIDQQI-QGSRIGGAQEMERlaQLQQCLqavLIFSGLEIATTFEHYYQHYMADRLLG--VVSSWLEGAVL---- 1289
Cdd:pfam00888  353 PELLAKYIDDLLkKGLKGKSEEELEE--KLDKVI---TLFRYIQDKDVFEAFYKKHLAKRLLLgkSASDDAERSMIsklk 427

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140   1290 EQIGPCFPNRLpQQMLQSLSTSKELQRQFHVYQLqqldqellklEDTEKKIQVglgasgkehksekeeeagaaavvdvae 1369
Cdd:pfam00888  428 EECGSEFTSKL-EGMFKDMELSKDLMKEFKEHLS----------ENKSSKKGI--------------------------- 469

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140   1370 geeeeeenedlyyegampEVSVLVLSRHSWPVasichTLNPRTCLPSYLRGTLNRYSNFYNKSQSHpalergsqRRLQWT 1449
Cdd:pfam00888  470 ------------------DLSVNVLTSGAWPT-----YLTSDFILPPELEKAIERFEKFYLSKHSG--------RKLTWL 518

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21707140   1450 W-LGWAEL--QFGNQT---LHVSTVQMW-LLLYLNDLKAVSVESLLAFSGLSADMLNQAIGPLT 1506
Cdd:pfam00888  519 HsLGTAELkaTFPKGKkheLNVSTYQMAiLLLFNDDGDSLSYEEIQEATGLPDEELKRTLQSLA 582
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
 1561-1639 1.07e-06

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: 47.54  E-value: 1.07e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21707140    1561 EKRRNLLNCLIVRILKAHGDegLHIDQLVCLVLEAWQKgpcppRGLVsslgkgsacSSTDVLSCILHLLGKGTLRRHDD 1639
Cdd:smart00884    3 EDRKLEIQAAIVRIMKSRKT--LSHSELVSEVIEQLKK-----RFKP---------SVSDIKKRIESLIEREYLERDED 65
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
856-969 1.07e-06

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 50.90  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140    856 LTDHNPKTYWESNGSAgSHYITLHMRRGILIRQLTLLVASE-DSSYMPARVVVCGGDSTSSLhTELNSVNV-MPSASRVI 933
Cdd:pfam03256   45 LRDDNLDTYWQSDGSQ-PHLVNIQFRKKTPVKYVAIYLDYKlDESYTPSKISVRAGTGFNDL-QEVRVVDLeEPTGWVHI 122

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 21707140    934 LL----ENLTRFWpIIQIRIKRCQQGGIDTRIRGLEILGP 969
Cdd:pfam03256  123 PLrdanGKPLRTF-MLQIAVLSNHQNGRDTHVRQIKIYGP 161
COG5647 COG5647
Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
 1387-1639 3.00e-06

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


Pssm-ID: 227934 [Multi-domain]  Cd Length: 773  Bit Score: 52.11  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140 1387 PEVSVLVLSRHSWPVASIchtlNPRTCLPSYLRGTLNRYSNFYnkSQSHpalergSQRRLQWTW-LGWAEL--QFGNQTL 1463
Cdd:COG5647  532 LDLFVWVLTQAYWPLSPE----EVSIRLPKELVPILEGFKKFY--SSKH------NGRKLKWYWhLGSGEVkaRFNEGQK 599

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140 1464 H-----VSTVQMWLLLYLNDLKAVSVESLLAFSGLSADMLNQAIGPL-TSSRGPLDLHEQKDIPGGVLKIRDGSKEPRSR 1537
Cdd:COG5647  600 YleistFSVYQLLVFLLFNDHEELTFEEILELTKLSTDDLKRVLQSLsCAKLVVLLKDDKLVSPNTKFYVNENFSSKLER 679

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140 1538 wdiVRL-IPPQTYLQAEGEDGQNL--EKRRNLLNCLIVRILKAHGDegLHIDQLVCLVLEAWQkgpcpPRG--LVSslgk 1612
Cdd:COG5647  680 ---IKInYIAESECMQDNLDTHETveEDRQAELQACIVRIMKARKK--LKHGDLVKEVIAQHK-----SRFepKVS---- 745

                        250       260
                 ....*....|....*....|....*..
gi 21707140 1613 gsacsstDVLSCILHLLGKGTLRRHDD 1639
Cdd:COG5647  746 -------MVKRAIETLIEKEYLERQAD 765
Cullin_Nedd8 pfam10557
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
 1563-1639 3.45e-03

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: 37.43  E-value: 3.45e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21707140   1563 RRNLLNCLIVRILKAHGDegLHIDQLVCLVLEAwqkgpcpprglVSSLGKgsaCSSTDVLSCILHLLGKGTLRRHDD 1639
Cdd:pfam10557    2 RKHEIQAAIVRIMKSRKT--LSHNELVNEVIEQ-----------LKSRFK---PSVSDIKKRIESLIEKEYLERDED 62
 
Name Accession Description Interval E-value
APC10-CUL7 cd08665
APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that ...
 838-968 1.46e-91

APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that mediates substrate ubiquitination; This model represents the APC10/DOC1 domain present in CUL7, a subunit of the SCF-ROC1-like E3 Ubiquitin (Ub) ligase complex, which mediates substrate ubiquitination (or ubiquitylation), and is a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling the SCF-ROC1-like E3 Ub ligase complex consisting of the adapter protein Skp1, CUL7, the WD40 repeat-containing F-box Fbw8 (also known as Fbx29), and ROC1 (RING-box protein 1). CUL7 is a large protein with a C-terminal cullin domain that binds ROC1 and additional domains, including an APC10/DOC1 domain. While the Fbw8 protein is responsible for substrate protein recognition, the ROC1 RING domain recruits an Ub-charged E2 Ub-conjugating enzyme for substrate ubiquitination. It remains to be determined how CUL7 binds to the Skp1-Fbw8 heterodimer. The CUL7 E3 Ub ligase has been implicated in the proteasomal degradation of the cellular proteins, cyclin D1, an important regulator of the G1 to S-phase cell cycle progression, and insulin receptor substrate 1, a critical component of the signaling pathways downstream of the insulin and insulin-like growth factor 1 receptor. CUL7 appears to be an important regulator of placental development. Germ line mutations of CUL7 are linked to 3-M syndrome and Yakuts short stature syndrome.


Pssm-ID: 176486  Cd Length: 131  Bit Score: 292.21  E-value: 1.46e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140  838 DKCWEKVEVSSNPHRASKLTDHNPKTYWESNGSAGSHYITLHMRRGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLH 917
Cdd:cd08665    1 DKCWEKVEVSSNPHRANKLTDGNPKTYWESNGSTGSHYINIHMHRGVVIRQLYMLVASEDSSYMPARVVVLGGDSPSCIT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 21707140  918 TELNSVNVMPSASRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLEILG 968
Cdd:cd08665   81 TELNAVNVSPTASRVVLLENMTRFWPIIQIRIKRCQQGGIDTRVRGLEILG 131
APC10-like1 cd08365
APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
 838-967 9.05e-70

APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This model represens the APC10-like DOC1 domain of multi-domain proteins present in E3 ubiquitin ligases. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. APC10/DOC1 domains such as those present in HECT (Homologous to the E6-AP Carboxyl Terminus) and Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase proteins, HECTD3, and CUL7, respectively, are also included here. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling a SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, Fbx29 F-box protein, and ROC1 (RING-box protein 1) and promotes ubiquitination. CUL7 is a multi-domain protein with a C-terminal cullin domain that binds ROC1 and a centrally positioned APC10/DOC1 domain. HECTD3 contains a C-terminal HECT domain which contains the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain which is responsible for substrate recognition and binding. An APC10/DOC1 domain homolog is also present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT domain. Recent studies have shown that the protein complex HERC2-RNF8 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Also included in this hierarchy is an uncharacterized APC10/DOC1-like domain found in a multi-domain protein, which also contains CUB, zinc finger ZZ-type, and EF-hand domains. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here.


Pssm-ID: 176483  Cd Length: 131  Bit Score: 230.08  E-value: 9.05e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140  838 DKCW-EKVEVSSNPHRASKLTDHNPKTYWESNGSAGSHYITLHMRRGILIRQLTLLVASEDSSYMPARVVVCGGDStSSL 916
Cdd:cd08365    1 TKCYvESIEVSSNPADASRLTDGNTSTYWQSDGSQGSHWIRLKMKPDVLVRHLSLAVDATDSSYMPQRVVVAGGRS-ASN 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 21707140  917 HTELNSVNVMPS-ASRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLEIL 967
Cdd:cd08365   80 LQELRDVNIPPSvTGYVTLLEDATISQPYIEIRIKRCRSDGIDTRIHGLRIL 131
APC10-like cd08159
APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
 839-967 1.02e-65

APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This family contains the single domain protein, APC10, a subunit of the anaphase-promoting complex (APC), as well as the DOC1 domain of multi-domain proteins present in E3 ubiquitin ligases. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. The APC, a multi-protein complex (or cyclosome), is a cell cycle-regulated, E3 ubiquitin ligase that controls important transitions in mitosis and the G1 phase by ubiquitinating regulatory proteins, thereby targeting them for degradation. APC10-like DOC1 domains such as those present in HECT (Homologous to the E6-AP Carboxyl Terminus) and Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase proteins, HECTD3, and CUL7, respectively, are also included in this hierarchy. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling a SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, Fbx29 F-box protein, and ROC1 (RING-box protein 1) and promotes ubiquitination. CUL7 is a multi-domain protein with a C-terminal cullin domain that binds ROC1 and a centrally positioned APC10/DOC1 domain. HECTD3 contains a C-terminal HECT domain which contains the active site for ubiquitin transfer onto substrates, and an N-terminal APC10 domain which is responsible for substrate recognition and binding. An APC10/DOC1 domain homolog is also present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT domain. Recent studies have shown that the protein complex HERC2-RNF8 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Also included in this hierarchy is an uncharacterized APC10/DOC1-like domain found in a multi-domain protein, which also contains CUB, zinc finger ZZ-type, and EF-hand domains. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here.


Pssm-ID: 176482  Cd Length: 129  Bit Score: 218.11  E-value: 1.02e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140  839 KCW-EKVEVSSNPHRASKLTDHNPKTYWESNGSAGSHYITLHMRRGILIRQLTLLVASEDSSYMPARVVVCGGDStSSLH 917
Cdd:cd08159    1 KCYtASIEVSSNPLPVSRLTDGNYDTYWQSDGSQGSHWIRLFMKKDVLIRVLAIFVDMADSSYMPSLVVVYGGHS-PSDL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 21707140  918 TELNSVNVMPSASRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLEIL 967
Cdd:cd08159   80 RELKDVNIRPSNGWVALLEDDTLKCPYIEIRIKRCRSDGIDTRIRGLRLL 129
Cul7 pfam11515
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ...
 362-434 3.22e-41

Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family member, Cul7, is required for normal mouse development and cellular proliferation. Cul7 has a CPH domain which is a p53 interaction domain. The CPH domain interaction surface of P53 is present in the tetramerization domain.


Pssm-ID: 463286  Cd Length: 78  Bit Score: 146.34  E-value: 3.22e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21707140    362 EFASGNTYALYVRDTLQPGMRVRMLDDYEEISAGDEGEFRQSNNGV---PPVQVFWESTGRTYWVHWHMLEILGFE 434
Cdd:pfam11515    3 DFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGlhdLNVQVDWQSKGRTYWVHWHHVEILGFP 78
APC10-HERC2 cd08664
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ...
 839-967 2.81e-37

APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the APC10/DOC1 domain present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including a zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT (Homologous to the E6-AP Carboxyl Terminus) domain. The APC10/DOC1 domain of HERC2 is a homolog of the APC10 subunit and the DOC1 domain present in E3 ubiquitin ligases which mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. As suggested by structural relationships between HERC2 and other proteins such as HERC1, the proposed role for HERC2 in protein trafficking and degradation pathways is consistent with observations that mutations in HERC2 lead to neuromuscular secretory vesicle and sperm acrosome defects, other developmental abnormalities, and juvenile lethality of jdf2 mice. Recent studies have shown that the protein complex, HERC2-RNF8, coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes.


Pssm-ID: 176485  Cd Length: 152  Bit Score: 137.89  E-value: 2.81e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140  839 KCWEKVEVSSNPHRASKLTDhNPKTYWESNGSAGSHYITLHMRRGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLhT 918
Cdd:cd08664   26 RCVRSLTVSSNENQAKRLID-GSGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVDPADSSYMPSLVVVSGGDSLNSL-K 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 21707140  919 ELNSVNVMPSASRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLEIL 967
Cdd:cd08664  104 ELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNGIDCKIHGLNII 152
APC10-HECTD3 cd08666
APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ...
 842-966 4.30e-36

APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ubiquitination; This model represents the APC10/DOC1 domain present in HECTD3, a HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein. HECT E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), and are a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. They also regulate the trafficking of many receptors, channels, transporters and viral proteins. HECTD3 (HECT domain-containing protein3) contains a C-terminal HECT domain with the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain, which is responsible for substrate recognition and binding. HECTD3 specifically recognizes the Trio-binding protein, Tara (Trio-associated repeat on actin), implicated in regulating actin cytoskeletal, cell motility and cell growth. Tara also binds to TRF1 and may participate in telomere maintenance and/or mitotic regulation through interacting with TRF1. HECTD3 interacts with and promotes the ubiquitination of Syntaxin 8, an endosomal syntaxin proposed to mediate distinct steps of endosomal protein trafficking. HECTD3-mediated Syntaxin 8 degradation has been suggested to contribute to the pathophysiology of neurodegenerative diseases.


Pssm-ID: 176487  Cd Length: 134  Bit Score: 133.69  E-value: 4.30e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140  842 EKVEVSS--NPHRASKLTDHNPKTYWESNGSAGSHYITLHMRRGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLHte 919
Cdd:cd08666    8 ESIEVSSytDDFNVSCLTDGDPDTYWESDGSQGQHWIRLHMKKGTIIKKLLLTVDATDDNYMPKRVAVYGGEGDNLKK-- 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 21707140  920 LNSVNV-MPSASRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLEI 966
Cdd:cd08666   86 LNDVSIdETLIGDVCILEDMTTHLPVIEIRIKECKDEGIDVRIRGIKI 133
APC10-ZZEF1 cd08667
APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing ...
 839-968 5.04e-35

APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing protein 1 (ZZEF1) and homologs; This model represents the APC10/DOC1-like domain present in the uncharacterized Zinc finger ZZ-type and EF-hand domain-containing protein 1 (ZZEF1) of Mus musculus. Members of this family contain EF-hand, APC10, CUB, and zinc finger ZZ-type domains. ZZEF1-like APC10 domains are homologous to the APC10 subunit/DOC1 domains present in E3 ubiquitin ligases, which mediate substrate ubiquitination (or ubiquitylation), and are components of the ubiquitin-26S proteasome pathway for selective proteolytic degradation.


Pssm-ID: 176488  Cd Length: 131  Bit Score: 130.41  E-value: 5.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140  839 KCWEKVEVSSNPHRASKLTDHNPKTYWESNGSAGSHYITLHMRRGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLHt 918
Cdd:cd08667    2 KCYAYIEVSSNSADIDRMTDGETSTYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVSVGRSASSLQ- 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 21707140  919 ELNSVNVmPS--ASRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLEILG 968
Cdd:cd08667   81 EVRDVHI-PSnvTGYVTLLENANISYLVVQINIKRCHSDGCDTRIHGLKTIG 131
APC10 cd08366
APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; ...
 856-968 1.38e-11

APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; This model represents the single domain protein APC10, a subunit of the anaphase-promoting complex (APC), which is a multi-subunit E3 ubiquitin ligase. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a vital component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. The APC (also known as the cyclosome), is a cell cycle-regulated E3 ubiquitin ligase that controls important transitions in mitosis and the G1 phase by ubiquitinating regulatory proteins, thereby targeting them for degradation. In mitosis, the APC initiates sister chromatid separation by ubiquitinating the anaphase inhibitor securin and triggers exit from mitosis by ubiquitinating cyclin B. The C-terminus of APC10 binds to CDC27/APC3, an APC subunit that contains multiple tetratrico peptide repeats. APC10 domains are homologous to the DOC1 domains present in the HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein, and the Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase complex. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here.


Pssm-ID: 176484  Cd Length: 139  Bit Score: 63.73  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140  856 LTDHNPKTYWESNGSAgSHYITLHMRRGILIRQLTLLVA-SEDSSYMPARVVVCGGDSTSSLH----TELNsvnvMPSAS 930
Cdd:cd08366   23 LRDDSLDTYWQSDGPQ-PHLINIQFSKKTDISAVALYLDyKLDESYTPSKISIRAGTSPHDLQevrtVELE----EPNGW 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 21707140  931 RVILLENLTRFWPI----IQIRIKRCQQGGIDTRIRGLEILG 968
Cdd:cd08366   98 VHIPLEDNRDGKPLrtffLQIAILSNHQNGRDTHIRQIKVYG 139
Cullin pfam00888
Cullin family;
1217-1506 2.89e-09

Cullin family;


Pssm-ID: 459983 [Multi-domain]  Cd Length: 610  Bit Score: 61.81  E-value: 2.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140   1217 SEQFARHIDQQI-QGSRIGGAQEMERlaQLQQCLqavLIFSGLEIATTFEHYYQHYMADRLLG--VVSSWLEGAVL---- 1289
Cdd:pfam00888  353 PELLAKYIDDLLkKGLKGKSEEELEE--KLDKVI---TLFRYIQDKDVFEAFYKKHLAKRLLLgkSASDDAERSMIsklk 427

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140   1290 EQIGPCFPNRLpQQMLQSLSTSKELQRQFHVYQLqqldqellklEDTEKKIQVglgasgkehksekeeeagaaavvdvae 1369
Cdd:pfam00888  428 EECGSEFTSKL-EGMFKDMELSKDLMKEFKEHLS----------ENKSSKKGI--------------------------- 469

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140   1370 geeeeeenedlyyegampEVSVLVLSRHSWPVasichTLNPRTCLPSYLRGTLNRYSNFYNKSQSHpalergsqRRLQWT 1449
Cdd:pfam00888  470 ------------------DLSVNVLTSGAWPT-----YLTSDFILPPELEKAIERFEKFYLSKHSG--------RKLTWL 518

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21707140   1450 W-LGWAEL--QFGNQT---LHVSTVQMW-LLLYLNDLKAVSVESLLAFSGLSADMLNQAIGPLT 1506
Cdd:pfam00888  519 HsLGTAELkaTFPKGKkheLNVSTYQMAiLLLFNDDGDSLSYEEIQEATGLPDEELKRTLQSLA 582
Cullin_Nedd8 smart00884
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
 1561-1639 1.07e-06

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: 47.54  E-value: 1.07e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21707140    1561 EKRRNLLNCLIVRILKAHGDegLHIDQLVCLVLEAWQKgpcppRGLVsslgkgsacSSTDVLSCILHLLGKGTLRRHDD 1639
Cdd:smart00884    3 EDRKLEIQAAIVRIMKSRKT--LSHSELVSEVIEQLKK-----RFKP---------SVSDIKKRIESLIEREYLERDED 65
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
856-969 1.07e-06

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 50.90  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140    856 LTDHNPKTYWESNGSAgSHYITLHMRRGILIRQLTLLVASE-DSSYMPARVVVCGGDSTSSLhTELNSVNV-MPSASRVI 933
Cdd:pfam03256   45 LRDDNLDTYWQSDGSQ-PHLVNIQFRKKTPVKYVAIYLDYKlDESYTPSKISVRAGTGFNDL-QEVRVVDLeEPTGWVHI 122

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 21707140    934 LL----ENLTRFWpIIQIRIKRCQQGGIDTRIRGLEILGP 969
Cdd:pfam03256  123 PLrdanGKPLRTF-MLQIAVLSNHQNGRDTHVRQIKIYGP 161
COG5647 COG5647
Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
 1387-1639 3.00e-06

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


Pssm-ID: 227934 [Multi-domain]  Cd Length: 773  Bit Score: 52.11  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140 1387 PEVSVLVLSRHSWPVASIchtlNPRTCLPSYLRGTLNRYSNFYnkSQSHpalergSQRRLQWTW-LGWAEL--QFGNQTL 1463
Cdd:COG5647  532 LDLFVWVLTQAYWPLSPE----EVSIRLPKELVPILEGFKKFY--SSKH------NGRKLKWYWhLGSGEVkaRFNEGQK 599

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140 1464 H-----VSTVQMWLLLYLNDLKAVSVESLLAFSGLSADMLNQAIGPL-TSSRGPLDLHEQKDIPGGVLKIRDGSKEPRSR 1537
Cdd:COG5647  600 YleistFSVYQLLVFLLFNDHEELTFEEILELTKLSTDDLKRVLQSLsCAKLVVLLKDDKLVSPNTKFYVNENFSSKLER 679

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140 1538 wdiVRL-IPPQTYLQAEGEDGQNL--EKRRNLLNCLIVRILKAHGDegLHIDQLVCLVLEAWQkgpcpPRG--LVSslgk 1612
Cdd:COG5647  680 ---IKInYIAESECMQDNLDTHETveEDRQAELQACIVRIMKARKK--LKHGDLVKEVIAQHK-----SRFepKVS---- 745

                        250       260
                 ....*....|....*....|....*..
gi 21707140 1613 gsacsstDVLSCILHLLGKGTLRRHDD 1639
Cdd:COG5647  746 -------MVKRAIETLIEKEYLERQAD 765
Cullin_Nedd8 pfam10557
Cullin protein neddylation domain; This is the neddylation site of cullin proteins which are a ...
 1563-1639 3.45e-03

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: 37.43  E-value: 3.45e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21707140   1563 RRNLLNCLIVRILKAHGDegLHIDQLVCLVLEAwqkgpcpprglVSSLGKgsaCSSTDVLSCILHLLGKGTLRRHDD 1639
Cdd:pfam10557    2 RKHEIQAAIVRIMKSRKT--LSHNELVNEVIEQ-----------LKSRFK---PSVSDIKKRIESLIEKEYLERDED 62
DOC1 COG5156
Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / ...
 856-969 4.47e-03

Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227485  Cd Length: 189  Bit Score: 40.34  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21707140  856 LTDHNPKTYWESNGSAgSHYITLHMRRGILIRQLTLLVA-SEDSSYMPARVVVCGGDSTSSLHtELNSVNVMPSASRVIL 934
Cdd:COG5156   46 LLDDNMDTYWQSDGVQ-PHSIQISFDKRRYIQSVQLFLSfTQDESYTPSKIGVRAGLTREDVR-EISSVEVVEPEGWVTL 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 21707140  935 -----LENLTRFWPIIQIRIKRCQQGGIDTRIRGLEILGP 969
Cdd:COG5156  124 svadkREDDLLKCIYILVVINSNHQEGKDSHVRHIKIYEP 163
 
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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