CSN4/RPN5/eIF3a helix turn helix domain; Cullin-RING E3 ubiquitin ligases (CRLs) are regulated by the eight-subunit COP9 signalosome (CSN). Enzymatically, CSN functions as an isopeptidase that removes the ubiquitin-like activator NEDD8 from CRLs, but it can also bind deneddylated CRLs and maintain them in an inactive state. The CSN subunits CSN1, CSN2, CSN3, CSN4, CSN7 and CSN8, share a common domain composition: an N-terminal array of tandem alpha-helical tetratricopeptide/-like repeats, a 34 residue motif, followed by a PCI domain, which encompasses a WH subdomain, a linker, and one or two alpha-helices at the C-terminus. This entry describes the C-terminal helices found on CSN4. The two helices from CSN4 (helices I and II) form a brace roughly perpendicular to the bundle axis in contact with the three C-terminal helices of CSN6. CSN5, whose two C-terminal helices form an antiparallel hairpin, inserts its final C-terminal helix (helix II) into the central CSN6 framework at the core of the bundle. Both CSN1 and CSN4 are dependent on the presence of their C-terminal helix (CSN1 isoform-2 residues: 466-527; and CSN4: 364-406) for integration into CSN. COP9 signalosome shares common architecture with the 26S proteasome lid and eIF3 where the 19S lid subunit RPN5 and the eIF3 core subunit eIF3a share significant structural similarity with CSN4.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1149728892 395 EALPTWDKQIQSLCFQVNNLLEKISQTAPEWTAQAMEAQMAQ 436
Cdd:pfam18420   1 EVLPTWDKQIQSLCYQVNNLIEKISQAEPEWMAKAMEEQMTQ 42

26S proteasome regulatory complex component [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149728892 171 VDYKLETylkiARLYLEDDDPVQAEAY---INRASLLQNEStnEQLQIHYKVCYARVLDYRRKFIEAAQRYNELsYKTIV 247
Cdd:COG5071   171 VAFILEQ----VRLFLLRSDYYMASTYtkkINKKFFEKEDV--QSLKLKYYELKVRIGLHDRAYLDVCKYYRAV-YDTAV 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149728892 248 HESERL---EALKHALHCTILASAGQQRSRMLATLFKDERCQQLAAYGILEKMYL-DRIIRGNQLQE-FAAMLMPHQKAT 322
Cdd:COG5071   244 VQEDPAkwkEVLSNVVCFALLTPYDNEQADLLHKINADHKLNSLPLLQQLVKCFIvNELMRWPKVAEiYGSALRSNVFAF 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149728892 323 TADGSSI----LDRAVIEHNLLSASKLYNNITFEELGALLEIPAAKAEKIASQMITEGRMNGFIDQIDGIVHFETR---- 394
Cdd:COG5071   324 NDEKGEKrwsdLRKRVIEHNIRVIANYYSRIHCSRLGVLLDMSPSETEQFISDLVNKGHFYAKINRPAQIISFEKSqnvq 403

                         250
                  ....*....|...
gi 1149728892 395 EALPTWDKQIQSL 407
Cdd:COG5071   404 EQLNEWGSNVTEL 416

CSN4/RPN5/eIF3a helix turn helix domain; Cullin-RING E3 ubiquitin ligases (CRLs) are regulated by the eight-subunit COP9 signalosome (CSN). Enzymatically, CSN functions as an isopeptidase that removes the ubiquitin-like activator NEDD8 from CRLs, but it can also bind deneddylated CRLs and maintain them in an inactive state. The CSN subunits CSN1, CSN2, CSN3, CSN4, CSN7 and CSN8, share a common domain composition: an N-terminal array of tandem alpha-helical tetratricopeptide/-like repeats, a 34 residue motif, followed by a PCI domain, which encompasses a WH subdomain, a linker, and one or two alpha-helices at the C-terminus. This entry describes the C-terminal helices found on CSN4. The two helices from CSN4 (helices I and II) form a brace roughly perpendicular to the bundle axis in contact with the three C-terminal helices of CSN6. CSN5, whose two C-terminal helices form an antiparallel hairpin, inserts its final C-terminal helix (helix II) into the central CSN6 framework at the core of the bundle. Both CSN1 and CSN4 are dependent on the presence of their C-terminal helix (CSN1 isoform-2 residues: 466-527; and CSN4: 364-406) for integration into CSN. COP9 signalosome shares common architecture with the 26S proteasome lid and eIF3 where the 19S lid subunit RPN5 and the eIF3 core subunit eIF3a share significant structural similarity with CSN4.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1149728892 395 EALPTWDKQIQSLCFQVNNLLEKISQTAPEWTAQAMEAQMAQ 436
Cdd:pfam18420   1 EVLPTWDKQIQSLCYQVNNLIEKISQAEPEWMAKAMEEQMTQ 42

motif in proteasome subunits, Int-6, Nip-1 and TRIP-15; Also called the PCI (Proteasome, COP9, Initiation factor 3) domain. Unknown function.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149728892  327 SSILDRAVIEHNLLSASKLYNNITFEELGALLEIPAAKAEKIASQMITEGRMNGFIDQIDGIVHFE-----TREALPTWD 401
Cdd:smart00088   3 VERLQRKIRLTNLLQLSEPYSSISLSDLAKLLGLSVPEVEKLVSKAIRDGEISAKIDQVNGIVEFEevdprRSEPLAQFA 82

                   ....*.
gi 1149728892  402 KQIQSL 407
Cdd:smart00088  83 ETLKKL 88

CSN4/RPN5/eIF3a helix turn helix domain; Cullin-RING E3 ubiquitin ligases (CRLs) are regulated by the eight-subunit COP9 signalosome (CSN). Enzymatically, CSN functions as an isopeptidase that removes the ubiquitin-like activator NEDD8 from CRLs, but it can also bind deneddylated CRLs and maintain them in an inactive state. The CSN subunits CSN1, CSN2, CSN3, CSN4, CSN7 and CSN8, share a common domain composition: an N-terminal array of tandem alpha-helical tetratricopeptide/-like repeats, a 34 residue motif, followed by a PCI domain, which encompasses a WH subdomain, a linker, and one or two alpha-helices at the C-terminus. This entry describes the C-terminal helices found on CSN4. The two helices from CSN4 (helices I and II) form a brace roughly perpendicular to the bundle axis in contact with the three C-terminal helices of CSN6. CSN5, whose two C-terminal helices form an antiparallel hairpin, inserts its final C-terminal helix (helix II) into the central CSN6 framework at the core of the bundle. Both CSN1 and CSN4 are dependent on the presence of their C-terminal helix (CSN1 isoform-2 residues: 466-527; and CSN4: 364-406) for integration into CSN. COP9 signalosome shares common architecture with the 26S proteasome lid and eIF3 where the 19S lid subunit RPN5 and the eIF3 core subunit eIF3a share significant structural similarity with CSN4.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1149728892 395 EALPTWDKQIQSLCFQVNNLLEKISQTAPEWTAQAMEAQMAQ 436
Cdd:pfam18420   1 EVLPTWDKQIQSLCYQVNNLIEKISQAEPEWMAKAMEEQMTQ 42

motif in proteasome subunits, Int-6, Nip-1 and TRIP-15; Also called the PCI (Proteasome, COP9, Initiation factor 3) domain. Unknown function.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149728892  327 SSILDRAVIEHNLLSASKLYNNITFEELGALLEIPAAKAEKIASQMITEGRMNGFIDQIDGIVHFE-----TREALPTWD 401
Cdd:smart00088   3 VERLQRKIRLTNLLQLSEPYSSISLSDLAKLLGLSVPEVEKLVSKAIRDGEISAKIDQVNGIVEFEevdprRSEPLAQFA 82

                   ....*.
gi 1149728892  402 KQIQSL 407
Cdd:smart00088  83 ETLKKL 88