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Conserved domains on  [gi|212001672|gb|EEB07332|]
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ubiquitin carboxy terminal hydrolase Ubp3 [Schizosaccharomyces japonicus yFS275]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 10115580)

ubiquitin carboxyl-terminal hydrolase is a C19 family peptidase that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the-terminal Gly of ubiquitin, a 76-residue protein attached to proteins as an intracellular targeting signal

CATH:  2.20.210.10
EC:  3.4.19.12
Gene Ontology:  GO:0004843|GO:0016579
SCOP:  4003158

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
252-520 5.82e-49

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


:

Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 169.59  E-value: 5.82e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 252 EQEDAEEFLNLFLDEMHEEFVRTGNLEKASSPNadavdkdkedkeeegwlevgkkqkpvitrsatvsHSPITEIFGGQLR 331
Cdd:cd02257   21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL----------------------------------KSLIHDLFGGKLE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 332 SVLK---VPNARDSVLLEPYQPLPLDIQPDHIHSVLDAMDHLTTPETLKG---WRSPKGHTVTATKQVFIEKLPAVLILH 405
Cdd:cd02257   67 STIVcleCGHESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGdncYKCEKKKKQEATKRLKIKKLPPVLIIH 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 406 LKRFLYDDQaGGTLKNTKLISYPLRLEIP---TRVISPGKRPLGPARYQLTAVVYHHGLSAQGGHYTVDVHQHDGSSWIR 482
Cdd:cd02257  147 LKRFSFNED-GTKEKLNTKVSFPLELDLSpylSEGEKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYK 225
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 212001672 483 IDDTTIRTISESDVEvteneatvnSSASSDRCAYLLFY 520
Cdd:cd02257  226 FNDDKVTEVSEEEVL---------EFGSLSSSAYILFY 254
 
Name Accession Description Interval E-value
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
252-520 5.82e-49

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 169.59  E-value: 5.82e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 252 EQEDAEEFLNLFLDEMHEEFVRTGNLEKASSPNadavdkdkedkeeegwlevgkkqkpvitrsatvsHSPITEIFGGQLR 331
Cdd:cd02257   21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL----------------------------------KSLIHDLFGGKLE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 332 SVLK---VPNARDSVLLEPYQPLPLDIQPDHIHSVLDAMDHLTTPETLKG---WRSPKGHTVTATKQVFIEKLPAVLILH 405
Cdd:cd02257   67 STIVcleCGHESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGdncYKCEKKKKQEATKRLKIKKLPPVLIIH 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 406 LKRFLYDDQaGGTLKNTKLISYPLRLEIP---TRVISPGKRPLGPARYQLTAVVYHHGLSAQGGHYTVDVHQHDGSSWIR 482
Cdd:cd02257  147 LKRFSFNED-GTKEKLNTKVSFPLELDLSpylSEGEKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYK 225
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 212001672 483 IDDTTIRTISESDVEvteneatvnSSASSDRCAYLLFY 520
Cdd:cd02257  226 FNDDKVTEVSEEEVL---------EFGSLSSSAYILFY 254
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
160-520 1.30e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 170.32  E-value: 1.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672  160 RGFVNTSNMCFMNSIFQALLYCVPFyvlmRNLGKKLPRLFRDKGSLLGSVIT--LTQEFRENWQPGEEEgdAYIPEVVYR 237
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPF----RDYLLRISPLSEDSRYNKDINLLcaLRDLFKALQKNSKSS--SVSPKMFKK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672  238 VM-KNNPRFdlvQTGEQEDAEEFLNLFLDEMHEEFVRTGNLEKASspnadavdkdkedkeeegwlevgkkqkpvitrsat 316
Cdd:pfam00443  75 SLgKLNPDF---SGYKQQDAQEFLLFLLDGLHEDLNGNHSTENES----------------------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672  317 vshsPITEIFGGQLRSVLKVPN-ARDSVLLEPYQPLPLDIQPD----HIHSVLDAMDHLTTPETLKG---WRSPKGH-TV 387
Cdd:pfam00443 117 ----LITDLFRGQLKSRLKCLScGEVSETFEPFSDLSLPIPGDsaelKTASLQICFLQFSKLEELDDeekYYCDKCGcKQ 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672  388 TATKQVFIEKLPAVLILHLKRFLYDdqAGGTLKNTKLISYPLRLEIpTRVISPGKRPLGPAR--YQLTAVVYHHGlSAQG 465
Cdd:pfam00443 193 DAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDL-SRYLAEELKPKTNNLqdYRLVAVVVHSG-SLSS 268
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 212001672  466 GHYTVDVHQHDGSSWIRIDDTTIRTISESDVEVTENeatvnssassdrcAYLLFY 520
Cdd:pfam00443 269 GHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSSS-------------AYILFY 310
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
161-522 7.58e-20

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 89.86  E-value: 7.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 161 GFVNTSNMCFMNSIFQALLYcvpfyvlmrnlgkKLPRLFRDKGSLLGSVITLTQEFRENWQPGEEEGDAYIPEVVyrVMK 240
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAL-------------YLPKLDELLDDLSKELKVLKNVIRKPEPDLNQEEALKLFTAL--WSS 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 241 NNPRFD-LVQTGEQEDAEEFLNLFLDEMHEEFVRTGNLEKAsspnadavdkdkedkeeegwlevgkkqkpvITRSATVSH 319
Cdd:COG5533   66 KEHKVGwIPPMGSQEDAHELLGKLLDELKLDLVNSFTIRIF------------------------------KTTKDKKKT 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 320 SpITEIFggqlrsvlkvpnardSVLLEPYQPLPLDIQPDhIHSVLDAMDHLTTPETLKGWRSPKGHTVTATKQ--VFIEK 397
Cdd:COG5533  116 S-TGDWF---------------DIIIELPDQTWVNNLKT-LQEFIDNMEELVDDETGVKAKENEELEVQAKQEyeVSFVK 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 398 LPAVLILHLKRFLYDdqaGGTLKNTKLISYPLRLEIPTRVISPGKRPLgpaRYQLTAVVYHHGlSAQGGHYTVDVHQhdG 477
Cdd:COG5533  179 LPKILTIQLKRFANL---GGNQKIDTEVDEKFELPVKHDQILNIVKET---YYDLVGFVLHQG-SLEGGHYIAYVKK--G 249
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 212001672 478 SSWIRIDDTTIRTISESDVevtENEATVNssassdrcAYLLFYTR 522
Cdd:COG5533  250 GKWEKANDSDVTPVSEEEA---INEKAKN--------AYLYFYER 283
 
Name Accession Description Interval E-value
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
252-520 5.82e-49

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 169.59  E-value: 5.82e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 252 EQEDAEEFLNLFLDEMHEEFVRTGNLEKASSPNadavdkdkedkeeegwlevgkkqkpvitrsatvsHSPITEIFGGQLR 331
Cdd:cd02257   21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL----------------------------------KSLIHDLFGGKLE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 332 SVLK---VPNARDSVLLEPYQPLPLDIQPDHIHSVLDAMDHLTTPETLKG---WRSPKGHTVTATKQVFIEKLPAVLILH 405
Cdd:cd02257   67 STIVcleCGHESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGdncYKCEKKKKQEATKRLKIKKLPPVLIIH 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 406 LKRFLYDDQaGGTLKNTKLISYPLRLEIP---TRVISPGKRPLGPARYQLTAVVYHHGLSAQGGHYTVDVHQHDGSSWIR 482
Cdd:cd02257  147 LKRFSFNED-GTKEKLNTKVSFPLELDLSpylSEGEKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYK 225
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 212001672 483 IDDTTIRTISESDVEvteneatvnSSASSDRCAYLLFY 520
Cdd:cd02257  226 FNDDKVTEVSEEEVL---------EFGSLSSSAYILFY 254
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
160-520 1.30e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 170.32  E-value: 1.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672  160 RGFVNTSNMCFMNSIFQALLYCVPFyvlmRNLGKKLPRLFRDKGSLLGSVIT--LTQEFRENWQPGEEEgdAYIPEVVYR 237
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPF----RDYLLRISPLSEDSRYNKDINLLcaLRDLFKALQKNSKSS--SVSPKMFKK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672  238 VM-KNNPRFdlvQTGEQEDAEEFLNLFLDEMHEEFVRTGNLEKASspnadavdkdkedkeeegwlevgkkqkpvitrsat 316
Cdd:pfam00443  75 SLgKLNPDF---SGYKQQDAQEFLLFLLDGLHEDLNGNHSTENES----------------------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672  317 vshsPITEIFGGQLRSVLKVPN-ARDSVLLEPYQPLPLDIQPD----HIHSVLDAMDHLTTPETLKG---WRSPKGH-TV 387
Cdd:pfam00443 117 ----LITDLFRGQLKSRLKCLScGEVSETFEPFSDLSLPIPGDsaelKTASLQICFLQFSKLEELDDeekYYCDKCGcKQ 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672  388 TATKQVFIEKLPAVLILHLKRFLYDdqAGGTLKNTKLISYPLRLEIpTRVISPGKRPLGPAR--YQLTAVVYHHGlSAQG 465
Cdd:pfam00443 193 DAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDL-SRYLAEELKPKTNNLqdYRLVAVVVHSG-SLSS 268
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 212001672  466 GHYTVDVHQHDGSSWIRIDDTTIRTISESDVEVTENeatvnssassdrcAYLLFY 520
Cdd:pfam00443 269 GHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSSS-------------AYILFY 310
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
159-520 4.91e-38

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 141.64  E-value: 4.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 159 PRGFVNTSNMCFMNSIFQALLYCVPF--YVLMRNLGKKLPRlfrDKGSLLGSVITLTQEFRENwqpgeeEGDAYIPEVVY 236
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLanYLLSREHSKDCCN---EGFCMMCALEAHVERALAS------SGPGSAPRIFS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 237 RVMKN-NPRFdlvQTGEQEDAEEFLNLFLDEMHeefvrtgnleKASSPNadavdkdkedkeeegwlevGKKQKPVITRSA 315
Cdd:cd02661   72 SNLKQiSKHF---RIGRQEDAHEFLRYLLDAMQ----------KACLDR-------------------FKKLKAVDPSSQ 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 316 TVShsPITEIFGGQLRSVLKVPNAR-DSVLLEPYQPLPLDIQPDHihSVLDAMDHLTTPETLKG---WRSPK-GHTVTAT 390
Cdd:cd02661  120 ETT--LVQQIFGGYLRSQVKCLNCKhVSNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGenkYKCERcKKKVKAS 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 391 KQVFIEKLPAVLILHLKRFlyddQAGGTLKNTKLISYPLRLEIPTRVISPGKrplGPARYQLTAVVYHHGLSAQGGHYTV 470
Cdd:cd02661  196 KQLTIHRAPNVLTIHLKRF----SNFRGGKINKQISFPETLDLSPYMSQPND---GPLKYKLYAVLVHSGFSPHSGHYYC 268
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 212001672 471 DVHQHDGsSWIRIDDTTIRTISESDVevteneatvnssaSSDRcAYLLFY 520
Cdd:cd02661  269 YVKSSNG-KWYNMDDSKVSPVSIETV-------------LSQK-AYILFY 303
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
252-521 5.44e-33

A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 125.48  E-value: 5.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 252 EQEDAEEFLNLFLDEMHeefvrtgnlekasspnadavdkdkedkeeegwlevgkkqkpvitrsatvshSPITEIFGGQLR 331
Cdd:cd02674   21 DQQDAQEFLLFLLDGLH---------------------------------------------------SIIVDLFQGQLK 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 332 SVLKVPNA-RDSVLLEPYQPLPLDI-----QPDHIhSVLDAMDHLTTPETLKG---WRSPKGHTVT-ATKQVFIEKLPAV 401
Cdd:cd02674   50 SRLTCLTCgKTSTTFEPFTYLSLPIpsgsgDAPKV-TLEDCLRLFTKEETLDGdnaWKCPKCKKKRkATKKLTISRLPKV 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 402 LILHLKRFLYDDqaGGTLKNTKLISYPLRLEIPTRVISPGkRPLGPARYQLTAVVYHHGlSAQGGHYTVDVHQHDGSSWI 481
Cdd:cd02674  129 LIIHLKRFSFSR--GSTRKLTTPVTFPLNDLDLTPYVDTR-SFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNETNDWY 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 212001672 482 RIDDTTIRTISESDVevteneatVNSSassdrcAYLLFYT 521
Cdd:cd02674  205 KFDDSRVTKVSESSV--------VSSS------AYILFYE 230
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
160-521 6.11e-31

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 122.48  E-value: 6.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 160 RGFVNTSNMCFMNSIFQALLYcVPfyvLMRN--LGKKLPRLFRDKGSLLGSVITLTQEFRENWQPGEEEGdaYIP-EVVY 236
Cdd:cd02660    1 RGLINLGATCFMNVILQALLH-NP---LLRNyfLSDRHSCTCLSCSPNSCLSCAMDEIFQEFYYSGDRSP--YGPiNLLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 237 RVMKNNPrfDLVQTGEQeDAEEFLNLFLDEMHEEFVrtGNLEKASSPNAdavdkdkedkeeegwlevgkkqkpvitrsat 316
Cdd:cd02660   75 LSWKHSR--NLAGYSQQ-DAHEFFQFLLDQLHTHYG--GDKNEANDESH------------------------------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 317 vSHSPITEIFGGQLRSVL------KVPNARDsvllePYQPLPLDIQPDHIHSVLDAMDHLTTPETLKG-----WRSPK-- 383
Cdd:cd02660  119 -CNCIIHQTFSGSLQSSVtcqrcgGVSTTVD-----PFLDLSLDIPNKSTPSWALGESGVSGTPTLSDcldrfTRPEKlg 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 384 ---------GHTVTATKQVFIEKLPAVLILHLKRFLYdDQAGGTLKNTKLISYPLRL--------EIPTRVISPGKRPLg 446
Cdd:cd02660  193 dfaykcsgcGSTQEATKQLSIKKLPPVLCFQLKRFEH-SLNKTSRKIDTYVQFPLELnmtpytssSIGDTQDSNSLDPD- 270
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212001672 447 pARYQLTAVVYHHGlSAQGGHYTVDVHQHDGsSWIRIDDTTIRTISESDVEVTEneatvnssassdrcAYLLFYT 521
Cdd:cd02660  271 -YTYDLFAVVVHKG-TLDTGHYTAYCRQGDG-QWFKFDDAMITRVSEEEVLKSQ--------------AYLLFYH 328
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
161-521 3.94e-26

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 108.17  E-value: 3.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 161 GFVNTSNMCFMNSIFQALLYCVPFYVLmrnlgKKLPRLFRDKGSLLGSVITltQEFrenwqpgeeegdayipevVYRVMK 240
Cdd:cd02663    1 GLENFGNTCYCNSVLQALYFENLLTCL-----KDLFESISEQKKRTGVISP--KKF------------------ITRLKR 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 241 NNPRFDlvqTGEQEDAEEFLNLFLDEMHEefvrtgNLEKASSPNAdavdkdkedkeeegwlevgKKQKPVITRSATVSHS 320
Cdd:cd02663   56 ENELFD---NYMHQDAHEFLNFLLNEIAE------ILDAERKAEK-------------------ANRKLNNNNNAEPQPT 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 321 PITEIFGGQLRSVLKVPN-----ARDsvllEPYQPLPLDIQPDHihSVLDAMDHLTTPETLKGwrSPKGHTVT------A 389
Cdd:cd02663  108 WVHEIFQGILTNETRCLTcetvsSRD----ETFLDLSIDVEQNT--SITSCLRQFSATETLCG--RNKFYCDEccslqeA 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 390 TKQVFIEKLPAVLILHLKRFLYDDQAGgtlKNTKL---ISYPLRLeiptRVISPGKRPLGPAR-YQLTAVVYHHGLSAQG 465
Cdd:cd02663  180 EKRMKIKKLPKILALHLKRFKYDEQLN---RYIKLfyrVVFPLEL----RLFNTTDDAENPDRlYELVAVVVHIGGGPNH 252
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 212001672 466 GHYTVDVHQHDGssWIRIDDTTIRTISESDVEvtenEATVNSSASSdrCAYLLFYT 521
Cdd:cd02663  253 GHYVSIVKSHGG--WLLFDDETVEKIDENAVE----EFFGDSPNQA--TAYVLFYQ 300
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
161-524 1.23e-24

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 104.65  E-value: 1.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 161 GFVNTSNMCFMNSIFQALlYCVPFYvlmRNLGKKLPRLFRDKGSllGSVITLTQEFRENWQPGEEEGDAYIPEVVYRVMK 240
Cdd:cd02659    4 GLKNQGATCYMNSLLQQL-YMTPEF---RNAVYSIPPTEDDDDN--KSVPLALQRLFLFLQLSESPVKTTELTDKTRSFG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 241 NNPrfdlVQTGEQEDAEEFLNLFLDEMHEEFVRTGnlekasspnadavdkdkedkeeegwlevgkkQKPVITRsatvshs 320
Cdd:cd02659   78 WDS----LNTFEQHDVQEFFRVLFDKLEEKLKGTG-------------------------------QEGLIKN------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 321 piteIFGGQLRS---VLKVPN--ARDsvllEPYQPLPLDIQPdhIHSVLDAMDHLTTPETLKG----WRSPKGHTVTATK 391
Cdd:cd02659  116 ----LFGGKLVNyiiCKECPHesERE----EYFLDLQVAVKG--KKNLEESLDAYVQGETLEGdnkyFCEKCGKKVDAEK 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 392 QVFIEKLPAVLILHLKRFLYDDQaggTLKNTKL---ISYPLRL--------EIPTRVISPGKRPLGPARYQLTAVVYHHG 460
Cdd:cd02659  186 GVCFKKLPPVLTLQLKRFEFDFE---TMMRIKIndrFEFPLELdmepytekGLAKKEGDSEKKDSESYIYELHGVLVHSG 262
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212001672 461 lSAQGGHYTVDVHQHDGSSWIRIDDTTIRTISESDVEVT--------ENEATVNSSASSDRCAYLLFYTRCE 524
Cdd:cd02659  263 -DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEEcfggeetqKTYDSGPRAFKRTTNAYMLFYERKS 333
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
161-520 3.50e-23

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 99.38  E-value: 3.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 161 GFVNTSNMCFMNSIFQALLYCVpfyvLMRNLGKKLPRLFrdkgsllgsvitltqeFREnwqpgeeegdayipevvyrVMK 240
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTP----ALRELLSETPKEL----------------FSQ-------------------VCR 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 241 NNPRFdlvQTGEQEDAEEFLNLFLDEMheefvrtgnlekasspnadavdkdkedkeeegwlevgkkqKPVITRsatvshs 320
Cdd:cd02667   42 KAPQF---KGYQQQDSHELLRYLLDGL----------------------------------------RTFIDS------- 71
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 321 piteIFGGQLRSVLKVPNARD-SVLLEPYQ--PLPLDIQPDHIHSVLDAMDHLTTPETLKGWRSPKGHTVT-ATKQVFIE 396
Cdd:cd02667   72 ----IFGGELTSTIMCESCGTvSLVYEPFLdlSLPRSDEIKSECSIESCLKQFTEVEILEGNNKFACENCTkAKKQYLIS 147
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 397 KLPAVLILHLKRFLyDDQAGGTLKNTKLISYPLRLEI-----PTRVISPGKRPLgpaRYQLTAVVYHHGLSaQGGHYTVD 471
Cdd:cd02667  148 KLPPVLVIHLKRFQ-QPRSANLRKVSRHVSFPEILDLapfcdPKCNSSEDKSSV---LYRLYGVVEHSGTM-RSGHYVAY 222
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 472 VHQH---------------------DGSSWIRIDDTTIRTISESdvEVTENEatvnssassdrcAYLLFY 520
Cdd:cd02667  223 VKVRppqqrlsdltkskpaadeagpGSGQWYYISDSDVREVSLE--EVLKSE------------AYLLFY 278
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
161-522 7.58e-20

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 89.86  E-value: 7.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 161 GFVNTSNMCFMNSIFQALLYcvpfyvlmrnlgkKLPRLFRDKGSLLGSVITLTQEFRENWQPGEEEGDAYIPEVVyrVMK 240
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAL-------------YLPKLDELLDDLSKELKVLKNVIRKPEPDLNQEEALKLFTAL--WSS 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 241 NNPRFD-LVQTGEQEDAEEFLNLFLDEMHEEFVRTGNLEKAsspnadavdkdkedkeeegwlevgkkqkpvITRSATVSH 319
Cdd:COG5533   66 KEHKVGwIPPMGSQEDAHELLGKLLDELKLDLVNSFTIRIF------------------------------KTTKDKKKT 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 320 SpITEIFggqlrsvlkvpnardSVLLEPYQPLPLDIQPDhIHSVLDAMDHLTTPETLKGWRSPKGHTVTATKQ--VFIEK 397
Cdd:COG5533  116 S-TGDWF---------------DIIIELPDQTWVNNLKT-LQEFIDNMEELVDDETGVKAKENEELEVQAKQEyeVSFVK 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 398 LPAVLILHLKRFLYDdqaGGTLKNTKLISYPLRLEIPTRVISPGKRPLgpaRYQLTAVVYHHGlSAQGGHYTVDVHQhdG 477
Cdd:COG5533  179 LPKILTIQLKRFANL---GGNQKIDTEVDEKFELPVKHDQILNIVKET---YYDLVGFVLHQG-SLEGGHYIAYVKK--G 249
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 212001672 478 SSWIRIDDTTIRTISESDVevtENEATVNssassdrcAYLLFYTR 522
Cdd:COG5533  250 GKWEKANDSDVTPVSEEEA---INEKAKN--------AYLYFYER 283
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
161-520 3.03e-18

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 85.45  E-value: 3.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 161 GFVNTSNMCFMNSIFQALLycvpfyvlmrNLGKKLPRLFRDKGSLLGSVITLTQEFRENW---------------QPGEE 225
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLF----------SIPSFQWRYDDLENKFPSDVVDPANDLNCQLikladgllsgryskpASLKS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 226 EGDAY---I-PEVVYRVM-KNNPRFdlvQTGEQEDAEEFLNLFLDEMHEEFVRTGNLEkassPNaDAVDkdkedkeeegw 300
Cdd:cd02658   71 ENDPYqvgIkPSMFKALIgKGHPEF---STMRQQDALEFLLHLIDKLDRESFKNLGLN----PN-DLFK----------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 301 LEVGKKQKPVITRSATVSHSPITEIfggQLrSVLKVPNARDSVLLEPYQPLPLDiqpdhihsvlDAMDHLTTPETLKGWR 380
Cdd:cd02658  132 FMIEDRLECLSCKKVKYTSELSEIL---SL-PVPKDEATEKEEGELVYEPVPLE----------DCLKAYFAPETIEDFC 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 381 SPKGHTVTATKQVFIEKLPAVLILHLKRFLYddQAGGTlkntklisyPLRLEIPtrVISPGKrpLGPARYQLTAVVYHHG 460
Cdd:cd02658  198 STCKEKTTATKTTGFKTFPDYLVINMKRFQL--LENWV---------PKKLDVP--IDVPEE--LGPGKYELIAFISHKG 262
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212001672 461 LSAQGGHYTVDVHQ--HDGSSWIRIDDTTIrTISESDVEVTENeatvnssassdrcAYLLFY 520
Cdd:cd02658  263 TSVHSGHYVAHIKKeiDGEGKWVLFNDEKV-VASQDPPEMKKL-------------GYIYFY 310
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
161-520 4.73e-18

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 83.57  E-value: 4.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 161 GFVNTSNMCFMNSIFQALLYCvpfyvlmrnlgkklprlfrdkgsllgsvitltQEFREnwqpgeeegdaYIPEVVyrvmk 240
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASL--------------------------------PSLIE-----------YLEEFL----- 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 241 nnprfdlvqtgEQEDAEEFLNLFLDEMHEEFvrtgnlekaSSPnadavdkdkedkeeegwLEVGKKQKPVITRSATVSHS 320
Cdd:cd02662   33 -----------EQQDAHELFQVLLETLEQLL---------KFP-----------------FDGLLASRIVCLQCGESSKV 75
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 321 PITEIFGGQLRsvlkVPNARDsvllepyqplpldiqpDHIHSVLDAMDHLTTPETLKGWRSPKghtvtatKQVFIEKLPA 400
Cdd:cd02662   76 RYESFTMLSLP----VPNQSS----------------GSGTTLEHCLDDFLSTEIIDDYKCDR-------CQTVIVRLPQ 128
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 401 VLILHLKRFLYDDQaGGTLKNTKLISYPLRLEIPtrvispgkrplgpaRYQLTAVVYHHGlSAQGGHYTVDVHQHD---- 476
Cdd:cd02662  129 ILCIHLSRSVFDGR-GTSTKNSCKVSFPERLPKV--------------LYRLRAVVVHYG-SHSSGHYVCYRRKPLfskd 192
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 477 ----------------GSSWIRIDDTTIRTISESDVevteneatVNSSAssdrcAYLLFY 520
Cdd:cd02662  193 kepgsfvrmregpsstSHPWWRISDTTVKEVSESEV--------LEQKS-----AYMLFY 239
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
250-521 1.60e-15

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 77.46  E-value: 1.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 250 TGEQEDAEEFLNLFLDEMHEEfvrtgnLEKASSPNADAVdkdkedkeeegwlevgkkqkpvitrsatvshspITEIFGGQ 329
Cdd:cd02668   85 TGQQQDAQEFSKLFLSLLEAK------LSKSKNPDLKNI---------------------------------VQDLFRGE 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 330 LRSVLK-VPNARDSVLLEPYQPLPLDIQpdhIHSVL-DAMDHLTTPETLKG---WRSPK-GHTVTATKQVFIEKLPAVLI 403
Cdd:cd02668  126 YSYVTQcSKCGRESSLPSKFYELELQLK---GHKTLeECIDEFLKEEQLTGdnqYFCEScNSKTDATRRIRLTTLPPTLN 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 404 LHLKRFLYDDQAGGTLKNTKLISYPLRLEIpTRVISPgkRPLGPARYQLTAVVYHHGLSAQGGHYTVDVHQHDGSSWIRI 483
Cdd:cd02668  203 FQLLRFVFDRKTGAKKKLNASISFPEILDM-GEYLAE--SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKF 279
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 212001672 484 DDTTIRTISESDVEVTENEATVNSSAS-------SDRCAYLLFYT 521
Cdd:cd02668  280 NDEDVEEMPGKPLKLGNSEDPAKPRKSeikkgthSSRTAYMLVYK 324
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
149-520 1.16e-14

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 75.31  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 149 PCIVKKTNIQP-RGFVNTSNMCFMNSIFQALLYCVPFYVLMRNLGkklprlfrdkgSLLGSVITLTQEFRENWQPGEEEG 227
Cdd:cd02671   13 TSCEKRENLLPfVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLV-----------SLISSVEQLQSSFLLNPEKYNDEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 228 DAYIPEVVYRVMKN-NPRFDLVQtgeQEDAEEFLNLFLDEMHEEFvrtgnlekasspnadavdkdkedkeeeGWLEVGKk 306
Cdd:cd02671   82 ANQAPRRLLNALREvNPMYEGYL---QHDAQEVLQCILGNIQELV---------------------------EKDFQGQ- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 307 qkpVITRSATVSHSPITEIFGGQLRSVLKVPNARDSVLLEPYqplplDIQPD---HIHSVLDAMDHLTTPETLKG---WR 380
Cdd:cd02671  131 ---LVLRTRCLECETFTERREDFQDISVPVQESELSKSEESS-----EISPDpktEMKTLKWAISQFASVERIVGedkYF 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 381 SPKGHTVT-ATKQVFIEKLPAVLILHLKRF----LYDDQAGGTLKNTKLISYPLRLEIPTRVISPgKRPLgparYQLTAV 455
Cdd:cd02671  203 CENCHHYTeAERSLLFDKLPEVITIHLKCFaangSEFDCYGGLSKVNTPLLTPLKLSLEEWSTKP-KNDV----YRLFAV 277
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212001672 456 VYHHGLSAQGGHYTVDVhqhdgsSWIRIDDTTIRTISESDVevtenEATVNSSASSDRCAYLLFY 520
Cdd:cd02671  278 VMHSGATISSGHYTAYV------RWLLFDDSEVKVTEEKDF-----LEALSPNTSSTSTPYLLFY 331
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
365-523 1.35e-13

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 73.76  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 365 DAMDHLTTPETL---KGWRSP--KGHTvTATKQVFIEKLPAVLILHLKRFLYDDQAggTLKNTKLISYPL-RLEIPTRVI 438
Cdd:COG5560  679 DCLNEFSKPEQLglsDSWYCPgcKEFR-QASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPIdDLDLSGVEY 755
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 439 SPGKRPLGparYQLTAVVYHHGLSAqGGHYTVDVHQHDGSSWIRIDDTTIRTISESDvevteneaTVNSSassdrcAYLL 518
Cdd:COG5560  756 MVDDPRLI---YDLYAVDNHYGGLS-GGHYTAYARNFANNGWYLFDDSRITEVDPED--------SVTSS------AYVL 817

                 ....*
gi 212001672 519 FYTRC 523
Cdd:COG5560  818 FYRRK 822
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
161-520 1.22e-12

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 69.06  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 161 GFVNTSNMCFMNSIFQALLYCVPF--YVLMRNLGKKLPRLFRDKgSLLGSVITLTQEFRENWQPGEEEGDAYIPEVVyrv 238
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFrrQVLSLNLPRLGDSQSVMK-KLQLLQAHLMHTQRRAEAPPDYFLEASRPPWF--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 239 mknNPRFdlvqtgeQEDAEEFLNLFLDEMHeefvrtgnlekasspnadavdkdkedkeeegwlevgkkqkpvitrsatvs 318
Cdd:cd02664   77 ---TPGS-------QQDCSEYLRYLLDRLH-------------------------------------------------- 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 319 hSPITEIFGGQLRSVLKVPNARD-SVLLEPYQPLPLDIQpdhihSVLDAMDHLTTPETLKG---WRSPKGHTV-TATKQV 393
Cdd:cd02664   97 -TLIEKMFGGKLSTTIRCLNCNStSARTERFRDLDLSFP-----SVQDLLNYFLSPEKLTGdnqYYCEKCASLqDAEKEM 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 394 FIEKLPAVLILHLKRFLYDDQAGGTLKNTKLISYPLRLEIPTRVISPGKRPLG----------------PARYQLTAVVY 457
Cdd:cd02664  171 KVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVESKSSESPLekkeeesgddgelvtrQVHYRLYAVVV 250
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 458 HHGLSAQGGHY--------TVDVHQHDGS------------SWIRIDDTtirTISESDVEVTENeatVNSSASSDrCAYL 517
Cdd:cd02664  251 HSGYSSESGHYftyardqtDADSTGQECPepkdaeendeskNWYLFNDS---RVTFSSFESVQN---VTSRFPKD-TPYI 323

                 ...
gi 212001672 518 LFY 520
Cdd:cd02664  324 LFY 326
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
161-520 1.35e-11

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 65.43  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 161 GFVNTSNMCFMNSIFQALlYCVPfyvlmrNLGKKLPRLFRDKGSLLGSVITLTQEFRENWQPGEEEGDAYIPEVVYRVM- 239
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCL-RSVP------ELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLr 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 240 KNNPRFdlVQTGE-----QEDAEEFLNlfldemheEFVRTGNLEkasspnadavdkdkedkeeegwLEVGKKQKPVITRs 314
Cdd:cd02657   74 MAFPQF--AEKQNqggyaQQDAEECWS--------QLLSVLSQK----------------------LPGAGSKGSFIDQ- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 315 atvshspiteIFGGQLRSVLKVPNARD--SVLLEPYQPLPLDIQPDHIHSVLDAMDHLTTPETLKGWRSPKGHTVTATKQ 392
Cdd:cd02657  121 ----------LFGIELETKMKCTESPDeeEVSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKT 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 393 VFIEKLPAVLILHLKRFLYDDQAGGTLKNTKLISYPLRLEIpTRVISPGkrplgpARYQLTAVVYHHGLSAQGGHYTVDV 472
Cdd:cd02657  191 SRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDL-YELCTPS------GYYELVAVITHQGRSADSGHYVAWV 263
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 212001672 473 HQHDGSSWIRIDDttirtiseSDV-EVTENEATVNSSASSDRCAYLLFY 520
Cdd:cd02657  264 RRKNDGKWIKFDD--------DKVsEVTEEDILKLSGGGDWHIAYILLY 304
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
145-500 8.08e-11

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 64.26  E-value: 8.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 145 KQFVPCIVKKTNIQPRGFVNtsnmcfmnSIFQALLYCVPFyvlmRN---LGKKLPRLFRDKGSLLGSVITLTqefRENWQ 221
Cdd:cd02669  113 KPYLPGFVGLNNIKNNDYAN--------VIIQALSHVKPI----RNfflLYENYENIKDRKSELVKRLSELI---RKIWN 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 222 PGEEEGDAYIPEVVYRVMK-NNPRFdlvQTGEQEDAEEFLNLFLDEMHEEfvrtgnLEKASSPNADAVDKDKEdkeeeGW 300
Cdd:cd02669  178 PRNFKGHVSPHELLQAVSKvSKKKF---SITEQSDPVEFLSWLLNTLHKD------LGGSKKPNSSIIHDCFQ-----GK 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 301 LEVgKKQKpvITRSATVSHSpiteifggqlRSVLKVPNARDSVLLEPYQPLPLDIQPDHIHSvlDAMDHLTTP-----ET 375
Cdd:cd02669  244 VQI-ETQK--IKPHAEEEGS----------KDKFFKDSRVKKTSVSPFLLLTLDLPPPPLFK--DGNEENIIPqvplkQL 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 376 LKGWRSPKGHTVTATKQVF-IEKLPAVLILHLKRFlyDDQAGGTLKNTKLISYPLRLEIPTRVISPGKRPLGP-ARYQLT 453
Cdd:cd02669  309 LKKYDGKTETELKDSLKRYlISRLPKYLIFHIKRF--SKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLsTKYNLV 386
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 212001672 454 AVVYHHGLSAQGGHYTVDVHQHDGSSWIRIDDTTIRTISESDVEVTE 500
Cdd:cd02669  387 ANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSE 433
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
395-520 8.89e-09

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 56.38  E-value: 8.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 395 IEKLPAVLILHLKRFLYDDQAGGTLKNTKLISYPLRLEIPTrvispgkrplgparYQLTAVVYHHGLSAQGGHY-TVDVH 473
Cdd:cd02673  143 IMTFPECLSINLKRYKLRIATSDYLKKNEEIMKKYCGTDAK--------------YSLVAVICHLGESPYDGHYiAYTKE 208
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 212001672 474 QHDGSSWIRIDDTTIRTISESDVevteneatvnsSASSDRCAYLLFY 520
Cdd:cd02673  209 LYNGSSWLYCSDDEIRPVSKNDV-----------STNARSSGYLIFY 244
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
161-496 9.57e-08

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 54.88  E-value: 9.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672  161 GFVNTSNMCFMNSIFQALLYCVPFyvlmRNLGKKLPRlfrDKGSLLGSVITLTQEFRENWQPGEEegdayiPEVVYRVMK 240
Cdd:COG5077   195 GLRNQGATCYMNSLLQSLFFIAKF----RKDVYGIPT---DHPRGRDSVALALQRLFYNLQTGEE------PVDTTELTR 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672  241 NNPRFDLVQTgEQEDAEEFLNLFLDemheefvrtgNLEKasspnadavdkdkedkeeegwlevgKKQKpvitrsaTVSHS 320
Cdd:COG5077   262 SFGWDSDDSF-MQHDIQEFNRVLQD----------NLEK-------------------------SMRG-------TVVEN 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672  321 PITEIFGGQLRSVLKVPNA-RDSVLLEPYQPLPLDIQpdHIHSVLDAMDHLTTPETLKG---WRSPKGHTVTATKQVFIE 396
Cdd:COG5077   299 ALNGIFVGKMKSYIKCVNVnYESARVEDFWDIQLNVK--GMKNLQESFRRYIQVETLDGdnrYNAEKHGLQDAKKGVIFE 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672  397 KLPAVLILHLKRFLYDDQAGGTLKNTKLISYPLRLEIPTRVISPGKRPL-GPARYQLTAVVYHHGlSAQGGHYTVDVHQH 475
Cdd:COG5077   377 SLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRDADKSEnSDAVYVLYGVLVHSG-DLHEGHYYALLKPE 455
                         330       340
                  ....*....|....*....|.
gi 212001672  476 DGSSWIRIDDTTIRTISESDV 496
Cdd:COG5077   456 KDGRWYKFDDTRVTRATEKEV 476
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
382-520 1.27e-05

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 46.40  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 382 PKGHTVTATKQVFIEKLPAVLILHLKRFLYDDQAGGTLKNtklisyplRLEIPtrvispgkRPLGPARYQLTAVVYHHGl 461
Cdd:cd02665  112 PSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPEKIHD--------KLEFP--------QIIQQVPYELHAVLVHEG- 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 212001672 462 SAQGGHYTVDVHQHDGSSWIRIDDttiRTISESDVEVTENEATVNSSASSdrcAYLLFY 520
Cdd:cd02665  175 QANAGHYWAYIYKQSRQEWEKYND---ISVTESSWEEVERDSFGGGRNPS---AYCLMY 227
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
161-359 3.51e-05

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 46.80  E-value: 3.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 161 GFVNTSNMCFMNSIFQALLYCVPF--YVLMRNLGKKLPRlfrdkGSLLGSVITLTQEFRENWQPGEEEGDAYIPEVVYRv 238
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTWELrdYFLSDEYEESINE-----ENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFK- 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672 239 mKNNPRFDLVQTG-EQEDAEEFLNLFLDEMHEEFVRTGNLEKASSPNADAVDKdkedkeeegwLEVGKKQKPVITRSATV 317
Cdd:COG5560  341 -KTIGSFNEEFSGyDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDD----------VVVKKKAKECWWEHLKR 409
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 212001672 318 SHSPITEIFGGQLRSVLKVPNARD-SVLLEPYQ----PLPLDIQPDH 359
Cdd:COG5560  410 NDSIITDLFQGMYKSTLTCPGCGSvSITFDPFMdltlPLPVSMVWKH 456
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
316-485 2.16e-04

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 43.41  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672  316 TVSHSPITEIFGGQLRSVLKVPN-----ARDSV-----LLEPYQPLPLDIQPdHIHSVLDAMDHLTTPETL-KGW-RSPK 383
Cdd:pfam13423 122 SPAESPLEQLFGIDAETTIRCSNcghesVRESSthvldLIYPRKPSSNNKKP-PNQTFSSILKSSLERETTtKAWcEKCK 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212001672  384 GHTVTATKQVfIEKLPAVLILHLKrfLYDDQAGGTLKNTKLIsyPLRLEIPTRVISPGKRPLgpARYQLTAVVYHHGLSA 463
Cdd:pfam13423 201 RYQPLESRRT-VRNLPPVLSLNAA--LTNEEWRQLWKTPGWL--PPEIGLTLSDDLQGDNEI--VKYELRGVVVHIGDSG 273
                         170       180
                  ....*....|....*....|....*....
gi 212001672  464 QGGHY--TVDV----HQHDG-SSWIRIDD 485
Cdd:pfam13423 274 TSGHLvsFVKVadseLEDPTeSQWYLFND 302
 
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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