|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
183-515 |
1.81e-154 |
|
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: 443.74 E-value: 1.81e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 183 RGIYNAGATCYQNVVLQSFIHNPILRNFYLSDGHQSSN--CDTPHCLSCAMDDMFQDFYALENTNGYTAANILSGFWISE 260
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTClsCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 261 KkafeNLVTTKEQDAHEFFQFLAEELHERNGDGKkPETGSEHSCNCIIHQTYYGKLQSTTTCQNCGGVTNQVQSFLDLSL 340
Cdd:cd02660 81 R----NLAGYSQQDAHEFFQFLLDQLHTHYGGDK-NEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 341 PLENLSQKKSKKAPSRPNgGVLTLQECLDEEYVKSDKCE--YRCNNCNSMQQARRQTSIKRLPNVLAIQLKRFEFKQgrN 418
Cdd:cd02660 156 DIPNKSTPSWALGESGVS-GTPTLSDCLDRFTRPEKLGDfaYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSL--N 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 419 ERAAKIDTPVQFPLQLNMLPYTnrARSAPESKENYELARSCTYDLLSVVVHVGEIDTGHYLSYCRVG-DQWFAFNDHKVE 497
Cdd:cd02660 233 KTSRKIDTYVQFPLELNMTPYT--SSSIGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGdGQWFKFDDAMIT 310
|
330
....*....|....*...
gi 367047331 498 LAQKSDVLNSQAYLLFYI 515
Cdd:cd02660 311 RVSEEEVLKSQAYLLFYH 328
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
183-514 |
1.09e-69 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 225.78 E-value: 1.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 183 RGIYNAGATCYQNVVLQSFIHNPILRNFYLSDGHQSSNC--DTPHCLSCAMDDMFQDFYALENTNGYTAanilSGFWISE 260
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSryNKDINLLCALRDLFKALQKNSKSSSVSP----KMFKKSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 261 KKAFENLVTTKEQDAHEFFQFLAEELHE-RNGDGKKPETgsehscnCIIHQTYYGKLQSTTTCQNCGGVTNQVQSFLDLS 339
Cdd:pfam00443 77 GKLNPDFSGYKQQDAQEFLLFLLDGLHEdLNGNHSTENE-------SLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 340 LPLENLSQKKSkkapsrpnggVLTLQECLDEEYVKSDKCE---YRCNNCNSMQQARRQTSIKRLPNVLAIQLKRFEFKQG 416
Cdd:pfam00443 150 LPIPGDSAELK----------TASLQICFLQFSKLEELDDeekYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 417 RNEraaKIDTPVQFPLQLNMLPYTnrarsAPESKENyeLARSCTYDLLSVVVHVGEIDTGHYLSYCRVGD--QWFAFNDH 494
Cdd:pfam00443 220 TWE---KLNTEVEFPLELDLSRYL-----AEELKPK--TNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYEnnRWYKFDDE 289
|
330 340
....*....|....*....|.
gi 367047331 495 KV-ELAQKSDVLNSQAYLLFY 514
Cdd:pfam00443 290 KVtEVDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
183-515 |
2.78e-63 |
|
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: 208.67 E-value: 2.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 183 RGIYNAGATCYQNVVLQSFIHNPILRNFYLSDGHQSSNCDTPHCLSCAMDDMFQdfYALENTNGYTAANILSgfwiSEKK 262
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVE--RALASSGPGSAPRIFS----SNLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 263 AF-ENLVTTKEQDAHEFFQFLAEELHERNGDGKKPETGSEHSC--NCIIHQTYYGKLQSTTTCQNCGGVTNQVQSFLDLS 339
Cdd:cd02661 76 QIsKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSqeTTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 340 LPLEnlsqkkskkapsrpngGVLTLQECLdEEYVKSDKCE----YRCNNCNSMQQARRQTSIKRLPNVLAIQLKRFEFKQ 415
Cdd:cd02661 156 LDIK----------------GADSLEDAL-EQFTKPEQLDgenkYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 416 GRneraaKIDTPVQFPLQLNMLPYtnrARSAPESkenyelarSCTYDLLSVVVHVG-EIDTGHYLSYCRVGD-QWFAFND 493
Cdd:cd02661 219 GG-----KINKQISFPETLDLSPY---MSQPNDG--------PLKYKLYAVLVHSGfSPHSGHYYCYVKSSNgKWYNMDD 282
|
330 340
....*....|....*....|..
gi 367047331 494 HKVELAQKSDVLNSQAYLLFYI 515
Cdd:cd02661 283 SKVSPVSIETVLSQKAYILFYI 304
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
184-515 |
1.18e-62 |
|
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: 205.41 E-value: 1.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 184 GIYNAGATCYQNVVLQSFIHNpilrnfylsdghqssncdtphclscamddmfqdfyalentngytaanilsgfwisekka 263
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 264 fenlvttkEQDAHEFFQFLAEELHERNGDGKKPETGSEhSCNCIIHQTYYGKLQSTTTCQNCGGVTNQVQSFLDLSLPLE 343
Cdd:cd02257 22 --------QQDAHEFLLFLLDKLHEELKKSSKRTSDSS-SLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 344 NLSQKKSkkapsrpnggvlTLQECLDEEYVKSDKCEYRCNNCN--SMQQARRQTSIKRLPNVLAIQLKRFEFKqgRNERA 421
Cdd:cd02257 93 VKGLPQV------------SLEDCLEKFFKEEILEGDNCYKCEkkKKQEATKRLKIKKLPPVLIIHLKRFSFN--EDGTK 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 422 AKIDTPVQFPLQLNMLPYTNRARSAPESKENyelarSCTYDLLSVVVHVGE-IDTGHYLSYCRVG--DQWFAFNDHKVEL 498
Cdd:cd02257 159 EKLNTKVSFPLELDLSPYLSEGEKDSDSDNG-----SYKYELVAVVVHSGTsADSGHYVAYVKDPsdGKWYKFNDDKVTE 233
|
330 340
....*....|....*....|..
gi 367047331 499 AQKSDVL-----NSQAYLLFYI 515
Cdd:cd02257 234 VSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
271-515 |
1.56e-52 |
|
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: 177.86 E-value: 1.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 271 KEQDAHEFFQFLAEELHErngdgkkpetgsehscncIIHQTYYGKLQSTTTCQNCGGVTNQVQSFLDLSLPLenlsqkks 350
Cdd:cd02674 21 DQQDAQEFLLFLLDGLHS------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPI-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 351 kkAPSRPNGGVLTLQECLDEeYVKSDK----CEYRCNNCNSMQQARRQTSIKRLPNVLAIQLKRFEFKQGrneRAAKIDT 426
Cdd:cd02674 75 --PSGSGDAPKVTLEDCLRL-FTKEETldgdNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRG---STRKLTT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 427 PVQFPLQ-LNMLPYTNRARSAPESKenyelarsctYDLLSVVVHVGEIDTGHYLSYCRVG--DQWFAFNDHKVELAQKSD 503
Cdd:cd02674 149 PVTFPLNdLDLTPYVDTRSFTGPFK----------YDLYAVVNHYGSLNGGHYTAYCKNNetNDWYKFDDSRVTKVSESS 218
|
250
....*....|..
gi 367047331 504 VLNSQAYLLFYI 515
Cdd:cd02674 219 VVSSSAYILFYE 230
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
181-515 |
2.23e-49 |
|
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: 172.83 E-value: 2.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 181 GLRGIYNAGATCYQNVVLQSFIHNPILRNFYLSDGHQSSNCDTPHcLSCAMDDMFQDFYALENTNGYTaanilSGFWISE 260
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKS-VPLALQRLFLFLQLSESPVKTT-----ELTDKTR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 261 KKAFENLVTTKEQDAHEFFQFLAEELherngDGKKPETGSEHscncIIHQTYYGKLQSTTTCQNCGGVTNQVQSFLDLSL 340
Cdd:cd02659 75 SFGWDSLNTFEQHDVQEFFRVLFDKL-----EEKLKGTGQEG----LIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 341 PLENlsqKKSkkapsrpnggvltLQECLDEeYVKSDKCE----YRCNNCNSMQQARRQTSIKRLPNVLAIQLKRFEFKQG 416
Cdd:cd02659 146 AVKG---KKN-------------LEESLDA-YVQGETLEgdnkYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 417 RNERAaKIDTPVQFPLQLNMLPYTNRARSAPESKENYELARSCTYDLLSVVVHVGEIDTGHYLSYCR--VGDQWFAFNDH 494
Cdd:cd02659 209 TMMRI-KINDRFEFPLELDMEPYTEKGLAKKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKdrDDGKWYKFNDD 287
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 367047331 495 KVELAQKSDVLNSQ----------------------AYLLFYI 515
Cdd:cd02659 288 VVTPFDPNDAEEECfggeetqktydsgprafkrttnAYMLFYE 330
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
184-514 |
1.91e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 142.45 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 184 GIYNAGATCYQNVVLQSFIHNPILrnfylsdghqssncdtpHCLScamdDMFQDFyaleNTNGYTAANILSGFWIS---- 259
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLL-----------------TCLK----DLFESI----SEQKKRTGVISPKKFITrlkr 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 260 EKKAFENlvtTKEQDAHEFFQFL----AEELHERNGDGKKPETGSEHSCNCI----IHQTYYGKLQSTTTCQNCGGVTNQ 331
Cdd:cd02663 56 ENELFDN---YMHQDAHEFLNFLlneiAEILDAERKAEKANRKLNNNNNAEPqptwVHEIFQGILTNETRCLTCETVSSR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 332 VQSFLDLSLPLENLSqkkskkapsrpnggvlTLQECL----DEEYVKSDKcEYRCNNCNSMQQARRQTSIKRLPNVLAIQ 407
Cdd:cd02663 133 DETFLDLSIDVEQNT----------------SITSCLrqfsATETLCGRN-KFYCDECCSLQEAEKRMKIKKLPKILALH 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 408 LKRFEFkQGRNERAAKIDTPVQFPLQLNMLPYTNRArsapeskENYELarscTYDLLSVVVHVGE-IDTGHYLSYCRVGD 486
Cdd:cd02663 196 LKRFKY-DEQLNRYIKLFYRVVFPLELRLFNTTDDA-------ENPDR----LYELVAVVVHIGGgPNHGHYVSIVKSHG 263
|
330 340 350
....*....|....*....|....*....|....*.
gi 367047331 487 QWFAFNDHKVELAQKSDVLN--------SQAYLLFY 514
Cdd:cd02663 264 GWLLFDDETVEKIDENAVEEffgdspnqATAYVLFY 299
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
184-514 |
2.92e-37 |
|
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: 138.67 E-value: 2.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 184 GIYNAGATCYQNVVLQSFIHNPILRNFYLsdghqssncDTPHCL---SCAMDDMFQDFyalentngytaanilsgfwise 260
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLS---------ETPKELfsqVCRKAPQFKGY---------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 261 kkafenlvttKEQDAHEFFQFLAEELherngdgkkpetgsehscNCIIHQTYYGKLQSTTTCQNCGGVTNQVQSFLDLSL 340
Cdd:cd02667 50 ----------QQQDSHELLRYLLDGL------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 341 PlenlsqkkSKKAPSRPNggvlTLQECLD---EEYVKSDKCEYRCNNCnsmQQARRQTSIKRLPNVLAIQLKRfeFKQGR 417
Cdd:cd02667 102 P--------RSDEIKSEC----SIESCLKqftEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKR--FQQPR 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 418 NERAAKIDTPVQFPLQLNMLPYTNRARSAPESKENYelarscTYDLLSVVVHVGEIDTGHYLSYCRVG------------ 485
Cdd:cd02667 165 SANLRKVSRHVSFPEILDLAPFCDPKCNSSEDKSSV------LYRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsdltks 238
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 367047331 486 -----------DQWFAFNDHKVELAQKSDVLNSQAYLLFY 514
Cdd:cd02667 239 kpaadeagpgsGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
184-497 |
3.54e-35 |
|
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: 134.09 E-value: 3.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 184 GIYNAGATCYQNVVLQSFIHNPILRN-FYL-----SDGHQSSNCDTPHCLSCAMDDMFQDFYALENTNgytaANIL--SG 255
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKaVYEcnsteDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGN----RSVVdpSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 256 FwiseKKAFEnLVTTKEQDAHEFFQFL-----AEELHERNGDGKKpetgsehscncIIHQTYYGKLQSTTTCQNCGGVTN 330
Cdd:cd02668 77 F----VKALG-LDTGQQQDAQEFSKLFlslleAKLSKSKNPDLKN-----------IVQDLFRGEYSYVTQCSKCGRESS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 331 QVQSFLDLSLPLEnlsqkkskkapsrpngGVLTLQECLDEeYVKSDKCE----YRCNNCNSMQQARRQTSIKRLPNVLAI 406
Cdd:cd02668 141 LPSKFYELELQLK----------------GHKTLEECIDE-FLKEEQLTgdnqYFCESCNSKTDATRRIRLTTLPPTLNF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 407 QLKRFEF--KQGRNEraaKIDTPVQFPLQLNMLPYTNrarsapESKENYelarsCTYDLLSVVVHVG-EIDTGHYLsyCR 483
Cdd:cd02668 204 QLLRFVFdrKTGAKK---KLNASISFPEILDMGEYLA------ESDEGS-----YVYELSGVLIHQGvSAYSGHYI--AH 267
|
330
....*....|....*...
gi 367047331 484 VGD----QWFAFNDHKVE 497
Cdd:cd02668 268 IKDeqtgEWYKFNDEDVE 285
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
176-505 |
4.60e-29 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 121.90 E-value: 4.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 176 SCKANGLRGIYNAGATCYQNVVLQSFIHNPILRN--FYLSDGHQSSNCDTPHCLSCAmddmfqdFYALE------NTNGY 247
Cdd:COG5077 187 SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRGRDSVALALQRL-------FYNLQtgeepvDTTEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 248 TAANIlsgfWISekkafenLVTTKEQDAHEFFQFLAEELhERNGDGKKPETgsehscncIIHQTYYGKLQSTTTCQNCGG 327
Cdd:COG5077 260 TRSFG----WDS-------DDSFMQHDIQEFNRVLQDNL-EKSMRGTVVEN--------ALNGIFVGKMKSYIKCVNVNY 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 328 VTNQVQSFLDLSLPLENLSqkkskkapsrpnggvlTLQECLDEeYVKSDKCEyrCNNC-----NSMQQARRQTSIKRLPN 402
Cdd:COG5077 320 ESARVEDFWDIQLNVKGMK----------------NLQESFRR-YIQVETLD--GDNRynaekHGLQDAKKGVIFESLPP 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 403 VLAIQLKRFEFKQGRNErAAKIDTPVQFPLQLNMLPYTNRARSAPESKEnyelarsCTYDLLSVVVHVGEIDTGHYLSYC 482
Cdd:COG5077 381 VLHLQLKRFEYDFERDM-MVKINDRYEFPLEIDLLPFLDRDADKSENSD-------AVYVLYGVLVHSGDLHEGHYYALL 452
|
330 340
....*....|....*....|....*
gi 367047331 483 RVG--DQWFAFNDHKVELAQKSDVL 505
Cdd:COG5077 453 KPEkdGRWYKFDDTRVTRATEKEVL 477
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
184-514 |
9.41e-29 |
|
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: 115.88 E-value: 9.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 184 GIYNAGATCYQNVVLQSF--IHNPIlRNFYLSDGHQSSNCDTPH-CLSCAM----DDMFQDFYALENTNGYTAANILSGF 256
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLfsIPSFQ-WRYDDLENKFPSDVVDPAnDLNCQLiklaDGLLSGRYSKPASLKSENDPYQVGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 257 WISekkAFENLV--------TTKEQDAHEFFQFLAEELHErngdgkkpETGSEHSCN-------CIIHqtyygKLQsttt 321
Cdd:cd02658 80 KPS---MFKALIgkghpefsTMRQQDALEFLLHLIDKLDR--------ESFKNLGLNpndlfkfMIED-----RLE---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 322 CQNCGGV--TNQVQSFLDLSLPLENLSqKKSKKAPSRPNggvLTLQECLDeEYVKSDKCEYRCNNCNSMQQARRQTSIKR 399
Cdd:cd02658 140 CLSCKKVkyTSELSEILSLPVPKDEAT-EKEEGELVYEP---VPLEDCLK-AYFAPETIEDFCSTCKEKTTATKTTGFKT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 400 LPNVLAIQLKRFEFKQgrNERAAKIDTPVQFPlqlnmlpytnrarsapeskenyELARSCTYDLLSVVVHVG-EIDTGHY 478
Cdd:cd02658 215 FPDYLVINMKRFQLLE--NWVPKKLDVPIDVP----------------------EELGPGKYELIAFISHKGtSVHSGHY 270
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 367047331 479 LSYCR----VGDQWFAFNDHKVELAQKSDVLNSQAYLLFY 514
Cdd:cd02658 271 VAHIKkeidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
159-514 |
6.34e-25 |
|
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: 105.36 E-value: 6.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 159 DPVRDNPTYISANTTAASCKANGLRGIYNAGATCYQNVVLQS------FIHN-PILRNFYLSDGHQSSNCDTPHclscam 231
Cdd:cd02671 1 DQVVPAPQPSSATSCEKRENLLPFVGLNNLGNTCYLNSVLQVlyfcpgFKHGlKHLVSLISSVEQLQSSFLLNP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 232 dDMFQDFYALENTNGYTAAnilsgfwISEKKA-FENlvtTKEQDAHEFFQFLAEELHErngdgkkpetgsehscncIIHQ 310
Cdd:cd02671 75 -EKYNDELANQAPRRLLNA-------LREVNPmYEG---YLQHDAQEVLQCILGNIQE------------------LVEK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 311 TYYGKLQSTTTCQNCGGVTNQVQSFLDLSLPL---ENLSQKKSKKAPSRPNGGVLTLQECL-----DEEYVKSDKceYRC 382
Cdd:cd02671 126 DFQGQLVLRTRCLECETFTERREDFQDISVPVqesELSKSEESSEISPDPKTEMKTLKWAIsqfasVERIVGEDK--YFC 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 383 NNCNSMQQARRQTSIKRLPNVLAIQLKRFEFKQGRNERAA---KIDTPVQFPLQLNMLPYTNRARSApeskenyelarsc 459
Cdd:cd02671 204 ENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYGglsKVNTPLLTPLKLSLEEWSTKPKND------------- 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 367047331 460 TYDLLSVVVHVG-EIDTGHYLSYCRvgdqWFAFNDHKVELAQKSDVLN---------SQAYLLFY 514
Cdd:cd02671 271 VYRLFAVVMHSGaTISSGHYTAYVR----WLLFDDSEVKVTEEKDFLEalspntsstSTPYLLFY 331
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
184-514 |
7.13e-25 |
|
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: 105.27 E-value: 7.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 184 GIYNAGATCYQNVVLQSFIHNPILRNFYLSDGHQSSNCDTPhclscAMDDMFQDFYALENTNGYTAANILSGFWISEKKA 263
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQS-----VMKKLQLLQAHLMHTQRRAEAPPDYFLEASRPPW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 264 FENlvtTKEQDAHEFFQFLAEELHErngdgkkpetgsehscncIIHQTYYGKLQSTTTCQNCGGVTNQVQSFLDLSLPLe 343
Cdd:cd02664 76 FTP---GSQQDCSEYLRYLLDRLHT------------------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 344 nlsqkkskkaPSRPNggVLTLQ---ECLDEEYvksdkcEYRCNNCNSMQQARRQTSIKRLPNVLAIQLKRFEFKQGRNER 420
Cdd:cd02664 134 ----------PSVQD--LLNYFlspEKLTGDN------QYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 421 aAKIDTPVQFPLQLNMLPYTNRARSAPESKENYELARSCT--------YDLLSVVVHVG-EIDTGHYLSYCR-------- 483
Cdd:cd02664 196 -EKIMDNVSINEVLSLPVRVESKSSESPLEKKEEESGDDGelvtrqvhYRLYAVVVHSGySSESGHYFTYARdqtdadst 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 367047331 484 --------------VGDQWFAFNDHKVELAQKSDVLNSQ-------AYLLFY 514
Cdd:cd02664 275 gqecpepkdaeendESKNWYLFNDSRVTFSSFESVQNVTsrfpkdtPYILFY 326
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
190-493 |
1.03e-23 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 101.19 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 190 ATCYQNVVLQSFIHNPILRNFYLSdgHQSSNCDTPHCLSCAMddMFQdFYALENTNGYT--AANILSGF-WISEKKAFeN 266
Cdd:pfam13423 8 PNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCEL--GFL-FDMLEKAKGKNcqASNFLRALsSIPEASAL-G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 267 LVTTKEQDAHE---------FFQFLAEELHeRNGDGKKPETGSEHScncIIHQTYYGKLQSTTTCQNCGGVTNQ--VQSF 335
Cdd:pfam13423 82 LLDEDRETNSAislssliqsFNRFLLDQLS-SEENSTPPNPSPAES---PLEQLFGIDAETTIRCSNCGHESVResSTHV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 336 LDLSLPlenlsqkkSKKAPSRPNGGVLTLQECLdEEYVKSDKcEYR--CNNCNSMQQARRQTSIKRLPNVLAIQLKRFEF 413
Cdd:pfam13423 158 LDLIYP--------RKPSSNNKKPPNQTFSSIL-KSSLERET-TTKawCEKCKRYQPLESRRTVRNLPPVLSLNAALTNE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 414 KQGRNERaakidTPVQFPLQLNMLPYTNRARSAPESKenyelarsctYDLLSVVVHVGEIDT-GHYLSYCRVGD------ 486
Cdd:pfam13423 228 EWRQLWK-----TPGWLPPEIGLTLSDDLQGDNEIVK----------YELRGVVVHIGDSGTsGHLVSFVKVADseledp 292
|
330
....*....|
gi 367047331 487 ---QWFAFND 493
Cdd:pfam13423 293 tesQWYLFND 302
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
270-514 |
9.69e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 97.05 E-value: 9.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 270 TKEQDAHEFFQFLAEELHerngdgKKPETGSEhscnciihqtyyGKLQSTTTCQNCGGVTN-QVQSFLDLSLPLenlsqk 348
Cdd:cd02662 32 LEQQDAHELFQVLLETLE------QLLKFPFD------------GLLASRIVCLQCGESSKvRYESFTMLSLPV------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 349 kskkaPSRPNGGVLTLQECLDEeYVKSDKCE-YRCNNCnsmqqarrQTSIKRLPNVLAIQLKRFEFkQGRNE---RAAKi 424
Cdd:cd02662 88 -----PNQSSGSGTTLEHCLDD-FLSTEIIDdYKCDRC--------QTVIVRLPQILCIHLSRSVF-DGRGTstkNSCK- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 425 dtpVQFPLQLNMLpytnrarsapeskenyelarscTYDLLSVVVHVGEIDTGHYLSY----------------------C 482
Cdd:cd02662 152 ---VSFPERLPKV----------------------LYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmregpS 206
|
250 260 270
....*....|....*....|....*....|...
gi 367047331 483 RVGDQWFAFNDHKVELAQKSDVL-NSQAYLLFY 514
Cdd:cd02662 207 STSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
184-514 |
1.82e-22 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 97.18 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 184 GIYNAGATCYQNVVLQSF-IHNPILRNFYLSDGHQSSncdtphclscAMDDMFQDFYALENTNGYTAAniLSGFWISEKK 262
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKELK----------VLKNVIRKPEPDLNQEEALKL--FTALWSSKEH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 263 AFENLVTTKEQ-DAHEFFQFLAEEL----HERNGDGKKPETGSEHScnciihqTYYGKLQSTTtcqncggVTNQVQSFLD 337
Cdd:COG5533 69 KVGWIPPMGSQeDAHELLGKLLDELkldlVNSFTIRIFKTTKDKKK-------TSTGDWFDII-------IELPDQTWVN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 338 lslplenlSQKkskkapsrpnggvlTLQECLDE-EYVKSDKCEYRC---NNCNSMQQARRQTSIKRLPNVLAIQLKRFEF 413
Cdd:COG5533 135 --------NLK--------------TLQEFIDNmEELVDDETGVKAkenEELEVQAKQEYEVSFVKLPKILTIQLKRFAN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 414 KQGRneraAKIDTPVQFPLQLNMLPytnrarsapesKENYELARSCTYDLLSVVVHVGEIDTGHYLSYCRVGDQWFAFND 493
Cdd:COG5533 193 LGGN----QKIDTEVDEKFELPVKH-----------DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKKGGKWEKAND 257
|
330 340
....*....|....*....|....
gi 367047331 494 HKVELAQKSDVLNS---QAYLLFY 514
Cdd:COG5533 258 SDVTPVSEEEAINEkakNAYLYFY 281
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
362-518 |
4.07e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 97.26 E-value: 4.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 362 LTLQECLDEEYVKSDKCE---YRCNNCNSMQQARRQTSIKRLPNVLAIQLKRFefkQGRNERAAKIDTPVQFPL-QLNML 437
Cdd:COG5560 675 ITLQDCLNEFSKPEQLGLsdsWYCPGCKEFRQASKQMELWRLPMILIIHLKRF---SSVRSFRDKIDDLVEYPIdDLDLS 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 438 PYTNrarsapeSKENYELArsctYDLLSVVVHVGEIDTGHYLSYCRVGD--QWFAFNDHKVELAQKSDVLNSQAYLLFYI 515
Cdd:COG5560 752 GVEY-------MVDDPRLI----YDLYAVDNHYGGLSGGHYTAYARNFAnnGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820
|
...
gi 367047331 516 VRS 518
Cdd:COG5560 821 RKS 823
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
184-514 |
2.74e-20 |
|
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: 91.24 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 184 GIYNAGATCYQNVVLQSFIHNPILRNFYL-SDGHQSSNCDTPHCLSCAMDDMFQDfyaLENTngyTAANILSGFWISEKK 262
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKnYNPARRGANQSSDNLTNALRDLFDT---MDKK---QEPVPPIEFLQLLRM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 263 AFENLVTT------KEQDAHEFFQFLAEEL-HERNGDGKKPETgsehscnciIHQTYYGKLQSTTTCQ-NCGGVTNQVQS 334
Cdd:cd02657 75 AFPQFAEKqnqggyAQQDAEECWSQLLSVLsQKLPGAGSKGSF---------IDQLFGIELETKMKCTeSPDEEEVSTES 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 335 FLDLSLpleNLSQKKSkkapsrpnggVLTLQECLDEEYVKSDKCEYRCNNCNSMQQarRQTSIKRLPNVLAIQLKRFEFK 414
Cdd:cd02657 146 EYKLQC---HISITTE----------VNYLQDGLKKGLEEEIEKHSPTLGRDAIYT--KTSRISRLPKYLTVQFVRFFWK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 415 QGRNERaAKIDTPVQFPLQLNMLPYtnrarsapeskenyeLARSCTYDLLSVVVHVG-EIDTGHYLSYCRV--GDQWFAF 491
Cdd:cd02657 211 RDIQKK-AKILRKVKFPFELDLYEL---------------CTPSGYYELVAVITHQGrSADSGHYVAWVRRknDGKWIKF 274
|
330 340 350
....*....|....*....|....*....|
gi 367047331 492 NDHKVELAQKSDVLN-------SQAYLLFY 514
Cdd:cd02657 275 DDDKVSEVTEEDILKlsgggdwHIAYILLY 304
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
180-514 |
8.35e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 66.96 E-value: 8.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 180 NGLRGIYNAGATCYQNVVLQSFIHNPILRNFYLSDGHQSSNCDTPHCLSCAMDDMFQDFYALENTNGYTAA-NILSGFWI 258
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRLSELIRKIWNPRNFKGHVSPhELLQAVSK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 259 SEKKAFENlvtTKEQDAHEFFQFLAEELHERNGDGKKPETGsehscncIIHQTYYGKLQSTTT-------------CQNC 325
Cdd:cd02669 197 VSKKKFSI---TEQSDPVEFLSWLLNTLHKDLGGSKKPNSS-------IIHDCFQGKVQIETQkikphaeeegskdKFFK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 326 GGVTNQVQS----FLDLSLPLENLSqKKSKKAPSRPNggvLTLQECLDeeyvKSDKCEYRCNNCNSMQQarrqtSIKRLP 401
Cdd:cd02669 267 DSRVKKTSVspflLLTLDLPPPPLF-KDGNEENIIPQ---VPLKQLLK----KYDGKTETELKDSLKRY-----LISRLP 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 402 NVLAIQLKRFE---FKQGRNEraakidTPVQFPLQLNMLPYTnrarsapESKENYELARSCTYDLLSVVVHVGEIDT-GH 477
Cdd:cd02669 334 KYLIFHIKRFSknnFFKEKNP------TIVNFPIKNLDLSDY-------VHFDKPSLNLSTKYNLVANIVHEGTPQEdGT 400
|
330 340 350
....*....|....*....|....*....|....*....
gi 367047331 478 YLSYCR--VGDQWFAFNDHKVELAQKSDVLNSQAYLLFY 514
Cdd:cd02669 401 WRVQLRhkSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
262-514 |
5.17e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 62.93 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 262 KAFENLVTTKEQDAHEFFQFLAE---ELHERNGDGKKPETGSEHSCNCIIHQTYygKLQSTTTCQNCGGVTNQVQSFLDL 338
Cdd:cd02673 23 KINTEFDNDDQQDAHEFLLTLLEaidDIMQVNRTNVPPSNIEIKRLNPLEAFKY--TIESSYVCIGCSFEENVSDVGNFL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 339 SLPLENLSqkkskkapsrpnggvLTLQECLDEEYVKSDKCEYRCNNCNSmQQARRQTSIKRLPNVLAIQLKRFEFKQGRN 418
Cdd:cd02673 101 DVSMIDNK---------------LDIDELLISNFKTWSPIEKDCSSCKC-ESAISSERIMTFPECLSINLKRYKLRIATS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 419 EraakidtpvqfplqlnmlpytnrarsapESKENYELARSCT-----YDLLSVVVHVGE-IDTGHYLSYCR---VGDQWF 489
Cdd:cd02673 165 D----------------------------YLKKNEEIMKKYCgtdakYSLVAVICHLGEsPYDGHYIAYTKelyNGSSWL 216
|
250 260
....*....|....*....|....*...
gi 367047331 490 AFNDHKVELAQKSDVLN---SQAYLLFY 514
Cdd:cd02673 217 YCSDDEIRPVSKNDVSTnarSSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
364-515 |
7.41e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 56.41 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 364 LQECLDEEYVKSDKCEYRCNNCNSMQQARRQTSikrLPNVLAIQLKRFEFKQGRNEraaKIDTPVQFPLQLNMLPYtnra 443
Cdd:cd02665 95 LHECLEAAMFEGEVELLPSDHSVKSGQERWFTE---LPPVLTFELSRFEFNQGRPE---KIHDKLEFPQIIQQVPY---- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 444 rsapeskenyelarsctyDLLSVVVHVGEIDTGHYLSYC--RVGDQWFAFNDHKVELAQKSDV--------LNSQAYLLF 513
Cdd:cd02665 165 ------------------ELHAVLVHEGQANAGHYWAYIykQSRQEWEKYNDISVTESSWEEVerdsfgggRNPSAYCLM 226
|
..
gi 367047331 514 YI 515
Cdd:cd02665 227 YI 228
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
354-514 |
2.91e-08 |
|
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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 54.46 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 354 PSRPNGGVLTLQECLDEEYVKSDkceyrcnncnsmqqarrqtsIKRLPNVLAIQLKRFEFKQGrneRAAKIDTPVQFPLQ 433
Cdd:cd02670 72 PDDDDGGGITLEQCLEQYFNNSV--------------------FAKAPSCLIICLKRYGKTEG---KAQKMFKKILIPDE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 434 LNMLPY---TNRARS-----APESKENYELARSC---TYDLLSVVVHVG-EIDTGHYLSYCRVG-------------DQW 488
Cdd:cd02670 129 IDIPDFvadDPRACSkcqleCRVCYDDKDFSPTCgkfKLSLCSAVCHRGtSLETGHYVAFVRYGsysltetdneaynAQW 208
|
170 180 190
....*....|....*....|....*....|..
gi 367047331 489 FAFNDHKVE--LAQKSDV----LNSQAYLLFY 514
Cdd:cd02670 209 VFFDDMADRdgVSNGFNIpaarLLEDPYMLFY 240
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
184-515 |
7.42e-08 |
|
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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 54.42 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 184 GIYNAGATCYQNVVLQS-FIHNPiLRNFYLSdgHQSSNCDTphclscaMDDMFQDfyALENTNGYTAANILSG--FWISE 260
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYfFTIKP-LRDLVLN--FDESKAEL-------ASDYPTE--RRIGGREVSRSELQRSnqFVYEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 261 KKAFENLVTTKE----------------QDAHE-----FFQFLAEELHERNGD-GKKPETGSEHscNCIIHQTYYGKLQS 318
Cdd:cd02666 71 RSLFNDLIHSNTrsvtpskelaylalrqQDVTEcidnvLFQLEVALEPISNAFaGPDTEDDKEQ--SDLIKRLFSGKTKQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 319 TTTCQNCG---GVTNQVQSFLdlSLPLENLSqkksKKAPSRPNGGVLTLQECLDEeYVKSDkceyrcnncnsmqqarrqt 395
Cdd:cd02666 149 QLVPESMGnqpSVRTKTERFL--SLLVDVGK----KGREIVVLLEPKDLYDALDR-YFDYD------------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 396 SIKRLPNVLAIQLKRFEFKQGRNERAAKIDTPVQFPLQLNMLPYTNRARSAPESKENYELA-------------RSCTYD 462
Cdd:cd02666 203 SLTKLPQRSQVQAQLAQPLQRELISMDRYELPSSIDDIDELIREAIQSESSLVRQAQNELAelkheiekqfddlKSYGYR 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 367047331 463 LLSVVVHVGEIDTGHYLSYCRVGDQ--WFAFNDHKVELAQKSDVLN------SQAYLLFYI 515
Cdd:cd02666 283 LHAVFIHRGEASSGHYWVYIKDFEEnvWRKYNDETVTVVPASEVFLftlgntATPYFLVYV 343
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
308-514 |
9.46e-06 |
|
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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 47.51 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 308 IHQTYYGKLQSTTTCQnCGGVTNQVQSFLDLSLPLENLSQKkskkAPSRPNGGVLTLQECLDEEYVKSDKCEYRCNNCNS 387
Cdd:cd02672 68 LIQNFTRFLLETISQD-QLGTPFSCGTSRNSVSLLYTLSLP----LGSTKTSKESTFLQLLKRSLDLEKVTKAWCDTCCK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367047331 388 MQQARRQTSIKRLPN----VLAIQLKRF--EFKQGR-NERAAKIDTP-VQFPLQLNMLPYTNRarsapESKENYelarsc 459
Cdd:cd02672 143 YQPLEQTTSIRHLPDilllVLVINLSVTngEFDDINvVLPSGKVMQNkVSPKAIDHDKLVKNR-----GQESIY------ 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 367047331 460 TYDLLSVVVHVGEIDTG-HYLSYCRVG------DQWFAFNDHKVELAQKSdvlnsqAYLLFY 514
Cdd:cd02672 212 KYELVGYVCEINDSSRGqHNVVFVIKVneesthGRWYLFNDFLVTPVSEL------AYILLY 267
|
|
| |
