|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
54-495 |
2.63e-78 |
|
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: 244.97 E-value: 2.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 54 GLINRGNDCFITSSLQGLAGIPRFVEYLKRIRtvlleletklsnnakgdnptvdnttrhsrlenssnslaplhesltsli 133
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFL------------------------------------------------ 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 134 ldlisvkdrktsispkivintlesifkskissKQNDAHEFTLILLQTLQeersklidyskqicnlNIPKFPFEGETSKFL 213
Cdd:cd02662 33 --------------------------------EQQDAHELFQVLLETLE----------------QLLKFPFDGLLASRI 64
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 214 VCLKCKGLSEPSYKQTFIRELSVPQQ----TSENLSNILAHDETEIIDDYSCLICQIrailnheeyrnfkdctpdeilml 289
Cdd:cd02662 65 VCLQCGESSKVRYESFTMLSLPVPNQssgsGTTLEHCLDDFLSTEIIDDYKCDRCQT----------------------- 121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 290 drlknyatkapinenlpfeveqyvkryskgnlqvsnikgkvikkdVVVQLPDILIVHLSRSTFNG-ITYSRNPCNVKFGE 368
Cdd:cd02662 122 ---------------------------------------------VIVRLPQILCIHLSRSVFDGrGTSTKNSCKVSFPE 156
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 369 RItlseytlaesgtitenRQVKYNLKSVVKHTGSHSSGHYMCYRRKTEIRFGKEDESSfrrapvvnnevnknreqnvahn 448
Cdd:cd02662 157 RL----------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKDKEPGSF---------------------- 198
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1147620 449 dykkSRYKKVKNALRYPYWQISDTAIKESTASTVLnEQKYAYMLYYE 495
Cdd:cd02662 199 ----VRMREGPSSTSHPWWRISDTTVKEVSESEVL-EQKSAYMLFYE 240
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
53-416 |
2.21e-49 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 171.86 E-value: 2.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 53 VGLINRGNDCFITSSLQGLAGIPRFVEYLKRIRTVLLELETKLSNNakgdnptvdnttrhsrlenssnslapLHESLTSL 132
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN--------------------------LLCALRDL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 133 ILDLISvKDRKTSISPKIVINTLESIFKSKISSKQNDAHEFTLILLQTLQEERSKLIDYSkqicNLNIPKFPFEGETSKF 212
Cdd:pfam00443 55 FKALQK-NSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTE----NESLITDLFRGQLKSR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 213 LVCLKCKGLSEPSYKQTFIRELSVPQQTSENLSnilahdeteiiddysclicqirailnheeyrnfkdctpdeilmldrl 292
Cdd:pfam00443 130 LKCLSCGEVSETFEPFSDLSLPIPGDSAELKTA----------------------------------------------- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 293 knyatkAPINENLPFEVEQYVKRYSKGNLQVSNIKGKVIKKDVVVQLPDILIVHLSRSTFNGITYSRNPCNVKFGERITL 372
Cdd:pfam00443 163 ------SLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDL 236
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1147620 373 SEYTLAESGTITENRQvKYNLKSVVKHTGSHSSGHYMCYRRKTE 416
Cdd:pfam00443 237 SRYLAEELKPKTNNLQ-DYRLVAVVVHSGSLSSGHYIAYIKAYE 279
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
163-495 |
6.62e-27 |
|
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: 109.11 E-value: 6.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 163 ISSKQNDAHEFTLILLQTLQEERSKLID-YSKQICNLNIPKFPFEGETSKFLVCLKCKGLSEPSYKQTFIrELSVPQQTS 241
Cdd:cd02257 18 LFSEQQDAHEFLLFLLDKLHEELKKSSKrTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFL-SLPLPVKGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 242 ENLS---NILAHDETEIIDDYSCLICQirailnheeyrnfkdctpdeilmldrlknyatkapinenlpfeveqyvkrysk 318
Cdd:cd02257 97 PQVSledCLEKFFKEEILEGDNCYKCE----------------------------------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 319 gnlqvSNIKGKVIKKDVVVQLPDILIVHLSRSTFNG-ITYSRNPCNVKFGERITLSEYTLAE-SGTITENRQVKYNLKSV 396
Cdd:cd02257 124 -----KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEdGTKEKLNTKVSFPLELDLSPYLSEGeKDSDSDNGSYKYELVAV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 397 VKHTGSH-SSGHYMCYrrkteirfgkedessfrrapvvnnevnknreqnvahndykksrykkVKNALRYPYWQISDTAIK 475
Cdd:cd02257 199 VVHSGTSaDSGHYVAY----------------------------------------------VKDPSDGKWYKFNDDKVT 232
|
330 340
....*....|....*....|...
gi 1147620 476 ESTASTVLNEQKY---AYMLYYE 495
Cdd:cd02257 233 EVSEEEVLEFGSLsssAYILFYE 255
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
54-414 |
5.24e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 66.58 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 54 GLINRGNDCFITSSLQGLAGIPRFVEYLkrirtvlLELETKLSNNAKgdNPTVDNTTRHSRLENssnslAPLHESLTSLI 133
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRY-------DDLENKFPSDVV--DPANDLNCQLIKLAD-----GLLSGRYSKPA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 134 LDLISVKDRKTSISPkivintleSIFKSKI--------SSKQNDAHEFTLILLQTLQEERSKlidysKQICNLNiPKFPF 205
Cdd:cd02658 67 SLKSENDPYQVGIKP--------SMFKALIgkghpefsTMRQQDALEFLLHLIDKLDRESFK-----NLGLNPN-DLFKF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 206 EGETSkfLVCLKCKglsepSYKQTfirelsvpQQTSENLS-NILAHDETEIIDDysclicqirailnhEEYRnfkdctpD 284
Cdd:cd02658 133 MIEDR--LECLSCK-----KVKYT--------SELSEILSlPVPKDEATEKEEG--------------ELVY-------E 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 285 EILMLDRLKNYATkapinenlPFEVEQYVKRYSKgnlqvsniKGKVIKKDVVVQLPDILIVHLSRstfngITYSRNPCNV 364
Cdd:cd02658 177 PVPLEDCLKAYFA--------PETIEDFCSTCKE--------KTTATKTTGFKTFPDYLVINMKR-----FQLLENWVPK 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1147620 365 KFGERITLSEYTLAEsgtitenrqvKYNLKSVVKHTG-SHSSGHYMCYRRK 414
Cdd:cd02658 236 KLDVPIDVPEELGPG----------KYELIAFISHKGtSVHSGHYVAHIKK 276
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
329-495 |
1.50e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 65.10 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 329 KVIKKDVVVQLPDILIVHLSRSTFNG-ITYSRNPCNVKFGERITLSEYTLAESGTITENRQVKYNLKSVVKHTGSHSSGH 407
Cdd:cd02667 139 KAKKQYLISKLPPVLVIHLKRFQQPRsANLRKVSRHVSFPEILDLAPFCDPKCNSSEDKSSVLYRLYGVVEHSGTMRSGH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 408 YMCYRRkteIRFGKEDESSFRRAPVVNNEVNKNREQnvahndykksrykkvknalrypYWQISDTAIKESTASTVLNEQk 487
Cdd:cd02667 219 YVAYVK---VRPPQQRLSDLTKSKPAADEAGPGSGQ----------------------WYYISDSDVREVSLEEVLKSE- 272
|
....*...
gi 1147620 488 yAYMLYYE 495
Cdd:cd02667 273 -AYLLFYE 279
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
53-499 |
1.08e-10 |
|
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: 63.05 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 53 VGLINRGNDCFITSSLQGLAGIPRFVEYLKRIRtvlleletklsnnakgdnPTVDNTtrhsrlENSSNSLAplhesLTSL 132
Cdd:cd02659 3 VGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIP------------------PTEDDD------DNKSVPLA-----LQRL 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 133 ILDLisvkdrKTSISPKIVINTLESIFK----SKISSKQNDAHEFTLILLQTLqEERSKLIDYSKQICNLnipkfpFEGE 208
Cdd:cd02659 54 FLFL------QLSESPVKTTELTDKTRSfgwdSLNTFEQHDVQEFFRVLFDKL-EEKLKGTGQEGLIKNL------FGGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 209 TSKFLVCLKCkglsepsykqtfirelsvpqqtsenlsnilaHDETEIIDDYSCLICQIRailnheeyrNFKDctpdeilM 288
Cdd:cd02659 121 LVNYIICKEC-------------------------------PHESEREEYFLDLQVAVK---------GKKN-------L 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 289 LDRLKNYatkapINENLPFEVEQYvkRYSKGNLQVSNIKGKVIKKdvvvqLPDILIVHLSRSTFNGITYSRNPCN--VKF 366
Cdd:cd02659 154 EESLDAY-----VQGETLEGDNKY--FCEKCGKKVDAEKGVCFKK-----LPPVLTLQLKRFEFDFETMMRIKINdrFEF 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 367 GERITLSEYT------LAESGTITENRQVKYNLKSVVKHTGSHSSGHYMCYRRktEIRFGK----EDEssfrrapvvnnE 436
Cdd:cd02659 222 PLELDMEPYTekglakKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIK--DRDDGKwykfNDD-----------V 288
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1147620 437 VNKNREQNVAHNDYKKSRYkkvknalrYPYWQISDTAIKESTAstvlneqkyAYMLYYERVNK 499
Cdd:cd02659 289 VTPFDPNDAEEECFGGEET--------QKTYDSGPRAFKRTTN---------AYMLFYERKSP 334
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-414 |
4.77e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 56.91 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 163 ISSKQNDAHEFTLILLQTLqeeRSKLIDYskqicnlnipkfpFEGETSKFLVCLKCkglsepsykqtfirelsvpqqtse 242
Cdd:cd02674 18 LSADQQDAQEFLLFLLDGL---HSIIVDL-------------FQGQLKSRLTCLTC------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 243 nlsnilaHDETEIIDDYSCLICQIRAILNHEEYRNFKDCtpdeilmldrLKNYATKapinENLPFEVEQYVKRYSKgnlq 322
Cdd:cd02674 58 -------GKTSTTFEPFTYLSLPIPSGSGDAPKVTLEDC----------LRLFTKE----ETLDGDNAWKCPKCKK---- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 323 vsniKGKVIKKDVVVQLPDILIVHLSRSTFNGITYSRNPCNVKFG-ERITLSEYTLAESGTItenrQVKYNLKSVVKHTG 401
Cdd:cd02674 113 ----KRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPlNDLDLTPYVDTRSFTG----PFKYDLYAVVNHYG 184
|
250
....*....|...
gi 1147620 402 SHSSGHYMCYRRK 414
Cdd:cd02674 185 SLNGGHYTAYCKN 197
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
54-413 |
4.41e-07 |
|
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: 51.60 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 54 GLINRGNDCFITSSLQGLAGIPRFVEYLkrirtvlleletkLSNnakgdnptvdnttRHSRLENSSNSLAPLHESLTSLI 133
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYF-------------LSD-------------RHSCTCLSCSPNSCLSCAMDEIF 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 134 LDLISVKDRktsiSPKIVINTLESIFKSKIS---SKQNDAHEFTLILLQTLQEE--RSKLIDYSKQICNLNIPKFpFEGE 208
Cdd:cd02660 56 QEFYYSGDR----SPYGPINLLYLSWKHSRNlagYSQQDAHEFFQFLLDQLHTHygGDKNEANDESHCNCIIHQT-FSGS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 209 TSKFLVCLKCKGLS---EPsykqtfIRELSVPQQtseNLSNILAHDETEIIDDYSCLIcqirailnheeyrnfkDCtpde 285
Cdd:cd02660 131 LQSSVTCQRCGGVSttvDP------FLDLSLDIP---NKSTPSWALGESGVSGTPTLS----------------DC---- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 286 ilmLDRlknyatkapinenlpFEVEQYVKrYSKGNLQVSNIKGKVIKKDVVVQLPDILIVHLSRSTFNGITYSRN-PCNV 364
Cdd:cd02660 182 ---LDR---------------FTRPEKLG-DFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKiDTYV 242
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1147620 365 KFGERITLSEYTLAESGTITE----NRQVKYNLKSVVKHTGSHSSGHYMCYRR 413
Cdd:cd02660 243 QFPLELNMTPYTSSSIGDTQDsnslDPDYTYDLFAVVVHKGTLDTGHYTAYCR 295
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
54-443 |
5.24e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 51.34 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 54 GLINRGNDCFITSSLQGLA-GIPRFVEYLKRIRTVLLELETKLSNNAKGDNptvdnttrhsrlenssnslapLHESLTSL 132
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVLKNVIRKPEPDLN---------------------QEEALKLF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 133 ILDLISVKDRKTSISPkivintlesifkskiSSKQNDAHEFTLILLQTLQEERSKLIDYSKqicnlnipKFPFEGETSkf 212
Cdd:COG5533 60 TALWSSKEHKVGWIPP---------------MGSQEDAHELLGKLLDELKLDLVNSFTIRI--------FKTTKDKKK-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 213 lvclkckglsePSYKQTFIRELSVPQQTSENLSNILahdeTEIIDdysclicqirailnheeyrNFKDCTPDEIlmldrl 292
Cdd:COG5533 115 -----------TSTGDWFDIIIELPDQTWVNNLKTL----QEFID-------------------NMEELVDDET------ 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 293 knyATKAPINENLpfeveqyvkryskgnlqvsNIKGKVIKKDVVVQLPDILIVHLSR-STFNGITYSRNPCNVKFgerit 371
Cdd:COG5533 155 ---GVKAKENEEL-------------------EVQAKQEYEVSFVKLPKILTIQLKRfANLGGNQKIDTEVDEKF----- 207
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1147620 372 lsEYTLAESGTITENRQVKYNLKSVVKHTGSHSSGHYMCYRRKTEIrFGKEDESSFRRAPVVnNEVNKNREQ 443
Cdd:COG5533 208 --ELPVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKKGGK-WEKANDSDVTPVSEE-EAINEKAKN 275
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
54-416 |
1.42e-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 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: 46.94 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 54 GLINRGNDCFITSSLQGLAGIPrfveylkrirtvllELETKLSNNakgdnptvdntTRHSRLENSSNSlaplheSLTSLI 133
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVP--------------ELRDALKNY-----------NPARRGANQSSD------NLTNAL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 134 LDLISVKDRKT-SISPKIVINTLESIF------KSKISSKQNDAHEFTLILLQTLQEERSKLIDYSKQICNLnipkfpFE 206
Cdd:cd02657 50 RDLFDTMDKKQePVPPIEFLQLLRMAFpqfaekQNQGGYAQQDAEECWSQLLSVLSQKLPGAGSKGSFIDQL------FG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 207 GEtskFLVCLKCKGLSEPsykqtfirelSVPQQTSENLSNILAHDETEIiddySCLICQIRAILNHEEYRNF----KDCT 282
Cdd:cd02657 124 IE---LETKMKCTESPDE----------EEVSTESEYKLQCHISITTEV----NYLQDGLKKGLEEEIEKHSptlgRDAI 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 283 PDEILMLDRLKNYATKapinenlpfeveQYVKRYSKGNlqvSNIKGKVIKKdvvvqlpdilivhlsrstfngitysrnpc 362
Cdd:cd02657 187 YTKTSRISRLPKYLTV------------QFVRFFWKRD---IQKKAKILRK----------------------------- 222
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1147620 363 nVKFGERITLSEYtLAESGtitenrqvKYNLKSVVKHTG-SHSSGHYMCYRRKTE 416
Cdd:cd02657 223 -VKFPFELDLYEL-CTPSG--------YYELVAVITHQGrSADSGHYVAWVRRKN 267
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
336-415 |
4.37e-04 |
|
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: 42.69 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 336 VVQLPDILIVHLSRSTFNGITYSRNPCNVKFGERITLSEYTLAESgTITENRQVKYNLKSVVKHTGS-HSSGHYMCYRRK 414
Cdd:cd02669 329 ISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFD-KPSLNLSTKYNLVANIVHEGTpQEDGTWRVQLRH 407
|
.
gi 1147620 415 T 415
Cdd:cd02669 408 K 408
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
115-410 |
4.73e-04 |
|
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: 42.30 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 115 LENSSNSL-------APLHESLTSLILDL---ISVKDRKT-SISPKIVINTLESIFKSKISSKQNDAHEFTLILLQT--- 180
Cdd:cd02663 2 LENFGNTCycnsvlqALYFENLLTCLKDLfesISEQKKRTgVISPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEiae 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 181 -LQEERSKLIDYSKQICNLNIPKFP------FEGETSKFLVCLKCKGLSepSYKQTFIrELSVPQQTSENLSNIL-AHDE 252
Cdd:cd02663 82 iLDAERKAEKANRKLNNNNNAEPQPtwvheiFQGILTNETRCLTCETVS--SRDETFL-DLSIDVEQNTSITSCLrQFSA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 253 TEII---DDYSCLICQirailNHEEyrnfkdctpdeilmldrlknyATKapinenlpfeveqyvkryskgnlqvsNIKgk 329
Cdd:cd02663 159 TETLcgrNKFYCDECC-----SLQE---------------------AEK--------------------------RMK-- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 330 vIKKdvvvqLPDILIVHLSRSTFNGiTYSRnpcNVKFGERITLS-EYTLAESGTITENRQVKYNLKSVVKHTGS---Hss 405
Cdd:cd02663 185 -IKK-----LPKILALHLKRFKYDE-QLNR---YIKLFYRVVFPlELRLFNTTDDAENPDRLYELVAVVVHIGGgpnH-- 252
|
....*
gi 1147620 406 GHYMC 410
Cdd:cd02663 253 GHYVS 257
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
54-410 |
8.67e-04 |
|
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: 41.64 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 54 GLINRGNDCFITSSLQGLAgipRFVEYlkriRTVLLELETKLSNNAKGDNPTVDnttrhsrlenssnslaplHESLTSLI 133
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWF---MNLEF----RKAVYECNSTEDAELKNMPPDKP------------------HEPQTIID 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 134 -LDLISVK---DRKTSISPKIVINTLEsifkskIS-SKQNDAHEFTLILLQTLQEERSKLIDYSKQicnlNIPKFPFEGE 208
Cdd:cd02668 56 qLQLIFAQlqfGNRSVVDPSGFVKALG------LDtGQQQDAQEFSKLFLSLLEAKLSKSKNPDLK----NIVQDLFRGE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 209 TSKFLVCLKCKglSEPSYKQTFIrELSVPQQTSENLsnilahdeTEIIDDYSCLicqirailnheeyrnfkdctpdEILm 288
Cdd:cd02668 126 YSYVTQCSKCG--RESSLPSKFY-ELELQLKGHKTL--------EECIDEFLKE----------------------EQL- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 289 ldrlknyatkapINENlpfeveqyvkRYSKGNLQVsniKGKVIKKDVVVQLPDILIVHLSRSTFNGITYSRNPCN--VKF 366
Cdd:cd02668 172 ------------TGDN----------QYFCESCNS---KTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNasISF 226
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1147620 367 GERITLSEYTLAESGTITEnrqvkYNLKSVVKHTG-SHSSGHYMC 410
Cdd:cd02668 227 PEILDMGEYLAESDEGSYV-----YELSGVLIHQGvSAYSGHYIA 266
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
336-495 |
2.44e-03 |
|
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: 40.17 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 336 VVQLPDILIVHLSRSTFNGITYSRN--------------PCNVKFGERITLSEYTLAESGTITE--NRQVKYNLKSVVKH 399
Cdd:cd02664 172 VTGAPEYLILTLLRFSYDQKTHVREkimdnvsinevlslPVRVESKSSESPLEKKEEESGDDGElvTRQVHYRLYAVVVH 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147620 400 TGSHS-SGHYMCYRRKteirfGKEDESSFRRAPVVNNEVNKNREQN-VAHNDykkSRykkvknalrypywqISDTAIKES 477
Cdd:cd02664 252 SGYSSeSGHYFTYARD-----QTDADSTGQECPEPKDAEENDESKNwYLFND---SR--------------VTFSSFESV 309
|
170
....*....|....*...
gi 1147620 478 TASTVLNEQKYAYMLYYE 495
Cdd:cd02664 310 QNVTSRFPKDTPYILFYE 327
|
|
| |
