|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
698-1027 |
3.66e-114 |
|
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: 351.20 E-value: 3.66e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCLCNtpamaeyfnnncymadinrynilghkgevaeefgvimkalwaglykfisprdfkvtigki 777
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 778 neqfagyDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddpmaadlawskhkllneSIIVALFQGQFKSTVQCL 857
Cdd:cd02674 21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 858 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKR 933
Cdd:cd02674 56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 934 FSYEGRWKQKLQTTVDFPLDSLDLAQYVIGP-KQNQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSEIS 1012
Cdd:cd02674 136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215
|
330
....*....|....*
gi 1395229732 1013 TSSVKSSAAYILFYS 1027
Cdd:cd02674 216 ESSVVSSSAYILFYE 230
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
697-1026 |
4.39e-112 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 349.05 E-value: 4.39e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 697 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNCYMADINRYNILGHkgeVAEEFGVIMKALW-AGLYKFISPRDFKVTIG 775
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQkNSKSSSVSPKMFKKSLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 776 KINEQFAGYDQQDSQELLLFLMDGLHEDLNkadnrkrykeeendhlddpmaadlawSKHKLLNESIIVALFQGQFKSTVQ 855
Cdd:pfam00443 78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 856 CLTCHRKSRTFETFMYLSLPL----ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHL 931
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIpgdsAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 932 KRFSYEGRWKQKLQTTVDFPLDsLDLAQYVIGPKQ----NQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHE 1007
Cdd:pfam00443 212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKpktnNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290
|
330 340
....*....|....*....|
gi 1395229732 1008 VSEISTS-SVKSSAAYILFY 1026
Cdd:pfam00443 291 VTEVDEEtAVLSSSAYILFY 310
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
696-876 |
1.77e-52 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 198.57 E-value: 1.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 696 LTGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNCYMADINRYNILGHKGEVAEEFGVIMKALWAGLYKFISPRDFKVTIG 775
Cdd:COG5560 265 TCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 776 KINEQFAGYDQQDSQELLLFLMDGLHEDLNKAdNRKRYKEEENDHLDDPMA----ADLAWSKHKLLNESIIVALFQGQFK 851
Cdd:COG5560 345 SFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKPDLSPGDDVVvkkkAKECWWEHLKRNDSIITDLFQGMYK 423
|
170 180
....*....|....*....|....*
gi 1395229732 852 STVQCLTCHRKSRTFETFMYLSLPL 876
Cdd:COG5560 424 STLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
707-1026 |
2.05e-43 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 170.45 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 707 YMNSILQCLCNTPAMAEYFNNNCYMADINRYNILghkgevaeefgvIMKALWAGLYKFISPRDFKVTIGKINEQFagydq 786
Cdd:COG5560 536 NDNGIEVPVVHLRIEKGYKSKRLFGDPFLQLNVL------------IKASIYDKLVKEFEELLVLVEMKKTDVDL----- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 787 qDSQELLLFLMD---GLHEDLNKADNRKRYK---EEENDHLDDPMAADLAWSKHKLLnesiivALFQGQFKSTVQCLTCH 860
Cdd:COG5560 599 -VSEQVRLLREEsspSSWLKLETEIDTKREEqveEEGQMNFNDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAA 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 861 RKSRTfetfmylslplastskcsLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRW 940
Cdd:COG5560 672 ERTIT------------------LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 941 KQKLQTTVDFPLDSLDLAQYVIGPKQNQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSEISTSSVKSSA 1020
Cdd:COG5560 734 RDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSS 813
|
....*.
gi 1395229732 1021 AYILFY 1026
Cdd:COG5560 814 AYVLFY 819
|
|
| USP8_dimer |
pfam08969 |
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ... |
8-116 |
1.27e-32 |
|
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.
Pssm-ID: 462647 Cd Length: 113 Bit Score: 122.41 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 8 VKELYLSSSLGDLNKKAEIRPD--KTSTRSYVQSACKIFKAAEEFRLDRDEEKAYVLYMKYLTVYEIIKKRPDFKEQPDY 85
Cdd:pfam08969 3 LKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVKAT 82
|
90 100 110
....*....|....*....|....*....|.
gi 1395229732 86 FMTILGPNSFKKAIVEAEKLSDSLKLRYEEV 116
Cdd:pfam08969 83 VRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
|
|
| TAF4 |
pfam05236 |
Transcription initiation factor TFIID component TAF4 family; This region of similarity is ... |
97-176 |
2.42e-04 |
|
Transcription initiation factor TFIID component TAF4 family; This region of similarity is found in Transcription initiation factor TFIID component TAF4.
Pssm-ID: 461598 [Multi-domain] Cd Length: 264 Bit Score: 44.18 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 97 KAIVEAEKLSDSLKL--RYEEV-EVRKKL---EEKDRQEEKKRREEitEKDGGRVSPKVSSTTNMKDSKKVKGE-----Q 165
Cdd:pfam05236 88 KLIVISRHRRDGEKTdhRYEQTsDVRKQLkflAQKDKEEEERRVAE--EREGLLKAAKSRSNQEDPEQLKLKQEakemqK 165
|
90
....*....|.
gi 1395229732 166 NELKTATTKAA 176
Cdd:pfam05236 166 EEDEKMRHRAA 176
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
292-540 |
3.24e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.78 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 292 ILRSEPLVLEGGYENWLLFYPMYTTNAKVRPPRQniiSTLPQLNFSYPSLIEPRPPTPTQQE-----PEVTPKPQETLDP 366
Cdd:PHA03307 79 APANESRSTPTWSLSTLAPASPAREGSPTPPGPS---SPDPPPPTPPPASPPPSPAPDLSEMlrpvgSPGPPPAASPPAA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 367 VLANGVTPADPPTSETSMVTDSLQEDTVDLPvkVSTSSALDLSKKGSAAAPSSQSP----ATAKAFPQFDRAKKPSIRVS 442
Cdd:PHA03307 156 GASPAAVASDAASSRQAALPLSSPEETARAP--SSPPAEPPPSTPPAAASPRPPRRsspiSASASSPAPAPGRSAADDAG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 443 DEPKPSQNGSAKDSNPFVPDRTAKPSFVPNTSLSKEEQSRIHSEAVAGiekaKQEQEKRIQERRRgkeqsSDAPSKSMSL 522
Cdd:PHA03307 234 ASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSR----PGPASSSSSPRER-----SPSPSPSSPG 304
|
250
....*....|....*...
gi 1395229732 523 DSPAPNPNHIVSEIKREP 540
Cdd:PHA03307 305 SGPAPSSPRASSSSSSSR 322
|
|
| FimV |
COG3170 |
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures]; |
314-529 |
6.33e-04 |
|
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];
Pssm-ID: 442403 [Multi-domain] Cd Length: 508 Bit Score: 43.63 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 314 YTtnAKVRPPRQNIISTLPQLNFSyPSLIEPRPPTPTQQEP-----------EVTPKPQETLDPVLANGVTPADPPTSET 382
Cdd:COG3170 100 YT--LLLDPPAYAAAAAAPAAAPA-PAPAAPAAAAAAADQPaaeaapaasgeYYPVRPGDTLWSIAARPVRPSSGVSLDQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 383 SMVtdSLQEDTVDLPVKvstsSALDLSKKG------SAAAPSSQSPATAKAFPQFDRAKKPSIRVSDEPKPSQNGSAKDS 456
Cdd:COG3170 177 MMV--ALYRANPDAFID----GNINRLKAGavlrvpAAEEVAALSPAEARQEVQAQSADWAAYRARLAAAVEPAPAAAAP 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395229732 457 NPFVPDRTAKPSfVP---NTSLSKEEQSRIHSEAVAgiekAKQEQEKRIQERRRGKEQSSDAPSKSMSLDSPAPNP 529
Cdd:COG3170 251 AAPPAAAAAAGP-VPaaaEDTLSPEVTAAAAAEEAD----ALPEAAAELAERLAALEAQLAELQRLLALKNPAPAA 321
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
698-1027 |
3.66e-114 |
|
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: 351.20 E-value: 3.66e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCLCNtpamaeyfnnncymadinrynilghkgevaeefgvimkalwaglykfisprdfkvtigki 777
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 778 neqfagyDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddpmaadlawskhkllneSIIVALFQGQFKSTVQCL 857
Cdd:cd02674 21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 858 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKR 933
Cdd:cd02674 56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 934 FSYEGRWKQKLQTTVDFPLDSLDLAQYVIGP-KQNQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSEIS 1012
Cdd:cd02674 136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215
|
330
....*....|....*
gi 1395229732 1013 TSSVKSSAAYILFYS 1027
Cdd:cd02674 216 ESSVVSSSAYILFYE 230
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
697-1026 |
4.39e-112 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 349.05 E-value: 4.39e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 697 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNCYMADINRYNILGHkgeVAEEFGVIMKALW-AGLYKFISPRDFKVTIG 775
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQkNSKSSSVSPKMFKKSLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 776 KINEQFAGYDQQDSQELLLFLMDGLHEDLNkadnrkrykeeendhlddpmaadlawSKHKLLNESIIVALFQGQFKSTVQ 855
Cdd:pfam00443 78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 856 CLTCHRKSRTFETFMYLSLPL----ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHL 931
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIpgdsAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 932 KRFSYEGRWKQKLQTTVDFPLDsLDLAQYVIGPKQ----NQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHE 1007
Cdd:pfam00443 212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKpktnNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290
|
330 340
....*....|....*....|
gi 1395229732 1008 VSEISTS-SVKSSAAYILFY 1026
Cdd:pfam00443 291 VTEVDEEtAVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
698-1026 |
6.96e-76 |
|
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: 250.09 E-value: 6.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCLCNtpamaeyfnnncymadinrynilghkgevaeefgvimkalwaglykfisprdfkvtigki 777
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 778 neqfagyDQQDSQELLLFLMDGLHEDLNKADNRKRYKEEendhlddpmaadlawskhkllNESIIVALFQGQFKSTVQCL 857
Cdd:cd02257 21 -------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSS---------------------LKSLIHDLFGGKLESTIVCL 72
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 858 TCHRKSRTFETFMYLSLPL--ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKaHRDSTKKLEIWKVPPILLVHLKRFS 935
Cdd:cd02257 73 ECGHESVSTEPELFLSLPLpvKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFS 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 936 YEGRW-KQKLQTTVDFPLdSLDLAQYV------IGPKQNQKRYGLYGVSNHYGGL-DGGHYTAYCKNALKQRWYKFDDHE 1007
Cdd:cd02257 152 FNEDGtKEKLNTKVSFPL-ELDLSPYLsegekdSDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDDK 230
|
330 340
....*....|....*....|....
gi 1395229732 1008 VSEISTSSV-----KSSAAYILFY 1026
Cdd:cd02257 231 VTEVSEEEVlefgsLSSSAYILFY 254
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
697-1027 |
7.53e-68 |
|
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: 229.47 E-value: 7.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 697 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNCYMADINRynilghkgevaEEFGV-------IMKALWAGLyKFISPRD 769
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCN-----------EGFCMmcaleahVERALASSG-PGSAPRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 770 FKVTIGKINEQFAGYDQQDSQELLLFLMDGLHedlnKADNRKRYKEEENDHLddpmAADLAWSKHkllnesiivaLFQGQ 849
Cdd:cd02661 70 FSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDPS----SQETTLVQQ----------IFGGY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 850 FKSTVQCLTCHRKSRTFETFMYLSLPLASTSkcSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLV 929
Cdd:cd02661 132 LRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 930 HLKRFSYEGRwkQKLQTTVDFPlDSLDLAQYVIGPKQNQKRYGLYGVSNHYGG-LDGGHYTAYCKNALKqRWYKFDDHEV 1008
Cdd:cd02661 210 HLKRFSNFRG--GKINKQISFP-ETLDLSPYMSQPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKSSNG-KWYNMDDSKV 285
|
330
....*....|....*....
gi 1395229732 1009 SEISTSSVKSSAAYILFYS 1027
Cdd:cd02661 286 SPVSIETVLSQKAYILFYI 304
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
698-1026 |
9.63e-65 |
|
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: 221.86 E-value: 9.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCLCNTPAMAEYF-----NNNCYMADINrynilghkGEVAEEFGVIMKALWAGLYK-FISPRDFK 771
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFlsdrhSCTCLSCSPN--------SCLSCAMDEIFQEFYYSGDRsPYGPINLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 772 VTIGKINEQFAGYDQQDSQELLLFLMDGLHEDLnkadnrKRYKEEENDHLDdpmaadlawskhkllNESIIVALFQGQFK 851
Cdd:cd02660 74 YLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHY------GGDKNEANDESH---------------CNCIIHQTFSGSLQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 852 STVQCLTCHRKSRTFETFMYLSLPLASTSKCS-------------LQDCLRLFSKEEKLTDNNkVFCRHCKAHRDSTKKL 918
Cdd:cd02660 133 SSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSwalgesgvsgtptLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 919 EIWKVPPILLVHLKRFSYE-GRWKQKLQTTVDFPLDsLDLAQYVIG---------PKQNQKRYGLYGVSNHYGGLDGGHY 988
Cdd:cd02660 212 SIKKLPPVLCFQLKRFEHSlNKTSRKIDTYVQFPLE-LNMTPYTSSsigdtqdsnSLDPDYTYDLFAVVVHKGTLDTGHY 290
|
330 340 350
....*....|....*....|....*....|....*...
gi 1395229732 989 TAYCKNALKQrWYKFDDHEVSEISTSSVKSSAAYILFY 1026
Cdd:cd02660 291 TAYCRQGDGQ-WFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
698-1026 |
4.09e-57 |
|
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: 198.76 E-value: 4.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCLCNTPAMAEYFNNNcymadinrynilghkgevaeefgvimkalwaglykfisPRDFKVTIGKI 777
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 778 NEQFAGYDQQDSQELLLFLMDGLhedlnkadnrkrykeeendhlddpmaadlawskhkllnESIIVALFQGQFKSTVQCL 857
Cdd:cd02667 43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 858 TCHRKSRTFETFMYLSLPLA--STSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKahrDSTKKLEIWKVPPILLVHLKRFS 935
Cdd:cd02667 85 SCGTVSLVYEPFLDLSLPRSdeIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQ 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 936 YEGRWK-QKLQTTVDFPlDSLDLAQYViGPKQN------QKRYGLYGVSNHYGGLDGGHYTAYCKNALKQR--------- 999
Cdd:cd02667 162 QPRSANlRKVSRHVSFP-EILDLAPFC-DPKCNssedksSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQrlsdltksk 239
|
330 340 350
....*....|....*....|....*....|....*....
gi 1395229732 1000 ------------WYKFDDHEVSEISTSSVKSSAAYILFY 1026
Cdd:cd02667 240 paadeagpgsgqWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
696-876 |
1.77e-52 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 198.57 E-value: 1.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 696 LTGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNCYMADINRYNILGHKGEVAEEFGVIMKALWAGLYKFISPRDFKVTIG 775
Cdd:COG5560 265 TCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 776 KINEQFAGYDQQDSQELLLFLMDGLHEDLNKAdNRKRYKEEENDHLDDPMA----ADLAWSKHKLLNESIIVALFQGQFK 851
Cdd:COG5560 345 SFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKPDLSPGDDVVvkkkAKECWWEHLKRNDSIITDLFQGMYK 423
|
170 180
....*....|....*....|....*
gi 1395229732 852 STVQCLTCHRKSRTFETFMYLSLPL 876
Cdd:COG5560 424 STLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
698-1027 |
2.23e-51 |
|
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: 182.89 E-value: 2.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCLcntpamaeYFNNNCY-MADInRYNILGHKGEVaeefGVImkalwaglykfiSPRDFKVTIGK 776
Cdd:cd02663 1 GLENFGNTCYCNSVLQAL--------YFENLLTcLKDL-FESISEQKKRT----GVI------------SPKKFITRLKR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 777 INEQFAGYDQQDSQELLLFLMDGLHEDLNKADNRKRYKEEENDHLDDPMAADlaWskhkllnesiIVALFQGQFKSTVQC 856
Cdd:cd02663 56 ENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPT--W----------VHEIFQGILTNETRC 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 857 LTCHRKSRTFETFMYLSLPLASTskCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSY 936
Cdd:cd02663 124 LTCETVSSRDETFLDLSIDVEQN--TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 937 EGRWKQ--KLQTTVDFPL-----DSLDLAQYVigpkqnQKRYGLYGVSNHYG-GLDGGHYTAYCKNalKQRWYKFDDHEV 1008
Cdd:cd02663 202 DEQLNRyiKLFYRVVFPLelrlfNTTDDAENP------DRLYELVAVVVHIGgGPNHGHYVSIVKS--HGGWLLFDDETV 273
|
330 340
....*....|....*....|....*..
gi 1395229732 1009 SEISTSSV-------KSSA-AYILFYS 1027
Cdd:cd02663 274 EKIDENAVeeffgdsPNQAtAYVLFYQ 300
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
698-1027 |
6.07e-48 |
|
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: 174.15 E-value: 6.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCL------------CNTPAMAEYFNNNCymadinryNILGHKGEVAEEFGVIMKALWAGLYKFI 765
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWfmnlefrkavyeCNSTEDAELKNMPP--------DKPHEPQTIIDQLQLIFAQLQFGNRSVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 766 SPRDFKVTIGKINEQfagydQQDSQELLLFLMDGLHEDLNKADNRKrykeeendhlddpmaadlawskhkllNESIIVAL 845
Cdd:cd02668 73 DPSGFVKALGLDTGQ-----QQDAQEFSKLFLSLLEAKLSKSKNPD--------------------------LKNIVQDL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 846 FQGQFKSTVQCLTCHRKSRTFETFMYLSLPLASTSKcsLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPP 925
Cdd:cd02668 122 FRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT--LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 926 ILLVHLKRFSY--EGRWKQKLQTTVDFPLDsLDLAQYVIGPKQNQKRYGLYGVSNHYG-GLDGGHYTAYCKNALKQRWYK 1002
Cdd:cd02668 200 TLNFQLLRFVFdrKTGAKKKLNASISFPEI-LDMGEYLAESDEGSYVYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYK 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1395229732 1003 FDDHEVSEISTSSVK---------------------SSAAYILFYS 1027
Cdd:cd02668 279 FNDEDVEEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVYK 324
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
698-1026 |
1.80e-47 |
|
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: 1.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCLCNTPamaeYFNNNCYMADINRYNIlGHKGEVAEeFGVIMKALWAGLYKFISPRDFKVTIGKI 777
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTP----EFRNAVYSIPPTEDDD-DNKSVPLA-LQRLFLFLQLSESPVKTTELTDKTRSFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 778 NEQFAGYDQQDSQELLLFLMDGLHEDLNKAdnrkrykEEENdhlddpmaadlawskhkllnesIIVALFQGQFKSTVQCL 857
Cdd:cd02659 78 WDSLNTFEQHDVQEFFRVLFDKLEEKLKGT-------GQEG----------------------LIKNLFGGKLVNYIICK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 858 TCHRKSRTFETFmyLSLPLASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYE 937
Cdd:cd02659 129 ECPHESEREEYF--LDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 938 GR--WKQKLQTTVDFPlDSLDLAQYVI----------GPKQNQK-RYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFD 1004
Cdd:cd02659 207 FEtmMRIKINDRFEFP-LELDMEPYTEkglakkegdsEKKDSESyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFN 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1395229732 1005 DHEVSEISTSSV----------------------KSSAAYILFY 1026
Cdd:cd02659 286 DDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFY 329
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
707-1026 |
2.05e-43 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 170.45 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 707 YMNSILQCLCNTPAMAEYFNNNCYMADINRYNILghkgevaeefgvIMKALWAGLYKFISPRDFKVTIGKINEQFagydq 786
Cdd:COG5560 536 NDNGIEVPVVHLRIEKGYKSKRLFGDPFLQLNVL------------IKASIYDKLVKEFEELLVLVEMKKTDVDL----- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 787 qDSQELLLFLMD---GLHEDLNKADNRKRYK---EEENDHLDDPMAADLAWSKHKLLnesiivALFQGQFKSTVQCLTCH 860
Cdd:COG5560 599 -VSEQVRLLREEsspSSWLKLETEIDTKREEqveEEGQMNFNDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAA 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 861 RKSRTfetfmylslplastskcsLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRW 940
Cdd:COG5560 672 ERTIT------------------LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 941 KQKLQTTVDFPLDSLDLAQYVIGPKQNQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSEISTSSVKSSA 1020
Cdd:COG5560 734 RDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSS 813
|
....*.
gi 1395229732 1021 AYILFY 1026
Cdd:COG5560 814 AYVLFY 819
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
698-1026 |
8.74e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 141.86 E-value: 8.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCLcntpAMAEYFNNncymaDINRYNILGHKGEVAEEFGVIM-KALWAglykfISPRDFKVTIGK 776
Cdd:cd02664 1 GLINLGNTCYMNSVLQAL----FMAKDFRR-----QVLSLNLPRLGDSQSVMKKLQLlQAHLM-----HTQRRAEAPPDY 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 777 INEQ-----FAGYDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddpmaadlawskhkllneSIIVALFQGQFK 851
Cdd:cd02664 67 FLEAsrppwFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 852 STVQCLTCHRKSRTFETFMYLSLplastSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHL 931
Cdd:cd02664 109 TTIRCLNCNSTSARTERFRDLDL-----SFPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 932 KRFSY--EGRWKQKLQTTVDFPLDsLDLAQYV----IGPKQNQKR---------------YGLYGVSNHYG-GLDGGHYT 989
Cdd:cd02664 184 LRFSYdqKTHVREKIMDNVSINEV-LSLPVRVesksSESPLEKKEeesgddgelvtrqvhYRLYAVVVHSGySSESGHYF 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395229732 990 AYCKN--------------------ALKQRWYKFDDHEVSEISTSSVK-------SSAAYILFY 1026
Cdd:cd02664 263 TYARDqtdadstgqecpepkdaeenDESKNWYLFNDSRVTFSSFESVQnvtsrfpKDTPYILFY 326
|
|
| USP8_dimer |
pfam08969 |
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ... |
8-116 |
1.27e-32 |
|
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.
Pssm-ID: 462647 Cd Length: 113 Bit Score: 122.41 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 8 VKELYLSSSLGDLNKKAEIRPD--KTSTRSYVQSACKIFKAAEEFRLDRDEEKAYVLYMKYLTVYEIIKKRPDFKEQPDY 85
Cdd:pfam08969 3 LKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVKAT 82
|
90 100 110
....*....|....*....|....*....|.
gi 1395229732 86 FMTILGPNSFKKAIVEAEKLSDSLKLRYEEV 116
Cdd:pfam08969 83 VRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
698-1026 |
7.60e-32 |
|
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: 126.68 E-value: 7.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCLCNTPAMAE---YFNNNCYMADINRYNILghkgevaeefgVIMKALWAGLYKF---ISPRDFK 771
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPARRGANQSSDNLT-----------NALRDLFDTMDKKqepVPPIEFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 772 VTIGKINEQFA------GYDQQDSQELLLFLMDGLHEDLNKADnrkrykeEENDHLDDpmaadlawskhkllnesiivaL 845
Cdd:cd02657 70 QLLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAG-------SKGSFIDQ---------------------L 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 846 FQGQFKSTVQCL-TCHRKSRTFETFMYLSLPLASTSKCS-LQDCLRLFSKEE--KLTDnnkvfcrhcKAHRDS--TKKLE 919
Cdd:cd02657 122 FGIELETKMKCTeSPDEEEVSTESEYKLQCHISITTEVNyLQDGLKKGLEEEieKHSP---------TLGRDAiyTKTSR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 920 IWKVPPILLVHLKRFSyegrWKQKLQT------TVDFPLDsLDLAQYVigpkQNQKRYGLYGVSNHYG-GLDGGHYTAYC 992
Cdd:cd02657 193 ISRLPKYLTVQFVRFF----WKRDIQKkakilrKVKFPFE-LDLYELC----TPSGYYELVAVITHQGrSADSGHYVAWV 263
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1395229732 993 KNALKQRWYKFDDHEVSEISTSSVKSSA-------AYILFY 1026
Cdd:cd02657 264 RRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
677-1026 |
8.71e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 124.23 E-value: 8.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 677 PSAAKIRNLNPtfgglgqsLTGLRNLGNTCYMNSILQCLCNTPAmaeyfnnncYMADINRYNILGHKGEVAEEFGVIMKA 756
Cdd:cd02671 13 TSCEKRENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPG---------FKHGLKHLVSLISSVEQLQSSFLLNPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 757 LWAGLYKFISPRDFKVTIGKINEQFAGYDQQDSQELLLFLMDGLHEDLNKadnrkrykeeendhlddpmaadlawskhkl 836
Cdd:cd02671 76 KYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK------------------------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 837 lnesiivaLFQGQFKSTVQCLTCHRKSRTFETFMYLSLPLASTSKCS-----------------LQDCLRLFSKEEKLTD 899
Cdd:cd02671 126 --------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKseesseispdpktemktLKWAISQFASVERIVG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 900 NNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRWK------QKLQTTVDFPLDsLDLAQYVIGPKQNQkrYGL 973
Cdd:cd02671 198 EDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPLK-LSLEEWSTKPKNDV--YRL 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395229732 974 YGVSNHYGG-LDGGHYTAYCknalkqRWYKFDDHEV---------SEISTSSVKSSAAYILFY 1026
Cdd:cd02671 275 FAVVMHSGAtISSGHYTAYV------RWLLFDDSEVkvteekdflEALSPNTSSTSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
698-1027 |
1.63e-28 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 116.44 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCLC-NTPAMAEYFNNNC--YMADINRYNiLGHKGEVAEEFGVIMKALWAglykfisprDFKVTI 774
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSkeLKVLKNVIR-KPEPDLNQEEALKLFTALWS---------SKEHKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 775 GKINEQfagYDQQDSQELLLFLMDGLHEDLNKADNRKRYK--EEENDHLDDPMAadlawskhkllneSIIVALFQGQF-- 850
Cdd:COG5533 71 GWIPPM---GSQEDAHELLGKLLDELKLDLVNSFTIRIFKttKDKKKTSTGDWF-------------DIIIELPDQTWvn 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 851 -KSTVQCltchrksrTFETFMYLsLPLASTSKcslqdclrlfskeEKLTDNNKVFCRHCKAHRDStkkleiwKVPPILLV 929
Cdd:COG5533 135 nLKTLQE--------FIDNMEEL-VDDETGVK-------------AKENEELEVQAKQEYEVSFV-------KLPKILTI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 930 HLKRFSYEGRwKQKLQTTVDFPLDsLDLAQYVIGPKQNQKRYGLYGVSNHYGGLDGGHYTAYCKNalKQRWYKFDDHEVS 1009
Cdd:COG5533 186 QLKRFANLGG-NQKIDTEVDEKFE-LPVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK--GGKWEKANDSDVT 261
|
330 340
....*....|....*....|.
gi 1395229732 1010 EISTS---SVKSSAAYILFYS 1027
Cdd:COG5533 262 PVSEEeaiNEKAKNAYLYFYE 282
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
698-1026 |
2.45e-28 |
|
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: 116.65 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCLCNTPAMAEYFNN--NCYMADIN--RYNI------LGHkGEVAEEFGVIM--KALWAGLYKFI 765
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDleNKFPSDVVdpANDLncqlikLAD-GLLSGRYSKPAslKSENDPYQVGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 766 SPRDFKVTIGKINEQFAGYDQQDSQELLLFLMDglhedlnKADNRKRYKEEENdhlddpmaadlawskhklLNEsiivaL 845
Cdd:cd02658 80 KPSMFKALIGKGHPEFSTMRQQDALEFLLHLID-------KLDRESFKNLGLN------------------PND-----L 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 846 FQGQFKSTVQCLTCHRKSRTFETFMYLSLPL------------ASTSKCSLQDCLRLFSKEEKLTDnnkvFCRHCKAHRD 913
Cdd:cd02658 130 FKFMIEDRLECLSCKKVKYTSELSEILSLPVpkdeatekeegeLVYEPVPLEDCLKAYFAPETIED----FCSTCKEKTT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 914 STKKLEIWKVPPILLVHLKRFSYEGRWKQKlqtTVDFPLDSLDlaqyVIGPkqnqKRYGLYGVSNHYG-GLDGGHYTAYC 992
Cdd:cd02658 206 ATKTTGFKTFPDYLVINMKRFQLLENWVPK---KLDVPIDVPE----ELGP----GKYELIAFISHKGtSVHSGHYVAHI 274
|
330 340 350
....*....|....*....|....*....|....*.
gi 1395229732 993 K--NALKQRWYKFDDHEVSEISTSSVKSSAAYILFY 1026
Cdd:cd02658 275 KkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
698-1026 |
1.93e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 108.99 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCLCNTPAMAEYfnnncymadINRYNilghkgevaeefgvimkalwaglykfisprdfkvtigki 777
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY---------LEEFL--------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 778 neqfagyDQQDSQELLLFLMDGLhedlnkadnrkrykeeendhlddpmaadlawskhkllnESIIVALFQGQFKSTVQCL 857
Cdd:cd02662 33 -------EQQDAHELFQVLLETL--------------------------------------EQLLKFPFDGLLASRIVCL 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 858 TCHRKSR-TFETFMYLSLPL---ASTSKCSLQDCLRLFSKEEKLTDnnkVFCRHCKahrdstkkLEIWKVPPILLVHLKR 933
Cdd:cd02662 68 QCGESSKvRYESFTMLSLPVpnqSSGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSR 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 934 FSYEGRWK-QKLQTTVDFPlDSLdlaqyvigpkqNQKRYGLYGVSNHYGGLDGGHYTAY--------------------C 992
Cdd:cd02662 137 SVFDGRGTsTKNSCKVSFP-ERL-----------PKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreG 204
|
330 340 350
....*....|....*....|....*....|....*
gi 1395229732 993 KNALKQRWYKFDDHEVSEISTSSVK-SSAAYILFY 1026
Cdd:cd02662 205 PSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
698-1016 |
5.13e-22 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 103.03 E-value: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCLCNTpamaEYFNNNCYmaDINRYNILGhKGEVAeefgVIMKALWAGLYKFISPRD-FKVTIGK 776
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFI----AKFRKDVY--GIPTDHPRG-RDSVA----LALQRLFYNLQTGEEPVDtTELTRSF 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 777 INEQFAGYDQQDSQELLLFLMDGLhedlnkadnrkrykeeENDHLDDPMaadlawskhkllnESIIVALFQGQFKSTVQC 856
Cdd:COG5077 264 GWDSDDSFMQHDIQEFNRVLQDNL----------------EKSMRGTVV-------------ENALNGIFVGKMKSYIKC 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 857 LTCHRKSRTFETFMYLSLPLASTSkcSLQDCLRLFSKEEKLTDNNKVFCRHcKAHRDSTKKLEIWKVPPILLVHLKRFSY 936
Cdd:COG5077 315 VNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEY 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 937 EGRWKQ--KLQTTVDFPlDSLDLAQYV---IGPKQNQK-RYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSE 1010
Cdd:COG5077 392 DFERDMmvKINDRYEFP-LEIDLLPFLdrdADKSENSDaVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTR 470
|
....*.
gi 1395229732 1011 ISTSSV 1016
Cdd:COG5077 471 ATEKEV 476
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
698-1026 |
1.30e-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 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: 95.85 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 698 GLRNLGNTCYMNSILQCLCNTPAMAEYF-NNNCYMADINRynilghKGEVAEEFGVIMKALW-AGLYK-FISPRDFKVTI 774
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFlLYENYENIKDR------KSELVKRLSELIRKIWnPRNFKgHVSPHELLQAV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 775 GKI-NEQFAGYDQQDSQELLLFLMDGLHEDLNKadNRKRykeeendhlddpmaadlawskhkllNESIIVALFQGQFKST 853
Cdd:cd02669 195 SKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGG--SKKP-------------------------NSSIIHDCFQGKVQIE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 854 VQCLTCHR---------------KSRTFETFMYLS--LPLASTSKCSLQD-CLRLFSKEEKLTDNNKVfcrHCKAHRDST 915
Cdd:cd02669 248 TQKIKPHAeeegskdkffkdsrvKKTSVSPFLLLTldLPPPPLFKDGNEEnIIPQVPLKQLLKKYDGK---TETELKDSL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 916 KKLEIWKVPPILLVHLKRFSYEGRWKQKLQTTVDFPLDSLDLAQYVIGPKQNQKRYGLYG-VSN--HYGG-LDGGHYTAY 991
Cdd:cd02669 325 KRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNlVANivHEGTpQEDGTWRVQ 404
|
330 340 350
....*....|....*....|....*....|....*
gi 1395229732 992 CKNALKQRWYKFDDHEVSEISTSSVKSSAAYILFY 1026
Cdd:cd02669 405 LRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
699-1026 |
1.61e-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: 65.63 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 699 LRNLGNTCYMNSILQCLCntpamaeyfnnncymadinrynilghkgevaeefgvimkalwaglykfisprdfkvTIGKIN 778
Cdd:cd02673 2 LVNTGNSCYFNSTMQALS--------------------------------------------------------SIGKIN 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 779 EQFAGYDQQDSQELLLFL---MDGLHEdlNKADNRKRYkEEENDHLdDPMAAdlawskHKLLNESIIValfqgqfkstvq 855
Cdd:cd02673 26 TEFDNDDQQDAHEFLLTLleaIDDIMQ--VNRTNVPPS-NIEIKRL-NPLEA------FKYTIESSYV------------ 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 856 CLTCHRKSRTFETFMYLSLPLASTSKCSLQDclrLFSKEEKLTDNNKVfCRHCKaHRDSTKKLEIWKVPPILLVHLKRFs 935
Cdd:cd02673 84 CIGCSFEENVSDVGNFLDVSMIDNKLDIDEL---LISNFKTWSPIEKD-CSSCK-CESAISSERIMTFPECLSINLKRY- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 936 yegrwkqKLQTTVdfpLDSLDLAQYVIGPKQNQ-KRYGLYGVSNHYG-GLDGGHYTAYCKNALK-QRWYKFDDHEVSEIS 1012
Cdd:cd02673 158 -------KLRIAT---SDYLKKNEEIMKKYCGTdAKYSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIRPVS 227
|
330
....*....|....*..
gi 1395229732 1013 TSSVK---SSAAYILFY 1026
Cdd:cd02673 228 KNDVStnaRSSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
786-1026 |
1.17e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 62.58 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 786 QQDSQELLLFLMDGLhEDlnkADNRKRYKEEENDHLDDPMaadlawskhkllnesiiVALFQGQFkSTVqclTCHRKSRT 865
Cdd:cd02665 22 QQDVSEFTHLLLDWL-ED---AFQAAAEAISPGEKSKNPM-----------------VQLFYGTF-LTE---GVLEGKPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 866 FETFMYLSLPLASTSKCSLQDCLrlfskeEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRWKQKLQ 945
Cdd:cd02665 77 CNCETFGQYPLQVNGYGNLHECL------EAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPEKIH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 946 TTVDFPldsldlaqyvigPKQNQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSEISTSSVKSSA----- 1020
Cdd:cd02665 151 DKLEFP------------QIIQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfgggr 218
|
....*....
gi 1395229732 1021 ---AYILFY 1026
Cdd:cd02665 219 npsAYCLMY 227
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
833-1026 |
3.55e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 52.90 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 833 KHKLLNE-----SIIVALFQGQFKSTVQC-----LTCHRKSRTFETFMY-LSLPLASTSKCSLQDCLRLFSKEEKLTDNN 901
Cdd:cd02672 54 ESCLLCElgylfSTLIQNFTRFLLETISQdqlgtPFSCGTSRNSVSLLYtLSLPLGSTKTSKESTFLQLLKRSLDLEKVT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 902 KVFCRHCKAHRDSTKKLEIWKVPPILL----VHLKRFSYEGRWKQ-------KLQTTVDFPLDSLDLAQYVIGPKQNQKr 970
Cdd:cd02672 134 KAWCDTCCKYQPLEQTTSIRHLPDILLlvlvINLSVTNGEFDDINvvlpsgkVMQNKVSPKAIDHDKLVKNRGQESIYK- 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395229732 971 YGLYG-VSNHYGGLDGGHYTA----YCKNALKQRWYKFDDHEVSEISTSsvkssaAYILFY 1026
Cdd:cd02672 213 YELVGyVCEINDSSRGQHNVVfvikVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
825-1005 |
8.06e-07 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 51.89 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 825 MAADLAWSKHKLL-NESIIVALFQGQFKSTVQCLTC-HRKSRTFETFM----YLSLPLASTSKCSLQD---CLRLFSKEE 895
Cdd:pfam13423 110 LSSEENSTPPNPSpAESPLEQLFGIDAETTIRCSNCgHESVRESSTHVldliYPRKPSSNNKKPPNQTfssILKSSLERE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 896 KLTdnnKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEgrWKQKLQTTVDFPLD-SLDLAQYVIGPkQNQKRYGLY 974
Cdd:pfam13423 190 TTT---KAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPEiGLTLSDDLQGD-NEIVKYELR 263
|
170 180 190
....*....|....*....|....*....|....*....
gi 1395229732 975 G-VSNHYGGLDGGHYTAYCK-------NALKQRWYKFDD 1005
Cdd:pfam13423 264 GvVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
697-1016 |
7.74e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 45.95 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 697 TGLRNLGNTCYMNSILQCL-CNTP---AMAEYFNNNCYMAD--INRYNILGHKGEVAEEFGVIMKALWAGL--YKFISPR 768
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFfTIKPlrdLVLNFDESKAELASdyPTERRIGGREVSRSELQRSNQFVYELRSlfNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 769 DFKVTIGKiNEQFAGYDQQDSQELLLFLMDglheDLNKADNRKRYKEEENDHLDDPMAADLawskhkllnesiIVALFQG 848
Cdd:cd02666 82 TRSVTPSK-ELAYLALRQQDVTECIDNVLF----QLEVALEPISNAFAGPDTEDDKEQSDL------------IKRLFSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 849 QFK-STVQCLTCHRKSRT--FETFMYLSLPLAST--------SKCSLQDCL----------------RLFSKEEKLTDNN 901
Cdd:cd02666 145 KTKqQLVPESMGNQPSVRtkTERFLSLLVDVGKKgreivvllEPKDLYDALdryfdydsltklpqrsQVQAQLAQPLQRE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 902 KVFCRHCKAHRDSTKKLEIWK--VPPILLVHLKRFSYEGRWKQKLQTTVDfpldslDLAQYVigpkqnqkrYGLYGVSNH 979
Cdd:cd02666 225 LISMDRYELPSSIDDIDELIReaIQSESSLVRQAQNELAELKHEIEKQFD------DLKSYG---------YRLHAVFIH 289
|
330 340 350
....*....|....*....|....*....|....*..
gi 1395229732 980 YGGLDGGHYTAYCKNALKQRWYKFDDHEVSEISTSSV 1016
Cdd:cd02666 290 RGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEV 326
|
|
| TAF4 |
pfam05236 |
Transcription initiation factor TFIID component TAF4 family; This region of similarity is ... |
97-176 |
2.42e-04 |
|
Transcription initiation factor TFIID component TAF4 family; This region of similarity is found in Transcription initiation factor TFIID component TAF4.
Pssm-ID: 461598 [Multi-domain] Cd Length: 264 Bit Score: 44.18 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 97 KAIVEAEKLSDSLKL--RYEEV-EVRKKL---EEKDRQEEKKRREEitEKDGGRVSPKVSSTTNMKDSKKVKGE-----Q 165
Cdd:pfam05236 88 KLIVISRHRRDGEKTdhRYEQTsDVRKQLkflAQKDKEEEERRVAE--EREGLLKAAKSRSNQEDPEQLKLKQEakemqK 165
|
90
....*....|.
gi 1395229732 166 NELKTATTKAA 176
Cdd:pfam05236 166 EEDEKMRHRAA 176
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
922-1026 |
2.68e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 43.67 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 922 KVPPILLVHLKRFSYEGRWKQKLQTTVDfPLDSLDLAQYV----------------------IGPKQNQKRYGLYGVSNH 979
Cdd:cd02670 97 KAPSCLIICLKRYGKTEGKAQKMFKKIL-IPDEIDIPDFVaddpracskcqlecrvcyddkdFSPTCGKFKLSLCSAVCH 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395229732 980 YG-GLDGGHYTAYCK-----------NALKQRWYKFDD-------HEVSEISTSSVKSSaAYILFY 1026
Cdd:cd02670 176 RGtSLETGHYVAFVRygsysltetdnEAYNAQWVFFDDmadrdgvSNGFNIPAARLLED-PYMLFY 240
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
292-540 |
3.24e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.78 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 292 ILRSEPLVLEGGYENWLLFYPMYTTNAKVRPPRQniiSTLPQLNFSYPSLIEPRPPTPTQQE-----PEVTPKPQETLDP 366
Cdd:PHA03307 79 APANESRSTPTWSLSTLAPASPAREGSPTPPGPS---SPDPPPPTPPPASPPPSPAPDLSEMlrpvgSPGPPPAASPPAA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 367 VLANGVTPADPPTSETSMVTDSLQEDTVDLPvkVSTSSALDLSKKGSAAAPSSQSP----ATAKAFPQFDRAKKPSIRVS 442
Cdd:PHA03307 156 GASPAAVASDAASSRQAALPLSSPEETARAP--SSPPAEPPPSTPPAAASPRPPRRsspiSASASSPAPAPGRSAADDAG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 443 DEPKPSQNGSAKDSNPFVPDRTAKPSFVPNTSLSKEEQSRIHSEAVAGiekaKQEQEKRIQERRRgkeqsSDAPSKSMSL 522
Cdd:PHA03307 234 ASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSR----PGPASSSSSPRER-----SPSPSPSSPG 304
|
250
....*....|....*...
gi 1395229732 523 DSPAPNPNHIVSEIKREP 540
Cdd:PHA03307 305 SGPAPSSPRASSSSSSSR 322
|
|
| FimV |
COG3170 |
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures]; |
314-529 |
6.33e-04 |
|
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];
Pssm-ID: 442403 [Multi-domain] Cd Length: 508 Bit Score: 43.63 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 314 YTtnAKVRPPRQNIISTLPQLNFSyPSLIEPRPPTPTQQEP-----------EVTPKPQETLDPVLANGVTPADPPTSET 382
Cdd:COG3170 100 YT--LLLDPPAYAAAAAAPAAAPA-PAPAAPAAAAAAADQPaaeaapaasgeYYPVRPGDTLWSIAARPVRPSSGVSLDQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 383 SMVtdSLQEDTVDLPVKvstsSALDLSKKG------SAAAPSSQSPATAKAFPQFDRAKKPSIRVSDEPKPSQNGSAKDS 456
Cdd:COG3170 177 MMV--ALYRANPDAFID----GNINRLKAGavlrvpAAEEVAALSPAEARQEVQAQSADWAAYRARLAAAVEPAPAAAAP 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395229732 457 NPFVPDRTAKPSfVP---NTSLSKEEQSRIHSEAVAgiekAKQEQEKRIQERRRGKEQSSDAPSKSMSLDSPAPNP 529
Cdd:COG3170 251 AAPPAAAAAAGP-VPaaaEDTLSPEVTAAAAAEEAD----ALPEAAAELAERLAALEAQLAELQRLLALKNPAPAA 321
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
322-557 |
4.84e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 322 PPRQNIISTLPQLNFSYPSLIEPRPPTPTQQEP--------EVTPKPQETLDPVLANGVTPADPPTSETSMVTDSlqEDT 393
Cdd:PHA03247 2679 PPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAphalvsatPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG--PAR 2756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 394 VDLPVKVSTSSAlDLSKKGSAAAPSSQSPATAKAFPQFDRAKKPSIR-------VSDEPKPSQNGSAKDSNPFVPDRTAK 466
Cdd:PHA03247 2757 PARPPTTAGPPA-PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWdpadppaAVLAPAAALPPAASPAGPLPPPTSAQ 2835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395229732 467 PSFVPNTSLSKEEQSRIHSEAVAGIE----------KAKQEQEKRIQERRRGKEQSSDAP-SKSMSLDSPAPNPNhivSE 535
Cdd:PHA03247 2836 PTAPPPPPGPPPPSLPLGGSVAPGGDvrrrppsrspAAKPAAPARPPVRRLARPAVSRSTeSFALPPDQPERPPQ---PQ 2912
|
250 260
....*....|....*....|..
gi 1395229732 536 IKREPLTRARSEEMGRSVPGLP 557
Cdd:PHA03247 2913 APPPPQPQPQPPPPPQPQPPPP 2934
|
|
| |
