|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1557-1960 |
2.36e-146 |
|
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: 458.65 E-value: 2.36e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1557 GFVGLKNAGATCYMNSVIQQLYMIPSIRNSILAIdsiwsdtdddifkgekqdsennvdprddvfryphqfedkptlsKVE 1636
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------------------------------------------PPT 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1637 DRKEYNIAVLKHLQITFGHLAASQLQYYVPKGFWQQFRLWGEPVNLREQHDALEFFNSLVDSLDEAFKALGYPTVLSKVL 1716
Cdd:cd02659 38 EDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1717 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCDKKVDTVKRLLIKKLPSVLT 1796
Cdd:cd02659 118 GGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1797 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGATKLEGDsvnpqtqlikqneqSESVIPGSTKYRLVGVLVHSGQ 1876
Cdd:cd02659 198 LQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKEGD--------------SEKKDSESYIYELHGVLVHSGD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1877 ANGGHYYSYIiqrngKDSKRSHWFKFDDGDVTECKMDDDEEmknQCFGGEYMGEVFDHMmkrmsYRRQKRWWNAYILFYE 1956
Cdd:cd02659 264 AHGGHYYSYI-----KDRDDGKWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYE 330
|
....
gi 120300980 1957 RMDI 1960
Cdd:cd02659 331 RKSP 334
|
|
| DUF3517 |
pfam12030 |
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ... |
2097-2457 |
1.07e-93 |
|
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 340 amino acids in length. This domain is found associated with pfam00443.
Pssm-ID: 463438 Cd Length: 407 Bit Score: 310.39 E-value: 1.07e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 2097 SNRFSEYLLECPSAEIRGTFAKLIVFIAH-----FSLQDGSSPspftspfanpgPYSQIYDNLSLSDHLLKAVLSLLRR- 2170
Cdd:pfam12030 1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCD-----------PDDLEEEWRSLSDSVLEAVVALLDHl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 2171 --EVSEHGRHLQQYFNLFIMYASLGLAEKTQLLKLN-VPATFMLVSLDEGPGPPVKYQYAEL------------SKLHSV 2235
Cdd:pfam12030 70 wkEFHTHLRSWDEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARMlrlvekrrppsyEKLIQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 2236 VSQLIRCCSVSSRMQSSINGNPPLPNpfgdpNLSQPIMPIQQNVADILFM--RT---TYMKKVIEDCSNSEDTVKLLLFC 2310
Cdd:pfam12030 150 LSVLLRCCDLSLPPQSINEGAEPLPN-----SLPDGPFPLTSEEADLLRPlgRTngsIFVKKLLEIDQNPEATRKILRFL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 2311 CWENPQFSCSVLSELLWQVAHSHAYELQPyLDLLLQIILFEDSWQAHRIHNALKGIPNDQDGLFDTIQHSKNHHQKRAYQ 2390
Cdd:pfam12030 225 LWENPELSDSILKTLLWGIRGAPAHLLRD-PFLRAAIVFCEDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQ 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 120300980 2391 CIKwMVTLFNSCPVAYQILQgngdlknkwtwamewlgdelerkpysgnpqyTYSNWSPPVQSNETAN 2457
Cdd:pfam12030 304 CIN-CRLGFDKEWFASQVLE-------------------------------NIPDWAPPLLSYPDSN 338
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1559-1955 |
1.82e-73 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 248.51 E-value: 1.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1559 VGLKNAGATCYMNSVIQQLYMIPSIRNSILaidsiwsdtdddifkgekqdsennvdprddvfRYPHQFEDkptlskveDR 1638
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLL--------------------------------RISPLSED--------SR 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1639 KEYNIAVLKHLQITFGHLA-ASQLQYYVPKGFWQQFRLWGEPVNLREQHDALEFFNSLVDSLDEAFKA---LGYPTVLSK 1714
Cdd:pfam00443 41 YNKDINLLCALRDLFKALQkNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1715 VLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLL------DSLEQYVKGDLLEGANAYHCEKCDKKVDTVKRLLI 1788
Cdd:pfam00443 121 LFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1789 KKLPSVLTIQLKRFDYDweRECAIKFNDYFEFPRELDMEPYTVAGATKLEGDSVnpqtqlikqneqsesvipgstKYRLV 1868
Cdd:pfam00443 201 SRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ---------------------DYRLV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1869 GVLVHSGQANGGHYYSYIiqrngKDSKRSHWFKFDDGDVTECKMDDDEEMknqcfggeymgevfdhmmkrmsyrrqkrwW 1948
Cdd:pfam00443 258 AVVVHSGSLSSGHYIAYI-----KAYENNRWYKFDDEKVTEVDEETAVLS-----------------------------S 303
|
....*..
gi 120300980 1949 NAYILFY 1955
Cdd:pfam00443 304 SAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1682-1956 |
8.98e-53 |
|
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: 186.92 E-value: 8.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1682 LREQHDALEFFNSLVDSLDEAFKALGY--------PTVLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDI----RNH 1749
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSKrtsdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1750 QNLLDSLEQYVKGDLLEGANAYHCEKCdKKVDTVKRLLIKKLPSVLTIQLKRFDYDwERECAIKFNDYFEFPRELDMEPY 1829
Cdd:cd02257 99 VSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1830 TVAGATKLEGDsvnpqtqlikqneqsesviPGSTKYRLVGVLVHSGQ-ANGGHYYSYIiqrngKDSKRSHWFKFDDGDVT 1908
Cdd:cd02257 177 LSEGEKDSDSD-------------------NGSYKYELVAVVVHSGTsADSGHYVAYV-----KDPSDGKWYKFNDDKVT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 120300980 1909 ECKMDDDEEMKNqcfggeymgevfdhmmkrmsyrrqkRWWNAYILFYE 1956
Cdd:cd02257 233 EVSEEEVLEFGS-------------------------LSSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1560-1956 |
6.85e-50 |
|
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: 181.08 E-value: 6.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1560 GLKNAGATCYMNSVIQQLYMIPSIRNSILAIDSiwsdTDDDIFKGEKQDSENNVDPrddvfryphqfedkptlskvedrk 1639
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNS----TEDAELKNMPPDKPHEPQT------------------------ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1640 eyniaVLKHLQITFGHLAASQLQYYVPKGFWQQFRLwgepvNLREQHDALEFFNSLVDSLDEAFKALGYP---TVLSKVL 1716
Cdd:cd02668 53 -----IIDQLQLIFAQLQFGNRSVVDPSGFVKALGL-----DTGQQQDAQEFSKLFLSLLEAKLSKSKNPdlkNIVQDLF 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1717 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCDKKVDTVKRLLIKKLPSVLT 1796
Cdd:cd02668 123 RGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1797 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVagatklegdsvnpqtqlikqnEQSEsvipGSTKYRLVGVLVHSGQ 1876
Cdd:cd02668 203 FQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLA---------------------ESDE----GSYVYELSGVLIHQGV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1877 -ANGGHYYSYIiqrngKDSKRSHWFKFDDGDVTE-----CKMDDDEEMKNQCFGgeymgevfDHMMKRMSYRrqkrwwNA 1950
Cdd:cd02668 258 sAYSGHYIAHI-----KDEQTGEWYKFNDEDVEEmpgkpLKLGNSEDPAKPRKS--------EIKKGTHSSR------TA 318
|
....*.
gi 120300980 1951 YILFYE 1956
Cdd:cd02668 319 YMLVYK 324
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1557-1963 |
1.12e-44 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 178.53 E-value: 1.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1557 GFVGLKNAGATCYMNSVIQQLYMIPSIRNSILAIDsiwsdTDDDifkgekqdsennvDPRDDVFR------YPHQFEDKP 1630
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP-----TDHP-------------RGRDSVALalqrlfYNLQTGEEP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1631 tLSKVEdrkeyniavlkhLQITFGhlaasqlqyyvpkgfwqqfrlWGEPVNLReQHDALEFFNSLVDSLDEAFKAlgypT 1710
Cdd:COG5077 254 -VDTTE------------LTRSFG---------------------WDSDDSFM-QHDIQEFNRVLQDNLEKSMRG----T 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1711 VLSKVLGGSFADQ-KICQGCPHR-YECE--ESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKcDKKVDTVKRL 1786
Cdd:COG5077 295 VVENALNGIFVGKmKSYIKCVNVnYESArvEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1787 LIKKLPSVLTIQLKRFDYDWERECAIKFNDYFEFPRELDMEPYtvagatkLEGDSvnpqtqliKQNEQSESVipgstkYR 1866
Cdd:COG5077 374 IFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPF-------LDRDA--------DKSENSDAV------YV 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1867 LVGVLVHSGQANGGHYYSYIiqrngKDSKRSHWFKFDDGDVTECKMdddEEMKNQCFGGEYMGEVfdhmmKRMSYRRQKR 1946
Cdd:COG5077 433 LYGVLVHSGDLHEGHYYALL-----KPEKDGRWYKFDDTRVTRATE---KEVLEENFGGDHPYKD-----KIRDHSGIKR 499
|
410
....*....|....*..
gi 120300980 1947 WWNAYILFYERMDITDE 1963
Cdd:COG5077 500 FMSAYMLVYLRKSMLDD 516
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1560-1914 |
1.97e-42 |
|
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: 158.59 E-value: 1.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1560 GLKNAGATCYMNSVIQQLYMIPSIRNSILaidsiwsdtdddifkgEKQDSENNVDPRDDVFRyphqfedkptlskvedrk 1639
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLL----------------SREHSKDCCNEGFCMMC------------------ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1640 eyniAVLKHLQitfgHLAASQLQYYVPKGFWQQFRLWGEPVNLREQHDALEFFNSLVDSLDEA----FKALGYP------ 1709
Cdd:cd02661 49 ----ALEAHVE----RALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKAcldrFKKLKAVdpssqe 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1710 -TVLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCDKKVDTVKRLLI 1788
Cdd:cd02661 121 tTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1789 KKLPSVLTIQLKRFDYDWERecaiKFNDYFEFPRELDMEPYTvagatklegdsVNPQTqlikqneqsesvipGSTKYRLV 1868
Cdd:cd02661 201 HRAPNVLTIHLKRFSNFRGG----KINKQISFPETLDLSPYM-----------SQPND--------------GPLKYKLY 251
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 120300980 1869 GVLVHSG-QANGGHYYSYIIQRNGKdskrshWFKFDDGDVTECKMDD 1914
Cdd:cd02661 252 AVLVHSGfSPHSGHYYCYVKSSNGK------WYNMDDSKVSPVSIET 292
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1684-1956 |
1.73e-35 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 136.26 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1684 EQHDALEFFNSLVDSLDeafkalgypTVLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDI------RNHQNLLDSLE 1757
Cdd:cd02674 21 DQQDAQEFLLFLLDGLH---------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLEDCLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1758 QYVKGDLLEGANAYHCEKCDKKVDTVKRLLIKKLPSVLTIQLKRFDYDweRECAIKFNDYFEFP-RELDMEPYTVAGAtk 1836
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPlNDLDLTPYVDTRS-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1837 legdsvnpqtqlikqneqsesvIPGSTKYRLVGVLVHSGQANGGHYYSYIiqrngKDSKRSHWFKFDDGDVTecKMDDDE 1916
Cdd:cd02674 168 ----------------------FTGPFKYDLYAVVNHYGSLNGGHYTAYC-----KNNETNDWYKFDDSRVT--KVSESS 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 120300980 1917 EMKNqcfggeymgevfdhmmkrmsyrrqkrwwNAYILFYE 1956
Cdd:cd02674 219 VVSS----------------------------SAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1560-1909 |
5.28e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 137.89 E-value: 5.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1560 GLKNAGATCYMNSVIQQLYMIPSIRNSILAidsiwsdtdDDIFKGEKQDSENN--VDPRDDVFrypHQFedkptlSKVED 1637
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLS---------DRHSCTCLSCSPNSclSCAMDEIF---QEF------YYSGD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1638 RKEYNIAvlkHLQITFGHLAASQLQYyvpkgfwqqfrlwgepvnlrEQHDALEFFNSLVDSL--------DEAFKALGYP 1709
Cdd:cd02660 64 RSPYGPI---NLLYLSWKHSRNLAGY--------------------SQQDAHEFFQFLLDQLhthyggdkNEANDESHCN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1710 TVLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRN---------------HQNLLDSLEQYVKGDLLeGANAYHCE 1774
Cdd:cd02660 121 CIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNkstpswalgesgvsgTPTLSDCLDRFTRPEKL-GDFAYKCS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1775 KCDKKVDTVKRLLIKKLPSVLTIQLKRFDYDwERECAIKFNDYFEFPRELDMEPYTVAGatklegdsvnpqtqliKQNEQ 1854
Cdd:cd02660 200 GCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-LNKTSRKIDTYVQFPLELNMTPYTSSS----------------IGDTQ 262
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 120300980 1855 SESVIPGSTKYRLVGVLVHSGQANGGHYYSYIiqRNGKDskrsHWFKFDDGDVTE 1909
Cdd:cd02660 263 DSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYC--RQGDG----QWFKFDDAMITR 311
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1560-1920 |
7.33e-34 |
|
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: 134.54 E-value: 7.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1560 GLKNAGATCYMNSVIQQLYMIPSIRNSILaidsiwsdtdddifkgekqdsennvdprddvfryphqfedkptlSKVEDRK 1639
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVL--------------------------------------------SLNLPRL 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1640 EYNIAVLKHLQITFGHLAASQLQYY-VPKGFWQQfrLWGEPVNLREQHDALEFFNSLVDSLDeafkalgypTVLSKVLGG 1718
Cdd:cd02664 37 GDSQSVMKKLQLLQAHLMHTQRRAEaPPDYFLEA--SRPPWFTPGSQQDCSEYLRYLLDRLH---------TLIEKMFGG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1719 SFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDsleQYVKGDLLEGANAYHCEKCDKKVDTVKRLLIKKLPSVLTIQ 1798
Cdd:cd02664 106 KLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDLLN---YFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1799 LKRFDYDWERECAIKFNDYFEFPRELDMepyTVAGATKLEGDSVNpqTQLIKQNEQSESVIPgSTKYRLVGVLVHSG-QA 1877
Cdd:cd02664 183 LLRFSYDQKTHVREKIMDNVSINEVLSL---PVRVESKSSESPLE--KKEEESGDDGELVTR-QVHYRLYAVVVHSGySS 256
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1878 NGGHYYSYIiqRNGKDSKRSH-----------------WFKFDDGDVTECKMdddEEMKN 1920
Cdd:cd02664 257 ESGHYFTYA--RDQTDADSTGqecpepkdaeendesknWYLFNDSRVTFSSF---ESVQN 311
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1685-1956 |
2.84e-29 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 119.80 E-value: 2.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1685 QHDALEFFNSLVDSLDeafkalgypTVLSKVLGGSFADQKICQGCPHRYECEESFTTLN----VDIRNHQNLLDSLEQYV 1760
Cdd:cd02667 51 QQDSHELLRYLLDGLR---------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSlprsDEIKSECSIESCLKQFT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1761 KGDLLEGANAYHCEKCDKkvdTVKRLLIKKLPSVLTIQLKRFDYDwERECAIKFNDYFEFPRELDMEPYTVAGATKLEGD 1840
Cdd:cd02667 122 EVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPFCDPKCNSSEDK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1841 SvnpqtqlikqneqsesvipgSTKYRLVGVLVHSGQANGGHYYSYI----------------IQRNGKDSKRSHWFKFDD 1904
Cdd:cd02667 198 S--------------------SVLYRLYGVVEHSGTMRSGHYVAYVkvrppqqrlsdltkskPAADEAGPGSGQWYYISD 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 120300980 1905 GDVTEckMDDDEEMKNQcfggeymgevfdhmmkrmsyrrqkrwwnAYILFYE 1956
Cdd:cd02667 258 SDVRE--VSLEEVLKSE----------------------------AYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1641-1956 |
6.91e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 110.48 E-value: 6.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1641 YNIAVLKHLQITFGHLAASQLQYYV--PKGFWQQFRLWGEPVNLREQHDALEFF----NSLVDSLDEAFKALGY------ 1708
Cdd:cd02663 19 YFENLLTCLKDLFESISEQKKRTGVisPKKFITRLKRENELFDNYMHQDAHEFLnfllNEIAEILDAERKAEKAnrklnn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1709 -------PTVLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCDKKVD 1781
Cdd:cd02663 99 nnnaepqPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1782 TVKRLLIKKLPSVLTIQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTvagatkleGDSVNPqTQLikqneqsesvipg 1861
Cdd:cd02663 179 AEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLFNTT--------DDAENP-DRL------------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1862 stkYRLVGVLVHSGQ-ANGGHYYSyIIQRNGkdskrsHWFKFDDGDVTecKMDDdeemknqcfggEYMGEVFDHmmkrms 1940
Cdd:cd02663 237 ---YELVAVVVHIGGgPNHGHYVS-IVKSHG------GWLLFDDETVE--KIDE-----------NAVEEFFGD------ 287
|
330
....*....|....*.
gi 120300980 1941 yrrQKRWWNAYILFYE 1956
Cdd:cd02663 288 ---SPNQATAYVLFYQ 300
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1560-1956 |
2.11e-19 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239122 [Multi-domain] Cd Length: 305 Bit Score: 91.62 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1560 GLKNAGATCYMNSVIQQLYMIPSIRNSILAIDSIWSDTDddifkgekqdsennvdprddvfryphQFEDKPTLSkvedrk 1639
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGAN--------------------------QSSDNLTNA------ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1640 eyniavLKHLqitFGHLAASQlQYYVPKGFWQQFRL----WGEP--VNLREQHDALEFFNSLVDSLDEAFK-ALGYPTVL 1712
Cdd:cd02657 49 ------LRDL---FDTMDKKQ-EPVPPIEFLQLLRMafpqFAEKqnQGGYAQQDAEECWSQLLSVLSQKLPgAGSKGSFI 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1713 SKVLGGSFADQKICQGCPHRYECE-ESFTTLNVDIrNHQNLLDSLEQYVKgDLLEGANAYHCEKCDKKVDTVKRLLIKKL 1791
Cdd:cd02657 119 DQLFGIELETKMKCTESPDEEEVStESEYKLQCHI-SITTEVNYLQDGLK-KGLEEEIEKHSPTLGRDAIYTKTSRISRL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1792 PSVLTIQLKRFDydWERECAI--KFNDYFEFPRELDMEPYtvagatklegdsvnpqtqlikqneqsesvIPGSTKYRLVG 1869
Cdd:cd02657 197 PKYLTVQFVRFF--WKRDIQKkaKILRKVKFPFELDLYEL-----------------------------CTPSGYYELVA 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1870 VLVHSGQ-ANGGHYYSYIiqrngKDSKRSHWFKFDDGDVTECKMDDDEEMKNqcfGGEYmgevfdHMmkrmsyrrqkrww 1948
Cdd:cd02657 246 VITHQGRsADSGHYVAWV-----RRKNDGKWIKFDDDKVSEVTEEDILKLSG---GGDW------HI------------- 298
|
....*...
gi 120300980 1949 nAYILFYE 1956
Cdd:cd02657 299 -AYILLYK 305
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1560-1920 |
2.64e-18 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 88.53 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1560 GLKNAGATCYMNSVIQQLYMIPSIRnsilaidsiwsdTDDDIFKGEKQDseNNVDPRDDVF-------------RYphqf 1626
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQ------------WRYDDLENKFPS--DVVDPANDLNcqlikladgllsgRY---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1627 edkptlSKVEDRKEYNIAVLKHLQ-ITFGHLAAsqlQYYvpkgfwQQFrlwgepvNLREQHDALEFFNSLVDSLD-EAFK 1704
Cdd:cd02658 63 ------SKPASLKSENDPYQVGIKpSMFKALIG---KGH------PEF-------STMRQQDALEFLLHLIDKLDrESFK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1705 ALGY-PTVLSKVlggsFADQKI-CQGCPHRYECEESFTTLNVDIRNH--------------QNLLDSLEQYVKGDLLEga 1768
Cdd:cd02658 121 NLGLnPNDLFKF----MIEDRLeCLSCKKVKYTSELSEILSLPVPKDeatekeegelvyepVPLEDCLKAYFAPETIE-- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1769 naYHCEKCDKKVDTVKRLLIKKLPSVLTIQLKRFDY--DWErecaikfndyfefPRELDMePYTVAGatklegdsvnpqt 1846
Cdd:cd02658 195 --DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLleNWV-------------PKKLDV-PIDVPE------------- 245
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 120300980 1847 qlikqneqsesvIPGSTKYRLVGVLVHSG-QANGGHYYSYIIQRNGKDSKrshWFKFDDGDVteCKMDDDEEMKN 1920
Cdd:cd02658 246 ------------ELGPGKYELIAFISHKGtSVHSGHYVAHIKKEIDGEGK---WVLFNDEKV--VASQDPPEMKK 303
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1685-1925 |
2.22e-17 |
|
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: 83.76 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1685 QHDALEFFNSLVDSLDEAFKALGYPTVLSK--------VLGGSFADQKICQGcpHRYECEESFTTLNVDIRNHQNLLDSL 1756
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEksknpmvqLFYGTFLTEGVLEG--KPFCNCETFGQYPLQVNGYGNLHECL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1757 E-QYVKGDLLEganayhcEKCDKKVDTVKRLLIKKLPSVLTIQLKRFDYDWERECaiKFNDYFEFPRELDMEPYtvagat 1835
Cdd:cd02665 100 EaAMFEGEVEL-------LPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPE--KIHDKLEFPQIIQQVPY------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1836 klegdsvnpqtqlikqneqsesvipgstkyRLVGVLVHSGQANGGHYYSYIIQRNgkdskRSHWFKFDDGDVTECkmdDD 1915
Cdd:cd02665 165 ------------------------------ELHAVLVHEGQANAGHYWAYIYKQS-----RQEWEKYNDISVTES---SW 206
|
250
....*....|
gi 120300980 1916 EEMKNQCFGG 1925
Cdd:cd02665 207 EEVERDSFGG 216
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1560-1957 |
2.90e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 81.77 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1560 GLKNAGATCYMNSVIQQL-YMIPSIRNSILAIDSIWSDTDDDIFKGEKQDsenNVDPRDDVFR-----YPHQFEDKPTLS 1633
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKELKVLKNVIRKPEPDL---NQEEALKLFTalwssKEHKVGWIPPMG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1634 KVEDRKEYNIAVLKHLQItfghlaasQLQYyvpkgfwQQFRLWGEPVNLREQHDALEFFNSLVdsldeafkalgyptvlS 1713
Cdd:COG5533 78 SQEDAHELLGKLLDELKL--------DLVN-------SFTIRIFKTTKDKKKTSTGDWFDIII----------------E 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1714 KVLGGSFADQKICQGCPhryECEESFTTLNVDIRNHQNllDSLEqyvkgdlleganayhcekCDKKVDTVkrLLIKKLPS 1793
Cdd:COG5533 127 LPDQTWVNNLKTLQEFI---DNMEELVDDETGVKAKEN--EELE------------------VQAKQEYE--VSFVKLPK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1794 VLTIQLKRFDYDwerecaikfndyfefpreldmepytvAGATKLEgDSVNPQTQLIKQNEQSESVIPgSTKYRLVGVLVH 1873
Cdd:COG5533 182 ILTIQLKRFANL--------------------------GGNQKID-TEVDEKFELPVKHDQILNIVK-ETYYDLVGFVLH 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1874 SGQANGGHYYSYIIQRNgkdskrsHWFKFDDGDVTECKMDDDEEMKNQcfggeymgevfdhmmkrmsyrrqkrwwNAYIL 1953
Cdd:COG5533 234 QGSLEGGHYIAYVKKGG-------KWEKANDSDVTPVSEEEAINEKAK---------------------------NAYLY 279
|
....
gi 120300980 1954 FYER 1957
Cdd:COG5533 280 FYER 283
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1534-1907 |
3.26e-13 |
|
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: 73.39 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1534 PVTTCEAVgewEYLPPvgprppkgFVGLKNAGATCYMNSVIQQLYMIPSIRNSILAIDSIWSDtdddifKGEKQDSennv 1613
Cdd:cd02671 11 SATSCEKR---ENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISS------VEQLQSS---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1614 dprddvfryphqFEDKPTLskvedrkeYNiavlkhlqitfgHLAASQLqyyvPKGFWQQFRLWGEPVNLREQHDALEFFN 1693
Cdd:cd02671 70 ------------FLLNPEK--------YN------------DELANQA----PRRLLNALREVNPMYEGYLQHDAQEVLQ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1694 SLVDSLDEAFkalgyptvlSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQ-------------------NLLD 1754
Cdd:cd02671 114 CILGNIQELV---------EKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESElskseesseispdpktemkTLKW 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1755 SLEQYVKGDLLEGANAYHCEKCDKKVDTVKRLLIKKLPSVLTIQLKRFDYDWERECAI----KFNDYFEFPRELDMEpyt 1830
Cdd:cd02671 185 AISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVNTPLLTPLKLSLE--- 261
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 120300980 1831 vagatklegdsvnpqtqlikqnEQSESviPGSTKYRLVGVLVHSG-QANGGHYYSYIiqrngkdskrsHWFKFDDGDV 1907
Cdd:cd02671 262 ----------------------EWSTK--PKNDVYRLFAVVMHSGaTISSGHYTAYV-----------RWLLFDDSEV 304
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1671-1914 |
1.61e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 69.70 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1671 QQFRLWGEpvNLREQHDALEFFNSLVDSLDEAFKALgyptvlskvLGGSFADQKICQGCPH----RYECeESFTTLNV-- 1744
Cdd:cd02662 22 PSLIEYLE--EFLEQQDAHELFQVLLETLEQLLKFP---------FDGLLASRIVCLQCGEsskvRYES-FTMLSLPVpn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1745 -DIRNHQNLLDSLEQYVKGDLLEGanaYHCEKCdkkvdtvkRLLIKKLPSVLTIQLKRFDYDwERECAIKFNDYFEFPRE 1823
Cdd:cd02662 90 qSSGSGTTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1824 LdmepytvagaTKLegdsvnpqtqlikqneqsesvipgstKYRLVGVLVHSGQANGGHYYSY--------------IIQR 1889
Cdd:cd02662 158 L----------PKV--------------------------LYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsFVRM 201
|
250 260
....*....|....*....|....*.
gi 120300980 1890 NGKDSKRSH-WFKFDDGDVTECKMDD 1914
Cdd:cd02662 202 REGPSSTSHpWWRISDTTVKEVSESE 227
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1559-1909 |
5.78e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 66.75 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1559 VGLKNAGATCYMNSVIQQLYMIPSIRNSILAIDsiwsdtdddifkgekqdsENNVDPRDdvfryphqfeDKPTLSKVEDR 1638
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFD------------------ESKAELAS----------DYPTERRIGGR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1639 KEYNIAVLKHLQIT------FGHLAASQLQYYVPKgfwqqfrlwGEPVNLR-EQHDALEFFNSLVDSLDEAFKALGYPTV 1711
Cdd:cd02666 54 EVSRSELQRSNQFVyelrslFNDLIHSNTRSVTPS---------KELAYLAlRQQDVTECIDNVLFQLEVALEPISNAFA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1712 LSK-VLGGSFADQ-------KICQ--------GCPHRYECEESFTTLNVDIR---------NH-QNLLDSLEQYVKGDLL 1765
Cdd:cd02666 125 GPDtEDDKEQSDLikrlfsgKTKQqlvpesmgNQPSVRTKTERFLSLLVDVGkkgreivvlLEpKDLYDALDRYFDYDSL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1766 EGANAYhcekcdkkvdtvkRLLIKKLPSVLTIQLkrfDYDWERECAIKFNDYFEFPRELDMEPYTVAGATKLEGDSVNPQ 1845
Cdd:cd02666 205 TKLPQR-------------SQVQAQLAQPLQREL---ISMDRYELPSSIDDIDELIREAIQSESSLVRQAQNELAELKHE 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 120300980 1846 TQLIKQNEQSESvipgstkYRLVGVLVHSGQANGGHYYSYIiqrngKDSKRSHWFKFDDGDVTE 1909
Cdd:cd02666 269 IEKQFDDLKSYG-------YRLHAVFIHRGEASSGHYWVYI-----KDFEENVWRKYNDETVTV 320
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1752-1909 |
4.16e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 65.67 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1752 LLDSLEQYVKGDLLEGANAYHCEKCDKKVDTVKRLLIKKLPSVLTIQLKRFDYDweRECAIKFNDYFEFP-RELDMEPYT 1830
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSV--RSFRDKIDDLVEYPiDDLDLSGVE 754
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 120300980 1831 VagatklegdsvnpqtqlikqneqseSVIPGSTKYRLVGVLVHSGQANGGHYYSYIiqRNGKDSKrshWFKFDDGDVTE 1909
Cdd:COG5560 755 Y-------------------------MVDDPRLIYDLYAVDNHYGGLSGGHYTAYA--RNFANNG---WYLFDDSRITE 803
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
1559-1904 |
2.01e-09 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 61.52 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1559 VGLKNAGATCYMNSVIQQLYMIPSIRNsiLAIDSIWSDtdddifkgekqdsennvDPRDD--------VFRYphqfedkp 1630
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRN--LALSHLATE-----------------CLKEHcllcelgfLFDM-------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1631 tLSKvedrkeyniAVLKHLQIT-----FGHLA-ASQLqyyvpkGFWQQFRLWGEPVNLR-----------EQ--HDALEF 1691
Cdd:pfam13423 54 -LEK---------AKGKNCQASnflraLSSIPeASAL------GLLDEDRETNSAISLSsliqsfnrfllDQlsSEENST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1692 FNSLVDSldeafkalgyPTVLSKVLGGSFADQKICQGCPHRYECEESFTTLN------VDIRNHQNLLDSLEQYVKGDLL 1765
Cdd:pfam13423 118 PPNPSPA----------ESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDliyprkPSSNNKKPPNQTFSSILKSSLE 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1766 -EGANAYHCEKCDKKVDTVKRLLIKKLPSVLTIQLKRFDYDWEREcaIKFNDYfeFPRELDMepytvagatklegdsvnp 1844
Cdd:pfam13423 188 rETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL--WKTPGW--LPPEIGL------------------ 245
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 120300980 1845 qtqlikQNEQSESVIPGSTKYRLVGVLVH-SGQANGGHYYSYI--IQRNGKDSKRSHWFKFDD 1904
Cdd:pfam13423 246 ------TLSDDLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVkvADSELEDPTESQWYLFND 302
|
|
| Ubl_UBP24 |
cd17065 |
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ... |
900-964 |
3.51e-09 |
|
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; UBP24 (EC 3.4.19.12), also termed deubiquitinating enzyme 24, or ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24 (USP24), is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain, a ubiquitin-like (Ubl) domain, and a C-terminal peptidase C19 domain.
Pssm-ID: 340585 Cd Length: 79 Bit Score: 55.39 E-value: 3.51e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 120300980 900 EDLDILSHTNATIGSVRRCILNRMNVNVAHtkIELFIGGELVASEDDRKLVEQLNLKDKSLITAK 964
Cdd:cd17065 17 QEFTLEVHSNETLGSVRQKIAERLNCPVDQ--VQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1777-1956 |
5.55e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 53.30 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1777 DKKVDTVKRLL--------IKKLPSVLTIQLKRfdYDWERECAIKFNDYFEFPRELDMePYTVAGATKleGDSVNPQTQL 1848
Cdd:cd02670 76 DGGGITLEQCLeqyfnnsvFAKAPSCLIICLKR--YGKTEGKAQKMFKKILIPDEIDI-PDFVADDPR--ACSKCQLECR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1849 IKQNEQSESVIPGSTKYRLVGVLVHSGQA-NGGHYYSYI------IQRNGKDSKRSHWFKFDDgdvteckMDDDEemknq 1921
Cdd:cd02670 151 VCYDDKDFSPTCGKFKLSLCSAVCHRGTSlETGHYVAFVrygsysLTETDNEAYNAQWVFFDD-------MADRD----- 218
|
170 180 190
....*....|....*....|....*....|....*
gi 120300980 1922 cfGGEYmgeVFDHMMKRmsyrrqkRWWNAYILFYE 1956
Cdd:cd02670 219 --GVSN---GFNIPAAR-------LLEDPYMLFYQ 241
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1545-1910 |
7.49e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 54.25 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1545 EYLPpvgprppkGFVGLKNAGATCYMNSVIQQLYMIPSIRNSILaidsiwsdtdddifkgekqdSENNvdprddvfrYPH 1624
Cdd:cd02669 114 PYLP--------GFVGLNNIKNNDYANVIIQALSHVKPIRNFFL--------------------LYEN---------YEN 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1625 QFEDKPTLSKVED---RKEYNIAVLKhlqitfGHLAASQLQYYVPKGFWQQFRLwgepvnlREQHDALEFF----NSLVD 1697
Cdd:cd02669 157 IKDRKSELVKRLSeliRKIWNPRNFK------GHVSPHELLQAVSKVSKKKFSI-------TEQSDPVEFLswllNTLHK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1698 SLDEAFKALgyPTVLSKVLGG--SFADQKIcqgcPHRYECEES-----------------FTTLNVDIRN-----HQNLL 1753
Cdd:cd02669 224 DLGGSKKPN--SSIIHDCFQGkvQIETQKI----KPHAEEEGSkdkffkdsrvkktsvspFLLLTLDLPPpplfkDGNEE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1754 DSLEQYVKGDLLEGANAYHCEKCDKKVdtvKRLLIKKLPSVLTIQLKRFDYdwerecaikfNDYF--------EFPRELD 1825
Cdd:cd02669 298 NIIPQVPLKQLLKKYDGKTETELKDSL---KRYLISRLPKYLIFHIKRFSK----------NNFFkeknptivNFPIKNL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120300980 1826 MEPYTVAGATKLEGDsvnpqtqlikqneqsesvipgSTKYRLVGVLVHSGQANGGHYYSYIIQRNGKDSkrshWFKFDDG 1905
Cdd:cd02669 365 DLSDYVHFDKPSLNL---------------------STKYNLVANIVHEGTPQEDGTWRVQLRHKSTNK----WFEIQDL 419
|
....*
gi 120300980 1906 DVTEC 1910
Cdd:cd02669 420 NVKEV 424
|
|
| |
