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Conserved domains on  [gi|14149627|ref|NP_006304|]
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ubiquitin carboxyl-terminal hydrolase 15 isoform 2 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 1000871)

ubiquitin carboxyl-terminal hydrolase is a C19 family peptidase that deubiquitinates polyubiquitinated target proteins

CATH:  3.90.70.10
EC:  3.4.19.12
Gene Ontology:  GO:0016579|GO:0046872|GO:0003723

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
12-903 9.35e-147

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


The actual alignment was detected with superfamily member COG5560:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 455.88  E-value: 9.35e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627  12 QRSDIATLLKTSLRKGDTWYLVDSRWFKqwkKYVGFDSWDkyqmGDqnvYPGPIdNSGLLKDGDAQSLKEHLIDELDYIL 91
Cdd:COG5560  29 QEELIDEKPAESSKQCEYAVIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSI 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627  92 LPTEGWNKLVSWYTLMEGQEPiaRKVV----EQGMFVKHCKVEVYLTELKLCENGNMN---NVVTRRFSKADTIDTIEKE 164
Cdd:COG5560  98 ISGAVWQLLVRWYGLAGLITP--RITVllpsESAPEVESYPVVFKLHWLFSINGSLINlghDPVPHSASSHGTLRDLSER 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 165 IRKIFSIPDEkETRLWNKYMSNTFEPLNKPDSTI-QDAGLYQGQVLVIEQKNEDGTwPRGPSTPNVKNSNYCLPSYTAYK 243
Cdd:COG5560 176 VMNAFVDPSD-DFRLWDVVPEIMGLRLGLDSFFRrYRVLASDGRVLHPLTRLELFE-DRSVLLLSKITRNPDWLVDSIVD 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 244 NYDYSepgrNNEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRGEIAKSYAELIKQMWSG 323
Cdd:COG5560 254 DHNRS----INKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDG 329
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 324 KFSYVTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIQ---LKDADGRPDKVVAEEAWENHLKR 400
Cdd:COG5560 330 NLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKR 409
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 401 NDSIIVDIFHGLFKSTLVCPECAKISVTFDPFCYLTLPLPMKKERTLEVYLVRMDPLTKPMQYKVVV-PKIGNILDLCTA 479
Cdd:COG5560 410 NDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQPLKIELDAsSTIRGLKKLVDA 489
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 480 LSALSGIpaDKMIVTDIYNHRFHRIF--AMDENLSSIMERDDIYVFEININrtedteHVIIPVclrekFRHSSYTHHTGS 557
Cdd:COG5560 490 EYGKLGC--FEIKVMCIYYGGNYNMLepADKVLLQDIPQTDFVYLYETNDN------GIEVPV-----VHLRIEKGYKSK 556
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 558 SLFGQPFLM--AVPRNNTEDKLYNLLLLRMCRYVKISTETEETEGSLHCckdqNINGNGPNGIHeegsPSEMETDEPDDE 635
Cdd:COG5560 557 RLFGDPFLQlnVLIKASIYDKLVKEFEELLVLVEMKKTDVDLVSEQVRL----LREESSPSSWL----KLETEIDTKREE 628
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 636 SSQDQELPSENENsqsedsvggdndsenglcTEDTCkgqLTGHKKRLFTFQFNNLGNtdinyikddtrhirfdDRQLRLD 715
Cdd:COG5560 629 QVEEEGQMNFNDA------------------VVISC---EWEEKRYLSLFSYDPLWT----------------IREIGAA 671
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 716 ERSflaldwdpdlkkryfdenaaedfekhesveykppkkpfVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDL 795
Cdd:COG5560 672 ERT--------------------------------------ITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMEL 713
                       810       820       830       840       850       860       870       880
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 796 WSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPINDLDMSEFLINPNAGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKW 875
Cdd:COG5560 714 WRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGW 793
                       890       900
                ....*....|....*....|....*...
gi 14149627 876 YYFDDSSVSTASEDQIVSKAAYVLFYQR 903
Cdd:COG5560 794 YLFDDSRITEVDPEDSVTSSAYVLFYRR 821
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
12-903 9.35e-147

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 455.88  E-value: 9.35e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627  12 QRSDIATLLKTSLRKGDTWYLVDSRWFKqwkKYVGFDSWDkyqmGDqnvYPGPIdNSGLLKDGDAQSLKEHLIDELDYIL 91
Cdd:COG5560  29 QEELIDEKPAESSKQCEYAVIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSI 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627  92 LPTEGWNKLVSWYTLMEGQEPiaRKVV----EQGMFVKHCKVEVYLTELKLCENGNMN---NVVTRRFSKADTIDTIEKE 164
Cdd:COG5560  98 ISGAVWQLLVRWYGLAGLITP--RITVllpsESAPEVESYPVVFKLHWLFSINGSLINlghDPVPHSASSHGTLRDLSER 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 165 IRKIFSIPDEkETRLWNKYMSNTFEPLNKPDSTI-QDAGLYQGQVLVIEQKNEDGTwPRGPSTPNVKNSNYCLPSYTAYK 243
Cdd:COG5560 176 VMNAFVDPSD-DFRLWDVVPEIMGLRLGLDSFFRrYRVLASDGRVLHPLTRLELFE-DRSVLLLSKITRNPDWLVDSIVD 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 244 NYDYSepgrNNEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRGEIAKSYAELIKQMWSG 323
Cdd:COG5560 254 DHNRS----INKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDG 329
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 324 KFSYVTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIQ---LKDADGRPDKVVAEEAWENHLKR 400
Cdd:COG5560 330 NLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKR 409
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 401 NDSIIVDIFHGLFKSTLVCPECAKISVTFDPFCYLTLPLPMKKERTLEVYLVRMDPLTKPMQYKVVV-PKIGNILDLCTA 479
Cdd:COG5560 410 NDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQPLKIELDAsSTIRGLKKLVDA 489
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 480 LSALSGIpaDKMIVTDIYNHRFHRIF--AMDENLSSIMERDDIYVFEININrtedteHVIIPVclrekFRHSSYTHHTGS 557
Cdd:COG5560 490 EYGKLGC--FEIKVMCIYYGGNYNMLepADKVLLQDIPQTDFVYLYETNDN------GIEVPV-----VHLRIEKGYKSK 556
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 558 SLFGQPFLM--AVPRNNTEDKLYNLLLLRMCRYVKISTETEETEGSLHCckdqNINGNGPNGIHeegsPSEMETDEPDDE 635
Cdd:COG5560 557 RLFGDPFLQlnVLIKASIYDKLVKEFEELLVLVEMKKTDVDLVSEQVRL----LREESSPSSWL----KLETEIDTKREE 628
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 636 SSQDQELPSENENsqsedsvggdndsenglcTEDTCkgqLTGHKKRLFTFQFNNLGNtdinyikddtrhirfdDRQLRLD 715
Cdd:COG5560 629 QVEEEGQMNFNDA------------------VVISC---EWEEKRYLSLFSYDPLWT----------------IREIGAA 671
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 716 ERSflaldwdpdlkkryfdenaaedfekhesveykppkkpfVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDL 795
Cdd:COG5560 672 ERT--------------------------------------ITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMEL 713
                       810       820       830       840       850       860       870       880
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 796 WSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPINDLDMSEFLINPNAGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKW 875
Cdd:COG5560 714 WRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGW 793
                       890       900
                ....*....|....*....|....*...
gi 14149627 876 YYFDDSSVSTASEDQIVSKAAYVLFYQR 903
Cdd:COG5560 794 YLFDDSRITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
755-902 4.74e-60

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: 204.44  E-value: 4.74e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 755 PFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPINDLDMSE 834
Cdd:cd02674  82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTP 161
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14149627 835 FLINPN-AGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQ 902
Cdd:cd02674 162 YVDTRSfTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
260-451 4.74e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 187.65  E-value: 4.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627   260 CGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDkyqEELNFDNPLGMRGEIAKSYAELIKQMWSG-KFSYVTPRAFKTQVG 338
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRI---SPLSEDSRYNKDINLLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627   339 RFAPQFSGYQQQDCQELLAFLLDGLHEDLNRirkkpyiqlkdadgrpdkvvaeeaweNHLKRNDSIIVDIFHGLFKSTLV 418
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                         170       180       190
                  ....*....|....*....|....*....|...
gi 14149627   419 CPECAKISVTFDPFCYLTLPLPMKKERTLEVYL 451
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASL 164
DUSP smart00695
Domain in ubiquitin-specific proteases;
24-121 2.97e-30

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 114.38  E-value: 2.97e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627     24 LRKGDTWYLVDSRWFKQWKKYVGfdswdkyqmGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSW 103
Cdd:smart00695   2 LEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRW 72
                           90
                   ....*....|....*...
gi 14149627    104 YTLMEGqePIARKVVEQG 121
Cdd:smart00695  73 YGGGPG--PIPRKVVCQG 88
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
12-903 9.35e-147

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 455.88  E-value: 9.35e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627  12 QRSDIATLLKTSLRKGDTWYLVDSRWFKqwkKYVGFDSWDkyqmGDqnvYPGPIdNSGLLKDGDAQSLKEHLIDELDYIL 91
Cdd:COG5560  29 QEELIDEKPAESSKQCEYAVIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSI 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627  92 LPTEGWNKLVSWYTLMEGQEPiaRKVV----EQGMFVKHCKVEVYLTELKLCENGNMN---NVVTRRFSKADTIDTIEKE 164
Cdd:COG5560  98 ISGAVWQLLVRWYGLAGLITP--RITVllpsESAPEVESYPVVFKLHWLFSINGSLINlghDPVPHSASSHGTLRDLSER 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 165 IRKIFSIPDEkETRLWNKYMSNTFEPLNKPDSTI-QDAGLYQGQVLVIEQKNEDGTwPRGPSTPNVKNSNYCLPSYTAYK 243
Cdd:COG5560 176 VMNAFVDPSD-DFRLWDVVPEIMGLRLGLDSFFRrYRVLASDGRVLHPLTRLELFE-DRSVLLLSKITRNPDWLVDSIVD 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 244 NYDYSepgrNNEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRGEIAKSYAELIKQMWSG 323
Cdd:COG5560 254 DHNRS----INKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDG 329
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 324 KFSYVTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIQ---LKDADGRPDKVVAEEAWENHLKR 400
Cdd:COG5560 330 NLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKR 409
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 401 NDSIIVDIFHGLFKSTLVCPECAKISVTFDPFCYLTLPLPMKKERTLEVYLVRMDPLTKPMQYKVVV-PKIGNILDLCTA 479
Cdd:COG5560 410 NDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQPLKIELDAsSTIRGLKKLVDA 489
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 480 LSALSGIpaDKMIVTDIYNHRFHRIF--AMDENLSSIMERDDIYVFEININrtedteHVIIPVclrekFRHSSYTHHTGS 557
Cdd:COG5560 490 EYGKLGC--FEIKVMCIYYGGNYNMLepADKVLLQDIPQTDFVYLYETNDN------GIEVPV-----VHLRIEKGYKSK 556
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 558 SLFGQPFLM--AVPRNNTEDKLYNLLLLRMCRYVKISTETEETEGSLHCckdqNINGNGPNGIHeegsPSEMETDEPDDE 635
Cdd:COG5560 557 RLFGDPFLQlnVLIKASIYDKLVKEFEELLVLVEMKKTDVDLVSEQVRL----LREESSPSSWL----KLETEIDTKREE 628
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 636 SSQDQELPSENENsqsedsvggdndsenglcTEDTCkgqLTGHKKRLFTFQFNNLGNtdinyikddtrhirfdDRQLRLD 715
Cdd:COG5560 629 QVEEEGQMNFNDA------------------VVISC---EWEEKRYLSLFSYDPLWT----------------IREIGAA 671
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 716 ERSflaldwdpdlkkryfdenaaedfekhesveykppkkpfVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDL 795
Cdd:COG5560 672 ERT--------------------------------------ITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMEL 713
                       810       820       830       840       850       860       870       880
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 796 WSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPINDLDMSEFLINPNAGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKW 875
Cdd:COG5560 714 WRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGW 793
                       890       900
                ....*....|....*....|....*...
gi 14149627 876 YYFDDSSVSTASEDQIVSKAAYVLFYQR 903
Cdd:COG5560 794 YLFDDSRITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
755-902 4.74e-60

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: 204.44  E-value: 4.74e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 755 PFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPINDLDMSE 834
Cdd:cd02674  82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTP 161
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14149627 835 FLINPN-AGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQ 902
Cdd:cd02674 162 YVDTRSfTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
260-451 4.74e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 187.65  E-value: 4.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627   260 CGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDkyqEELNFDNPLGMRGEIAKSYAELIKQMWSG-KFSYVTPRAFKTQVG 338
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRI---SPLSEDSRYNKDINLLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627   339 RFAPQFSGYQQQDCQELLAFLLDGLHEDLNRirkkpyiqlkdadgrpdkvvaeeaweNHLKRNDSIIVDIFHGLFKSTLV 418
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                         170       180       190
                  ....*....|....*....|....*....|...
gi 14149627   419 CPECAKISVTFDPFCYLTLPLPMKKERTLEVYL 451
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASL 164
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
746-901 7.60e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 178.79  E-value: 7.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627   746 SVEYKPPKK--PFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLV 823
Cdd:pfam00443 149 SLPIPGDSAelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEV 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627   824 DFPInDLDMSEFLINPNAGP----CRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASED-QIVSKAAYV 898
Cdd:pfam00443 229 EFPL-ELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSAYI 307

                  ...
gi 14149627   899 LFY 901
Cdd:pfam00443 308 LFY 310
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
135-222 7.44e-47

Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin carboxyl-terminal hydrolases and in gametogenetin-binding protein.


Pssm-ID: 405518  Cd Length: 88  Bit Score: 161.95  E-value: 7.44e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627   135 ELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFSIPDEKETRLWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQK 214
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 14149627   215 NEDGTWPR 222
Cdd:pfam14836  81 NEDGNWPR 88
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
746-902 3.19e-37

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: 140.70  E-value: 3.19e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 746 SVEYKPPKKPFVKLKDCIELFTTKEKLGAEDPWYCpNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMR-DKLDTLVD 824
Cdd:cd02257  88 SLPLPVKGLPQVSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTkEKLNTKVS 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 825 FPINdLDMSEFLI------NPNAGPCRYNLIAVSNHYGGMGGG-HYTAFAKNKDDGKWYYFDDSSVSTASEDQIV----- 892
Cdd:cd02257 167 FPLE-LDLSPYLSegekdsDSDNGSYKYELVAVVVHSGTSADSgHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLefgsl 245
                       170
                ....*....|
gi 14149627 893 SKAAYVLFYQ 902
Cdd:cd02257 246 SSSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
759-901 2.90e-33

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 130.47  E-value: 2.90e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 759 LKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYmrDKLDTLVDFPiNDLDMSEFLIN 838
Cdd:cd02661 164 LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRG--GKINKQISFP-ETLDLSPYMSQ 240
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14149627 839 PNAGPCRYNLIAVSNHYGGMGGG-HYTAFAKNkDDGKWYYFDDSSVSTASEDQIVSKAAYVLFY 901
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSgHYYCYVKS-SNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
758-901 4.20e-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 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: 127.87  E-value: 4.20e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 758 KLKDCIELFTTKEKLGaEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRY-MRDKLDTLVDFPInDLDMSEFL 836
Cdd:cd02660 177 TLSDCLDRFTRPEKLG-DFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKIDTYVQFPL-ELNMTPYT 254
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14149627 837 I---------NPNAGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDgKWYYFDDSSVSTASEDQIVSKAAYVLFY 901
Cdd:cd02660 255 SssigdtqdsNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDG-QWFKFDDAMITRVSEEEVLKSQAYLLFY 327
DUSP smart00695
Domain in ubiquitin-specific proteases;
24-121 2.97e-30

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 114.38  E-value: 2.97e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627     24 LRKGDTWYLVDSRWFKQWKKYVGfdswdkyqmGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSW 103
Cdd:smart00695   2 LEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRW 72
                           90
                   ....*....|....*...
gi 14149627    104 YTLMEGqePIARKVVEQG 121
Cdd:smart00695  73 YGGGPG--PIPRKVVCQG 88
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
261-445 5.51e-24

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 103.99  E-value: 5.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 261 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMrgeIAKSYAELIKQMW-SGKFSYVTPRAFKTQVGR 339
Cdd:cd02660   2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSC---LSCAMDEIFQEFYySGDRSPYGPINLLYLSWK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 340 FAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPyiqlkdadgrpdkvvaeeaweNHLKRNDSIIVDIFHGLFKSTLVC 419
Cdd:cd02660  79 HSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEA---------------------NDESHCNCIIHQTFSGSLQSSVTC 137
                       170       180
                ....*....|....*....|....*.
gi 14149627 420 PECAKISVTFDPFCYLTLPLPMKKER 445
Cdd:cd02660 138 QRCGGVSTTVDPFLDLSLDIPNKSTP 163
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
260-448 6.17e-23

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 100.43  E-value: 6.17e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 260 CGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRgEIAKsyaeLIKQMWSGKFSYVTPRAFKTQVGR 339
Cdd:cd02661   2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMC-ALEA----HVERALASSGPGSAPRIFSSNLKQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 340 FAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIqlkdadgrpdkvvaeeawENHLKRNDSIIVDIFHGLFKSTLVC 419
Cdd:cd02661  77 ISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKA------------------VDPSSQETTLVQQIFGGYLRSQVKC 138
                       170       180
                ....*....|....*....|....*....
gi 14149627 420 PECAKISVTFDPFcyLTLPLPMKKERTLE 448
Cdd:cd02661 139 LNCKHVSNTYDPF--LDLSLDIKGADSLE 165
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
27-119 6.18e-23

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


Pssm-ID: 399383  Cd Length: 80  Bit Score: 93.20  E-value: 6.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627    27 GDTWYLVDSRWFKQWKKYVGfdswdkyqmgDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYtl 106
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVK----------EPNNEPGPIDNSDLLDDESNGQLKPNLQEGVDYVIVPEEVWEFLVEWY-- 68
                          90
                  ....*....|...
gi 14149627   107 mEGQEPIARKVVE 119
Cdd:pfam06337  69 -GGGPEIKRNVVN 80
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
754-901 1.18e-22

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: 100.19  E-value: 1.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 754 KPFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYM--RDKLDTLVDFPiNDLD 831
Cdd:cd02668 153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTgaKKKLNASISFP-EILD 231
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 832 MSEFLINPNAGPCRYNLIAVSNHY-GGMGGGHYTAFAKNKDDGKWYYFDDSSVS--------------TASEDQ------ 890
Cdd:cd02668 232 MGEYLAESDEGSYVYELSGVLIHQgVSAYSGHYIAHIKDEQTGEWYKFNDEDVEempgkplklgnsedPAKPRKseikkg 311
                       170
                ....*....|..
gi 14149627 891 -IVSKAAYVLFY 901
Cdd:cd02668 312 tHSSRTAYMLVY 323
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
261-451 1.33e-22

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: 97.36  E-value: 1.33e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 261 GLSNLGNTCFMNSAIQCLSNtpplteyflndkyqeelnfdnplgmrgeiaksyaelikqmwsgkfsyvtprafktqvgrf 340
Cdd:cd02674   1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 341 apqfsgyQQQDCQELLAFLLDGLHedlnrirkkpyiqlkdadgrpdkvvaeeawenhlkrndSIIVDIFHGLFKSTLVCP 420
Cdd:cd02674  21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                       170       180       190
                ....*....|....*....|....*....|.
gi 14149627 421 ECAKISVTFDPFCYLTLPLPMKKERTLEVYL 451
Cdd:cd02674  56 TCGKTSTTFEPFTYLSLPIPSGSGDAPKVTL 86
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
748-902 5.17e-22

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: 97.07  E-value: 5.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 748 EYKPPKKPfVKLKDCIELFTTKEKLGAEDPWYCPNCkehQQATKKLDLWSLPPVLVVHLKRFSYSRYMRD-KLDTLVDFP 826
Cdd:cd02667 103 RSDEIKSE-CSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSANLrKVSRHVSFP 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 827 iNDLDMSEFLiNPNAGPC------RYNLIAVSNHYGGMGGGHYTAFAK---------------------NKDDGKWYYFD 879
Cdd:cd02667 179 -EILDLAPFC-DPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadeaGPGSGQWYYIS 256
                       170       180
                ....*....|....*....|...
gi 14149627 880 DSSVSTASEDQIVSKAAYVLFYQ 902
Cdd:cd02667 257 DSDVREVSLEEVLKSEAYLLFYE 279
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
754-906 1.40e-21

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: 96.94  E-value: 1.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 754 KPFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYS--RYMRDKLDTLVDFPInDLD 831
Cdd:cd02659 148 KGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPL-ELD 226
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 832 MSEFLINPNA-----------GPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSK------ 894
Cdd:cd02659 227 MEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEEcfggee 306
                       170       180
                ....*....|....*....|....*...
gi 14149627 895 ----------------AAYVLFYQRQDT 906
Cdd:cd02659 307 tqktydsgprafkrttNAYMLFYERKSP 334
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
261-448 4.16e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 91.68  E-value: 4.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 261 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLNdkyqeelnfdnplgmrgeiaksyaelikqmwsgkfsyvTPRAFKTQVGRF 340
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE--------------------------------------TPKELFSQVCRK 42
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 341 APQFSGYQQQDCQELLAFLLDGLhedlnrirkKPYIqlkdadgrpdkvvaeeawenhlkrnDSiivdIFHGLFKSTLVCP 420
Cdd:cd02667  43 APQFKGYQQQDSHELLRYLLDGL---------RTFI-------------------------DS----IFGGELTSTIMCE 84
                       170       180       190
                ....*....|....*....|....*....|
gi 14149627 421 ECAKISVTFDPFCYLTLPL--PMKKERTLE 448
Cdd:cd02667  85 SCGTVSLVYEPFLDLSLPRsdEIKSECSIE 114
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
261-450 5.48e-20

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: 90.62  E-value: 5.48e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 261 GLSNLGNTCFMNSAIQCLSNtpplteyflndkyqeelnfdnplgmrgeiaksyaelikqmwsgkfsyvtprafktqvgrf 340
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 341 apqfsgyQQQDCQELLAFLLDGLHEDLNRIRKKpyiqlkdadgrpdkvvaeeawENHLKRNDSIIVDIFHGLFKSTLVCP 420
Cdd:cd02257  21 -------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                       170       180       190
                ....*....|....*....|....*....|
gi 14149627 421 ECAKISVTFDPFCYLTLPLPMKKERTLEVY 450
Cdd:cd02257  73 ECGHESVSTEPELFLSLPLPVKGLPQVSLE 102
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
759-902 8.63e-16

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: 79.28  E-value: 8.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 759 LKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYS-RYMR-DKLDTLVDFPindLDMSEFL 836
Cdd:cd02663 149 ITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDeQLNRyIKLFYRVVFP---LELRLFN 225
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14149627 837 INPNA-GPCR-YNLIAVSNHY-GGMGGGHYTAFAKNKddGKWYYFDDSSVSTASEDQIV--------SKAAYVLFYQ 902
Cdd:cd02663 226 TTDDAeNPDRlYELVAVVVHIgGGPNHGHYVSIVKSH--GGWLLFDDETVEKIDENAVEeffgdspnQATAYVLFYQ 300
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
739-902 1.79e-15

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 78.52  E-value: 1.79e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 739 EDFEKHESVEYKPPKKPfVKLKDCIELFTTKEKLgaEDpwYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRD- 817
Cdd:cd02658 161 PKDEATEKEEGELVYEP-VPLEDCLKAYFAPETI--ED--FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPk 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 818 KLDTLVDFPindldmsEFLinpnaGPCRYNLIAVSNHY-GGMGGGHYTAFAKNKDD--GKWYYFDDSSVSTASEDQIVSK 894
Cdd:cd02658 236 KLDVPIDVP-------EEL-----GPGKYELIAFISHKgTSVHSGHYVAHIKKEIDgeGKWVLFNDEKVVASQDPPEMKK 303

                ....*...
gi 14149627 895 AAYVLFYQ 902
Cdd:cd02658 304 LGYIYFYQ 311
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
797-901 1.53e-14

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 75.45  E-value: 1.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 797 SLPPVLVVHLKRFSYSRYMRDKLDTL--VDFPINdLDMSEFLinpnAGPCRYNLIAVSNHYGGMGGG-HYTAFAKNKDDG 873
Cdd:cd02657 195 RLPKYLTVQFVRFFWKRDIQKKAKILrkVKFPFE-LDLYELC----TPSGYYELVAVITHQGRSADSgHYVAWVRRKNDG 269
                        90       100       110
                ....*....|....*....|....*....|....*
gi 14149627 874 KWYYFDDSSVSTASEDQIVSKA-------AYVLFY 901
Cdd:cd02657 270 KWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
261-441 6.01e-14

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 73.90  E-value: 6.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 261 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNP-LGMRGEIAKsyaeLIKQMWSGKFSY------------ 327
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPaNDLNCQLIK----LADGLLSGRYSKpaslksendpyq 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 328 --VTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDglhedlnRIRKKPYIQLKDADGRPDKVVAEEawenhlkrndsii 405
Cdd:cd02658  77 vgIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLID-------KLDRESFKNLGLNPNDLFKFMIED------------- 136
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 14149627 406 vdifhglfksTLVCPECAKISVTFDPFCYLTLPLPM 441
Cdd:cd02658 137 ----------RLECLSCKKVKYTSELSEILSLPVPK 162
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
261-374 1.28e-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 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: 72.75  E-value: 1.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 261 GLSNLGNTCFMNSAIQCLSNTPPLteyflndkyQEELNFDNPLGMRGE-----IAKSYAELIKQMwSGKFSYVTPRAFKT 335
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPEL---------RDALKNYNPARRGANqssdnLTNALRDLFDTM-DKKQEPVPPIEFLQ 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 14149627 336 QVGRFAPQFS------GYQQQDCQELLAFLLDGLHEDLNRIRKKP 374
Cdd:cd02657  71 LLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKG 115
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
257-440 2.86e-12

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 70.04  E-value: 2.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 257 PGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFL-NDKYQEELNFDNPLGmrgeiaKSYAELIKQMWSgkfsyvtPRAFKT 335
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLlYENYENIKDRKSELV------KRLSELIRKIWN-------PRNFKG 183
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 336 QVG----------RFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKpyiqlkdadgrpdkvvaeeawenhlkrNDSII 405
Cdd:cd02669 184 HVSphellqavskVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKP---------------------------NSSII 236
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 14149627 406 VDIFHGLFK---------------STLVCPECAKISVTFDPFCYLTLPLP 440
Cdd:cd02669 237 HDCFQGKVQietqkikphaeeegsKDKFFKDSRVKKTSVSPFLLLTLDLP 286
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
751-902 3.84e-11

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 66.19  E-value: 3.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 751 PPKKPF--VKLKDCIELFTTKEKLGAEDPwycPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPIN 828
Cdd:cd02669 286 PPPPLFkdGNEENIIPQVPLKQLLKKYDG---KTETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIK 362
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14149627 829 DLDMSEFLINPNAGPCR---YNLIA-VSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQ 902
Cdd:cd02669 363 NLDLSDYVHFDKPSLNLstkYNLVAnIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
759-902 1.34e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 62.77  E-value: 1.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 759 LKDCIELFTTKEKLgaEDPwYCPNCkehQQATKKLdlwslPPVLVVHLKRFSYS-RYMRDKLDTLVDFPindldmsEFLi 837
Cdd:cd02662  98 LEHCLDDFLSTEII--DDY-KCDRC---QTVIVRL-----PQILCIHLSRSVFDgRGTSTKNSCKVSFP-------ERL- 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 838 npnaGPCRYNLIAVSNHYGGMGGGHYTAF--------------------AKNKDDGKWYYFDDSSVSTASEDQIV-SKAA 896
Cdd:cd02662 159 ----PKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLeQKSA 234

                ....*.
gi 14149627 897 YVLFYQ 902
Cdd:cd02662 235 YMLFYE 240
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
739-901 2.08e-10

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 63.37  E-value: 2.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 739 EDFEKHESVEYKP-PKKPFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRD 817
Cdd:cd02671 161 ELSKSEESSEISPdPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFD 240
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 818 ------KLDTLVDFPInDLDMSEFLINPNAGpcRYNLIAVSNHY-GGMGGGHYTAFAknkddgKWYYFDDSSVSTASEDQ 890
Cdd:cd02671 241 cygglsKVNTPLLTPL-KLSLEEWSTKPKND--VYRLFAVVMHSgATISSGHYTAYV------RWLLFDDSEVKVTEEKD 311
                       170       180
                ....*....|....*....|
gi 14149627 891 IV---------SKAAYVLFY 901
Cdd:cd02671 312 FLealspntssTSTPYLLFY 331
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
756-902 3.70e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 62.51  E-value: 3.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 756 FVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSR--YMRDKL------DTLVDFPI 827
Cdd:cd02664 133 FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQktHVREKImdnvsiNEVLSLPV 212
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 828 ND-LDMSEFLINPNAGPCR-----------YNLIAV---------SNHY-----------GGMGGGHYTAFAKNKDDGK- 874
Cdd:cd02664 213 RVeSKSSESPLEKKEEESGddgelvtrqvhYRLYAVvvhsgysseSGHYftyardqtdadSTGQECPEPKDAEENDESKn 292
                       170       180       190
                ....*....|....*....|....*....|....*
gi 14149627 875 WYYFDDSSVS--TASEDQIV-----SKAAYVLFYQ 902
Cdd:cd02664 293 WYLFNDSRVTfsSFESVQNVtsrfpKDTPYILFYE 327
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
780-891 4.36e-10

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 63.74  E-value: 4.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627  780 CPNCKEH--QQATKKLDLWSLPPVLVVHLKRFSYS--RYMRDKLDTLVDFPInDLDMSEFLiNPNA-----GPCRYNLIA 850
Cdd:COG5077  358 RYNAEKHglQDAKKGVIFESLPPVLHLQLKRFEYDfeRDMMVKINDRYEFPL-EIDLLPFL-DRDAdksenSDAVYVLYG 435
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 14149627  851 VSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQI 891
Cdd:COG5077  436 VLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
261-440 1.35e-09

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 60.58  E-value: 1.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 261 GLSNLGNTCFMNSAIQCLSntppLTEYFLNDKYQEelnfdNPLGMRGEIAKSYAELIKQMW---SGKFSYVTPRAFKTQV 337
Cdd:cd02664   1 GLINLGNTCYMNSVLQALF----MAKDFRRQVLSL-----NLPRLGDSQSVMKKLQLLQAHlmhTQRRAEAPPDYFLEAS 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 338 grFAPQFSGYQQQDCQELLAFLLDGLHedlnrirkkpyiqlkdadgrpdkvvaeeawenhlkrndSIIVDIFHGLFKSTL 417
Cdd:cd02664  72 --RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTI 111
                       170       180
                ....*....|....*....|...
gi 14149627 418 VCPECAKISVTFDPFCYLTLPLP 440
Cdd:cd02664 112 RCLNCNSTSARTERFRDLDLSFP 134
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
261-374 2.61e-09

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 59.43  E-value: 2.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 261 GLSNLGNTCFMNSAIQCLS-NTPPLTEYFLNDKYQ-----EELNFDNPLGMRGEIAKsyaeLIKQMWSGKfsyvtprafK 334
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKElkvlkNVIRKPEPDLNQEEALK----LFTALWSSK---------E 67
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 14149627 335 TQVGRFAPQfsgYQQQDCQELLAFLLDGLHEDL---NRIRKKP 374
Cdd:COG5533  68 HKVGWIPPM---GSQEDAHELLGKLLDELKLDLvnsFTIRIFK 107
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
250-365 3.15e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 53.36  E-value: 3.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 250 PGRNNEQPGLCGLSNLGNTCFMNSAIQCLSNTPplteyflndKYQEELNFDNPLGMRGEIAKSYAELIKQMWSGKFSYVT 329
Cdd:cd02671  15 CEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCP---------GFKHGLKHLVSLISSVEQLQSSFLLNPEKYNDELANQA 85
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 14149627 330 PRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHE 365
Cdd:cd02671  86 PRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
261-440 4.09e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 52.70  E-value: 4.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 261 GLSNLGNTCFMNSAIQCLsntpplteYFLNdkyqeelnfdnplgmrgeIAKSYAELIKQMWSGKFSY--VTPRAFKTQVG 338
Cdd:cd02663   1 GLENFGNTCYCNSVLQAL--------YFEN------------------LLTCLKDLFESISEQKKRTgvISPKKFITRLK 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 339 RFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKpyiqlkdaDGRPDKVVAEEAWENHlkrnDSIIVDIFHGLFKSTLV 418
Cdd:cd02663  55 RENELFDNYMHQDAHEFLNFLLNEIAEILDAERKA--------EKANRKLNNNNNAEPQ----PTWVHEIFQGILTNETR 122
                       170       180
                ....*....|....*....|..
gi 14149627 419 CPECAKISVTFDPFCYLTLPLP 440
Cdd:cd02663 123 CLTCETVSSRDETFLDLSIDVE 144
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
261-448 8.02e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 52.04  E-value: 8.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 261 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLN-----DKYQEELNFDNPLGMRGeIAKSYAELIKQMWSGKFSYVTPRAFKT 335
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnsteDAELKNMPPDKPHEPQT-IIDQLQLIFAQLQFGNRSVVDPSGFVK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 336 QVGrfapqFSGYQQQDCQELLAFLLDGLHEDLNrirkkpyiQLKDADGRpdkvvaeeawenhlkrndSIIVDIFHGLFKS 415
Cdd:cd02668  80 ALG-----LDTGQQQDAQEFSKLFLSLLEAKLS--------KSKNPDLK------------------NIVQDLFRGEYSY 128
                       170       180       190
                ....*....|....*....|....*....|...
gi 14149627 416 TLVCPECAKISVTFDPFcyLTLPLPMKKERTLE 448
Cdd:cd02668 129 VTQCSKCGRESSLPSKF--YELELQLKGHKTLE 159
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
258-448 1.40e-06

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 51.49  E-value: 1.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 258 GLCGLSNLGNTCFMNSAIQCLSNTPplteYFLNDKYQEELNFDNPlgmrGEIAKSYAeLIKQMwsgKFSYVTPRAFKTQV 337
Cdd:cd02659   1 GYVGLKNQGATCYMNSLLQQLYMTP----EFRNAVYSIPPTEDDD----DNKSVPLA-LQRLF---LFLQLSESPVKTTE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 338 GRFAPQFSG------YQQQDCQELLAFLLDGLhedlnrirkkpyiqlkdadgrpdkvvaEEAWENhLKRnDSIIVDIFHG 411
Cdd:cd02659  69 LTDKTRSFGwdslntFEQHDVQEFFRVLFDKL---------------------------EEKLKG-TGQ-EGLIKNLFGG 119
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 14149627 412 LFKSTLVCPECAKISVTFDPFcyLTLPLPMKKERTLE 448
Cdd:cd02659 120 KLVNYIICKECPHESEREEYF--LDLQVAVKGKKNLE 154
USP7_C2 pfam14533
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ...
431-568 5.16e-06

Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific proteases has no known function.


Pssm-ID: 464201  Cd Length: 204  Bit Score: 48.25  E-value: 5.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627   431 PFCYLTLPLPMK---KERTLEVYLVrMDPLTKPMQYKVVVPKIGNILDLCTALSALSGIP---ADKMIVTDIYNHRFHRI 504
Cdd:pfam14533   1 ALYYEVLDISLSeleNKKSIKVTWL-SPGLKKEEELELLVPKNGTVADLLEELQKKVKLSeegSGKIRLYEVSNHKIYKE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14149627   505 FAMDENLSSIMERDDIYVFEI---NINRTEDTehVIIPVClrekfrHssYtHHTGSSLFGQPFLMAV 568
Cdd:pfam14533  80 LSEDEPIDSLNDYLTLYAEEIpeeELNLDEGE--RLIPVF------H--F-QKEPSRTHGIPFLFVL 135
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
261-287 1.09e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 47.75  E-value: 1.09e-05
                        10        20
                ....*....|....*....|....*..
gi 14149627 261 GLSNLGNTCFMNSAIQCLSNTPPLTEY 287
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIEY 27
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
780-901 1.49e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 44.44  E-value: 1.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 780 CPNCKeHQQATKKLDLWSLPPVLVVHLKRFsYSRYMrdkldTLVDFPINDLDMSEFLINPNagpcRYNLIAVSNHY-GGM 858
Cdd:cd02673 129 CSSCK-CESAISSERIMTFPECLSINLKRY-KLRIA-----TSDYLKKNEEIMKKYCGTDA----KYSLVAVICHLgESP 197
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 14149627 859 GGGHYTAFAKNKDDG-KWYYFDDSSVSTASEDQI---VSKAAYVLFY 901
Cdd:cd02673 198 YDGHYIAYTKELYNGsSWLYCSDDEIRPVSKNDVstnARSSGYLIFY 244
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
261-418 1.12e-03

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 42.48  E-value: 1.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 261 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLN-DKYQEELNFDNPLGMR-GEIAKSYAE-------------LIKQMWSGKF 325
Cdd:cd02666   3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNfDESKAELASDYPTERRiGGREVSRSElqrsnqfvyelrsLFNDLIHSNT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 326 SYVTPRAfktqvgRFApqFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIQLKDAD------------GRPDKVVAEEA 393
Cdd:cd02666  83 RSVTPSK------ELA--YLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDkeqsdlikrlfsGKTKQQLVPES 154
                       170       180
                ....*....|....*....|....*
gi 14149627 394 WenhlkrNDSIIVDIFHGLFKSTLV 418
Cdd:cd02666 155 M------GNQPSVRTKTERFLSLLV 173
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
798-901 7.94e-03

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 39.08  E-value: 7.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 798 LPPVLVVHLKRFSYSRYMRDKLDTLVDFPindldmSEFLINPnagpcrYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYY 877
Cdd:cd02665 128 LPPVLTFELSRFEFNQGRPEKIHDKLEFP------QIIQQVP------YELHAVLVHEGQANAGHYWAYIYKQSRQEWEK 195
                        90       100       110
                ....*....|....*....|....*....|..
gi 14149627 878 FDDSSVSTASEDQIVSKA--------AYVLFY 901
Cdd:cd02665 196 YNDISVTESSWEEVERDSfgggrnpsAYCLMY 227
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
762-902 8.15e-03

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


Pssm-ID: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 39.42  E-value: 8.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149627 762 CIELFTTKEKlgaEDPWYCPNCKEHQQATKKLDLWSLPP----VLVVHLKRFSYSRYMR-------DKLDTLVDFPINDL 830
Cdd:cd02672 122 LLKRSLDLEK---VTKAWCDTCCKYQPLEQTTSIRHLPDilllVLVINLSVTNGEFDDInvvlpsgKVMQNKVSPKAIDH 198
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14149627 831 DmSEFLINPNAGPCRYNLIA-VSNHYGGMGGGHYTAF----AKNKDDGKWYYFDDSSVSTasedqiVSKAAYVLFYQ 902
Cdd:cd02672 199 D-KLVKNRGQESIYKYELVGyVCEINDSSRGQHNVVFvikvNEESTHGRWYLFNDFLVTP------VSELAYILLYQ 268
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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