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Conserved domains on  [gi|188035917|ref|NP_036039|]
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ubl carboxyl-terminal hydrolase 18 [Mus musculus]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 11995783)

ubiquitin carboxyl-terminal hydrolase family protein may remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds

CATH:  3.90.70.10
EC:  3.4.19.12
Gene Ontology:  GO:0016579|GO:0004843
MEROPS:  C19
SCOP:  4003158

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
52-363 5.05e-54

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 180.33  E-value: 5.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917   52 VGLHNIGQTCCLNSLLQVFMMNMDFRMILKRITVPRSAEERKRSVPF--QLLLLLEKMQD-SRQKAVLPTELVQCLQKYN 128
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLlcALRDLFKALQKnSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  129 VPL--FVQHDAAQLYLTIWNLTKDQITDTDLTERLQG---LFTIWTQESLICVGCTAESSRRSKLLTLSLPLFDKDA-KP 202
Cdd:pfam00443  81 PDFsgYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLitdLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAeLK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  203 LKTLEDALRCFVQPKELASSDMC-CESCGEKTPWKQVLKLTHLPQTLTIHLMRFSARNSRTEKICHSVNFPQSLDFSQVL 281
Cdd:pfam00443 161 TASLQICFLQFSKLEELDDEEKYyCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRYL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  282 PTEEDlgdTKEQSEIHYELFAVIAHVGMADFGHYCAYIRNPVDGKWFCFNDSHVCWVTWKDVQCTygnhryrwrETAYLL 361
Cdd:pfam00443 241 AEELK---PKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS---------SSAYIL 308

                  ..
gi 188035917  362 VY 363
Cdd:pfam00443 309 FY 310
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
52-363 5.05e-54

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 180.33  E-value: 5.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917   52 VGLHNIGQTCCLNSLLQVFMMNMDFRMILKRITVPRSAEERKRSVPF--QLLLLLEKMQD-SRQKAVLPTELVQCLQKYN 128
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLlcALRDLFKALQKnSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  129 VPL--FVQHDAAQLYLTIWNLTKDQITDTDLTERLQG---LFTIWTQESLICVGCTAESSRRSKLLTLSLPLFDKDA-KP 202
Cdd:pfam00443  81 PDFsgYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLitdLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAeLK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  203 LKTLEDALRCFVQPKELASSDMC-CESCGEKTPWKQVLKLTHLPQTLTIHLMRFSARNSRTEKICHSVNFPQSLDFSQVL 281
Cdd:pfam00443 161 TASLQICFLQFSKLEELDDEEKYyCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRYL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  282 PTEEDlgdTKEQSEIHYELFAVIAHVGMADFGHYCAYIRNPVDGKWFCFNDSHVCWVTWKDVQCTygnhryrwrETAYLL 361
Cdd:pfam00443 241 AEELK---PKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS---------SSAYIL 308

                  ..
gi 188035917  362 VY 363
Cdd:pfam00443 309 FY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
53-363 1.73e-52

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: 174.59  E-value: 1.73e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  53 GLHNIGQTCCLNSLLQVFMMNM-DfrmilkritvprsAEErkrsvpFqLLLLLEKMQDSRQKAVlptelvqclqkynvpl 131
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFSEQqD-------------AHE------F-LLFLLDKLHEELKKSS---------------- 44
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 132 fvqhdaaqlyltiwnltKDQITDTDLTERLQGLFTIWTQESLICVGCTAESSRRSKLLTLSLPLFDKDAKPlKTLEDALR 211
Cdd:cd02257   45 -----------------KRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGLPQ-VSLEDCLE 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 212 CFVQPKELASSDMCCESCGEKTPWKQVLKLTHLPQTLTIHLMRFSA-RNSRTEKICHSVNFPQSLDFSQVLpTEEDLGDT 290
Cdd:cd02257  107 KFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFnEDGTKEKLNTKVSFPLELDLSPYL-SEGEKDSD 185
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188035917 291 KEQSEIHYELFAVIAHVG-MADFGHYCAYIRNPVDGKWFCFNDSHVCWVTWKDVQCTYGNHryrwrETAYLLVY 363
Cdd:cd02257  186 SDNGSYKYELVAVVVHSGtSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLS-----SSAYILFY 254
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
50-363 3.50e-29

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 119.20  E-value: 3.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917   50 GLVGLHNIGQTCCLNSLLQVFMMNMDFRMILKRItvPRSAEERKRSVPFQLLLLLEKMQDSRQkAVLPTELVQCLQKYNV 129
Cdd:COG5077   192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI--PTDHPRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFGWDSD 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  130 PLFVQHDAAQLYLTIWNLTKDQITDTDLTERLQGLFTIWTQESLICVGCTAESSRRSKLLTLSLplfdkDAKPLKTLEDA 209
Cdd:COG5077   269 DSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL-----NVKGMKNLQES 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  210 LRCFVQpKELASSDMC--CESCGEKTPWKQVLkLTHLPQTLTIHLMRFSARNSRTE--KICHSVNFPQSLDFSQVLPTEe 285
Cdd:COG5077   344 FRRYIQ-VETLDGDNRynAEKHGLQDAKKGVI-FESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLEIDLLPFLDRD- 420
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  286 dlGDTKEQSEIHYELFAVIAHVGMADFGHYCAYIRNPVDGKWFCFNDSHVCWVTWKDV-QCTYG-NHRYRWR-------- 355
Cdd:COG5077   421 --ADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVlEENFGgDHPYKDKirdhsgik 498
                         330
                  ....*....|
gi 188035917  356 --ETAYLLVY 363
Cdd:COG5077   499 rfMSAYMLVY 508
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
52-363 5.05e-54

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 180.33  E-value: 5.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917   52 VGLHNIGQTCCLNSLLQVFMMNMDFRMILKRITVPRSAEERKRSVPF--QLLLLLEKMQD-SRQKAVLPTELVQCLQKYN 128
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLlcALRDLFKALQKnSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  129 VPL--FVQHDAAQLYLTIWNLTKDQITDTDLTERLQG---LFTIWTQESLICVGCTAESSRRSKLLTLSLPLFDKDA-KP 202
Cdd:pfam00443  81 PDFsgYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLitdLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAeLK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  203 LKTLEDALRCFVQPKELASSDMC-CESCGEKTPWKQVLKLTHLPQTLTIHLMRFSARNSRTEKICHSVNFPQSLDFSQVL 281
Cdd:pfam00443 161 TASLQICFLQFSKLEELDDEEKYyCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRYL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  282 PTEEDlgdTKEQSEIHYELFAVIAHVGMADFGHYCAYIRNPVDGKWFCFNDSHVCWVTWKDVQCTygnhryrwrETAYLL 361
Cdd:pfam00443 241 AEELK---PKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS---------SSAYIL 308

                  ..
gi 188035917  362 VY 363
Cdd:pfam00443 309 FY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
53-363 1.73e-52

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: 174.59  E-value: 1.73e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  53 GLHNIGQTCCLNSLLQVFMMNM-DfrmilkritvprsAEErkrsvpFqLLLLLEKMQDSRQKAVlptelvqclqkynvpl 131
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFSEQqD-------------AHE------F-LLFLLDKLHEELKKSS---------------- 44
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 132 fvqhdaaqlyltiwnltKDQITDTDLTERLQGLFTIWTQESLICVGCTAESSRRSKLLTLSLPLFDKDAKPlKTLEDALR 211
Cdd:cd02257   45 -----------------KRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGLPQ-VSLEDCLE 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 212 CFVQPKELASSDMCCESCGEKTPWKQVLKLTHLPQTLTIHLMRFSA-RNSRTEKICHSVNFPQSLDFSQVLpTEEDLGDT 290
Cdd:cd02257  107 KFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFnEDGTKEKLNTKVSFPLELDLSPYL-SEGEKDSD 185
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188035917 291 KEQSEIHYELFAVIAHVG-MADFGHYCAYIRNPVDGKWFCFNDSHVCWVTWKDVQCTYGNHryrwrETAYLLVY 363
Cdd:cd02257  186 SDNGSYKYELVAVVVHSGtSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLS-----SSAYILFY 254
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
50-365 4.94e-49

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 168.20  E-value: 4.94e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  50 GLVGLHNIGQTCCLNSLLQVFMMNMDFR-MILKRITVPRSAEERKRSVPFQLLLLLEKMQDSRQKAVLPTELVQCLQKYN 128
Cdd:cd02659    1 GYVGLKNQGATCYMNSLLQQLYMTPEFRnAVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 129 VPLFVQHDAAQLYLTIWNLTKDQITDTDLTERLQGLF--TIWTQesLICVGCTAESSRRSKLLTLSLplfdkDAKPLKTL 206
Cdd:cd02659   81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFggKLVNY--IICKECPHESEREEYFLDLQV-----AVKGKKNL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 207 EDALRCFVQPKELASSDMC-CESCGEKTPWKQVLKLTHLPQTLTIHLMRFS---ARNSRtEKICHSVNFPQSLDFSQ--- 279
Cdd:cd02659  154 EESLDAYVQGETLEGDNKYfCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfdfETMMR-IKINDRFEFPLELDMEPyte 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 280 --VLPTEEDLGDTKEQSEIhYELFAVIAHVGMADFGHYCAYIRNPVDGKWFCFNDSHVCWVTWKDV--QCTYGNHRYRWR 355
Cdd:cd02659  233 kgLAKKEGDSEKKDSESYI-YELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAeeECFGGEETQKTY 311
                        330       340
                 ....*....|....*....|
gi 188035917 356 ET----------AYLLVYTK 365
Cdd:cd02659  312 DSgprafkrttnAYMLFYER 331
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
53-364 1.77e-40

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: 145.26  E-value: 1.77e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  53 GLHNIGQTCCLNSLLQVFMMNMDFRMILKRITVPRSAEER--KRSVPF-------QLLLLLEKMQDSRQKAVLPTELVQC 123
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKnmPPDKPHepqtiidQLQLIFAQLQFGNRSVVDPSGFVKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 124 LQKYNVplfVQHDAAQ---LYLTIWNLTKDQITDTDLTERLQGLFTIWTQESLICVGCTAESSRRSKLLTLSLPLfdkda 200
Cdd:cd02668   81 LGLDTG---QQQDAQEfskLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL----- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 201 KPLKTLEDALRCFVQPKELASSDM-CCESCGEKTPWKQVLKLTHLPQTLTIHLMRFS-ARNSRTEKICH-SVNFPQSLDF 277
Cdd:cd02668  153 KGHKTLEECIDEFLKEEQLTGDNQyFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfDRKTGAKKKLNaSISFPEILDM 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 278 SQVLpTEEDLGDTKeqseihYELFAVIAHVGM-ADFGHYCAYIRNPVDGKWFCFNDSHVCWVTWKDVQC----------- 345
Cdd:cd02668  233 GEYL-AESDEGSYV------YELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLgnsedpakprk 305
                        330       340
                 ....*....|....*....|
gi 188035917 346 -TYGNHRYRWReTAYLLVYT 364
Cdd:cd02668  306 sEIKKGTHSSR-TAYMLVYK 324
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
134-364 2.77e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 123.55  E-value: 2.77e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 134 QHDAAQLYLTIWNLTKDQITDTdlterLQGLFtiwtQESLICVGCTAESSRRSKLLTLSLPLFDKDAKPLK-TLEDALRC 212
Cdd:cd02674   22 QQDAQEFLLFLLDGLHSIIVDL-----FQGQL----KSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKvTLEDCLRL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 213 FVQPKELASSDM-CCESCGEKTPWKQVLKLTHLPQTLTIHLMRFSARNSRTEKICHSVNFP-QSLDFSQVLPTEEDLGDT 290
Cdd:cd02674   93 FTKEETLDGDNAwKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPlNDLDLTPYVDTRSFTGPF 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188035917 291 KeqseihYELFAVIAHVGMADFGHYCAYIRNPVDGKWFCFNDSHVcwvtwkdvqcTYGNHRYRWRETAYLLVYT 364
Cdd:cd02674  173 K------YDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRV----------TKVSESSVVSSSAYILFYE 230
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
53-363 4.35e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 122.99  E-value: 4.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  53 GLHNIGQTCCLNSLLQVFMMNMDFRMILKRITVPRSAEErkRSVPFQLLLLLEKMQDSRQKAVLPTELV--QCLQKYNVP 130
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDS--QSVMKKLQLLQAHLMHTQRRAEAPPDYFleASRPPWFTP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 131 LFvQHDAAQlYLTIwnltkdqitdtdLTERLQGLFTIWTQESLI----CVGC--TAESSRRSKLLTLSLPLfdkdakplk 204
Cdd:cd02664   79 GS-QQDCSE-YLRY------------LLDRLHTLIEKMFGGKLSttirCLNCnsTSARTERFRDLDLSFPS--------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 205 tLEDALRCFVQPKELASSDMC-CESCGEKTPWKQVLKLTHLPQTLTIHLMRFS---ARNSRtEKICHSVNFPQSLDF--- 277
Cdd:cd02664  136 -VQDLLNYFLSPEKLTGDNQYyCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydqKTHVR-EKIMDNVSINEVLSLpvr 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 278 ----SQVLPTEEDLGDTKEQSE-----IHYELFAVIAHVGMA-DFGHYCAYIRNPVD--------------------GKW 327
Cdd:cd02664  214 veskSSESPLEKKEEESGDDGElvtrqVHYRLYAVVVHSGYSsESGHYFTYARDQTDadstgqecpepkdaeendesKNW 293
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 188035917 328 FCFNDSHVCWVTWKDVQctygNHRYRWR-ETAYLLVY 363
Cdd:cd02664  294 YLFNDSRVTFSSFESVQ----NVTSRFPkDTPYILFY 326
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
53-363 2.47e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 115.07  E-value: 2.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  53 GLHNIGQTCCLNSLLQVFMMnmdfrmilkriTVP-------RSAEERKRSVPFQLLLLLEKM-QDSRQ--KAVLPTELVQ 122
Cdd:cd02661    3 GLQNLGNTCFLNSVLQCLTH-----------TPPlanyllsREHSKDCCNEGFCMMCALEAHvERALAssGPGSAPRIFS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 123 CLQKYNVPLFV---QHDAAQL-----------YLTIWNLTKDQITDTDLTERLQGLFTIWTQESLICVGCTAESSRRSKL 188
Cdd:cd02661   72 SNLKQISKHFRigrQEDAHEFlrylldamqkaCLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 189 LTLSLplfdkDAKPLKTLEDALRCFVQPKELASSDMC-CESCGEKTPWKQVLKLTHLPQTLTIHLMRFSarNSRTEKICH 267
Cdd:cd02661  152 LDLSL-----DIKGADSLEDALEQFTKPEQLDGENKYkCERCKKKVKASKQLTIHRAPNVLTIHLKRFS--NFRGGKINK 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 268 SVNFPQSLDFSQVlpteedLGDTKEQSEIhYELFAVIAHVGM-ADFGHYCAYIRNPvDGKWFCFNDSHVCWVTWKDVqct 346
Cdd:cd02661  225 QISFPETLDLSPY------MSQPNDGPLK-YKLYAVLVHSGFsPHSGHYYCYVKSS-NGKWYNMDDSKVSPVSIETV--- 293
                        330
                 ....*....|....*..
gi 188035917 347 ygnhryrWRETAYLLVY 363
Cdd:cd02661  294 -------LSQKAYILFY 303
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
50-363 3.50e-29

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 119.20  E-value: 3.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917   50 GLVGLHNIGQTCCLNSLLQVFMMNMDFRMILKRItvPRSAEERKRSVPFQLLLLLEKMQDSRQkAVLPTELVQCLQKYNV 129
Cdd:COG5077   192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI--PTDHPRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFGWDSD 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  130 PLFVQHDAAQLYLTIWNLTKDQITDTDLTERLQGLFTIWTQESLICVGCTAESSRRSKLLTLSLplfdkDAKPLKTLEDA 209
Cdd:COG5077   269 DSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL-----NVKGMKNLQES 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  210 LRCFVQpKELASSDMC--CESCGEKTPWKQVLkLTHLPQTLTIHLMRFSARNSRTE--KICHSVNFPQSLDFSQVLPTEe 285
Cdd:COG5077   344 FRRYIQ-VETLDGDNRynAEKHGLQDAKKGVI-FESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLEIDLLPFLDRD- 420
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  286 dlGDTKEQSEIHYELFAVIAHVGMADFGHYCAYIRNPVDGKWFCFNDSHVCWVTWKDV-QCTYG-NHRYRWR-------- 355
Cdd:COG5077   421 --ADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVlEENFGgDHPYKDKirdhsgik 498
                         330
                  ....*....|
gi 188035917  356 --ETAYLLVY 363
Cdd:COG5077   499 rfMSAYMLVY 508
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
170-364 5.95e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 106.30  E-value: 5.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 170 QESLICVGCTAESSRRSKLLTLSLPLFDK----------DAKPLKTLEDALRCFVQPKELASSDMCCESCGEKTPWKQVL 239
Cdd:cd02660  132 QSSVTCQRCGGVSTTVDPFLDLSLDIPNKstpswalgesGVSGTPTLSDCLDRFTRPEKLGDFAYKCSGCGSTQEATKQL 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 240 KLTHLPQTLTIHLMRFS-ARNSRTEKICHSVNFPQSLDFSQVLPTEEdlGDTKE----QSEIHYELFAVIAHVGMADFGH 314
Cdd:cd02660  212 SIKKLPPVLCFQLKRFEhSLNKTSRKIDTYVQFPLELNMTPYTSSSI--GDTQDsnslDPDYTYDLFAVVVHKGTLDTGH 289
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 188035917 315 YCAYIRNPvDGKWFCFNDSHVCWVTWKDVQctygnhryrwRETAYLLVYT 364
Cdd:cd02660  290 YTAYCRQG-DGQWFKFDDAMITRVSEEEVL----------KSQAYLLFYH 328
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
200-363 1.32e-25

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 108.43  E-value: 1.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 200 AKPLKTLEDALRCFVQPKELASSD-MCCESCGEKTPWKQVLKLTHLPQTLTIHLMRFSARNSRTEKICHSVNFP-QSLDF 277
Cdd:COG5560  671 AERTITLQDCLNEFSKPEQLGLSDsWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPiDDLDL 750
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 278 SQVLpteedlgDTKEQSEIHYELFAVIAHVGMADFGHYCAYIRNPVDGKWFCFNDSHVCWVTWKDVQctygnhryrwRET 357
Cdd:COG5560  751 SGVE-------YMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSV----------TSS 813

                 ....*.
gi 188035917 358 AYLLVY 363
Cdd:COG5560  814 AYVLFY 819
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
53-363 5.54e-25

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 103.18  E-value: 5.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  53 GLHNIGQTCCLNSLLQVFMMNMDFRMILKRIT-VPRSAEERKRSVPFQLLLLLEKMqDSRQKAVLPTELVQCL------- 124
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNpARRGANQSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLrmafpqf 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 125 -QKYNVPLFVQHDAAQLYLTIWN-LTKDQITDTDLTERLQGLFTIWTQESLICVGC-TAESSRRSKLLTLSLPLFDKDAK 201
Cdd:cd02657   80 aEKQNQGGYAQQDAEECWSQLLSvLSQKLPGAGSKGSFIDQLFGIELETKMKCTESpDEEEVSTESEYKLQCHISITTEV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 202 plKTLEDALRCFVQPKELASSdmccESCGEKTPWKQVLKLTHLPQTLTIHLMRFSARNS--RTEKICHSVNFPQSLDFSQ 279
Cdd:cd02657  160 --NYLQDGLKKGLEEEIEKHS----PTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDiqKKAKILRKVKFPFELDLYE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 280 VLpteedlgdtkEQSEIhYELFAVIAHVGM-ADFGHYCAYIRNPVDGKWFCFNDSHVCWVTWKDVQCTYGNHRYrwrETA 358
Cdd:cd02657  234 LC----------TPSGY-YELVAVITHQGRsADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSGGGDW---HIA 299

                 ....*
gi 188035917 359 YLLVY 363
Cdd:cd02657  300 YILLY 304
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
42-363 4.39e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 98.43  E-value: 4.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  42 CSAWDSPHGLVGLHNIGQTCCLNSLLQVFMMNMDFRMILKRITVPRSAEERKRSVpfqlLLLLEKMQDSRQKAVLPTELV 121
Cdd:cd02671   15 CEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSS----FLLNPEKYNDELANQAPRRLL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 122 QCLQKYNvPLF---VQHDAAQLYLTIWNLTKDQitdtdLTERLQGLFTIWTQesliCVGCTAESSRRSKLLTLSLPL--- 195
Cdd:cd02671   91 NALREVN-PMYegyLQHDAQEVLQCILGNIQEL-----VEKDFQGQLVLRTR----CLECETFTERREDFQDISVPVqes 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 196 ------FDKDAKP-----LKTLEDALRCFVQPKELASSD-MCCESCGEKTPWKQVLKLTHLPQTLTIHLMRFSARNSRTE 263
Cdd:cd02671  161 elskseESSEISPdpkteMKTLKWAISQFASVERIVGEDkYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 264 KI--CHSVNFPQSLDFsqVLPTEEdlGDTKEQSEIhYELFAVIAHVGMA-DFGHYCAYIRnpvdgkWFCFNDSHVCWVTW 340
Cdd:cd02671  241 CYggLSKVNTPLLTPL--KLSLEE--WSTKPKNDV-YRLFAVVMHSGATiSSGHYTAYVR------WLLFDDSEVKVTEE 309
                        330       340
                 ....*....|....*....|...
gi 188035917 341 KDVQCTYGNHRyRWRETAYLLVY 363
Cdd:cd02671  310 KDFLEALSPNT-SSTSTPYLLFY 331
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
53-363 1.54e-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: 95.92  E-value: 1.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  53 GLHNIGQTCCLNSLLQVFmmnmdfrmilkritvprsaeerkrsvpFQLLLLLEKMQDSrqkavlPTELVQCLQKYNVPL- 131
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNL---------------------------SQTPALRELLSET------PKELFSQVCRKAPQFk 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 132 -FVQHDAAQL--YLTiwnltkdqitdTDLTERLQGLFTIWTQESLICVGCTAESSRRSKLLTLSLPLFDkDAKPLKTLED 208
Cdd:cd02667   48 gYQQQDSHELlrYLL-----------DGLRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSD-EIKSECSIES 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 209 ALRCFVQPKELASSDM-CCESCGEKTpwKQVLkLTHLPQTLTIHLMRFSA-RNSRTEKICHSVNFPQSLDFSQVLPTEED 286
Cdd:cd02667  116 CLKQFTEVEILEGNNKfACENCTKAK--KQYL-ISKLPPVLVIHLKRFQQpRSANLRKVSRHVSFPEILDLAPFCDPKCN 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 287 LGDTKEQSEihYELFAVIAHVGMADFGHYCAYI--RNPVD-------------------GKWFCFNDSHVCWVTWKDVQc 345
Cdd:cd02667  193 SSEDKSSVL--YRLYGVVEHSGTMRSGHYVAYVkvRPPQQrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEEVL- 269
                        330
                 ....*....|....*...
gi 188035917 346 tygnhryrwRETAYLLVY 363
Cdd:cd02667  270 ---------KSEAYLLFY 278
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
53-336 1.28e-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: 85.45  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  53 GLHNIGQTCCLNSLLQV-----------FMMNMDFRMILKRITVPRSAEERK-----RSVPFQLLLLLEKMQDSRQKAVL 116
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVlfsipsfqwryDDLENKFPSDVVDPANDLNCQLIKladglLSGRYSKPASLKSENDPYQVGIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 117 PTELVQCLQKYNvPLFV---QHDAAQ--LYLtIWNLTKD--QITDTDLTErlqgLFTIWTQESLICVGCTAESSRRSKLL 189
Cdd:cd02658   81 PSMFKALIGKGH-PEFStmrQQDALEflLHL-IDKLDREsfKNLGLNPND----LFKFMIEDRLECLSCKKVKYTSELSE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 190 TLSLPL-------FDKDAKPLK--TLEDALRCFVQPKELassDMCCESCGEKTPWKQVLKLTHLPQTLTIHLMRFSArns 260
Cdd:cd02658  155 ILSLPVpkdeateKEEGELVYEpvPLEDCLKAYFAPETI---EDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQL--- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 261 rtekichSVNF-PQSLDFSQVLPteEDLGDTKeqseihYELFAVIAHVGM-ADFGHYCAYIRNPVD--GKWFCFNDSHVC 336
Cdd:cd02658  229 -------LENWvPKKLDVPIDVP--EELGPGK------YELIAFISHKGTsVHSGHYVAHIKKEIDgeGKWVLFNDEKVV 293
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
53-364 6.27e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 83.13  E-value: 6.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  53 GLHNIGQTCCLNSLLQ-VFMMNMdfrmilkritvprsaeerkrsvpFQLL-LLLEKMQDSRQK--AVLPTELVQCLQKYN 128
Cdd:cd02663    1 GLENFGNTCYCNSVLQaLYFENL-----------------------LTCLkDLFESISEQKKRtgVISPKKFITRLKREN 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 129 vPLF---VQHDAAQLY---------------------LTIWNLTKDQITDTDLTERLQGLFTIWTQesliCVGCTAESSR 184
Cdd:cd02663   58 -ELFdnyMHQDAHEFLnfllneiaeildaerkaekanRKLNNNNNAEPQPTWVHEIFQGILTNETR----CLTCETVSSR 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 185 RSKLLTLSLplfdkDAKPLKTLEDALRCFVQPKELASSD-MCCESCGEKTPWKQVLKLTHLPQTLTIHLMRF--SARNSR 261
Cdd:cd02663  133 DETFLDLSI-----DVEQNTSITSCLRQFSATETLCGRNkFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkyDEQLNR 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 262 TEKICHSVNFPQSLdfsQVLPTEEDlgdtKEQSEIHYELFAVIAHVGM-ADFGHYCAYIRnpVDGKWFCFNDSHVCWVTW 340
Cdd:cd02663  208 YIKLFYRVVFPLEL---RLFNTTDD----AENPDRLYELVAVVVHIGGgPNHGHYVSIVK--SHGGWLLFDDETVEKIDE 278
                        330       340
                 ....*....|....*....|....
gi 188035917 341 KDVQCTYGNHRYrwRETAYLLVYT 364
Cdd:cd02663  279 NAVEEFFGDSPN--QATAYVLFYQ 300
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
53-366 1.14e-17

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 82.16  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  53 GLHNIGQTCCLNSLLQVFMMNMDfrmilkritvprSAEERKRSVPFQLLLLLEKMQDSRQ--KAVLPTELVQCLQKYNVP 130
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILALYLP------------KLDELLDDLSKELKVLKNVIRKPEPdlNQEEALKLFTALWSSKEH 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 131 LFVQhdaaqlyltiwnlTKDQITDTDLTERLQGLF------TIWTQESLIcvGCTAESSRRSKL-----LTLSLPLFDKD 199
Cdd:COG5533   69 KVGW-------------IPPMGSQEDAHELLGKLLdelkldLVNSFTIRI--FKTTKDKKKTSTgdwfdIIIELPDQTWV 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 200 aKPLKTLEdalrCFVQPKELASSDMCCESCGEKTPWKQVLKLTH------LPQTLTIHLMRFSARNSRTeKICHSVNFPQ 273
Cdd:COG5533  134 -NNLKTLQ----EFIDNMEELVDDETGVKAKENEELEVQAKQEYevsfvkLPKILTIQLKRFANLGGNQ-KIDTEVDEKF 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 274 SLDFSqvlpTEEDLGDTKEqseIHYELFAVIAHVGMADFGHYCAYIRnpVDGKWFCFNDSHVCWVTWKDVQCTYgnhryr 353
Cdd:COG5533  208 ELPVK----HDQILNIVKE---TYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDSDVTPVSEEEAINEK------ 272
                        330
                 ....*....|...
gi 188035917 354 wRETAYLLVYTKT 366
Cdd:COG5533  273 -AKNAYLYFYERI 284
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
52-363 1.24e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 82.92  E-value: 1.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  52 VGLHNIGQTCCLNSLLQVF---------MMNMD---FRMILKRITVPR------SAEERKRSVPF--QLLLLLEKMQDSR 111
Cdd:cd02666    2 AGLDNIGNTCYLNSLLQYFftikplrdlVLNFDeskAELASDYPTERRiggrevSRSELQRSNQFvyELRSLFNDLIHSN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 112 QKAVLPT-ELV----------QCLQkyNVpLFvQHDAAQLYLTIWNLTKDQITDTDLTERLQGLFTIWTQESLICVGCTA 180
Cdd:cd02666   82 TRSVTPSkELAylalrqqdvtECID--NV-LF-QLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLVPESMGN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 181 ESSRRSKLLT-LSLPLFDKDAKPL-------KTLEDAL-RCFVQpkelassdmccESCGEKTPWKQVLKltHLPQTLTIH 251
Cdd:cd02666  158 QPSVRTKTERfLSLLVDVGKKGREivvllepKDLYDALdRYFDY-----------DSLTKLPQRSQVQA--QLAQPLQRE 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 252 LMRFSARN-----SRTEKICHSVNFPQSldfSQVLPTEEDLGDTKEQSE--------IHYELFAVIAHVGMADFGHYCAY 318
Cdd:cd02666  225 LISMDRYElpssiDDIDELIREAIQSES---SLVRQAQNELAELKHEIEkqfddlksYGYRLHAVFIHRGEASSGHYWVY 301
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 188035917 319 IRNPVDGKWFCFNDSHVCWVTWKDV-QCTYGNhryrwRETAYLLVY 363
Cdd:cd02666  302 IKDFEENVWRKYNDETVTVVPASEVfLFTLGN-----TATPYFLVY 342
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
53-363 1.69e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 75.10  E-value: 1.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  53 GLHNIGQTCCLNSLLQVFmmnmdfrmilkritvprsaeerkrsvpfqlllllekmqdsrqkAVLPtELVQCLQKYNVplf 132
Cdd:cd02662    1 GLVNLGNTCFMNSVLQAL-------------------------------------------ASLP-SLIEYLEEFLE--- 33
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 133 vQHDAAQLYLtiwnltkdQITDTdLTERLQGLFTIWTQESLICVGCTAESS-RRSKLLTLSLPLFDKDAKPLKTLEDALR 211
Cdd:cd02662   34 -QQDAHELFQ--------VLLET-LEQLLKFPFDGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSSGSGTTLEHCLD 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 212 CFVQPKELasSDMCCESCGektpwkqvLKLTHLPQTLTIHLMR--FSARNSRTEKICHsVNFPQSLdfSQVLpteedlgd 289
Cdd:cd02662  104 DFLSTEII--DDYKCDRCQ--------TVIVRLPQILCIHLSRsvFDGRGTSTKNSCK-VSFPERL--PKVL-------- 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 290 tkeqseihYELFAVIAHVGMADFGHYCAYIRNPV--------------------DGKWFCFNDSHVCWVTWKDVQCTYGn 349
Cdd:cd02662  163 --------YRLRAVVVHYGSHSSGHYVCYRRKPLfskdkepgsfvrmregpsstSHPWWRISDTTVKEVSESEVLEQKS- 233
                        330
                 ....*....|....
gi 188035917 350 hryrwretAYLLVY 363
Cdd:cd02662  234 --------AYMLFY 239
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
33-335 3.08e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 73.51  E-value: 3.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  33 RKRVLSRDLCSAWDSPhGLVGLHNIGQTCCLNSLLQVFMMNMDFRMILKRITVPRSAEERKRSVPFQLLLLLEKMQDSRQ 112
Cdd:cd02669  102 RDPKLSRDLDGKPYLP-GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRLSELIRKIWNPRN 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 113 -KAVL-PTELVQCLQKY---NVPLFVQHDAAQLYLTIWNLTKDQITDTD------LTERLQGLFTIWTQE---------- 171
Cdd:cd02669  181 fKGHVsPHELLQAVSKVskkKFSITEQSDPVEFLSWLLNTLHKDLGGSKkpnssiIHDCFQGKVQIETQKikphaeeegs 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 172 -SLICVGCTAESSRRSKLLTLSL-----PLF----DKDAKPLKTLEDALRCFVQPKELASSDMccescgektpwKQVLKL 241
Cdd:cd02669  261 kDKFFKDSRVKKTSVSPFLLLTLdlpppPLFkdgnEENIIPQVPLKQLLKKYDGKTETELKDS-----------LKRYLI 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 242 THLPQTLTIHLMRFSARNSRTEKICHSVNFPQS-LDFSQVLPTEEDLGdtkeQSEIHYELFAVIAHVGM-ADFGHYCAYI 319
Cdd:cd02669  330 SRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKnLDLSDYVHFDKPSL----NLSTKYNLVANIVHEGTpQEDGTWRVQL 405
                        330
                 ....*....|....*.
gi 188035917 320 RNPVDGKWFCFNDSHV 335
Cdd:cd02669  406 RHKSTNKWFEIQDLNV 421
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
161-335 1.16e-13

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 70.76  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  161 LQGLFTIWTQESLICVGCTAESSRRSKLLTLSL----PLFDKDAKPLKT-----LEDALRCFVQPKelassdMCCESCGE 231
Cdd:pfam13423 128 LEQLFGIDAETTIRCSNCGHESVRESSTHVLDLiyprKPSSNNKKPPNQtfssiLKSSLERETTTK------AWCEKCKR 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  232 KTPWKQVLKLTHLPQTLTIHLMRFSARNSRTEKichSVNFpqsldfsqvLPTE----EDLGDTKEQSEIHYELFAVIAHV 307
Cdd:pfam13423 202 YQPLESRRTVRNLPPVLSLNAALTNEEWRQLWK---TPGW---------LPPEigltLSDDLQGDNEIVKYELRGVVVHI 269
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 188035917  308 GMADF-GHYCAYIR-------NPVDGKWFCFNDSHV 335
Cdd:pfam13423 270 GDSGTsGHLVSFVKvadseleDPTESQWYLFNDFLV 305
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
242-363 3.63e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 65.27  E-value: 3.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 242 THLPQTLTIHLMRFSARNSRTEKICHSVNFPQSLdfsqvlpteedlgdtkeqSEIHYELFAVIAHVGMADFGHYCAYIRN 321
Cdd:cd02665  126 TELPPVLTFELSRFEFNQGRPEKIHDKLEFPQII------------------QQVPYELHAVLVHEGQANAGHYWAYIYK 187
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 188035917 322 PVDGKWFCFNDSHVCWVTWKDVQC-TYGNHRyrwRETAYLLVY 363
Cdd:cd02665  188 QSRQEWEKYNDISVTESSWEEVERdSFGGGR---NPSAYCLMY 227
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
174-332 3.68e-04

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


Pssm-ID: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 41.73  E-value: 3.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 174 ICVGCTAESSrrSKLLTLSLPLfdkDAKPLKTLEDALRCFVQPKELASSDMC-CESCGEKTPWKQVLKLTHLPQT----L 248
Cdd:cd02672   89 FSCGTSRNSV--SLLYTLSLPL---GSTKTSKESTFLQLLKRSLDLEKVTKAwCDTCCKYQPLEQTTSIRHLPDIlllvL 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 249 TIHLMRFSarnsrTEKICHSVNFPQSLDFSQ-VLPTEEDLGDTKEQSEIH----YELFAVIAHVGMADFG-HYCAYIR-- 320
Cdd:cd02672  164 VINLSVTN-----GEFDDINVVLPSGKVMQNkVSPKAIDHDKLVKNRGQEsiykYELVGYVCEINDSSRGqHNVVFVIkv 238
                        170
                 ....*....|....
gi 188035917 321 --NPVDGKWFCFND 332
Cdd:cd02672  239 neESTHGRWYLFND 252
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
54-343 7.65e-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: 40.59  E-value: 7.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917  54 LHNIGQTCCLNSLLQ----VFMMNMDFrmilkritvprsAEERKRSVPFQLLLLLEKMQDsrqkavlptelvqcLQKYNV 129
Cdd:cd02673    2 LVNTGNSCYFNSTMQalssIGKINTEF------------DNDDQQDAHEFLLTLLEAIDD--------------IMQVNR 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 130 PLFVqhdaaqlyltiwnltkdqiTDTDLTERLQGL--FTIWTQESLICVGCTAESSRRSKLLTLSLPLFDKDakpLKTLE 207
Cdd:cd02673   56 TNVP-------------------PSNIEIKRLNPLeaFKYTIESSYVCIGCSFEENVSDVGNFLDVSMIDNK---LDIDE 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035917 208 DALRCFVQPKElasSDMCCESCGEKTPwKQVLKLTHLPQTLTIHLMRFSARNSrtekichsvnfpqsldfsqvlpTEEDL 287
Cdd:cd02673  114 LLISNFKTWSP---IEKDCSSCKCESA-ISSERIMTFPECLSINLKRYKLRIA----------------------TSDYL 167
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188035917 288 GDTKE-----QSEI-HYELFAVIAHVG-MADFGHYCAYIRNPVDG-KWFCFNDSHVCWVTWKDV 343
Cdd:cd02673  168 KKNEEimkkyCGTDaKYSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKNDV 231
 
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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