NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|351642211|gb|EHA50073|]
View 

hypothetical protein MGG_03527 [Pyricularia oryzae 70-15]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 2709)

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

EC:  3.4.19.12
PubMed:  10603300

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 179-513 1.16e-140

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.


The actual alignment was detected with superfamily member cd02660:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 328  Bit Score: 408.30  E-value: 1.16e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 179 RGIYNAGATCYQNVILQSFLHNPFLRNYYLSDGHQ--SGECQTQYCMSCAMDDIFQDFYSQETTNGYTAANMLCGFWSLE 256
Cdd:cd02660    1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSctCLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 257 RkafaNLVTTKEQDAHEFFQLLAEELHERNGDGKrPESGSEHLCDCIIHQTYYGKLQSNTTCQGCGSVTNQVQSFLDLSL 336
Cdd:cd02660   81 R----NLAGYSQQDAHEFFQFLLDQLHTHYGGDK-NEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 337 GLDSTQKKKKLAGTKSEGGSKgaslSLQDCLEEEYVKSDKCE--YRCNKCSSTQQARRNTSLKRLPNVLSIQLKRFEYKQ 414
Cdd:cd02660  156 DIPNKSTPSWALGESGVSGTP----TLSDCLDRFTRPEKLGDfaYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 415 grHDKAVKVDTPVKFPLQLNMFPYTDRGpSTESKENYELARTCQYDLFSVVEHVGEIDTGHYTCYCKVQ-DQWFAFNDHR 493
Cdd:cd02660  232 --NKTSRKIDTYVQFPLELNMTPYTSSS-IGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGdGQWFKFDDAM 308

                        330       340
                 ....*....|....*....|
gi 351642211 494 VEMASVSQVLSAKAYLLFYI 513
Cdd:cd02660  309 ITRVSEEEVLKSQAYLLFYH 328
zf-UBP super family cl09957
Zn-finger in ubiquitin-hydrolases and other protein;
78-129 6.67e-04

Zn-finger in ubiquitin-hydrolases and other protein;


The actual alignment was detected with superfamily member pfam02148:

Pssm-ID: 471956  Cd Length: 63  Bit Score: 38.01  E-value: 6.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 351642211   78 TSNYLCLQCPQILGVEER----LEHGNKKSHRFYVDSRNGMLYCQMCDDYVWDPTL 129
Cdd:pfam02148   8 SNLWLCLTCGHVGCGRYQnshaLEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
 
Name Accession Description Interval E-value
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 179-513 1.16e-140

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: 408.30  E-value: 1.16e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 179 RGIYNAGATCYQNVILQSFLHNPFLRNYYLSDGHQ--SGECQTQYCMSCAMDDIFQDFYSQETTNGYTAANMLCGFWSLE 256
Cdd:cd02660    1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSctCLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 257 RkafaNLVTTKEQDAHEFFQLLAEELHERNGDGKrPESGSEHLCDCIIHQTYYGKLQSNTTCQGCGSVTNQVQSFLDLSL 336
Cdd:cd02660   81 R----NLAGYSQQDAHEFFQFLLDQLHTHYGGDK-NEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 337 GLDSTQKKKKLAGTKSEGGSKgaslSLQDCLEEEYVKSDKCE--YRCNKCSSTQQARRNTSLKRLPNVLSIQLKRFEYKQ 414
Cdd:cd02660  156 DIPNKSTPSWALGESGVSGTP----TLSDCLDRFTRPEKLGDfaYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 415 grHDKAVKVDTPVKFPLQLNMFPYTDRGpSTESKENYELARTCQYDLFSVVEHVGEIDTGHYTCYCKVQ-DQWFAFNDHR 493
Cdd:cd02660  232 --NKTSRKIDTYVQFPLELNMTPYTSSS-IGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGdGQWFKFDDAM 308

                        330       340
                 ....*....|....*....|
gi 351642211 494 VEMASVSQVLSAKAYLLFYI 513
Cdd:cd02660  309 ITRVSEEEVLKSQAYLLFYH 328
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
179-512 1.33e-64

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 212.30  E-value: 1.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  179 RGIYNAGATCYQNVILQSFLHNPFLRNYYLSDGHQSGECQTQYC--MSCAMDDIFQDFYSQETTNGYTAanmlCGFWSLE 256
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSKSSSVSP----KMFKKSL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  257 RKAFANLVTTKEQDAHEFFQLLAEELHE-RNGDGKRPesgsehlCDCIIHQTYYGKLQSNTTCQGCGSVTNQVQSFLDLS 335
Cdd:pfam00443  77 GKLNPDFSGYKQQDAQEFLLFLLDGLHEdLNGNHSTE-------NESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLS 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  336 LGLDSTQKKKKLAgtkseggskgaslSLQDCLEEEYVKSDKCE---YRCNKCSSTQQARRNTSLKRLPNVLSIQLKRFEY 412
Cdd:pfam00443 150 LPIPGDSAELKTA-------------SLQICFLQFSKLEELDDeekYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  413 KQgrhDKAVKVDTPVKFPLQLNMFPYTDRGPSTESKENYElartcqYDLFSVVEHVGEIDTGHYTCYCKVQD--QWFAFN 490
Cdd:pfam00443 217 NR---STWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD------YRLVAVVVHSGSLSSGHYIAYIKAYEnnRWYKFD 287

                         330       340
                  ....*....|....*....|...
gi 351642211  491 DHRVEMASVS-QVLSAKAYLLFY 512
Cdd:pfam00443 288 DEKVTEVDEEtAVLSSSAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 174-503 1.03e-29

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 124.21  E-value: 1.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  174 KATGLRGIYNAGATCYQNVILQSFLHNPFLRN--YYLSDGHQSGECQTQYcmscAMDDIFQDFYSQE---TTNGYTAANM 248
Cdd:COG5077   189 KETGYVGLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRGRDSVAL----ALQRLFYNLQTGEepvDTTELTRSFG 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  249 lcgfWSlerkafaNLVTTKEQDAHEFFQLLAEELhERNGDGKRPESgsehlcdcIIHQTYYGKLQSNTTCQGCGSVTNQV 328
Cdd:COG5077   265 ----WD-------SDDSFMQHDIQEFNRVLQDNL-EKSMRGTVVEN--------ALNGIFVGKMKSYIKCVNVNYESARV 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  329 QSFLDLSLGLDstqkkkklagtksegGSKGASLSLQDCLEEEYVKSDKCeYRCNKcSSTQQARRNTSLKRLPNVLSIQLK 408
Cdd:COG5077   325 EDFWDIQLNVK---------------GMKNLQESFRRYIQVETLDGDNR-YNAEK-HGLQDAKKGVIFESLPPVLHLQLK 387

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  409 RFEYKQGRhDKAVKVDTPVKFPLQLNMFPYTDrgPSTESKENYElartCQYDLFSVVEHVGEIDTGHYTCYCK--VQDQW 486
Cdd:COG5077   388 RFEYDFER-DMMVKINDRYEFPLEIDLLPFLD--RDADKSENSD----AVYVLYGVLVHSGDLHEGHYYALLKpeKDGRW 460

                         330
                  ....*....|....*..
gi 351642211  487 FAFNDHRVEMASVSQVL 503
Cdd:COG5077   461 YKFDDTRVTRATEKEVL 477
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
78-129 6.67e-04

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 38.01  E-value: 6.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 351642211   78 TSNYLCLQCPQILGVEER----LEHGNKKSHRFYVDSRNGMLYCQMCDDYVWDPTL 129
Cdd:pfam02148   8 SNLWLCLTCGHVGCGRYQnshaLEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
 
Name Accession Description Interval E-value
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 179-513 1.16e-140

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: 408.30  E-value: 1.16e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 179 RGIYNAGATCYQNVILQSFLHNPFLRNYYLSDGHQ--SGECQTQYCMSCAMDDIFQDFYSQETTNGYTAANMLCGFWSLE 256
Cdd:cd02660    1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSctCLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 257 RkafaNLVTTKEQDAHEFFQLLAEELHERNGDGKrPESGSEHLCDCIIHQTYYGKLQSNTTCQGCGSVTNQVQSFLDLSL 336
Cdd:cd02660   81 R----NLAGYSQQDAHEFFQFLLDQLHTHYGGDK-NEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 337 GLDSTQKKKKLAGTKSEGGSKgaslSLQDCLEEEYVKSDKCE--YRCNKCSSTQQARRNTSLKRLPNVLSIQLKRFEYKQ 414
Cdd:cd02660  156 DIPNKSTPSWALGESGVSGTP----TLSDCLDRFTRPEKLGDfaYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 415 grHDKAVKVDTPVKFPLQLNMFPYTDRGpSTESKENYELARTCQYDLFSVVEHVGEIDTGHYTCYCKVQ-DQWFAFNDHR 493
Cdd:cd02660  232 --NKTSRKIDTYVQFPLELNMTPYTSSS-IGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGdGQWFKFDDAM 308

                        330       340
                 ....*....|....*....|
gi 351642211 494 VEMASVSQVLSAKAYLLFYI 513
Cdd:cd02660  309 ITRVSEEEVLKSQAYLLFYH 328
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
179-512 1.33e-64

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 212.30  E-value: 1.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  179 RGIYNAGATCYQNVILQSFLHNPFLRNYYLSDGHQSGECQTQYC--MSCAMDDIFQDFYSQETTNGYTAanmlCGFWSLE 256
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSKSSSVSP----KMFKKSL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  257 RKAFANLVTTKEQDAHEFFQLLAEELHE-RNGDGKRPesgsehlCDCIIHQTYYGKLQSNTTCQGCGSVTNQVQSFLDLS 335
Cdd:pfam00443  77 GKLNPDFSGYKQQDAQEFLLFLLDGLHEdLNGNHSTE-------NESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLS 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  336 LGLDSTQKKKKLAgtkseggskgaslSLQDCLEEEYVKSDKCE---YRCNKCSSTQQARRNTSLKRLPNVLSIQLKRFEY 412
Cdd:pfam00443 150 LPIPGDSAELKTA-------------SLQICFLQFSKLEELDDeekYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  413 KQgrhDKAVKVDTPVKFPLQLNMFPYTDRGPSTESKENYElartcqYDLFSVVEHVGEIDTGHYTCYCKVQD--QWFAFN 490
Cdd:pfam00443 217 NR---STWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD------YRLVAVVVHSGSLSSGHYIAYIKAYEnnRWYKFD 287

                         330       340
                  ....*....|....*....|...
gi 351642211  491 DHRVEMASVS-QVLSAKAYLLFY 512
Cdd:pfam00443 288 DEKVTEVDEEtAVLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 180-513 1.28e-57

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: 192.31  E-value: 1.28e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 180 GIYNAGATCYQNVILQSFLHNpflrnyylsdghqsgecqtqycmscamddifqdfysqettngytaanmlcgfwslerka 259
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 260 fanlvttkEQDAHEFFQLLAEELHERNGDGKRPESGSEHlCDCIIHQTYYGKLQSNTTCQGCGSVTNQVQSFLDLSLGLD 339
Cdd:cd02257   22 --------QQDAHEFLLFLLDKLHEELKKSSKRTSDSSS-LKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 340 STQKKKKlagtkseggskgaslSLQDCLEEEYVKSDKCEYRCNKCS--STQQARRNTSLKRLPNVLSIQLKRFEYKqgRH 417
Cdd:cd02257   93 VKGLPQV---------------SLEDCLEKFFKEEILEGDNCYKCEkkKKQEATKRLKIKKLPPVLIIHLKRFSFN--ED 155

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 418 DKAVKVDTPVKFPLQLNMFPYTDRGPSTESKENyelaRTCQYDLFSVVEHVGE-IDTGHYTCYCKV--QDQWFAFNDHRV 494
Cdd:cd02257  156 GTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDN----GSYKYELVAVVVHSGTsADSGHYVAYVKDpsDGKWYKFNDDKV 231

                        330       340
                 ....*....|....*....|....
gi 351642211 495 EMASVSQVL-----SAKAYLLFYI 513
Cdd:cd02257  232 TEVSEEEVLefgslSSSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 179-513 3.03e-56

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: 190.18  E-value: 3.03e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 179 RGIYNAGATCYQNVILQSFLHNPFLRNYYLSDGHQSGECQTQYCMSCAMddifQDFYSQETTNGYTAANMlcGFWSLERK 258
Cdd:cd02661    2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCAL----EAHVERALASSGPGSAP--RIFSSNLK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 259 AFA-NLVTTKEQDAHEFFQLLAEELHERNGDGKRPESGSEHLC--DCIIHQTYYGKLQSNTTCQGCGSVTNQVQSFLDLS 335
Cdd:cd02661   76 QISkHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSqeTTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 336 LGLdstqkkkklagtkseggsKGASlSLQDCLeEEYVKSDKCE----YRCNKCSSTQQARRNTSLKRLPNVLSIQLKRFE 411
Cdd:cd02661  156 LDI------------------KGAD-SLEDAL-EQFTKPEQLDgenkYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 412 YKQGRhdkavKVDTPVKFPLQLNMFPYTDRGPSTEskenyelartCQYDLFSVVEHVG-EIDTGHYTCYCKVQD-QWFAF 489
Cdd:cd02661  216 NFRGG-----KINKQISFPETLDLSPYMSQPNDGP----------LKYKLYAVLVHSGfSPHSGHYYCYVKSSNgKWYNM 280

                        330       340
                 ....*....|....*....|....
gi 351642211 490 NDHRVEMASVSQVLSAKAYLLFYI 513
Cdd:cd02661  281 DDSKVSPVSIETVLSQKAYILFYI 304
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 267-513 8.61e-48

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 165.15  E-value: 8.61e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 267 KEQDAHEFFQLLAEELHErngdgkrpesgsehlcdcIIHQTYYGKLQSNTTCQGCGSVTNQVQSFLDLSLGLDStqkkkk 346
Cdd:cd02674   21 DQQDAQEFLLFLLDGLHS------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPS------ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 347 lagtkseGGSKGASLSLQDCLEEeYVKSDK----CEYRCNKCSSTQQARRNTSLKRLPNVLSIQLKRFEYKQGRhdkAVK 422
Cdd:cd02674   77 -------GSGDAPKVTLEDCLRL-FTKEETldgdNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGS---TRK 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 423 VDTPVKFPLQ-LNMFPYTDRGPSTESKEnyelartcqYDLFSVVEHVGEIDTGHYTCYCKVQ--DQWFAFNDHRVEMASV 499
Cdd:cd02674  146 LTTPVTFPLNdLDLTPYVDTRSFTGPFK---------YDLYAVVNHYGSLNGGHYTAYCKNNetNDWYKFDDSRVTKVSE 216

                        250
                 ....*....|....
gi 351642211 500 SQVLSAKAYLLFYI 513
Cdd:cd02674  217 SSVVSSSAYILFYE 230
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 177-513 6.29e-46

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: 163.58  E-value: 6.29e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 177 GLRGIYNAGATCYQNVILQSFLHNPFLRNYYLSDGHQSGECQTQYcMSCAMDDIFqdFYSQETTNGYTAANMLC-----G 251
Cdd:cd02659    1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKS-VPLALQRLF--LFLQLSESPVKTTELTDktrsfG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 252 FWSLErkafanlvTTKEQDAHEFFQLLAEELherngDGKRPESGSEHLcdciIHQTYYGKLQSNTTCQGCGSVTNQVQSF 331
Cdd:cd02659   78 WDSLN--------TFEQHDVQEFFRVLFDKL-----EEKLKGTGQEGL----IKNLFGGKLVNYIICKECPHESEREEYF 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 332 LDLSLGLdstqKKKKlagtkseggskgaslSLQDCLEEeYVKSDKCE----YRCNKCSSTQQARRNTSLKRLPNVLSIQL 407
Cdd:cd02659  141 LDLQVAV----KGKK---------------NLEESLDA-YVQGETLEgdnkYFCEKCGKKVDAEKGVCFKKLPPVLTLQL 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 408 KRFEYkQGRHDKAVKVDTPVKFPLQLNMFPYTDRGPSTESKENYELAR-TCQYDLFSVVEHVGEIDTGHYTCYCK--VQD 484
Cdd:cd02659  201 KRFEF-DFETMMRIKINDRFEFPLELDMEPYTEKGLAKKEGDSEKKDSeSYIYELHGVLVHSGDAHGGHYYSYIKdrDDG 279

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 351642211 485 QWFAFNDHRVEMASVSQVLSA----------------------KAYLLFYI 513
Cdd:cd02659  280 KWYKFNDDVVTPFDPNDAEEEcfggeetqktydsgprafkrttNAYMLFYE 330
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 180-512 4.72e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 146.69  E-value: 4.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 180 GIYNAGATCYQNVILQSFLHNPFLrnyylsdghqsgecqtqYCMScamdDIFQDFYSQETTNGYTAANMLCGFWSLERKA 259
Cdd:cd02663    1 GLENFGNTCYCNSVLQALYFENLL-----------------TCLK----DLFESISEQKKRTGVISPKKFITRLKRENEL 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 260 FANlvtTKEQDAHEFFQLL----AEELHERNGDGKRPESGSEHLCDCI----IHQTYYGKLQSNTTCQGCGSVTNQVQSF 331
Cdd:cd02663   60 FDN---YMHQDAHEFLNFLlneiAEILDAERKAEKANRKLNNNNNAEPqptwVHEIFQGILTNETRCLTCETVSSRDETF 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 332 LDLSLGLDStqkkkklagtkseggskgaSLSLQDCL----EEEYVKSDKcEYRCNKCSSTQQARRNTSLKRLPNVLSIQL 407
Cdd:cd02663  137 LDLSIDVEQ-------------------NTSITSCLrqfsATETLCGRN-KFYCDECCSLQEAEKRMKIKKLPKILALHL 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 408 KRFEY--KQGRHdkaVKVDTPVKFPLQLNMFPYTDRGPSTESKenyelartcqYDLFSVVEHVGE-IDTGHYTCYCKVQD 484
Cdd:cd02663  197 KRFKYdeQLNRY---IKLFYRVVFPLELRLFNTTDDAENPDRL----------YELVAVVVHIGGgPNHGHYVSIVKSHG 263

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 351642211 485 QWFAFNDHRVEMASVSQVL--------SAKAYLLFY 512
Cdd:cd02663  264 GWLLFDDETVEKIDENAVEeffgdspnQATAYVLFY 299
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 180-512 1.07e-34

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 131.74  E-value: 1.07e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 180 GIYNAGATCYQNVILQSFLHNPFLRnyylsdghqsgecqtqycmscamdDIFQDfysqettngyTAANMlcgFWSLERKA 259
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALR------------------------ELLSE----------TPKEL---FSQVCRKA 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 260 fANLVTTKEQDAHEFFQLLAeelherngDGKRPesgsehlcdcIIHQTYYGKLQSNTTCQGCGSVTNQVQSFLDLSLGLD 339
Cdd:cd02667   44 -PQFKGYQQQDSHELLRYLL--------DGLRT----------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRS 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 340 STQKKKKlagtkseggskgaslSLQDCLE---EEYVKSDKCEYRCNKCsstQQARRNTSLKRLPNVLSIQLKRFeyKQGR 416
Cdd:cd02667  105 DEIKSEC---------------SIESCLKqftEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRF--QQPR 164

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 417 HDKAVKVDTPVKFPLQLNMFPYTD-RGPSTESKENYelartcQYDLFSVVEHVGEIDTGHYTCYCKV------------- 482
Cdd:cd02667  165 SANLRKVSRHVSFPEILDLAPFCDpKCNSSEDKSSV------LYRLYGVVEHSGTMRSGHYVAYVKVrppqqrlsdltks 238

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 351642211 483 ----------QDQWFAFNDHRVEMASVSQVLSAKAYLLFY 512
Cdd:cd02667  239 kpaadeagpgSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 180-495 4.26e-31

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 122.91  E-value: 4.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 180 GIYNAGATCYQNVILQSFLHNPFLRNYYLS------DGHQSGECQTQYCMSCAMDDIFQDFYSQETTN-GYtaanmlcgf 252
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnstedAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNrSV--------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 253 wsLERKAFAN---LVTTKEQDAHEFFQLL-----AEELHERNGDGKRpesgsehlcdcIIHQTYYGKLQSNTTCQGCGSV 324
Cdd:cd02668   72 --VDPSGFVKalgLDTGQQQDAQEFSKLFlslleAKLSKSKNPDLKN-----------IVQDLFRGEYSYVTQCSKCGRE 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 325 TNQVQSFLDLSLgldstqkkkKLAGTKSeggskgaslsLQDCLEEeYVKSDKCE----YRCNKCSSTQQARRNTSLKRLP 400
Cdd:cd02668  139 SSLPSKFYELEL---------QLKGHKT----------LEECIDE-FLKEEQLTgdnqYFCESCNSKTDATRRIRLTTLP 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 401 NVLSIQLKRFEY-KQGRHDKavKVDTPVKFPLQLNMFPYTDrgpstESKENYelartCQYDLFSVVEHVG-EIDTGHYTC 478
Cdd:cd02668  199 PTLNFQLLRFVFdRKTGAKK--KLNASISFPEILDMGEYLA-----ESDEGS-----YVYELSGVLIHQGvSAYSGHYIA 266

                        330
                 ....*....|....*....
gi 351642211 479 YCK--VQDQWFAFNDHRVE 495
Cdd:cd02668  267 HIKdeQTGEWYKFNDEDVE 285
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 174-503 1.03e-29

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 124.21  E-value: 1.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  174 KATGLRGIYNAGATCYQNVILQSFLHNPFLRN--YYLSDGHQSGECQTQYcmscAMDDIFQDFYSQE---TTNGYTAANM 248
Cdd:COG5077   189 KETGYVGLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRGRDSVAL----ALQRLFYNLQTGEepvDTTELTRSFG 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  249 lcgfWSlerkafaNLVTTKEQDAHEFFQLLAEELhERNGDGKRPESgsehlcdcIIHQTYYGKLQSNTTCQGCGSVTNQV 328
Cdd:COG5077   265 ----WD-------SDDSFMQHDIQEFNRVLQDNL-EKSMRGTVVEN--------ALNGIFVGKMKSYIKCVNVNYESARV 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  329 QSFLDLSLGLDstqkkkklagtksegGSKGASLSLQDCLEEEYVKSDKCeYRCNKcSSTQQARRNTSLKRLPNVLSIQLK 408
Cdd:COG5077   325 EDFWDIQLNVK---------------GMKNLQESFRRYIQVETLDGDNR-YNAEK-HGLQDAKKGVIFESLPPVLHLQLK 387

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  409 RFEYKQGRhDKAVKVDTPVKFPLQLNMFPYTDrgPSTESKENYElartCQYDLFSVVEHVGEIDTGHYTCYCK--VQDQW 486
Cdd:COG5077   388 RFEYDFER-DMMVKINDRYEFPLEIDLLPFLD--RDADKSENSD----AVYVLYGVLVHSGDLHEGHYYALLKpeKDGRW 460

                         330
                  ....*....|....*..
gi 351642211  487 FAFNDHRVEMASVSQVL 503
Cdd:COG5077   461 YKFDDTRVTRATEKEVL 477
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 180-512 1.78e-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: 101.12  E-value: 1.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 180 GIYNAGATCYQNVILQSFLHNP-FLRN-YYLSDGHQSGECQTQYCMScamddifqdfySQETTNGYTAANMLCGFWSLER 257
Cdd:cd02671   26 GLNNLGNTCYLNSVLQVLYFCPgFKHGlKHLVSLISSVEQLQSSFLL-----------NPEKYNDELANQAPRRLLNALR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 258 KAFANLVTTKEQDAHEFFQLLAEELHErngdgkrpesgsehlcdcIIHQTYYGKLQSNTTCQGCGSVTNQVQSFLDLSLG 337
Cdd:cd02671   95 EVNPMYEGYLQHDAQEVLQCILGNIQE------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 338 LDSTQKKKKLAGTKSEGGSKGASLSLQDCLEEEYvkSDKC-----EYRCNKCSSTQQARRNTSLKRLPNVLSIQLKRFEY 412
Cdd:cd02671  157 VQESELSKSEESSEISPDPKTEMKTLKWAISQFA--SVERivgedKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 413 KQGRHDKA---VKVDTPVKFPLQLNMFPYTDrGPSTESkenyelartcqYDLFSVVEHVG-EIDTGHYTCYCKvqdqWFA 488
Cdd:cd02671  235 NGSEFDCYgglSKVNTPLLTPLKLSLEEWST-KPKNDV-----------YRLFAVVMHSGaTISSGHYTAYVR----WLL 298

                        330       340       350
                 ....*....|....*....|....*....|...
gi 351642211 489 FNDHRV---------EMASVSQVLSAKAYLLFY 512
Cdd:cd02671  299 FDDSEVkvteekdflEALSPNTSSTSTPYLLFY 331
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 180-512 1.32e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 96.67  E-value: 1.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 180 GIYNAGATCYQNVILQSFLHNPFLRNYylsdghqsgecqtqycmscamddifqdfysqettngytaanmlcgfwsLERka 259
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEY------------------------------------------------LEE-- 30

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 260 fanlvTTKEQDAHEFFQLLAEELherngdgkrpESGSEHLCDciihqtyyGKLQSNTTCQGCGSVTN-QVQSFLDLSLGL 338
Cdd:cd02662   31 -----FLEQQDAHELFQVLLETL----------EQLLKFPFD--------GLLASRIVCLQCGESSKvRYESFTMLSLPV 87

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 339 DSTqkkkklagtkseggSKGASLSLQDCLEEeYVKSDKCE-YRCNKCSstqqarrnTSLKRLPNVLSIQLKRFEYkqGRH 417
Cdd:cd02662   88 PNQ--------------SSGSGTTLEHCLDD-FLSTEIIDdYKCDRCQ--------TVIVRLPQILCIHLSRSVF--DGR 142

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 418 DKAVKVDTPVKFPLQLnmfpytdrgpsteskenyelaRTCQYDLFSVVEHVGEIDTGHYTCY------------------ 479
Cdd:cd02662  143 GTSTKNSCKVSFPERL---------------------PKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrm 201

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 351642211 480 ----CKVQDQWFAFNDHRVEMASVSQVLSAK-AYLLFY 512
Cdd:cd02662  202 regpSSTSHPWWRISDTTVKEVSESEVLEQKsAYMLFY 239
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 180-512 2.19e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 97.78  E-value: 2.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 180 GIYNAGATCYQNVILQS-FLHNPFLRNYYLSDGHQSgecqtqycmsCAMDDIFQDFYSQETT--NGytaanMLCGFWSLE 256
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVlFSIPSFQWRYDDLENKFP----------SDVVDPANDLNCQLIKlaDG-----LLSGRYSKP 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 257 R---------------KAFANLV--------TTKEQDAHEFFQLLAEELhERNgdgKRPESGSE--HLCDCIIHQtyygK 311
Cdd:cd02658   66 AslksendpyqvgikpSMFKALIgkghpefsTMRQQDALEFLLHLIDKL-DRE---SFKNLGLNpnDLFKFMIED----R 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 312 LQsnttCQGCGSV--TNQVQSFLDLSLGLDstqkkkkLAGTKSEGGSKGASLSLQDCLEEeYVKSDKCEYRCNKCSSTQQ 389
Cdd:cd02658  138 LE----CLSCKKVkyTSELSEILSLPVPKD-------EATEKEEGELVYEPVPLEDCLKA-YFAPETIEDFCSTCKEKTT 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 390 ARRNTSLKRLPNVLSIQLKRFEYKQGRhdKAVKVDTPVKFPLqlnmfpytDRGPSTeskenyelartcqYDLFSVVEHVG 469
Cdd:cd02658  206 ATKTTGFKTFPDYLVINMKRFQLLENW--VPKKLDVPIDVPE--------ELGPGK-------------YELIAFISHKG 262

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 351642211 470 -EIDTGHYTCYCK----VQDQWFAFNDHRVEMASVSQVLSAKAYLLFY 512
Cdd:cd02658  263 tSVHSGHYVAHIKkeidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 180-512 1.81e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 92.17  E-value: 1.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 180 GIYNAGATCYQNVILQSFLHNPFLRNYYLSDGHQSGECQtqycmSCAMDDIFQDFYSQETTNGYTAANMLCGFWSLERKA 259
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDS-----QSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASRPPW 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 260 FANlvtTKEQDAHEFFQLLAEELHErngdgkrpesgsehlcdcIIHQTYYGKLQSNTTCQGCGSVTNQVQSFLDLSLGLD 339
Cdd:cd02664   76 FTP---GSQQDCSEYLRYLLDRLHT------------------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 340 STQK--KKKLAGTKSEGGSKgaslslqdcleeeyvksdkceYRCNKCSSTQQARRNTSLKRLPNVLSIQLKRFEYKQGRH 417
Cdd:cd02664  135 SVQDllNYFLSPEKLTGDNQ---------------------YYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTH 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 418 DKAvKVDTPVKFPLQLNMfPYTDRGPSTESKENYELA----------RTCQYDLFSVVEHVG-EIDTGHYTCYCKVQ--- 483
Cdd:cd02664  194 VRE-KIMDNVSINEVLSL-PVRVESKSSESPLEKKEEesgddgelvtRQVHYRLYAVVVHSGySSESGHYFTYARDQtda 271

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 351642211 484 -------------------DQWFAFNDHRVEMAS---VSQVLSAK----AYLLFY 512
Cdd:cd02664  272 dstgqecpepkdaeendesKNWYLFNDSRVTFSSfesVQNVTSRFpkdtPYILFY 326
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
349-515 6.38e-20

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 93.41  E-value: 6.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 349 GTKSEGGSKGASLSLQDCLEEEYVKSDKCE---YRCNKCSSTQQARRNTSLKRLPNVLSIQLKRFEYKQGRHDkavKVDT 425
Cdd:COG5560  663 WTIREIGAAERTITLQDCLNEFSKPEQLGLsdsWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRD---KIDD 739

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 426 PVKFP---LQLNMFPYtdrgpsteSKENYELArtcqYDLFSVVEHVGEIDTGHYTCYCKVQD--QWFAFNDHRVEMASVS 500
Cdd:COG5560  740 LVEYPiddLDLSGVEY--------MVDDPRLI----YDLYAVDNHYGGLSGGHYTAYARNFAnnGWYLFDDSRITEVDPE 807

                        170
                 ....*....|....*
gi 351642211 501 QVLSAKAYLLFYIVR 515
Cdd:COG5560  808 DSVTSSAYVLFYRRK 822
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
180-512 1.20e-17

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 83.31  E-value: 1.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 180 GIYNAGATCYQNVILQSF-LHNPFLRNYYLSDGHQSGECQTQYcmscamDDIFQDFYSQETTNGYTAanmlcgFWSLERK 258
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKELKVLKNVI------RKPEPDLNQEEALKLFTA------LWSSKEH 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 259 AFANLVTTKEQ-DAHEFFQLLAEELherngdgKRPESGSehlcdciiHQTYYGKLQSNTTCQGCGSVtNQVQsfldlslg 337
Cdd:COG5533   69 KVGWIPPMGSQeDAHELLGKLLDEL-------KLDLVNS--------FTIRIFKTTKDKKKTSTGDW-FDII-------- 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 338 lDSTQKKKKLAGTKSeggskgaslsLQDCLEE-EYVKSDKCEYRC--NKCSSTQ-QARRNTSLKRLPNVLSIQLKRFEYK 413
Cdd:COG5533  125 -IELPDQTWVNNLKT----------LQEFIDNmEELVDDETGVKAkeNEELEVQaKQEYEVSFVKLPKILTIQLKRFANL 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 414 QGRhdkaVKVDTPVKFPLQLnmfPYTDRGPSTESKENYelartcqYDLFSVVEHVGEIDTGHYTCYCKVQDQWFAFNDHR 493
Cdd:COG5533  194 GGN----QKIDTEVDEKFEL---PVKHDQILNIVKETY-------YDLVGFVLHQGSLEGGHYIAYVKKGGKWEKANDSD 259

                        330       340
                 ....*....|....*....|..
gi 351642211 494 VEMASVSQVLSAK---AYLLFY 512
Cdd:COG5533  260 VTPVSEEEAINEKaknAYLYFY 281
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 180-512 1.92e-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 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: 83.15  E-value: 1.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 180 GIYNAGATCYQNVILQSFLHNPFLRNYYL-SDGHQSGECQTQYCMSCAMDDIFQDFysQETTNGYTAANmlcgFWSLERK 258
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKnYNPARRGANQSSDNLTNALRDLFDTM--DKKQEPVPPIE----FLQLLRM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 259 AFANLVTT------KEQDAHEFF-QLLAEELHERNGDGKRPESgsehlcdciIHQTYYGKLQSNTTCQGCG-SVTNQVQS 330
Cdd:cd02657   75 AFPQFAEKqnqggyAQQDAEECWsQLLSVLSQKLPGAGSKGSF---------IDQLFGIELETKMKCTESPdEEEVSTES 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 331 FLDLSLGLDSTQKKKKL-AGTKSEGGSKGASLSLQDCLEEEYVKsdkceyrcnkcsstqqarrNTSLKRLPNVLSIQLKR 409
Cdd:cd02657  146 EYKLQCHISITTEVNYLqDGLKKGLEEEIEKHSPTLGRDAIYTK-------------------TSRISRLPKYLTVQFVR 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 410 FEYKQGRHDKAvKVDTPVKFPLQLNMFPYtdrgpsteskenyeLARTCQYDLFSVVEHVG-EIDTGHYTCY--CKVQDQW 486
Cdd:cd02657  207 FFWKRDIQKKA-KILRKVKFPFELDLYEL--------------CTPSGYYELVAVITHQGrSADSGHYVAWvrRKNDGKW 271

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 351642211 487 FAFNDhrvemASVSQVLSAK------------AYLLFY 512
Cdd:cd02657  272 IKFDD-----DKVSEVTEEDilklsgggdwhiAYILLY 304
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
186-491 1.82e-12

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 68.07  E-value: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  186 ATCYQNVILQSFLHNPFLRNYYLSdgHQSGECQTQYCMSC-------AMDDifqdfysQETTNgYTAANMLcgfwslerK 258
Cdd:pfam13423   8 PNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCelgflfdMLEK-------AKGKN-CQASNFL--------R 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  259 AFANL--------------------VTTKEQDAHEFF-QLLAEELHERNGDGKRPESgsehlcdcIIHQTYYGKLQSNTT 317
Cdd:pfam13423  70 ALSSIpeasalglldedretnsaisLSSLIQSFNRFLlDQLSSEENSTPPNPSPAES--------PLEQLFGIDAETTIR 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  318 CQGCGSVTNQVQSFLDLSLgldstqkkkKLAGTKSEGGSKGASLSLQDCLE-----EEYVKSdkceyRCNKCSSTQQARR 392
Cdd:pfam13423 142 CSNCGHESVRESSTHVLDL---------IYPRKPSSNNKKPPNQTFSSILKsslerETTTKA-----WCEKCKRYQPLES 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211  393 NTSLKRLPNVLSIQLKRFEYKQGRHDKavkvdTPVKFPLQLNMFPYTDRGPSTESKEnyelartcqYDLFSVVEHVGEID 472
Cdd:pfam13423 208 RRTVRNLPPVLSLNAALTNEEWRQLWK-----TPGWLPPEIGLTLSDDLQGDNEIVK---------YELRGVVVHIGDSG 273

                         330       340
                  ....*....|....*....|....*....
gi 351642211  473 T-GHYTCYCKV---------QDQWFAFND 491
Cdd:pfam13423 274 TsGHLVSFVKVadseledptESQWYLFND 302
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 363-513 6.03e-08

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: 53.33  E-value: 6.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 363 LQDCLEEEYVksdkcEYRCNKCSSTQQARRNTS--LKRLPNVLSIQLKRFEYKQGR----HDKavkvdtpVKFPLQLNMF 436
Cdd:cd02665   95 LHECLEAAMF-----EGEVELLPSDHSVKSGQErwFTELPPVLTFELSRFEFNQGRpekiHDK-------LEFPQIIQQV 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 437 PYtdrgpsteskenyelartcqyDLFSVVEHVGEIDTGHYTCYC--KVQDQWFAFNDHRVEMASVSQVLS--------AK 506
Cdd:cd02665  163 PY---------------------ELHAVLVHEGQANAGHYWAYIykQSRQEWEKYNDISVTESSWEEVERdsfgggrnPS 221


                 ....*..
gi 351642211 507 AYLLFYI 513
Cdd:cd02665  222 AYCLMYI 228
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 257-512 1.35e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 49.83  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 257 RKAFANlvtTKEQDAHEFFQLLAE---ELHERNGDGKRPESGSEHLCDCIIHQTYygKLQSNTTCQGCG--SVTNQVQSF 331
Cdd:cd02673   25 NTEFDN---DDQQDAHEFLLTLLEaidDIMQVNRTNVPPSNIEIKRLNPLEAFKY--TIESSYVCIGCSfeENVSDVGNF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 332 LDLSLgLDSTqkkkklagtkseggskgasLSLQDCLEEEYVKSDKCEYRCNKCSStQQARRNTSLKRLPNVLSIQLKRFe 411
Cdd:cd02673  100 LDVSM-IDNK-------------------LDIDELLISNFKTWSPIEKDCSSCKC-ESAISSERIMTFPECLSINLKRY- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 412 ykqgrhdkavkvdtpvkfplqlnmfpYTDRGPSTESKENYELARTCQ-----YDLFSVVEHVGE-IDTGHYTCYCK---V 482
Cdd:cd02673  158 --------------------------KLRIATSDYLKKNEEIMKKYCgtdakYSLVAVICHLGEsPYDGHYIAYTKelyN 211

                        250       260       270
                 ....*....|....*....|....*....|...
gi 351642211 483 QDQWFAFND---HRVEMASVSQVLSAKAYLLFY 512
Cdd:cd02673  212 GSSWLYCSDdeiRPVSKNDVSTNARSSGYLIFY 244
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 177-512 1.96e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 50.39  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 177 GLRGIYNAGATCYQNVILQSFLHNPFLRNYYLSdghqsgecqtqycmscamddifQDFYSQETTNgytAANMLCGFWSLE 256
Cdd:cd02669  118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL----------------------YENYENIKDR---KSELVKRLSELI 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 257 RK-----AFANLV------------------TTKEQDAHEFFQLLAEELHER-NGDGKRPESgsehlcdcIIHQTYYGKL 312
Cdd:cd02669  173 RKiwnprNFKGHVsphellqavskvskkkfsITEQSDPVEFLSWLLNTLHKDlGGSKKPNSS--------IIHDCFQGKV 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 313 Q-------------SNTTCQGCGSVTNQVQS--FLDLSLGLDSTqkkkklAGTKSEGGSKGAS-LSLQDCLEeeyvKSDK 376
Cdd:cd02669  245 QietqkikphaeeeGSKDKFFKDSRVKKTSVspFLLLTLDLPPP------PLFKDGNEENIIPqVPLKQLLK----KYDG 314

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 377 CEyrcnkCSSTQQARRNTSLKRLPNVLSIQLKRFEYKQGRHDKAvkvDTPVKFPLQLNMFPYTDRGPSTESKENyelart 456
Cdd:cd02669  315 KT-----ETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKN---PTIVNFPIKNLDLSDYVHFDKPSLNLS------ 380

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 351642211 457 CQYDLFSVVEHVGEIDT-GHYTC--YCKVQDQWFAFNDHRVEMASVSQVLSAKAYLLFY 512
Cdd:cd02669  381 TKYNLVANIVHEGTPQEdGTWRVqlRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 357-512 7.76e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 47.14  E-value: 7.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 357 KGASLSLQDCLEEEYvksdkceyrcnkcsstqqarRNTSLKRLPNVLSIQLKRFEYKQGrhdKAVKVDTPVKFPLQLNMF 436
Cdd:cd02670   76 DGGGITLEQCLEQYF--------------------NNSVFAKAPSCLIICLKRYGKTEG---KAQKMFKKILIPDEIDIP 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351642211 437 PYTDRGPSTESKENYELARTCQYDLF------------SVVEHVG-EIDTGHYTCYCKVQ-------------DQWFAFN 490
Cdd:cd02670  133 DFVADDPRACSKCQLECRVCYDDKDFsptcgkfklslcSAVCHRGtSLETGHYVAFVRYGsysltetdneaynAQWVFFD 212

                        170       180
                 ....*....|....*....|....*...
gi 351642211 491 D----HRVEMASVSQV--LSAKAYLLFY 512
Cdd:cd02670  213 DmadrDGVSNGFNIPAarLLEDPYMLFY 240
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
78-129 6.67e-04

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 38.01  E-value: 6.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 351642211   78 TSNYLCLQCPQILGVEER----LEHGNKKSHRFYVDSRNGMLYCQMCDDYVWDPTL 129
Cdd:pfam02148   8 SNLWLCLTCGHVGCGRYQnshaLEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH