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Conserved domains on  [gi|148746183|ref|NP_065849|]
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ubiquitin carboxyl-terminal hydrolase 35 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 913)

ubiquitin carboxyl-terminal hydrolase family protein is a C19 family peptidase that may deubiquitinate polyubiquitinated target proteins

Graphical summary

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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 ...
442-924 1.64e-96

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 cd02664:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 327  Bit Score: 308.27  E-value: 1.64e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  442 GLINLGNTCYVNSILQALFMASDFRHCVLRLT---ENNSQPLMTKLQWLFGFLEHSQRPAISPEN-FLSASWTPWFSPGT 517
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNlprLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDyFLEASRPPWFTPGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  518 QQDCSEYLKYLLDRLHeeektgtricqklkqssspsppeeppapssTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDLS 597
Cdd:cd02664    81 QQDCSEYLRYLLDRLH------------------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLD 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  598 LAFPppercrrrrlgsvmrpteditarelppptsaqgpgrvgprrqrkhcitedtpptslyiegldskeaggqssqeeri 677
Cdd:cd02664   131 LSFP---------------------------------------------------------------------------- 134
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  678 ereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpdaaipsgertcgseg 757
Cdd:cd02664       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  758 srSVLDLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVSIPLLLRLPL 837
Cdd:cd02664   135 --SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPV 212
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  838 -----------------AGGRGQA------YDLCSVVVHSGVSSESGHYYCYAR-----EGAARPAASLGTADRPEPENQ 889
Cdd:cd02664   213 rveskssesplekkeeeSGDDGELvtrqvhYRLYAVVVHSGYSSESGHYFTYARdqtdaDSTGQECPEPKDAEENDESKN 292
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 148746183  890 WYLFNDTRVSFSSFESVSNVTSFFPKDTAYVLFYR 924
Cdd:cd02664   293 WYLFNDSRVTFSSFESVQNVTSRFPKDTPYILFYE 327
COG1365 super family cl42514
Predicted ATPase, PP-loop superfamily [General function prediction only];
55-97 9.61e-03

Predicted ATPase, PP-loop superfamily [General function prediction only];


The actual alignment was detected with superfamily member COG1365:

Pssm-ID: 440976  Cd Length: 256  Bit Score: 38.88  E-value: 9.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 148746183   55 ELPRRVGCQLLHVAGRHHPDVfaEFFSARRVLRLLQGGAGPPG 97
Cdd:COG1365   207 ELSMKYGCPLLREAHKRHPSL--RKFSIQRVLREVRAGVLEPG 247
 
Name Accession Description Interval E-value
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-924 1.64e-96

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: 308.27  E-value: 1.64e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  442 GLINLGNTCYVNSILQALFMASDFRHCVLRLT---ENNSQPLMTKLQWLFGFLEHSQRPAISPEN-FLSASWTPWFSPGT 517
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNlprLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDyFLEASRPPWFTPGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  518 QQDCSEYLKYLLDRLHeeektgtricqklkqssspsppeeppapssTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDLS 597
Cdd:cd02664    81 QQDCSEYLRYLLDRLH------------------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLD 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  598 LAFPppercrrrrlgsvmrpteditarelppptsaqgpgrvgprrqrkhcitedtpptslyiegldskeaggqssqeeri 677
Cdd:cd02664   131 LSFP---------------------------------------------------------------------------- 134
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  678 ereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpdaaipsgertcgseg 757
Cdd:cd02664       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  758 srSVLDLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVSIPLLLRLPL 837
Cdd:cd02664   135 --SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPV 212
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  838 -----------------AGGRGQA------YDLCSVVVHSGVSSESGHYYCYAR-----EGAARPAASLGTADRPEPENQ 889
Cdd:cd02664   213 rveskssesplekkeeeSGDDGELvtrqvhYRLYAVVVHSGYSSESGHYFTYARdqtdaDSTGQECPEPKDAEENDESKN 292
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 148746183  890 WYLFNDTRVSFSSFESVSNVTSFFPKDTAYVLFYR 924
Cdd:cd02664   293 WYLFNDSRVTFSSFESVQNVTSRFPKDTPYILFYE 327
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
441-923 4.39e-29

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 118.70  E-value: 4.39e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183   441 IGLINLGNTCYVNSILQALFMASDFRHCVLRL-------TENNSQPLMTKLQWLF-GFLEHSQRPAISPENFLSA--SWT 510
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIsplsedsRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSlgKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183   511 PWFSPGTQQDCSEYLKYLLDRLHEEEKTGTricqklkqssspsppeepPAPSSTSVEKMFGGKIVTRICCLCCLNVSSRE 590
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNH------------------STENESLITDLFRGQLKSRLKCLSCGEVSETF 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183   591 EAFTDLSLafpppercrrrrlgsvmrpteditarelppptsaqgpgrvgprrqrkhcitedtpptslyiegldskeaggq 670
Cdd:pfam00443  143 EPFSDLSL------------------------------------------------------------------------ 150
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183   671 ssqeeriereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpDAAIPSGE 750
Cdd:pfam00443  151 ------------------------------------------------------------------------PIPGDSAE 158
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183   751 RTCGSEGSRSVLdlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTmrRRKILDDVSIP 830
Cdd:pfam00443  159 LKTASLQICFLQ-----FSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFP 231
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183   831 LLLRLplaggrgqaYDLCSVVVHSGVSSES----------------GHYYCYAregaarpaaslgtadRPEPENQWYLFN 894
Cdd:pfam00443  232 LELDL---------SRYLAEELKPKTNNLQdyrlvavvvhsgslssGHYIAYI---------------KAYENNRWYKFD 287
                          490       500
                   ....*....|....*....|....*....
gi 148746183   895 DTRVSFSSFESVSNvtsffpKDTAYVLFY 923
Cdd:pfam00443  288 DEKVTEVDEETAVL------SSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
763-926 1.62e-14

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 78.39  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  763 DLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRtmRRRKILDDVSIPlLLRLPLAGGRG 842
Cdd:COG5560   679 DCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRS--FRDKIDDLVEYP-IDDLDLSGVEY 755
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  843 Q------AYDLcSVVVHSGVSSESGHYYCYAREGAarpaaslgtadrpepENQWYLFNDTRvsfssfesvsnVTSFFPKD 916
Cdd:COG5560   756 MvddprlIYDL-YAVDNHYGGLSGGHYTAYARNFA---------------NNGWYLFDDSR-----------ITEVDPED 808
                         170
                  ....*....|....
gi 148746183  917 T----AYVLFYRQR 926
Cdd:COG5560   809 SvtssAYVLFYRRK 822
COG1365 COG1365
Predicted ATPase, PP-loop superfamily [General function prediction only];
55-97 9.61e-03

Predicted ATPase, PP-loop superfamily [General function prediction only];


Pssm-ID: 440976  Cd Length: 256  Bit Score: 38.88  E-value: 9.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 148746183   55 ELPRRVGCQLLHVAGRHHPDVfaEFFSARRVLRLLQGGAGPPG 97
Cdd:COG1365   207 ELSMKYGCPLLREAHKRHPSL--RKFSIQRVLREVRAGVLEPG 247
 
Name Accession Description Interval E-value
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-924 1.64e-96

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: 308.27  E-value: 1.64e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  442 GLINLGNTCYVNSILQALFMASDFRHCVLRLT---ENNSQPLMTKLQWLFGFLEHSQRPAISPEN-FLSASWTPWFSPGT 517
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNlprLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDyFLEASRPPWFTPGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  518 QQDCSEYLKYLLDRLHeeektgtricqklkqssspsppeeppapssTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDLS 597
Cdd:cd02664    81 QQDCSEYLRYLLDRLH------------------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLD 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  598 LAFPppercrrrrlgsvmrpteditarelppptsaqgpgrvgprrqrkhcitedtpptslyiegldskeaggqssqeeri 677
Cdd:cd02664   131 LSFP---------------------------------------------------------------------------- 134
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  678 ereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpdaaipsgertcgseg 757
Cdd:cd02664       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  758 srSVLDLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVSIPLLLRLPL 837
Cdd:cd02664   135 --SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPV 212
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  838 -----------------AGGRGQA------YDLCSVVVHSGVSSESGHYYCYAR-----EGAARPAASLGTADRPEPENQ 889
Cdd:cd02664   213 rveskssesplekkeeeSGDDGELvtrqvhYRLYAVVVHSGYSSESGHYFTYARdqtdaDSTGQECPEPKDAEENDESKN 292
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 148746183  890 WYLFNDTRVSFSSFESVSNVTSFFPKDTAYVLFYR 924
Cdd:cd02664   293 WYLFNDSRVTFSSFESVQNVTSRFPKDTPYILFYE 327
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
439-924 2.53e-30

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: 123.14  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  439 GKIGLINLGNTCYVNSILQALFMASDFRHCVLRLTEN----NSQPLMTKLQWLFGFLEHSQRPAISPENFLSASWTPWFS 514
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTedddDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  515 --PGTQQDCSEYLKYLLDRLhEEEKTGTricqKLKQssspsppeeppapsstSVEKMFGGKIVTRICCLCCLNVSSREEA 592
Cdd:cd02659    81 lnTFEQHDVQEFFRVLFDKL-EEKLKGT----GQEG----------------LIKNLFGGKLVNYIICKECPHESEREEY 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  593 FTDLSLAfpppercrrrrlgsvmrpteditarelppptsaqgpgrvgprrqrkhciteDTPPTSLYiEGLDSkeaggqss 672
Cdd:cd02659   140 FLDLQVA---------------------------------------------------VKGKKNLE-ESLDA-------- 159
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  673 qeeriereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpdaaipsgert 752
Cdd:cd02659       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  753 cgsegsrsvldlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVSIPLL 832
Cdd:cd02659   160 ---------------YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLE 224
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  833 LRL------PLAGGRGQAYDLCSVVVHSGV--------SSESGHYYCYAregaarpaaslgtadRPEPENQWYLFNDTRv 898
Cdd:cd02659   225 LDMepytekGLAKKEGDSEKKDSESYIYELhgvlvhsgDAHGGHYYSYI---------------KDRDDGKWYKFNDDV- 288
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 148746183  899 sfssfesvsnVTSF-------------------------FPKDT-AYVLFYR 924
Cdd:cd02659   289 ----------VTPFdpndaeeecfggeetqktydsgpraFKRTTnAYMLFYE 330
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
441-923 4.39e-29

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 118.70  E-value: 4.39e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183   441 IGLINLGNTCYVNSILQALFMASDFRHCVLRL-------TENNSQPLMTKLQWLF-GFLEHSQRPAISPENFLSA--SWT 510
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIsplsedsRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSlgKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183   511 PWFSPGTQQDCSEYLKYLLDRLHEEEKTGTricqklkqssspsppeepPAPSSTSVEKMFGGKIVTRICCLCCLNVSSRE 590
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNH------------------STENESLITDLFRGQLKSRLKCLSCGEVSETF 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183   591 EAFTDLSLafpppercrrrrlgsvmrpteditarelppptsaqgpgrvgprrqrkhcitedtpptslyiegldskeaggq 670
Cdd:pfam00443  143 EPFSDLSL------------------------------------------------------------------------ 150
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183   671 ssqeeriereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpDAAIPSGE 750
Cdd:pfam00443  151 ------------------------------------------------------------------------PIPGDSAE 158
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183   751 RTCGSEGSRSVLdlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTmrRRKILDDVSIP 830
Cdd:pfam00443  159 LKTASLQICFLQ-----FSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFP 231
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183   831 LLLRLplaggrgqaYDLCSVVVHSGVSSES----------------GHYYCYAregaarpaaslgtadRPEPENQWYLFN 894
Cdd:pfam00443  232 LELDL---------SRYLAEELKPKTNNLQdyrlvavvvhsgslssGHYIAYI---------------KAYENNRWYKFD 287
                          490       500
                   ....*....|....*....|....*....
gi 148746183   895 DTRVSFSSFESVSNvtsffpKDTAYVLFY 923
Cdd:pfam00443  288 DEKVTEVDEETAVL------SSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
442-924 9.49e-28

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: 113.35  E-value: 9.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  442 GLINLGNTCYVNSILQALFMasdfrhcvlrltennsqplmtklqwlfgflehsqrpaispenflsaswtpwfspgTQQDC 521
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS-------------------------------------------------------EQQDA 25
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  522 SEYLKYLLDRLHEEEKTGTRICQKLKQSSspsppeeppapssTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDLSLafp 601
Cdd:cd02257    26 HEFLLFLLDKLHEELKKSSKRTSDSSSLK-------------SLIHDLFGGKLESTIVCLECGHESVSTEPELFLSL--- 89
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  602 ppercrrrrlgsvmrpteditarELPPPtsaqgpgrvgprrqrkhciteDTPPTSLYiegldskeaggqssqeerieree 681
Cdd:cd02257    90 -----------------------PLPVK---------------------GLPQVSLE----------------------- 102
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  682 egkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpdaaipsgertcgsegsrsv 761
Cdd:cd02257       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  762 lDLVNYFLSPEKLTAENRYYCESCaSLQDAEKVVELSQGPCYLILTLLRFSFDlRTMRRRKILDDVSIPLLLRL------ 835
Cdd:cd02257   103 -DCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLspylse 179
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  836 ----PLAGGRGQAYDLCSVVVHSGVSSESGHYYCYAREGaarpaaslgtadrpePENQWYLFNDTRVSFSSFESVSNVTS 911
Cdd:cd02257   180 gekdSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDP---------------SDGKWYKFNDDKVTEVSEEEVLEFGS 244
                         490
                  ....*....|...
gi 148746183  912 FfpKDTAYVLFYR 924
Cdd:cd02257   245 L--SSSAYILFYE 255
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-895 3.15e-24

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 104.81  E-value: 3.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  442 GLINLGNTCYVNSILQALFMASDFRHCVLRL--------------TENNSQPLMTKLQWLFGFLEHSQRPAISPENFLSA 507
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECnstedaelknmppdKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  508 SWtpwFSPGTQQDCSEYLKYLLDRLheEEKTGTRICQKLKQSsspsppeeppapsstsVEKMFGGKIVTRICCLCCLNVS 587
Cdd:cd02668    81 LG---LDTGQQQDAQEFSKLFLSLL--EAKLSKSKNPDLKNI----------------VQDLFRGEYSYVTQCSKCGRES 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  588 SREEAFTDLSLafpppercrrrrlgsvmrpteditarelppptsaqgpgRVGPRRQRKHCITEdtpptslyiegldskea 667
Cdd:cd02668   140 SLPSKFYELEL--------------------------------------QLKGHKTLEECIDE----------------- 164
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  668 ggqssqeeriereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpdaaip 747
Cdd:cd02668       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  748 sgertcgsegsrsvldlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDV 827
Cdd:cd02668   165 --------------------FLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASI 224
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148746183  828 SIPLLLRLP--LAGGRGQ--AYDLCSVVVHSGVSSESGHYYCYAREgaarpaaslgtadrpEPENQWYLFND 895
Cdd:cd02668   225 SFPEILDMGeyLAESDEGsyVYELSGVLIHQGVSAYSGHYIAHIKD---------------EQTGEWYKFND 281
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-923 2.47e-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: 86.98  E-value: 2.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  442 GLINLGNTCYVNSILQALFMASdfrhcvlrltennsqpLMTKLQWLFGFLEHSQRP--AISPENFLSASWT--PWFSPGT 517
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYFEN----------------LLTCLKDLFESISEQKKRtgVISPKKFITRLKRenELFDNYM 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  518 QQDCSEYLKYLLDRLHEE-EKTgtricQKLKQSSSPSPPEEPPAPSSTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDL 596
Cdd:cd02663    65 HQDAHEFLNFLLNEIAEIlDAE-----RKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  597 SLafpppercrrrrlgsvmrpteditarELPPPTSAQgpgrvgprrqrkHCItedtpptslyiegldskeaggqssqeer 676
Cdd:cd02663   140 SI--------------------------DVEQNTSIT------------SCL---------------------------- 153
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  677 iereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpdaaipsgertcgse 756
Cdd:cd02663       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  757 gsRSvldlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVSIPLLLRLP 836
Cdd:cd02663   154 --RQ-------FSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLF 224
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  837 LAGGRG----QAYDLCSVVVHSGVSSESGHYYCYAREGaarpaaslgtadrpepeNQWYLFNDtrvSFSSFESVSNVTSF 912
Cdd:cd02663   225 NTTDDAenpdRLYELVAVVVHIGGGPNHGHYVSIVKSH-----------------GGWLLFDD---ETVEKIDENAVEEF 284
                         490
                  ....*....|....*
gi 148746183  913 F----PKDTAYVLFY 923
Cdd:cd02663   285 FgdspNQATAYVLFY 299
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-923 1.93e-16

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 81.17  E-value: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  442 GLINLGNTCYVNSILQAL--------FMASdFRH---------CVLRLTENNSQplmtklqwlfGFLEhSQRPAISPENF 504
Cdd:cd02661     3 GLQNLGNTCFLNSVLQCLthtpplanYLLS-REHskdccnegfCMMCALEAHVE----------RALA-SSGPGSAPRIF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  505 LSA--SWTPWFSPGTQQDCSEYLKYLLDRLHeeeKTGTRICQKLKQSSSPSPPEeppapssTSVEKMFGGKIVTRICCLC 582
Cdd:cd02661    71 SSNlkQISKHFRIGRQEDAHEFLRYLLDAMQ---KACLDRFKKLKAVDPSSQET-------TLVQQIFGGYLRSQVKCLN 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  583 CLNVSSREEAFTDLSLafpppercrrrrlgsvmrpteDItarelppptsaqgpgrvgprrqrkhcitedtpptslyiegl 662
Cdd:cd02661   141 CKHVSNTYDPFLDLSL---------------------DI----------------------------------------- 158
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  663 dskeaggqssqeeriereeegkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthp 742
Cdd:cd02661       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  743 daaipsgertcgsEGSRSVLDLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDlrtmRRRK 822
Cdd:cd02661   159 -------------KGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNF----RGGK 221
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  823 ILDDVSIPLLLRL-PL---AGGRGQAYDLCSVVVHSGVSSESGHYYCYARegaarpaASLGtadrpepenQWYLFNDTRV 898
Cdd:cd02661   222 INKQISFPETLDLsPYmsqPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVK-------SSNG---------KWYNMDDSKV 285
                         490       500
                  ....*....|....*....|....*
gi 148746183  899 SFSSFESVSNvtsffpkDTAYVLFY 923
Cdd:cd02661   286 SPVSIETVLS-------QKAYILFY 303
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-924 6.87e-16

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 78.10  E-value: 6.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  442 GLINLGNTCYVNSILQALFmasdfrhcvlrltennsqplmtklqwlfgflehsqrpaispenflsaswtpwfspGTQQDC 521
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLS-------------------------------------------------------ADQQDA 25
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  522 SEYLKYLLDRLHeeektgtRIcqklkqssspsppeeppapsstsVEKMFGGKIVTRICCLCCLNVSSREEAFTDLSLAfp 601
Cdd:cd02674    26 QEFLLFLLDGLH-------SI-----------------------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLP-- 73
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  602 ppercrrrrLGSVMRPTEDITArelppptsaqgpgrvgprrqrKHCITEdtpptslyiegldskeaggqssqeerieree 681
Cdd:cd02674    74 ---------IPSGSGDAPKVTL---------------------EDCLRL------------------------------- 92
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  682 egkeertekeevgeeeestrgegerekeeeveeeeekveketekeaeqekeedslgagthpdaaipsgertcgsegsrsv 761
Cdd:cd02674       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  762 ldlvnyFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDlrTMRRRKILDDVSIPL--LLRLPLAG 839
Cdd:cd02674    93 ------FTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPLndLDLTPYVD 164
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  840 GRGQA----YDLCsVVVHSGVSSESGHYYCYARegaarpaaslgtadRPEPeNQWYLFNDTRvsfssfesvsnVTSFFP- 914
Cdd:cd02674   165 TRSFTgpfkYDLY-AVVNHYGSLNGGHYTAYCK--------------NNET-NDWYKFDDSR-----------VTKVSEs 217
                         490
                  ....*....|...
gi 148746183  915 ---KDTAYVLFYR 924
Cdd:cd02674   218 svvSSSAYILFYE 230
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
763-926 1.62e-14

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 78.39  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  763 DLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRtmRRRKILDDVSIPlLLRLPLAGGRG 842
Cdd:COG5560   679 DCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRS--FRDKIDDLVEYP-IDDLDLSGVEY 755
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  843 Q------AYDLcSVVVHSGVSSESGHYYCYAREGAarpaaslgtadrpepENQWYLFNDTRvsfssfesvsnVTSFFPKD 916
Cdd:COG5560   756 MvddprlIYDL-YAVDNHYGGLSGGHYTAYARNFA---------------NNGWYLFDDSR-----------ITEVDPED 808
                         170
                  ....*....|....
gi 148746183  917 T----AYVLFYRQR 926
Cdd:COG5560   809 SvtssAYVLFYRRK 822
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-598 1.16e-13

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 73.18  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  442 GLINLGNTCYVNSILQAL--------FMASDFRHC-VLRLTENNSQPL-MTKLQWLFGFLEHSQrpAISPENFLSASWTP 511
Cdd:cd02660     2 GLINLGATCFMNVILQALlhnpllrnYFLSDRHSCtCLSCSPNSCLSCaMDEIFQEFYYSGDRS--PYGPINLLYLSWKH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  512 WFSPGT--QQDCSEYLKYLLDRLHEEEKTGTRICQKLKQSSSPsppeeppapsstsVEKMFGGKIVTRICCLCCLNVSSR 589
Cdd:cd02660    80 SRNLAGysQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCI-------------IHQTFSGSLQSSVTCQRCGGVSTT 146

                  ....*....
gi 148746183  590 EEAFTDLSL 598
Cdd:cd02660   147 VDPFLDLSL 155
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-598 2.58e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 68.89  E-value: 2.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  442 GLINLGNTCYVNSILQALF-----------MASDFRHCVLRLTEN-NSQplMTKLqwLFGFLEH----------SQRP-- 497
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFsipsfqwryddLENKFPSDVVDPANDlNCQ--LIKL--ADGLLSGryskpaslksENDPyq 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  498 -AISPENF--LSASWTPWFSPGTQQDCSEYLKYLLDRLHEEEKTgtricqklkqssspsppeeppaPSSTSVEKMFGGKI 574
Cdd:cd02658    77 vGIKPSMFkaLIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFK----------------------NLGLNPNDLFKFMI 134
                         170       180
                  ....*....|....*....|....
gi 148746183  575 VTRICCLCCLNVSSREEAFTDLSL 598
Cdd:cd02658   135 EDRLECLSCKKVKYTSELSEILSL 158
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-598 5.29e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 67.41  E-value: 5.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  442 GLINLGNTCYVNSILQALFmASDFRHCVLRLTennsqplmtklqwlfgflehsqrpaisPENFLS--ASWTPWFSPGTQQ 519
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLS-QTPALRELLSET---------------------------PKELFSqvCRKAPQFKGYQQQ 52
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148746183  520 DCSEYLKYLLDRLheeektgtricqklkqssspsppeeppapsSTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDLSL 598
Cdd:cd02667    53 DSHELLRYLLDGL------------------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSL 101
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
434-598 5.57e-12

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 70.28  E-value: 5.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  434 AKSDTGKIGLINLGNTCYVNSILQALFMASDFRHCVLRLTENNSQP---LMTKLQWLFGFLEHSQRPAISPENFLSASWT 510
Cdd:COG5077   187 SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGrdsVALALQRLFYNLQTGEEPVDTTELTRSFGWD 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  511 PwFSPGTQQDCSEYLKYLLDRLhEEEKTGTRicqklkqssspsppeeppapsstsVEKMFGGKIVTRICCLC-CLNV--- 586
Cdd:COG5077   267 S-DDSFMQHDIQEFNRVLQDNL-EKSMRGTV------------------------VENALNGIFVGKMKSYIkCVNVnye 320
                         170
                  ....*....|..
gi 148746183  587 SSREEAFTDLSL 598
Cdd:COG5077   321 SARVEDFWDIQL 332
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
441-598 1.51e-11

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 66.84  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  441 IGLINLGNTCYVNSILQALFMASDFRHCVLRLTENNSQplMTKLQWLFGFLE---HSQRPAISPENFLSA--SWTPWFSP 515
Cdd:cd02671    25 VGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISS--VEQLQSSFLLNPekyNDELANQAPRRLLNAlrEVNPMYEG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  516 GTQQDCSEYLKYLLDRLHEeektgtricqklkqssspsppeeppapsstSVEKMFGGKIVTRICCLCCLNVSSREEAFTD 595
Cdd:cd02671   103 YLQHDAQEVLQCILGNIQE------------------------------LVEKDFQGQLVLRTRCLECETFTERREDFQD 152

                  ...
gi 148746183  596 LSL 598
Cdd:cd02671   153 ISV 155
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-581 1.11e-07

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 54.64  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  442 GLINLGNTCYVNSILQALFMASDFRHCVLRLTEN------NSQPLMTKLQWLFGFLEHSQRPaISPENFLSASWT--PWF 513
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPArrganqSSDNLTNALRDLFDTMDKKQEP-VPPIEFLQLLRMafPQF 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148746183  514 SPGT------QQDCSEYLKYLLdrlheeektgTRICQKLKqssspsppeePPAPSSTSVEKMFGGKIVTRICCL 581
Cdd:cd02657    80 AEKQnqggyaQQDAEECWSQLL----------SVLSQKLP----------GAGSKGSFIDQLFGIELETKMKCT 133
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-599 2.00e-05

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 46.98  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  442 GLINLGNTCYVNSILQALfmASdfrhcvlrltennsqplmtkLQWLFGFLehsqrpaispENFLSaswtpwfspgtQQDC 521
Cdd:cd02662     1 GLVNLGNTCFMNSVLQAL--AS--------------------LPSLIEYL----------EEFLE-----------QQDA 37
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148746183  522 SEYLKYLLDRLHeeektgtricQKLKQSsspsppeeppapsstsvekmFGGKIVTRICCLCCLNVSS-REEAFTDLSLA 599
Cdd:cd02662    38 HELFQVLLETLE----------QLLKFP--------------------FDGLLASRIVCLQCGESSKvRYESFTMLSLP 86
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
441-539 2.74e-05

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 47.49  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  441 IGLINLGNTCYVNSILQALFMASDFRHCVLRLTENN-------------------------SQPLMTKLQWLFGFLEHSQ 495
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKaelasdypterriggrevsrselqrSNQFVYELRSLFNDLIHSN 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 148746183  496 RPAISPENFLSaswtpwFSPGTQQDCSEYLKYLLDRLHEEEKTG 539
Cdd:cd02666    82 TRSVTPSKELA------YLALRQQDVTECIDNVLFQLEVALEPI 119
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
442-532 3.51e-05

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 46.72  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  442 GLINLGNTCYVNSILQALFMASD----------FRHCVLRLTENNSQPLMTKLQWLFGFlehsqrPAISPENFLSASWTP 511
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILALYLPkldellddlsKELKVLKNVIRKPEPDLNQEEALKLF------TALWSSKEHKVGWIP 74
                          90       100
                  ....*....|....*....|.
gi 148746183  512 wfSPGTQQDCSEYLKYLLDRL 532
Cdd:COG5533    75 --PMGSQEDAHELLGKLLDEL 93
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
760-896 1.71e-03

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 41.20  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  760 SVLDLVNYFLSPEKLtaENrYYCESCASLqdaekvveLSQGPCYLILTLLRFSFDLR-TMRRRKIldDVSIPLLLRLPLa 838
Cdd:cd02662    97 TLEHCLDDFLSTEII--DD-YKCDRCQTV--------IVRLPQILCIHLSRSVFDGRgTSTKNSC--KVSFPERLPKVL- 162
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148746183  839 ggrgqaYDLCSVvVHSGVSSESGHYYCYAR-----EGAARPAASLGTADRPEPENQWYLFNDT 896
Cdd:cd02662   163 ------YRLRAV-VVHYGSHSSGHYVCYRRkplfsKDKEPGSFVRMREGPSSTSHPWWRISDT 218
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
439-533 3.21e-03

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 41.15  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148746183  439 GKIGLINLGNTCYVNSILQALFMASDFR-HCVL----RLTENNSQPLMTKLQWLFGFLEHSQ--RPAISPENFLSA---- 507
Cdd:cd02669   118 GFVGLNNIKNNDYANVIIQALSHVKPIRnFFLLyenyENIKDRKSELVKRLSELIRKIWNPRnfKGHVSPHELLQAvskv 197
                          90       100
                  ....*....|....*....|....*.
gi 148746183  508 SWTPwFSPGTQQDCSEYLKYLLDRLH 533
Cdd:cd02669   198 SKKK-FSITEQSDPVEFLSWLLNTLH 222
COG1365 COG1365
Predicted ATPase, PP-loop superfamily [General function prediction only];
55-97 9.61e-03

Predicted ATPase, PP-loop superfamily [General function prediction only];


Pssm-ID: 440976  Cd Length: 256  Bit Score: 38.88  E-value: 9.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 148746183   55 ELPRRVGCQLLHVAGRHHPDVfaEFFSARRVLRLLQGGAGPPG 97
Cdd:COG1365   207 ELSMKYGCPLLREAHKRHPSL--RKFSIQRVLREVRAGVLEPG 247
 
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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