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Conserved domains on  [gi|119579811|gb|EAW59407|]
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ubiquitin specific peptidase 9, X-linked, isoform CRA_b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1380-1783 5.60e-154

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: 479.83  E-value: 5.60e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1380 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIegtgsdvdddmsgdekqdnesnvdprddvfgypqqfedkpalsKTE 1459
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------------------------------------------PPT 37

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1460 DRKEYNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAMLSKVL 1539
Cdd:cd02659    38 EDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLF 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1540 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLA 1619
Cdd:cd02659   118 GGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLT 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1620 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDnvnpesqliqqseqSESETAGSTKYRLVGVLVHSGQ 1699
Cdd:cd02659   198 LQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKEGD--------------SEKKDSESYIYELHGVLVHSGD 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1700 ASGGHYYSYIIQRNGGdgernRWYKFDDGDVTECKMDDDEEmknQCFGGEYMGEVFDHMmkrmsYRRQKRWWNAYILFYE 1779
Cdd:cd02659   264 AHGGHYYSYIKDRDDG-----KWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYE 330


                  ....
gi 119579811 1780 RMDT 1783
Cdd:cd02659   331 RKSP 334
DUF3517 pfam12030
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ...
 1922-2301 4.31e-104

Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 340 amino acids in length. This domain is found associated with pfam00443.


:

Pssm-ID: 463438  Cd Length: 407  Bit Score: 340.43  E-value: 4.31e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1922 SNRFSEYLLECPSAEVRGAFAKLIVFIAH-----FSLQDGPCPspfaspgPSSQAYDNLSLSDHLLRAVLNLLRR---EV 1993
Cdd:pfam12030    1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCD-------PDDLEEEWRSLSDSVLEAVVALLDHlwkEF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1994 SEHGRHLQQYFNLFVMYANLGVAEKTQLLKLS-VPATFMLVSLDEGPGPPIKYQYAEL------------GKLYSVVSQL 2060
Cdd:pfam12030   74 HTHLRSWDEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARMlrlvekrrppsyEKLIQLLSVL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  2061 IRCCNVSSRMQSSINGNPPLPNpfgdpNLSQPIMPIQQNVADIL--FVRT---SYVKKIIEDCSNSEETVKLLRFCCWEN 2135
Cdd:pfam12030  154 LRCCDLSLPPQSINEGAEPLPN-----SLPDGPFPLTSEEADLLrpLGRTngsIFVKKLLEIDQNPEATRKILRFLLWEN 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  2136 PQFSSTVLSELLWQVAYSYTYELR-PYLDLLLQILliEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIK 2214
Cdd:pfam12030  229 PELSDSILKTLLWGIRGAPAHLLRdPFLRAAIVFC--EDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQCIN 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  2215 CMvALFSNCPVAYQILQgngdlkrkwtwavewlgdelerrpytgnpqyTYNNWSPPVQSNETSN---------------- 2278
Cdd:pfam12030  307 CR-LGFDKEWFASQVLE-------------------------------NIPDWAPPLLSYPDSNvrsetedflqeelfsh 354

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 119579811  2279 ---------------------------GYFLERS---HSARMTLAKACELCPE 2301
Cdd:pfam12030  355 emgpdpqfrlreaarrlgiacleylrgTYVLRRSqveRSAVETLQRVIELCPE 407
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
 725-789 1.04e-05

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd17065:

Pssm-ID: 475130  Cd Length: 79  Bit Score: 45.38  E-value: 1.04e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119579811  725 DDLEVWSHTNDTIGSVRRCILNRIKANVAHtkIELFVGGELIDPADDRKLIGQLNLKDKSLITAK 789
Cdd:cd17065    17 QEFTLEVHSNETLGSVRQKIAERLNCPVDQ--VQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
 
Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1380-1783 5.60e-154

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: 479.83  E-value: 5.60e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1380 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIegtgsdvdddmsgdekqdnesnvdprddvfgypqqfedkpalsKTE 1459
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------------------------------------------PPT 37

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1460 DRKEYNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAMLSKVL 1539
Cdd:cd02659    38 EDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLF 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1540 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLA 1619
Cdd:cd02659   118 GGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLT 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1620 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDnvnpesqliqqseqSESETAGSTKYRLVGVLVHSGQ 1699
Cdd:cd02659   198 LQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKEGD--------------SEKKDSESYIYELHGVLVHSGD 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1700 ASGGHYYSYIIQRNGGdgernRWYKFDDGDVTECKMDDDEEmknQCFGGEYMGEVFDHMmkrmsYRRQKRWWNAYILFYE 1779
Cdd:cd02659   264 AHGGHYYSYIKDRDDG-----KWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYE 330


                  ....
gi 119579811 1780 RMDT 1783
Cdd:cd02659   331 RKSP 334
DUF3517 pfam12030
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ...
 1922-2301 4.31e-104

Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 340 amino acids in length. This domain is found associated with pfam00443.


Pssm-ID: 463438  Cd Length: 407  Bit Score: 340.43  E-value: 4.31e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1922 SNRFSEYLLECPSAEVRGAFAKLIVFIAH-----FSLQDGPCPspfaspgPSSQAYDNLSLSDHLLRAVLNLLRR---EV 1993
Cdd:pfam12030    1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCD-------PDDLEEEWRSLSDSVLEAVVALLDHlwkEF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1994 SEHGRHLQQYFNLFVMYANLGVAEKTQLLKLS-VPATFMLVSLDEGPGPPIKYQYAEL------------GKLYSVVSQL 2060
Cdd:pfam12030   74 HTHLRSWDEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARMlrlvekrrppsyEKLIQLLSVL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  2061 IRCCNVSSRMQSSINGNPPLPNpfgdpNLSQPIMPIQQNVADIL--FVRT---SYVKKIIEDCSNSEETVKLLRFCCWEN 2135
Cdd:pfam12030  154 LRCCDLSLPPQSINEGAEPLPN-----SLPDGPFPLTSEEADLLrpLGRTngsIFVKKLLEIDQNPEATRKILRFLLWEN 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  2136 PQFSSTVLSELLWQVAYSYTYELR-PYLDLLLQILliEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIK 2214
Cdd:pfam12030  229 PELSDSILKTLLWGIRGAPAHLLRdPFLRAAIVFC--EDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQCIN 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  2215 CMvALFSNCPVAYQILQgngdlkrkwtwavewlgdelerrpytgnpqyTYNNWSPPVQSNETSN---------------- 2278
Cdd:pfam12030  307 CR-LGFDKEWFASQVLE-------------------------------NIPDWAPPLLSYPDSNvrsetedflqeelfsh 354

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 119579811  2279 ---------------------------GYFLERS---HSARMTLAKACELCPE 2301
Cdd:pfam12030  355 emgpdpqfrlreaarrlgiacleylrgTYVLRRSqveRSAVETLQRVIELCPE 407
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1382-1778 3.90e-79

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 264.69  E-value: 3.90e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1382 VGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDvdddmsgdekqdnesnvdprddvfgypqqfedkpalskteDR 1461
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSED----------------------------------------SR 40

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1462 KEYNIGVLRHLQVIFGHLA-ASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKA---LGHPAMLSK 1537
Cdd:pfam00443   41 YNKDINLLCALRDLFKALQkNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITD 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1538 VLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLL------DSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLI 1611
Cdd:pfam00443  121 LFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKI 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1612 KKLPPVLAIQLKRFDYDweRECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDNVnpesqliqqseqsesetagstKYRLV 1691
Cdd:pfam00443  201 SRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ---------------------DYRLV 257

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1692 GVLVHSGQASGGHYYSYIIQrnggdGERNRWYKFDDGDVTECKMDDDEEMknqcfggeymgevfdhmmkrmsyrrqkrwW 1771
Cdd:pfam00443  258 AVVVHSGSLSSGHYIAYIKA-----YENNRWYKFDDEKVTEVDEETAVLS-----------------------------S 303


                   ....*..
gi 119579811  1772 NAYILFY 1778
Cdd:pfam00443  304 SAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 1380-1826 5.66e-49

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 192.01  E-value: 5.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1380 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEgtgsdvdddmsgdekQDNEsnvDPRDDV-------FgYPQQFEDK 1452
Cdd:COG5077   192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP---------------TDHP---RGRDSValalqrlF-YNLQTGEE 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1453 PaLSKTEdrkeynigvlrhLQVIFGhlaasrlqyyvprgfwkqfrlWGEPVNLReQHDALEFFNSLVDSLDEALKALGHP 1532
Cdd:COG5077   253 P-VDTTE------------LTRSFG---------------------WDSDDSFM-QHDIQEFNRVLQDNLEKSMRGTVVE 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1533 AMLSKVLGGSFadqKICQGCPHR-YECE--ESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKcNKKVDTVKRL 1609
Cdd:COG5077   298 NALNGIFVGKM---KSYIKCVNVnYESArvEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGV 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1610 LIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDMEPYtvagvaklegdnVNPESqliQQSEQSESEtagstkYR 1689
Cdd:COG5077   374 IFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPF------------LDRDA---DKSENSDAV------YV 432

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1690 LVGVLVHSGQASGGHYYSYIiqRNGGDGernRWYKFDDGDVTECKMdddEEMKNQCFGGEYMGEVfdhmmKRMSYRRQKR 1769
Cdd:COG5077   433 LYGVLVHSGDLHEGHYYALL--KPEKDG---RWYKFDDTRVTRATE---KEVLEENFGGDHPYKD-----KIRDHSGIKR 499

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119579811 1770 WWNAYILFYERMdtiDQDDELIRYISELAITTRPHQIIMPSAIERSVRKQNVQFMHN 1826
Cdd:COG5077   500 FMSAYMLVYLRK---SMLDDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHL 553
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
 725-789 1.04e-05

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; UBP24 (EC 3.4.19.12), also termed deubiquitinating enzyme 24, or ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24 (USP24), is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain, a ubiquitin-like (Ubl) domain, and a C-terminal peptidase C19 domain.


Pssm-ID: 340585  Cd Length: 79  Bit Score: 45.38  E-value: 1.04e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119579811  725 DDLEVWSHTNDTIGSVRRCILNRIKANVAHtkIELFVGGELIDPADDRKLIGQLNLKDKSLITAK 789
Cdd:cd17065    17 QEFTLEVHSNETLGSVRQKIAERLNCPVDQ--VQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
 
Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1380-1783 5.60e-154

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: 479.83  E-value: 5.60e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1380 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIegtgsdvdddmsgdekqdnesnvdprddvfgypqqfedkpalsKTE 1459
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------------------------------------------PPT 37

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1460 DRKEYNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAMLSKVL 1539
Cdd:cd02659    38 EDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLF 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1540 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLA 1619
Cdd:cd02659   118 GGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLT 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1620 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDnvnpesqliqqseqSESETAGSTKYRLVGVLVHSGQ 1699
Cdd:cd02659   198 LQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKEGD--------------SEKKDSESYIYELHGVLVHSGD 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1700 ASGGHYYSYIIQRNGGdgernRWYKFDDGDVTECKMDDDEEmknQCFGGEYMGEVFDHMmkrmsYRRQKRWWNAYILFYE 1779
Cdd:cd02659   264 AHGGHYYSYIKDRDDG-----KWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYE 330


                  ....
gi 119579811 1780 RMDT 1783
Cdd:cd02659   331 RKSP 334
DUF3517 pfam12030
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ...
 1922-2301 4.31e-104

Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 340 amino acids in length. This domain is found associated with pfam00443.


Pssm-ID: 463438  Cd Length: 407  Bit Score: 340.43  E-value: 4.31e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1922 SNRFSEYLLECPSAEVRGAFAKLIVFIAH-----FSLQDGPCPspfaspgPSSQAYDNLSLSDHLLRAVLNLLRR---EV 1993
Cdd:pfam12030    1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCD-------PDDLEEEWRSLSDSVLEAVVALLDHlwkEF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1994 SEHGRHLQQYFNLFVMYANLGVAEKTQLLKLS-VPATFMLVSLDEGPGPPIKYQYAEL------------GKLYSVVSQL 2060
Cdd:pfam12030   74 HTHLRSWDEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARMlrlvekrrppsyEKLIQLLSVL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  2061 IRCCNVSSRMQSSINGNPPLPNpfgdpNLSQPIMPIQQNVADIL--FVRT---SYVKKIIEDCSNSEETVKLLRFCCWEN 2135
Cdd:pfam12030  154 LRCCDLSLPPQSINEGAEPLPN-----SLPDGPFPLTSEEADLLrpLGRTngsIFVKKLLEIDQNPEATRKILRFLLWEN 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  2136 PQFSSTVLSELLWQVAYSYTYELR-PYLDLLLQILliEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIK 2214
Cdd:pfam12030  229 PELSDSILKTLLWGIRGAPAHLLRdPFLRAAIVFC--EDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQCIN 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  2215 CMvALFSNCPVAYQILQgngdlkrkwtwavewlgdelerrpytgnpqyTYNNWSPPVQSNETSN---------------- 2278
Cdd:pfam12030  307 CR-LGFDKEWFASQVLE-------------------------------NIPDWAPPLLSYPDSNvrsetedflqeelfsh 354

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 119579811  2279 ---------------------------GYFLERS---HSARMTLAKACELCPE 2301
Cdd:pfam12030  355 emgpdpqfrlreaarrlgiacleylrgTYVLRRSqveRSAVETLQRVIELCPE 407
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1382-1778 3.90e-79

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 264.69  E-value: 3.90e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1382 VGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDvdddmsgdekqdnesnvdprddvfgypqqfedkpalskteDR 1461
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSED----------------------------------------SR 40

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1462 KEYNIGVLRHLQVIFGHLA-ASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKA---LGHPAMLSK 1537
Cdd:pfam00443   41 YNKDINLLCALRDLFKALQkNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITD 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1538 VLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLL------DSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLI 1611
Cdd:pfam00443  121 LFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKI 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1612 KKLPPVLAIQLKRFDYDweRECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDNVnpesqliqqseqsesetagstKYRLV 1691
Cdd:pfam00443  201 SRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ---------------------DYRLV 257

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1692 GVLVHSGQASGGHYYSYIIQrnggdGERNRWYKFDDGDVTECKMDDDEEMknqcfggeymgevfdhmmkrmsyrrqkrwW 1771
Cdd:pfam00443  258 AVVVHSGSLSSGHYIAYIKA-----YENNRWYKFDDEKVTEVDEETAVLS-----------------------------S 303


                   ....*..
gi 119579811  1772 NAYILFY 1778
Cdd:pfam00443  304 SAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 1505-1779 1.21e-54

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: 191.93  E-value: 1.21e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1505 LREQHDALEFFNSLVDSLDEALKALG--------HPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDI----RNH 1572
Cdd:cd02257    19 FSEQQDAHEFLLFLLDKLHEELKKSSkrtsdsssLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1573 QNLLDSLEQYVKGDLLEGANAYHCEKCnKKVDTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPY 1652
Cdd:cd02257    99 VSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPY 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1653 TVAGVAKLEGDNvnpesqliqqseqsesetaGSTKYRLVGVLVHSGQ-ASGGHYYSYIIqrnggDGERNRWYKFDDGDVT 1731
Cdd:cd02257   177 LSEGEKDSDSDN-------------------GSYKYELVAVVVHSGTsADSGHYVAYVK-----DPSDGKWYKFNDDKVT 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 119579811 1732 ECKMDDDEEMKNqcfggeymgevfdhmmkrmsyrrqkRWWNAYILFYE 1779
Cdd:cd02257   233 EVSEEEVLEFGS-------------------------LSSSAYILFYE 255
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1383-1779 6.53e-52

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: 186.86  E-value: 6.53e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1383 GLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSGDekQDNESNvdprddvfgypqqfedkpalsktedrk 1462
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPD--KPHEPQ--------------------------- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1463 eyniGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLwgepvNLREQHDALEFFNSLVDSLDEALKALGHP---AMLSKVL 1539
Cdd:cd02668    52 ----TIIDQLQLIFAQLQFGNRSVVDPSGFVKALGL-----DTGQQQDAQEFSKLFLSLLEAKLSKSKNPdlkNIVQDLF 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1540 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLA 1619
Cdd:cd02668   123 RGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLN 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1620 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVagvaklegdnvnpesqliqqsEQSEsetaGSTKYRLVGVLVHSGQ 1699
Cdd:cd02668   203 FQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLA---------------------ESDE----GSYVYELSGVLIHQGV 257

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1700 -ASGGHYYSYIiqrngGDGERNRWYKFDDGDVTE-----CKMDDDEEMKNQCFGgeymgevfDHMMKRMSYRrqkrwwNA 1773
Cdd:cd02668   258 sAYSGHYIAHI-----KDEQTGEWYKFNDEDVEEmpgkpLKLGNSEDPAKPRKS--------EIKKGTHSSR------TA 318


                  ....*.
gi 119579811 1774 YILFYE 1779
Cdd:cd02668   319 YMLVYK 324
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 1380-1826 5.66e-49

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 192.01  E-value: 5.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1380 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEgtgsdvdddmsgdekQDNEsnvDPRDDV-------FgYPQQFEDK 1452
Cdd:COG5077   192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP---------------TDHP---RGRDSValalqrlF-YNLQTGEE 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1453 PaLSKTEdrkeynigvlrhLQVIFGhlaasrlqyyvprgfwkqfrlWGEPVNLReQHDALEFFNSLVDSLDEALKALGHP 1532
Cdd:COG5077   253 P-VDTTE------------LTRSFG---------------------WDSDDSFM-QHDIQEFNRVLQDNLEKSMRGTVVE 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1533 AMLSKVLGGSFadqKICQGCPHR-YECE--ESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKcNKKVDTVKRL 1609
Cdd:COG5077   298 NALNGIFVGKM---KSYIKCVNVnYESArvEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGV 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1610 LIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDMEPYtvagvaklegdnVNPESqliQQSEQSESEtagstkYR 1689
Cdd:COG5077   374 IFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPF------------LDRDA---DKSENSDAV------YV 432

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1690 LVGVLVHSGQASGGHYYSYIiqRNGGDGernRWYKFDDGDVTECKMdddEEMKNQCFGGEYMGEVfdhmmKRMSYRRQKR 1769
Cdd:COG5077   433 LYGVLVHSGDLHEGHYYALL--KPEKDG---RWYKFDDTRVTRATE---KEVLEENFGGDHPYKD-----KIRDHSGIKR 499

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119579811 1770 WWNAYILFYERMdtiDQDDELIRYISELAITTRPHQIIMPSAIERSVRKQNVQFMHN 1826
Cdd:COG5077   500 FMSAYMLVYLRK---SMLDDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHL 553
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1383-1737 8.76e-44

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: 162.45  E-value: 8.76e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1383 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEKQDNESNvdprddvfgypqqfedkpalsktedrk 1462
Cdd:cd02661     3 GLQNLGNTCFLNSVLQCLTHTPPLANYLL-------------SREHSKDCCNE--------------------------- 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1463 eyNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEA-------LKALGHPA-- 1533
Cdd:cd02661    43 --GFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKAcldrfkkLKAVDPSSqe 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1534 --MLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLI 1611
Cdd:cd02661   121 ttLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTI 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1612 KKLPPVLAIQLKRFDYDWERecaiKFNDYFEFPRELDMEPYTVagvaklegdnvnpesqliqqseqseSETAGSTKYRLV 1691
Cdd:cd02661   201 HRAPNVLTIHLKRFSNFRGG----KINKQISFPETLDLSPYMS-------------------------QPNDGPLKYKLY 251

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 119579811 1692 GVLVHSG-QASGGHYYSYIIQRNGgdgernRWYKFDDGDVTECKMDD 1737
Cdd:cd02661   252 AVLVHSGfSPHSGHYYCYVKSSNG------KWYNMDDSKVSPVSIET 292
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1507-1779 6.69e-38

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: 142.81  E-value: 6.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1507 EQHDALEFFNSLVDSLDealkalghpAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDI------RNHQNLLDSLE 1580
Cdd:cd02674    21 DQQDAQEFLLFLLDGLH---------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLEDCLR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1581 QYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDweRECAIKFNDYFEFP-RELDMEPYTVAgvak 1659
Cdd:cd02674    92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPlNDLDLTPYVDT---- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1660 legdnvnpesqliqqseqseSETAGSTKYRLVGVLVHSGQASGGHYYSYIiqrngGDGERNRWYKFDDGDVTecKMDDDE 1739
Cdd:cd02674   166 --------------------RSFTGPFKYDLYAVVNHYGSLNGGHYTAYC-----KNNETNDWYKFDDSRVT--KVSESS 218

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 119579811 1740 EMKNqcfggeymgevfdhmmkrmsyrrqkrwwNAYILFYE 1779
Cdd:cd02674   219 VVSS----------------------------SAYILFYE 230
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1383-1732 4.74e-35

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 137.89  E-value: 4.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1383 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgSDvDDDMSGDEKQDNESNVDPRDDVFgypQQFedkpalSKTEDRK 1462
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFL------SD-RHSCTCLSCSPNSCLSCAMDEIF---QEF------YYSGDRS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1463 EYnigvlrhlqvifghlAASRLQYyvprGFWKQFRlwgepvNL--REQHDALEFFNSLVDSLDE-ALKALGHPAMLS--- 1536
Cdd:cd02660    66 PY---------------GPINLLY----LSWKHSR------NLagYSQQDAHEFFQFLLDQLHThYGGDKNEANDEShcn 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1537 ----KVLGGSFADQKICQGCPHRYECEESFTTLNVDIRN---------------HQNLLDSLEQYVKGDLLeGANAYHCE 1597
Cdd:cd02660   121 ciihQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNkstpswalgesgvsgTPTLSDCLDRFTRPEKL-GDFAYKCS 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1598 KCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPYTVAGvaklegdnvnpesqliQQSEQ 1677
Cdd:cd02660   200 GCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-LNKTSRKIDTYVQFPLELNMTPYTSSS----------------IGDTQ 262

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119579811 1678 SESETAGSTKYRLVGVLVHSGQASGGHYYSYIIQRNGgdgernRWYKFDDGDVTE 1732
Cdd:cd02660   263 DSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDG------QWFKFDDAMITR 311
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1383-1743 4.44e-32

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 129.15  E-value: 4.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1383 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEKQDNESNVdprddvfgypqqfedkpalsktedrk 1462
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVL-------------SLNLPRLGDSQS-------------------------- 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1463 eynigVLRHLQVIFGHLAASRLQYY-VPRGFWKQfrLWGEPVNLREQHDALEFFNSLVDSLDealkalghpAMLSKVLGG 1541
Cdd:cd02664    42 -----VMKKLQLLQAHLMHTQRRAEaPPDYFLEA--SRPPWFTPGSQQDCSEYLRYLLDRLH---------TLIEKMFGG 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1542 SFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDsleQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQ 1621
Cdd:cd02664   106 KLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDLLN---YFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILT 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1622 LKRFDYDWERECAIKFNDYFEFPRELDMePYTVAgvaklegdNVNPESQLIQQSEQSESETAGSTK---YRLVGVLVHSG 1698
Cdd:cd02664   183 LLRFSYDQKTHVREKIMDNVSINEVLSL-PVRVE--------SKSSESPLEKKEEESGDDGELVTRqvhYRLYAVVVHSG 253

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119579811 1699 QAS-GGHYYSYIIQRNGGDG---------------ERNRWYKFDDGDVTECKMdddEEMKN 1743
Cdd:cd02664   254 YSSeSGHYFTYARDQTDADStgqecpepkdaeendESKNWYLFNDSRVTFSSF---ESVQN 311
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1508-1779 1.52e-27

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: 114.79  E-value: 1.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1508 QHDALEFFNSLVDSLDEALKalghpamlsKVLGGSFADQKICQGCPHRYECEESFTTLN----VDIRNHQNLLDSLEQYV 1583
Cdd:cd02667    51 QQDSHELLRYLLDGLRTFID---------SIFGGELTSTIMCESCGTVSLVYEPFLDLSlprsDEIKSECSIESCLKQFT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1584 KGDLLEGANAYHCEKCNKkvdTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPYTvagvaklegd 1663
Cdd:cd02667   122 EVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPFC---------- 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1664 nvnpesqliqQSEQSESETAGSTKYRLVGVLVHSGQASGGHYYSYI----------------IQRNGGDGERNRWYKFDD 1727
Cdd:cd02667   188 ----------DPKCNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVkvrppqqrlsdltkskPAADEAGPGSGQWYYISD 257

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119579811 1728 GDVTEckMDDDEEMKNQcfggeymgevfdhmmkrmsyrrqkrwwnAYILFYE 1779
Cdd:cd02667   258 SDVRE--VSLEEVLKSE----------------------------AYLLFYE 279
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1508-1779 5.60e-27

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: 113.56  E-value: 5.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1508 QHDALEFFNSLVDSLDEALKALG-----------------HPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIR 1570
Cdd:cd02663    65 HQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVE 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1571 NHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDME 1650
Cdd:cd02663   145 QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLF 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1651 PYTvagvakleGDNVNPESqliqqseqsesetagstKYRLVGVLVHSGQ-ASGGHYYSyIIQRNGGdgernrWYKFDDGD 1729
Cdd:cd02663   225 NTT--------DDAENPDR-----------------LYELVAVVVHIGGgPNHGHYVS-IVKSHGG------WLLFDDET 272

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 119579811 1730 VTecKMDDdeemknqcfggEYMGEVFDHmmkrmsyrrQKRWWNAYILFYE 1779
Cdd:cd02663   273 VE--KIDE-----------NAVEEFFGD---------SPNQATAYVLFYQ 300
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1383-1779 8.17e-21

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 95.48  E-value: 8.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1383 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvddDMSGDEKQDNESNVDPrddVFGYPQQFEDkpaLSKTEDRk 1462
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALK-----------NYNPARRGANQSSDNL---TNALRDLFDT---MDKKQEP- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1463 eynigvlrhlqvifghlaasrlqyYVPRGFWKQFRL----WGEP--VNLREQHDALEFFNSLVDSLDEALK-ALGHPAML 1535
Cdd:cd02657    63 ------------------------VPPIEFLQLLRMafpqFAEKqnQGGYAQQDAEECWSQLLSVLSQKLPgAGSKGSFI 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1536 SKVLGGSFADQKICQGCPHRYECE-ESFTTLNVDIrNHQNLLDSLEQYVKgDLLEGANAYHCEKCNKKVDTVKRLLIKKL 1614
Cdd:cd02657   119 DQLFGIELETKMKCTESPDEEEVStESEYKLQCHI-SITTEVNYLQDGLK-KGLEEEIEKHSPTLGRDAIYTKTSRISRL 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1615 PPVLAIQLKRFDydWERECAI--KFNDYFEFPRELDMEPYTvagvaklegdnvnpesqliqqseqsesetAGSTKYRLVG 1692
Cdd:cd02657   197 PKYLTVQFVRFF--WKRDIQKkaKILRKVKFPFELDLYELC-----------------------------TPSGYYELVA 245

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1693 VLVHSGQ-ASGGHYYSYIIQRNggdgeRNRWYKFDDGDVTECKMDDDEEMKNqcfGGEYmgevfdHMmkrmsyrrqkrww 1771
Cdd:cd02657   246 VITHQGRsADSGHYVAWVRRKN-----DGKWIKFDDDKVSEVTEEDILKLSG---GGDW------HI------------- 298


                  ....*...
gi 119579811 1772 nAYILFYE 1779
Cdd:cd02657   299 -AYILLYK 305
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1383-1743 1.08e-17

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 86.61  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1383 GLKNAGATCYMNSVIQQLYMIPSirngilaiegtgsdVDDDMSGDEKQDNESNVDPRDDvfgYPQQF-----------ED 1451
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPS--------------FQWRYDDLENKFPSDVVDPAND---LNCQLikladgllsgrYS 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1452 KPALSKTEDrKEYNIGVLrhlqvifghlaasrlqyyvPRGFwKqfRLWGEpvNLRE-----QHDALEFFNSLVDSLDEAL 1526
Cdd:cd02658    64 KPASLKSEN-DPYQVGIK-------------------PSMF-K--ALIGK--GHPEfstmrQQDALEFLLHLIDKLDRES 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1527 KALG--HPAMLSKVlggsFADQKI-CQGCPHRYECEESFTTLNVDIRNH--------------QNLLDSLEQYVKGDLLE 1589
Cdd:cd02658   119 FKNLglNPNDLFKF----MIEDRLeCLSCKKVKYTSELSEILSLPVPKDeatekeegelvyepVPLEDCLKAYFAPETIE 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1590 ganaYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDY--DWErecaikfndyfefPRELDMEpytvagvakLEGDNVnp 1667
Cdd:cd02658   195 ----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLleNWV-------------PKKLDVP---------IDVPEE-- 246

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119579811 1668 esqliqqseqsesetAGSTKYRLVGVLVHSG-QASGGHYYSYIIQRNGGDGernRWYKFDDGDVteCKMDDDEEMKN 1743
Cdd:cd02658   247 ---------------LGPGKYELIAFISHKGtSVHSGHYVAHIKKEIDGEG---KWVLFNDEKV--VASQDPPEMKK 303
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1358-1730 5.29e-17

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 84.94  E-value: 5.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1358 ITTCEALtewEYLPPvgprppkgFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSgdekqdnesnvd 1437
Cdd:cd02671    12 ATSCEKR---ENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQS------------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1438 prddvfgypqQFEDKPALSKTEDRKEYNIGVLRHLQVIfghlaASRLQYYvprgfwkqfrlwgepvnlrEQHDALEFFNS 1517
Cdd:cd02671    69 ----------SFLLNPEKYNDELANQAPRRLLNALREV-----NPMYEGY-------------------LQHDAQEVLQC 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1518 LVDSLDEalkalghpaMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQ-------------------NLLDS 1578
Cdd:cd02671   115 ILGNIQE---------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESElskseesseispdpktemkTLKWA 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1579 LEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAI----KFNDYFEFPRELDMEpytv 1654
Cdd:cd02671   186 ISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVNTPLLTPLKLSLE---- 261

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119579811 1655 agvaklegdnvnpesqliqqsEQSESETagSTKYRLVGVLVHSG-QASGGHYYSYIiqrnggdgernRWYKFDDGDV 1730
Cdd:cd02671   262 ---------------------EWSTKPK--NDVYRLFAVVMHSGaTISSGHYTAYV-----------RWLLFDDSEV 304
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1382-1732 1.07e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 84.08  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1382 VGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSGDEKQdnesnvdprddvfgypqqfedkPALSKTEDR 1461
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTERRI----------------------GGREVSRSE 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1462 KEYNIGVLRHLQVIFGHLAASRLQYYVPRGfwkqfrlwgEPVNLR-EQHDALEFFNSLVDSLDEALKALG-HPAMLSKVL 1539
Cdd:cd02666    60 LQRSNQFVYELRSLFNDLIHSNTRSVTPSK---------ELAYLAlRQQDVTECIDNVLFQLEVALEPISnAFAGPDTED 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1540 GGSFADQ-------KICQ--------GCPHRYECEESFTTLNVDIR---------NH-QNLLDSLEQYVKGDLLEganay 1594
Cdd:cd02666   131 DKEQSDLikrlfsgKTKQqlvpesmgNQPSVRTKTERFLSLLVDVGkkgreivvlLEpKDLYDALDRYFDYDSLT----- 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1595 hcekcnkkvdtvkrllikKLPPVLAIQLKrfdydwerecaikfNDYFEFPRELDMEPYT----VAGVAKLEGDNVNPESQ 1670
Cdd:cd02666   206 ------------------KLPQRSQVQAQ--------------LAQPLQRELISMDRYElpssIDDIDELIREAIQSESS 253

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119579811 1671 LIQQSEQSESETAG----------STKYRLVGVLVHSGQASGGHYYSYIiqrngGDGERNRWYKFDDGDVTE 1732
Cdd:cd02666   254 LVRQAQNELAELKHeiekqfddlkSYGYRLHAVFIHRGEASSGHYWVYI-----KDFEENVWRKYNDETVTV 320
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1383-1780 4.65e-16

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 81.00  E-value: 4.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1383 GLKNAGATCYMNSVIQQL-YMIPSIRNGILAIEGTGSDVDDDMSGDEKQDNesnvdprddvfgypqQFEDKPALSKTEDR 1461
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKELKVLKNVIRKPEPDLN---------------QEEALKLFTALWSS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1462 KEYNIGVLRhlqvifghlaasrlqyyvprgfwkqfrlwgepvNLREQHDALEFFNSLVDSLDEALKALG----HPAMLSK 1537
Cdd:COG5533    66 KEHKVGWIP---------------------------------PMGSQEDAHELLGKLLDELKLDLVNSFtiriFKTTKDK 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1538 V--LGGSFADQKICQgcPHRYECEESFTTlnvdirnhQNLLDSLEQYVkgDLLEGANAyhceKCNKKVDTVKRLL----I 1611
Cdd:COG5533   113 KktSTGDWFDIIIEL--PDQTWVNNLKTL--------QEFIDNMEELV--DDETGVKA----KENEELEVQAKQEyevsF 176

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1612 KKLPPVLAIQLKRFDYDwerecaikfndyfefpreldmepytvAGVAKLEgDNVNPESQLIQQSEQSeSETAGSTKYRLV 1691
Cdd:COG5533   177 VKLPKILTIQLKRFANL--------------------------GGNQKID-TEVDEKFELPVKHDQI-LNIVKETYYDLV 228

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1692 GVLVHSGQASGGHYYSYIiqRNGGDgernrWYKFDDGDVTECKMDDDEEMKNQcfggeymgevfdhmmkrmsyrrqkrww 1771
Cdd:COG5533   229 GFVLHQGSLEGGHYIAYV--KKGGK-----WEKANDSDVTPVSEEEAINEKAK--------------------------- 274


                  ....*....
gi 119579811 1772 NAYILFYER 1780
Cdd:COG5533   275 NAYLYFYER 283
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1508-1748 1.67e-15

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 77.98  E-value: 1.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1508 QHDALEFFNSLVDSLDEALKALGHPAMLSK--------VLGGSFADQKICQGcpHRYECEESFTTLNVDIRNHQNLLDSL 1579
Cdd:cd02665    22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEksknpmvqLFYGTFLTEGVLEG--KPFCNCETFGQYPLQVNGYGNLHECL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1580 E-QYVKGDLlEGANAYHCEKCNKkvdtvkRLLIKKLPPVLAIQLKRFDYDWERECaiKFNDYFEFPRELDMEPYtvagva 1658
Cdd:cd02665   100 EaAMFEGEV-ELLPSDHSVKSGQ------ERWFTELPPVLTFELSRFEFNQGRPE--KIHDKLEFPQIIQQVPY------ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1659 klegdnvnpesqliqqseqsesetagstkyRLVGVLVHSGQASGGHYYSYIIQRNggdgeRNRWYKFDDGDVTECkmdDD 1738
Cdd:cd02665   165 ------------------------------ELHAVLVHEGQANAGHYWAYIYKQS-----RQEWEKYNDISVTES---SW 206

                         250
                  ....*....|
gi 119579811 1739 EEMKNQCFGG 1748
Cdd:cd02665   207 EEVERDSFGG 216
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1494-1737 2.44e-15

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 77.79  E-value: 2.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1494 KQFRLWGEpvNLREQHDALEFFNSLVDSLDEALKalgHPamlskvLGGSFADQKICQGCPH----RYECeESFTTLNV-- 1567
Cdd:cd02662    22 PSLIEYLE--EFLEQQDAHELFQVLLETLEQLLK---FP------FDGLLASRIVCLQCGEsskvRYES-FTMLSLPVpn 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1568 -DIRNHQNLLDSLEQYVKGDLLEGanaYHCEKCnkkvdtvkRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRE 1646
Cdd:cd02662    90 qSSGSGTTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPER 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1647 LDmepytvagvaklegdnvnpesqliqqseqsesetagSTKYRLVGVLVHSGQASGGHYYSY----IIQRNGGDGE---- 1718
Cdd:cd02662   158 LP------------------------------------KVLYRLRAVVVHYGSHSSGHYVCYrrkpLFSKDKEPGSfvrm 201

                         250       260
                  ....*....|....*....|....*.
gi 119579811 1719 -------RNRWYKFDDGDVTECKMDD 1737
Cdd:cd02662   202 regpsstSHPWWRISDTTVKEVSESE 227
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1575-1780 4.14e-12

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 71.84  E-value: 4.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1575 LLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDweRECAIKFNDYFEFP-RELDMEPYT 1653
Cdd:COG5560   677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSV--RSFRDKIDDLVEYPiDDLDLSGVE 754

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1654 VAgvaklegdnvNPESQLIqqseqsesetagstkYRLVGVLVHSGQASGGHYYSYIiqRNGGDgerNRWYKFDDGDVTEc 1733
Cdd:COG5560   755 YM----------VDDPRLI---------------YDLYAVDNHYGGLSGGHYTAYA--RNFAN---NGWYLFDDSRITE- 803

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 119579811 1734 kMDDDEEMKNqcfggeymgevfdhmmkrmsyrrqkrwwNAYILFYER 1780
Cdd:COG5560   804 -VDPEDSVTS----------------------------SAYVLFYRR 821
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
1382-1727 5.35e-11

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 66.14  E-value: 5.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1382 VGLKNAGATCYMNSVIQQLYMIPSIRNgiLAIEGTGSDVDD------------DMSGDEKQDN--ESNvdprddvfgypq 1447
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRN--LALSHLATECLKehcllcelgflfDMLEKAKGKNcqASN------------ 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1448 qFEDkpALSKTEDRKeyNIGVLRHLQVIFGHLAASRL-QYyvprgfWKQFRLwgepvnlrEQ--HDALEFFNSLVDSlde 1524
Cdd:pfam13423   67 -FLR--ALSSIPEAS--ALGLLDEDRETNSAISLSSLiQS------FNRFLL--------DQlsSEENSTPPNPSPA--- 124

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1525 alkalghPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLN------VDIRNHQNLLDSLEQYVKGDLL-EGANAYHCE 1597
Cdd:pfam13423  125 -------ESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDliyprkPSSNNKKPPNQTFSSILKSSLErETTTKAWCE 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811  1598 KCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWEREcaIKFNDYfeFPRELDMepytvagvaklegdnvnpesqliqQSEQ 1677
Cdd:pfam13423  198 KCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL--WKTPGW--LPPEIGL------------------------TLSD 249

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 119579811  1678 SESETAGSTKYRLVGVLVH-SGQASGGHYYSYI--IQRNGGDGERNRWYKFDD 1727
Cdd:pfam13423  250 DLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVkvADSELEDPTESQWYLFND 302
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1368-1733 3.54e-10

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 64.65  E-value: 3.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1368 EYLPpvgprppkGFVGLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEKQDNESNVDPRDDVFGypq 1447
Cdd:cd02669   114 PYLP--------GFVGLNNIKNNDYANVIIQALSHVKPIRNFFL-------------LYENYENIKDRKSELVKRLS--- 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1448 qfedkpALSktedRKEYNIGVLRhlqvifGHLAASRLQYYVPRGFWKQFRLwgepvnlREQHDALEFFNSLVDSLdealk 1527
Cdd:cd02669   170 ------ELI----RKIWNPRNFK------GHVSPHELLQAVSKVSKKKFSI-------TEQSDPVEFLSWLLNTL----- 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1528 algHPAmlskvLGGSFAD-----QKICQG---------CPHRYECEES----------------FTTLNVDIRN-----H 1572
Cdd:cd02669   222 ---HKD-----LGGSKKPnssiiHDCFQGkvqietqkiKPHAEEEGSKdkffkdsrvkktsvspFLLLTLDLPPpplfkD 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1573 QNLLDSLEQYVKGDLLEGANAYHCEKCNKKVdtvKRLLIKKLPPVLAIQLKRFDYdwerecaikfNDYF--------EFP 1644
Cdd:cd02669   294 GNEENIIPQVPLKQLLKKYDGKTETELKDSL---KRYLISRLPKYLIFHIKRFSK----------NNFFkeknptivNFP 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1645 RELDMEPYTVAGVAKLEGDnvnpesqliqqseqsesetagSTKYRLVGVLVHSGQASGGHYYSYIIQRNGgdgeRNRWYK 1724
Cdd:cd02669   361 IKNLDLSDYVHFDKPSLNL---------------------STKYNLVANIVHEGTPQEDGTWRVQLRHKS----TNKWFE 415


                  ....*....
gi 119579811 1725 FDDGDVTEC 1733
Cdd:cd02669   416 IQDLNVKEV 424
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1507-1779 3.80e-07

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


Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 53.68  E-value: 3.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1507 EQHDALEFFNSLVDSLDealkalgHPAMLSKVlggsfadqKICQGcPHRYECEESFttlnVDIRNHQNLLDSLEQyVKGD 1586
Cdd:cd02670    22 EQQDPEEFFNFITDKLL-------MPLLEPKV--------DIIHG-GKKDQDDDKL----VNERLLQIPVPDDDD-GGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1587 LLEganayHCEKC--NKKVdtvkrllIKKLPPVLAIQLKRfdYDWERECAIKFNDYFEFPRELDMePYTVAGvAKLEGDN 1664
Cdd:cd02670    81 TLE-----QCLEQyfNNSV-------FAKAPSCLIICLKR--YGKTEGKAQKMFKKILIPDEIDI-PDFVAD-DPRACSK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1665 VNPESQlIQQSEQSESETAGSTKYRLVGVLVHSGQA-SGGHYYSYI------IQRNGGDGERNRWYKFDDgdvteckMDD 1737
Cdd:cd02670   145 CQLECR-VCYDDKDFSPTCGKFKLSLCSAVCHRGTSlETGHYVAFVrygsysLTETDNEAYNAQWVFFDD-------MAD 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 119579811 1738 DEemknqcfGGEYmgeVFDHMMKRmsyrrqkRWWNAYILFYE 1779
Cdd:cd02670   217 RD-------GVSN---GFNIPAAR-------LLEDPYMLFYQ 241
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
 725-789 1.04e-05

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; UBP24 (EC 3.4.19.12), also termed deubiquitinating enzyme 24, or ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24 (USP24), is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain, a ubiquitin-like (Ubl) domain, and a C-terminal peptidase C19 domain.


Pssm-ID: 340585  Cd Length: 79  Bit Score: 45.38  E-value: 1.04e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119579811  725 DDLEVWSHTNDTIGSVRRCILNRIKANVAHtkIELFVGGELIDPADDRKLIGQLNLKDKSLITAK 789
Cdd:cd17065    17 QEFTLEVHSNETLGSVRQKIAERLNCPVDQ--VQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1546-1732 2.79e-04

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


Pssm-ID: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 45.20  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1546 QKICQGCPHRYECEESFTTLNVDIRNHQNL-----LDSLEQYVKGDL-LEGANAYHCEKCNKKVDTVKRLLIKKLPP--- 1616
Cdd:cd02672    81 SQDQLGTPFSCGTSRNSVSLLYTLSLPLGStktskESTFLQLLKRSLdLEKVTKAWCDTCCKYQPLEQTTSIRHLPDill 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579811 1617 -VLAIQLKRFDydweRECAIKFNDYFEFpreLDMEPytvaGVAKLEGDNVNPESQLIQQSeqsesetagSTKYRLVGVLV 1695
Cdd:cd02672   161 lVLVINLSVTN----GEFDDINVVLPSG---KVMQN----KVSPKAIDHDKLVKNRGQES---------IYKYELVGYVC 220

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 119579811 1696 H-SGQASGGHYYSYIIQRNgGDGERNRWYKFDDGDVTE 1732
Cdd:cd02672   221 EiNDSSRGQHNVVFVIKVN-EESTHGRWYLFNDFLVTP 257
 
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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