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Conserved domains on  [gi|145309311|ref|NP_001034680|]
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ubiquitin carboxyl-terminal hydrolase 9X isoform 4 [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 ...
 1555-1958 2.64e-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: 481.37  E-value: 2.64e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1555 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIegtgsdvdddmsgdekqdnesnvdprddvfgypqqfedkpalsKTE 1634
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------------------------------------------PPT 37

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1635 DRKEYNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAMLSKVL 1714
Cdd:cd02659    38 EDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLF 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1715 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLA 1794
Cdd:cd02659   118 GGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLT 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1795 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDnvnpesqliqqseqSESETAGSTKYRLVGVLVHSGQ 1874
Cdd:cd02659   198 LQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKEGD--------------SEKKDSESYIYELHGVLVHSGD 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1875 ASGGHYYSYIIQRNGGdgernRWYKFDDGDVTECKMDDDEEmknQCFGGEYMGEVFDHMmkrmsYRRQKRWWNAYILFYE 1954
Cdd:cd02659   264 AHGGHYYSYIKDRDDG-----KWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYE 330


                  ....
gi 145309311 1955 RMDT 1958
Cdd:cd02659   331 RKSP 334
DUF3517 pfam12030
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ...
 2097-2476 2.60e-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: 341.20  E-value: 2.60e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2097 SNRFSEYLLECPSAEVRGAFAKLIVFIAH-----FSLQDGPCPspfaspgPSSQAYDNLSLSDHLLRAVLNLLRR---EV 2168
Cdd:pfam12030    1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCD-------PDDLEEEWRSLSDSVLEAVVALLDHlwkEF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2169 SEHGRHLQQYFNLFVMYANLGVAEKTQLLKLS-VPATFMLVSLDEGPGPPIKYQYAEL------------GKLYSVVSQL 2235
Cdd:pfam12030   74 HTHLRSWDEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARMlrlvekrrppsyEKLIQLLSVL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2236 IRCCNVSSRMQSSINGNPPLPNpfgdpNLSQPIMPIQQNVADIL--FVRT---SYVKKIIEDCSNSEETVKLLRFCCWEN 2310
Cdd:pfam12030  154 LRCCDLSLPPQSINEGAEPLPN-----SLPDGPFPLTSEEADLLrpLGRTngsIFVKKLLEIDQNPEATRKILRFLLWEN 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2311 PQFSSTVLSELLWQVAYSYTYELR-PYLDLLLQILliEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIK 2389
Cdd:pfam12030  229 PELSDSILKTLLWGIRGAPAHLLRdPFLRAAIVFC--EDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQCIN 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2390 CMvALFSNCPVAYQILQgngdlkrkwtwavewlgdelerrpytgnpqyTYNNWSPPVQSNETSN---------------- 2453
Cdd:pfam12030  307 CR-LGFDKEWFASQVLE-------------------------------NIPDWAPPLLSYPDSNvrsetedflqeelfsh 354

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 145309311  2454 ---------------------------GYFLERS---HSARMTLAKACELCPE 2476
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 ...
 900-964 1.02e-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: 45.76  E-value: 1.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309311  900 DDLEVWSHTNDTIGSVRRCILNRIKANVAHtkIELFVGGELIDPADDRKLIGQLNLKDKSLITAK 964
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 ...
 1555-1958 2.64e-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: 481.37  E-value: 2.64e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1555 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIegtgsdvdddmsgdekqdnesnvdprddvfgypqqfedkpalsKTE 1634
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------------------------------------------PPT 37

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1635 DRKEYNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAMLSKVL 1714
Cdd:cd02659    38 EDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLF 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1715 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLA 1794
Cdd:cd02659   118 GGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLT 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1795 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDnvnpesqliqqseqSESETAGSTKYRLVGVLVHSGQ 1874
Cdd:cd02659   198 LQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKEGD--------------SEKKDSESYIYELHGVLVHSGD 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1875 ASGGHYYSYIIQRNGGdgernRWYKFDDGDVTECKMDDDEEmknQCFGGEYMGEVFDHMmkrmsYRRQKRWWNAYILFYE 1954
Cdd:cd02659   264 AHGGHYYSYIKDRDDG-----KWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYE 330


                  ....
gi 145309311 1955 RMDT 1958
Cdd:cd02659   331 RKSP 334
DUF3517 pfam12030
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ...
 2097-2476 2.60e-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: 341.20  E-value: 2.60e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2097 SNRFSEYLLECPSAEVRGAFAKLIVFIAH-----FSLQDGPCPspfaspgPSSQAYDNLSLSDHLLRAVLNLLRR---EV 2168
Cdd:pfam12030    1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCD-------PDDLEEEWRSLSDSVLEAVVALLDHlwkEF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2169 SEHGRHLQQYFNLFVMYANLGVAEKTQLLKLS-VPATFMLVSLDEGPGPPIKYQYAEL------------GKLYSVVSQL 2235
Cdd:pfam12030   74 HTHLRSWDEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARMlrlvekrrppsyEKLIQLLSVL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2236 IRCCNVSSRMQSSINGNPPLPNpfgdpNLSQPIMPIQQNVADIL--FVRT---SYVKKIIEDCSNSEETVKLLRFCCWEN 2310
Cdd:pfam12030  154 LRCCDLSLPPQSINEGAEPLPN-----SLPDGPFPLTSEEADLLrpLGRTngsIFVKKLLEIDQNPEATRKILRFLLWEN 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2311 PQFSSTVLSELLWQVAYSYTYELR-PYLDLLLQILliEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIK 2389
Cdd:pfam12030  229 PELSDSILKTLLWGIRGAPAHLLRdPFLRAAIVFC--EDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQCIN 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2390 CMvALFSNCPVAYQILQgngdlkrkwtwavewlgdelerrpytgnpqyTYNNWSPPVQSNETSN---------------- 2453
Cdd:pfam12030  307 CR-LGFDKEWFASQVLE-------------------------------NIPDWAPPLLSYPDSNvrsetedflqeelfsh 354

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 145309311  2454 ---------------------------GYFLERS---HSARMTLAKACELCPE 2476
Cdd:pfam12030  355 emgpdpqfrlreaarrlgiacleylrgTYVLRRSqveRSAVETLQRVIELCPE 407
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1557-1953 1.56e-79

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 265.85  E-value: 1.56e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  1557 VGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDvdddmsgdekqdnesnvdprddvfgypqqfedkpalskteDR 1636
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSED----------------------------------------SR 40

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  1637 KEYNIGVLRHLQVIFGHLA-ASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKA---LGHPAMLSK 1712
Cdd:pfam00443   41 YNKDINLLCALRDLFKALQkNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITD 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  1713 VLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLL------DSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLI 1786
Cdd:pfam00443  121 LFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKI 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  1787 KKLPPVLAIQLKRFDYDweRECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDNVnpesqliqqseqsesetagstKYRLV 1866
Cdd:pfam00443  201 SRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ---------------------DYRLV 257

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  1867 GVLVHSGQASGGHYYSYIIQrnggdGERNRWYKFDDGDVTECKMDDDEEMknqcfggeymgevfdhmmkrmsyrrqkrwW 1946
Cdd:pfam00443  258 AVVVHSGSLSSGHYIAYIKA-----YENNRWYKFDDEKVTEVDEETAVLS-----------------------------S 303


                   ....*..
gi 145309311  1947 NAYILFY 1953
Cdd:pfam00443  304 SAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 1555-2001 4.61e-49

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 192.78  E-value: 4.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1555 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEgtgsdvdddmsgdekQDNEsnvDPRDDV-------FgYPQQFEDK 1627
Cdd:COG5077   192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP---------------TDHP---RGRDSValalqrlF-YNLQTGEE 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1628 PaLSKTEdrkeynigvlrhLQVIFGhlaasrlqyyvprgfwkqfrlWGEPVNLReQHDALEFFNSLVDSLDEALKALGHP 1707
Cdd:COG5077   253 P-VDTTE------------LTRSFG---------------------WDSDDSFM-QHDIQEFNRVLQDNLEKSMRGTVVE 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1708 AMLSKVLGGSFadqKICQGCPHR-YECE--ESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKcNKKVDTVKRL 1784
Cdd:COG5077   298 NALNGIFVGKM---KSYIKCVNVnYESArvEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGV 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1785 LIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDMEPYtvagvaklegdnVNPESqliQQSEQSESEtagstkYR 1864
Cdd:COG5077   374 IFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPF------------LDRDA---DKSENSDAV------YV 432

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1865 LVGVLVHSGQASGGHYYSYIiqRNGGDGernRWYKFDDGDVTECKMdddEEMKNQCFGGEYMGEVfdhmmKRMSYRRQKR 1944
Cdd:COG5077   433 LYGVLVHSGDLHEGHYYALL--KPEKDG---RWYKFDDTRVTRATE---KEVLEENFGGDHPYKD-----KIRDHSGIKR 499

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145309311 1945 WWNAYILFYERMdtiDQDDELIRYISELAITTRPHQIIMPSAIERSVRKQNVQFMHN 2001
Cdd:COG5077   500 FMSAYMLVYLRK---SMLDDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHL 553
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
 900-964 1.02e-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: 45.76  E-value: 1.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309311  900 DDLEVWSHTNDTIGSVRRCILNRIKANVAHtkIELFVGGELIDPADDRKLIGQLNLKDKSLITAK 964
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 ...
 1555-1958 2.64e-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: 481.37  E-value: 2.64e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1555 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIegtgsdvdddmsgdekqdnesnvdprddvfgypqqfedkpalsKTE 1634
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------------------------------------------PPT 37

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1635 DRKEYNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAMLSKVL 1714
Cdd:cd02659    38 EDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLF 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1715 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLA 1794
Cdd:cd02659   118 GGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLT 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1795 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDnvnpesqliqqseqSESETAGSTKYRLVGVLVHSGQ 1874
Cdd:cd02659   198 LQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKEGD--------------SEKKDSESYIYELHGVLVHSGD 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1875 ASGGHYYSYIIQRNGGdgernRWYKFDDGDVTECKMDDDEEmknQCFGGEYMGEVFDHMmkrmsYRRQKRWWNAYILFYE 1954
Cdd:cd02659   264 AHGGHYYSYIKDRDDG-----KWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYE 330


                  ....
gi 145309311 1955 RMDT 1958
Cdd:cd02659   331 RKSP 334
DUF3517 pfam12030
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ...
 2097-2476 2.60e-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: 341.20  E-value: 2.60e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2097 SNRFSEYLLECPSAEVRGAFAKLIVFIAH-----FSLQDGPCPspfaspgPSSQAYDNLSLSDHLLRAVLNLLRR---EV 2168
Cdd:pfam12030    1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCD-------PDDLEEEWRSLSDSVLEAVVALLDHlwkEF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2169 SEHGRHLQQYFNLFVMYANLGVAEKTQLLKLS-VPATFMLVSLDEGPGPPIKYQYAEL------------GKLYSVVSQL 2235
Cdd:pfam12030   74 HTHLRSWDEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARMlrlvekrrppsyEKLIQLLSVL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2236 IRCCNVSSRMQSSINGNPPLPNpfgdpNLSQPIMPIQQNVADIL--FVRT---SYVKKIIEDCSNSEETVKLLRFCCWEN 2310
Cdd:pfam12030  154 LRCCDLSLPPQSINEGAEPLPN-----SLPDGPFPLTSEEADLLrpLGRTngsIFVKKLLEIDQNPEATRKILRFLLWEN 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2311 PQFSSTVLSELLWQVAYSYTYELR-PYLDLLLQILliEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIK 2389
Cdd:pfam12030  229 PELSDSILKTLLWGIRGAPAHLLRdPFLRAAIVFC--EDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQCIN 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  2390 CMvALFSNCPVAYQILQgngdlkrkwtwavewlgdelerrpytgnpqyTYNNWSPPVQSNETSN---------------- 2453
Cdd:pfam12030  307 CR-LGFDKEWFASQVLE-------------------------------NIPDWAPPLLSYPDSNvrsetedflqeelfsh 354

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 145309311  2454 ---------------------------GYFLERS---HSARMTLAKACELCPE 2476
Cdd:pfam12030  355 emgpdpqfrlreaarrlgiacleylrgTYVLRRSqveRSAVETLQRVIELCPE 407
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1557-1953 1.56e-79

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 265.85  E-value: 1.56e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  1557 VGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDvdddmsgdekqdnesnvdprddvfgypqqfedkpalskteDR 1636
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSED----------------------------------------SR 40

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  1637 KEYNIGVLRHLQVIFGHLA-ASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKA---LGHPAMLSK 1712
Cdd:pfam00443   41 YNKDINLLCALRDLFKALQkNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITD 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  1713 VLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLL------DSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLI 1786
Cdd:pfam00443  121 LFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKI 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  1787 KKLPPVLAIQLKRFDYDweRECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDNVnpesqliqqseqsesetagstKYRLV 1866
Cdd:pfam00443  201 SRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ---------------------DYRLV 257

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  1867 GVLVHSGQASGGHYYSYIIQrnggdGERNRWYKFDDGDVTECKMDDDEEMknqcfggeymgevfdhmmkrmsyrrqkrwW 1946
Cdd:pfam00443  258 AVVVHSGSLSSGHYIAYIKA-----YENNRWYKFDDEKVTEVDEETAVLS-----------------------------S 303


                   ....*..
gi 145309311  1947 NAYILFY 1953
Cdd:pfam00443  304 SAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 1680-1954 5.17e-55

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: 193.08  E-value: 5.17e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1680 LREQHDALEFFNSLVDSLDEALKALG--------HPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDI----RNH 1747
Cdd:cd02257    19 FSEQQDAHEFLLFLLDKLHEELKKSSkrtsdsssLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1748 QNLLDSLEQYVKGDLLEGANAYHCEKCnKKVDTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPY 1827
Cdd:cd02257    99 VSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPY 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1828 TVAGVAKLEGDNvnpesqliqqseqsesetaGSTKYRLVGVLVHSGQ-ASGGHYYSYIIqrnggDGERNRWYKFDDGDVT 1906
Cdd:cd02257   177 LSEGEKDSDSDN-------------------GSYKYELVAVVVHSGTsADSGHYVAYVK-----DPSDGKWYKFNDDKVT 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 145309311 1907 ECKMDDDEEMKNqcfggeymgevfdhmmkrmsyrrqkRWWNAYILFYE 1954
Cdd:cd02257   233 EVSEEEVLEFGS-------------------------LSSSAYILFYE 255
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1558-1954 4.96e-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: 187.24  E-value: 4.96e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1558 GLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSGDekQDNESNvdprddvfgypqqfedkpalsktedrk 1637
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPD--KPHEPQ--------------------------- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1638 eyniGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLwgepvNLREQHDALEFFNSLVDSLDEALKALGHP---AMLSKVL 1714
Cdd:cd02668    52 ----TIIDQLQLIFAQLQFGNRSVVDPSGFVKALGL-----DTGQQQDAQEFSKLFLSLLEAKLSKSKNPdlkNIVQDLF 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1715 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLA 1794
Cdd:cd02668   123 RGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLN 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1795 IQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVagvaklegdnvnpesqliqqsEQSEsetaGSTKYRLVGVLVHSGQ 1874
Cdd:cd02668   203 FQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLA---------------------ESDE----GSYVYELSGVLIHQGV 257

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1875 -ASGGHYYSYIiqrngGDGERNRWYKFDDGDVTE-----CKMDDDEEMKNQCFGgeymgevfDHMMKRMSYRrqkrwwNA 1948
Cdd:cd02668   258 sAYSGHYIAHI-----KDEQTGEWYKFNDEDVEEmpgkpLKLGNSEDPAKPRKS--------EIKKGTHSSR------TA 318


                  ....*.
gi 145309311 1949 YILFYE 1954
Cdd:cd02668   319 YMLVYK 324
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 1555-2001 4.61e-49

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 192.78  E-value: 4.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1555 GFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEgtgsdvdddmsgdekQDNEsnvDPRDDV-------FgYPQQFEDK 1627
Cdd:COG5077   192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP---------------TDHP---RGRDSValalqrlF-YNLQTGEE 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1628 PaLSKTEdrkeynigvlrhLQVIFGhlaasrlqyyvprgfwkqfrlWGEPVNLReQHDALEFFNSLVDSLDEALKALGHP 1707
Cdd:COG5077   253 P-VDTTE------------LTRSFG---------------------WDSDDSFM-QHDIQEFNRVLQDNLEKSMRGTVVE 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1708 AMLSKVLGGSFadqKICQGCPHR-YECE--ESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKcNKKVDTVKRL 1784
Cdd:COG5077   298 NALNGIFVGKM---KSYIKCVNVnYESArvEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGV 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1785 LIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDMEPYtvagvaklegdnVNPESqliQQSEQSESEtagstkYR 1864
Cdd:COG5077   374 IFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPF------------LDRDA---DKSENSDAV------YV 432

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1865 LVGVLVHSGQASGGHYYSYIiqRNGGDGernRWYKFDDGDVTECKMdddEEMKNQCFGGEYMGEVfdhmmKRMSYRRQKR 1944
Cdd:COG5077   433 LYGVLVHSGDLHEGHYYALL--KPEKDG---RWYKFDDTRVTRATE---KEVLEENFGGDHPYKD-----KIRDHSGIKR 499

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145309311 1945 WWNAYILFYERMdtiDQDDELIRYISELAITTRPHQIIMPSAIERSVRKQNVQFMHN 2001
Cdd:COG5077   500 FMSAYMLVYLRK---SMLDDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHL 553
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1558-1912 5.33e-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: 163.22  E-value: 5.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1558 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEKQDNESNvdprddvfgypqqfedkpalsktedrk 1637
Cdd:cd02661     3 GLQNLGNTCFLNSVLQCLTHTPPLANYLL-------------SREHSKDCCNE--------------------------- 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1638 eyNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEA-------LKALGHPA-- 1708
Cdd:cd02661    43 --GFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKAcldrfkkLKAVDPSSqe 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1709 --MLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLI 1786
Cdd:cd02661   121 ttLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTI 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1787 KKLPPVLAIQLKRFDYDWERecaiKFNDYFEFPRELDMEPYTVagvaklegdnvnpesqliqqseqseSETAGSTKYRLV 1866
Cdd:cd02661   201 HRAPNVLTIHLKRFSNFRGG----KINKQISFPETLDLSPYMS-------------------------QPNDGPLKYKLY 251

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 145309311 1867 GVLVHSG-QASGGHYYSYIIQRNGgdgernRWYKFDDGDVTECKMDD 1912
Cdd:cd02661   252 AVLVHSGfSPHSGHYYCYVKSSNG------KWYNMDDSKVSPVSIET 292
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1682-1954 3.86e-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: 143.58  E-value: 3.86e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1682 EQHDALEFFNSLVDSLDealkalghpAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDI------RNHQNLLDSLE 1755
Cdd:cd02674    21 DQQDAQEFLLFLLDGLH---------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLEDCLR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1756 QYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDweRECAIKFNDYFEFP-RELDMEPYTVAgvak 1834
Cdd:cd02674    92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPlNDLDLTPYVDT---- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1835 legdnvnpesqliqqseqseSETAGSTKYRLVGVLVHSGQASGGHYYSYIiqrngGDGERNRWYKFDDGDVTecKMDDDE 1914
Cdd:cd02674   166 --------------------RSFTGPFKYDLYAVVNHYGSLNGGHYTAYC-----KNNETNDWYKFDDSRVT--KVSESS 218

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 145309311 1915 EMKNqcfggeymgevfdhmmkrmsyrrqkrwwNAYILFYE 1954
Cdd:cd02674   219 VVSS----------------------------SAYILFYE 230
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1558-1907 3.54e-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: 138.27  E-value: 3.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1558 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgSDvDDDMSGDEKQDNESNVDPRDDVFgypQQFedkpalSKTEDRK 1637
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFL------SD-RHSCTCLSCSPNSCLSCAMDEIF---QEF------YYSGDRS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1638 EYnigvlrhlqvifghlAASRLQYyvprGFWKQFRlwgepvNL--REQHDALEFFNSLVDSLDE-ALKALGHPAMLS--- 1711
Cdd:cd02660    66 PY---------------GPINLLY----LSWKHSR------NLagYSQQDAHEFFQFLLDQLHThYGGDKNEANDEShcn 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1712 ----KVLGGSFADQKICQGCPHRYECEESFTTLNVDIRN---------------HQNLLDSLEQYVKGDLLeGANAYHCE 1772
Cdd:cd02660   121 ciihQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNkstpswalgesgvsgTPTLSDCLDRFTRPEKL-GDFAYKCS 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1773 KCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPYTVAGvaklegdnvnpesqliQQSEQ 1852
Cdd:cd02660   200 GCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-LNKTSRKIDTYVQFPLELNMTPYTSSS----------------IGDTQ 262

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145309311 1853 SESETAGSTKYRLVGVLVHSGQASGGHYYSYIIQRNGgdgernRWYKFDDGDVTE 1907
Cdd:cd02660   263 DSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDG------QWFKFDDAMITR 311
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1558-1918 3.68e-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: 129.53  E-value: 3.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1558 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEKQDNESNVdprddvfgypqqfedkpalsktedrk 1637
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVL-------------SLNLPRLGDSQS-------------------------- 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1638 eynigVLRHLQVIFGHLAASRLQYY-VPRGFWKQfrLWGEPVNLREQHDALEFFNSLVDSLDealkalghpAMLSKVLGG 1716
Cdd:cd02664    42 -----VMKKLQLLQAHLMHTQRRAEaPPDYFLEA--SRPPWFTPGSQQDCSEYLRYLLDRLH---------TLIEKMFGG 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1717 SFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDsleQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQ 1796
Cdd:cd02664   106 KLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDLLN---YFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILT 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1797 LKRFDYDWERECAIKFNDYFEFPRELDMePYTVAgvaklegdNVNPESQLIQQSEQSESETAGSTK---YRLVGVLVHSG 1873
Cdd:cd02664   183 LLRFSYDQKTHVREKIMDNVSINEVLSL-PVRVE--------SKSSESPLEKKEEESGDDGELVTRqvhYRLYAVVVHSG 253

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309311 1874 QAS-GGHYYSYIIQRNGGDG---------------ERNRWYKFDDGDVTECKMdddEEMKN 1918
Cdd:cd02664   254 YSSeSGHYFTYARDQTDADStgqecpepkdaeendESKNWYLFNDSRVTFSSF---ESVQN 311
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1683-1954 1.37e-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: 1.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1683 QHDALEFFNSLVDSLDEALKalghpamlsKVLGGSFADQKICQGCPHRYECEESFTTLN----VDIRNHQNLLDSLEQYV 1758
Cdd:cd02667    51 QQDSHELLRYLLDGLRTFID---------SIFGGELTSTIMCESCGTVSLVYEPFLDLSlprsDEIKSECSIESCLKQFT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1759 KGDLLEGANAYHCEKCNKkvdTVKRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMEPYTvagvaklegd 1838
Cdd:cd02667   122 EVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPFC---------- 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1839 nvnpesqliqQSEQSESETAGSTKYRLVGVLVHSGQASGGHYYSYI----------------IQRNGGDGERNRWYKFDD 1902
Cdd:cd02667   188 ----------DPKCNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVkvrppqqrlsdltkskPAADEAGPGSGQWYYISD 257

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 145309311 1903 GDVTEckMDDDEEMKNQcfggeymgevfdhmmkrmsyrrqkrwwnAYILFYE 1954
Cdd:cd02667   258 SDVRE--VSLEEVLKSE----------------------------AYLLFYE 279
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1683-1954 4.30e-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: 113.94  E-value: 4.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1683 QHDALEFFNSLVDSLDEALKALG-----------------HPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIR 1745
Cdd:cd02663    65 HQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVE 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1746 NHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDME 1825
Cdd:cd02663   145 QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLF 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1826 PYTvagvakleGDNVNPESqliqqseqsesetagstKYRLVGVLVHSGQ-ASGGHYYSyIIQRNGGdgernrWYKFDDGD 1904
Cdd:cd02663   225 NTT--------DDAENPDR-----------------LYELVAVVVHIGGgPNHGHYVS-IVKSHGG------WLLFDDET 272

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 145309311 1905 VTecKMDDdeemknqcfggEYMGEVFDHmmkrmsyrrQKRWWNAYILFYE 1954
Cdd:cd02663   273 VE--KIDE-----------NAVEEFFGD---------SPNQATAYVLFYQ 300
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1558-1954 7.32e-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: 95.86  E-value: 7.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1558 GLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvddDMSGDEKQDNESNVDPrddVFGYPQQFEDkpaLSKTEDRk 1637
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALK-----------NYNPARRGANQSSDNL---TNALRDLFDT---MDKKQEP- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1638 eynigvlrhlqvifghlaasrlqyYVPRGFWKQFRL----WGEP--VNLREQHDALEFFNSLVDSLDEALK-ALGHPAML 1710
Cdd:cd02657    63 ------------------------VPPIEFLQLLRMafpqFAEKqnQGGYAQQDAEECWSQLLSVLSQKLPgAGSKGSFI 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1711 SKVLGGSFADQKICQGCPHRYECE-ESFTTLNVDIrNHQNLLDSLEQYVKgDLLEGANAYHCEKCNKKVDTVKRLLIKKL 1789
Cdd:cd02657   119 DQLFGIELETKMKCTESPDEEEVStESEYKLQCHI-SITTEVNYLQDGLK-KGLEEEIEKHSPTLGRDAIYTKTSRISRL 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1790 PPVLAIQLKRFDydWERECAI--KFNDYFEFPRELDMEPYTvagvaklegdnvnpesqliqqseqsesetAGSTKYRLVG 1867
Cdd:cd02657   197 PKYLTVQFVRFF--WKRDIQKkaKILRKVKFPFELDLYELC-----------------------------TPSGYYELVA 245

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1868 VLVHSGQ-ASGGHYYSYIIQRNggdgeRNRWYKFDDGDVTECKMDDDEEMKNqcfGGEYmgevfdHMmkrmsyrrqkrww 1946
Cdd:cd02657   246 VITHQGRsADSGHYVAWVRRKN-----DGKWIKFDDDKVSEVTEEDILKLSG---GGDW------HI------------- 298


                  ....*...
gi 145309311 1947 nAYILFYE 1954
Cdd:cd02657   299 -AYILLYK 305
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1558-1918 9.08e-18

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 86.61  E-value: 9.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1558 GLKNAGATCYMNSVIQQLYMIPSirngilaiegtgsdVDDDMSGDEKQDNESNVDPRDDvfgYPQQF-----------ED 1626
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPS--------------FQWRYDDLENKFPSDVVDPAND---LNCQLikladgllsgrYS 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1627 KPALSKTEDrKEYNIGVLrhlqvifghlaasrlqyyvPRGFwKqfRLWGEpvNLRE-----QHDALEFFNSLVDSLDEAL 1701
Cdd:cd02658    64 KPASLKSEN-DPYQVGIK-------------------PSMF-K--ALIGK--GHPEfstmrQQDALEFLLHLIDKLDRES 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1702 KALG--HPAMLSKVlggsFADQKI-CQGCPHRYECEESFTTLNVDIRNH--------------QNLLDSLEQYVKGDLLE 1764
Cdd:cd02658   119 FKNLglNPNDLFKF----MIEDRLeCLSCKKVKYTSELSEILSLPVPKDeatekeegelvyepVPLEDCLKAYFAPETIE 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1765 ganaYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDY--DWErecaikfndyfefPRELDMEpytvagvakLEGDNVnp 1842
Cdd:cd02658   195 ----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLleNWV-------------PKKLDVP---------IDVPEE-- 246

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309311 1843 esqliqqseqsesetAGSTKYRLVGVLVHSG-QASGGHYYSYIIQRNGGDGernRWYKFDDGDVteCKMDDDEEMKN 1918
Cdd:cd02658   247 ---------------LGPGKYELIAFISHKGtSVHSGHYVAHIKKEIDGEG---KWVLFNDEKV--VASQDPPEMKK 303
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1533-1905 5.67e-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: 5.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1533 ITTCEALtewEYLPPvgprppkgFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSgdekqdnesnvd 1612
Cdd:cd02671    12 ATSCEKR---ENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQS------------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1613 prddvfgypqQFEDKPALSKTEDRKEYNIGVLRHLQVIfghlaASRLQYYvprgfwkqfrlwgepvnlrEQHDALEFFNS 1692
Cdd:cd02671    69 ----------SFLLNPEKYNDELANQAPRRLLNALREV-----NPMYEGY-------------------LQHDAQEVLQC 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1693 LVDSLDEalkalghpaMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQ-------------------NLLDS 1753
Cdd:cd02671   115 ILGNIQE---------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESElskseesseispdpktemkTLKWA 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1754 LEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAI----KFNDYFEFPRELDMEpytv 1829
Cdd:cd02671   186 ISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVNTPLLTPLKLSLE---- 261

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309311 1830 agvaklegdnvnpesqliqqsEQSESETagSTKYRLVGVLVHSG-QASGGHYYSYIiqrnggdgernRWYKFDDGDV 1905
Cdd:cd02671   262 ---------------------EWSTKPK--NDVYRLFAVVMHSGaTISSGHYTAYV-----------RWLLFDDSEV 304
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1557-1907 9.75e-17

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 84.47  E-value: 9.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1557 VGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSGDEKQdnesnvdprddvfgypqqfedkPALSKTEDR 1636
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTERRI----------------------GGREVSRSE 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1637 KEYNIGVLRHLQVIFGHLAASRLQYYVPRGfwkqfrlwgEPVNLR-EQHDALEFFNSLVDSLDEALKALG-HPAMLSKVL 1714
Cdd:cd02666    60 LQRSNQFVYELRSLFNDLIHSNTRSVTPSK---------ELAYLAlRQQDVTECIDNVLFQLEVALEPISnAFAGPDTED 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1715 GGSFADQ-------KICQ--------GCPHRYECEESFTTLNVDIR---------NH-QNLLDSLEQYVKGDLLEganay 1769
Cdd:cd02666   131 DKEQSDLikrlfsgKTKQqlvpesmgNQPSVRTKTERFLSLLVDVGkkgreivvlLEpKDLYDALDRYFDYDSLT----- 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1770 hcekcnkkvdtvkrllikKLPPVLAIQLKrfdydwerecaikfNDYFEFPRELDMEPYT----VAGVAKLEGDNVNPESQ 1845
Cdd:cd02666   206 ------------------KLPQRSQVQAQ--------------LAQPLQRELISMDRYElpssIDDIDELIREAIQSESS 253

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309311 1846 LIQQSEQSESETAG----------STKYRLVGVLVHSGQASGGHYYSYIiqrngGDGERNRWYKFDDGDVTE 1907
Cdd:cd02666   254 LVRQAQNELAELKHeiekqfddlkSYGYRLHAVFIHRGEASSGHYWVYI-----KDFEENVWRKYNDETVTV 320
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1558-1955 5.02e-16

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 81.00  E-value: 5.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1558 GLKNAGATCYMNSVIQQL-YMIPSIRNGILAIEGTGSDVDDDMSGDEKQDNesnvdprddvfgypqQFEDKPALSKTEDR 1636
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKELKVLKNVIRKPEPDLN---------------QEEALKLFTALWSS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1637 KEYNIGVLRhlqvifghlaasrlqyyvprgfwkqfrlwgepvNLREQHDALEFFNSLVDSLDEALKALG----HPAMLSK 1712
Cdd:COG5533    66 KEHKVGWIP---------------------------------PMGSQEDAHELLGKLLDELKLDLVNSFtiriFKTTKDK 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1713 V--LGGSFADQKICQgcPHRYECEESFTTlnvdirnhQNLLDSLEQYVkgDLLEGANAyhceKCNKKVDTVKRLL----I 1786
Cdd:COG5533   113 KktSTGDWFDIIIEL--PDQTWVNNLKTL--------QEFIDNMEELV--DDETGVKA----KENEELEVQAKQEyevsF 176

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1787 KKLPPVLAIQLKRFDYDwerecaikfndyfefpreldmepytvAGVAKLEgDNVNPESQLIQQSEQSeSETAGSTKYRLV 1866
Cdd:COG5533   177 VKLPKILTIQLKRFANL--------------------------GGNQKID-TEVDEKFELPVKHDQI-LNIVKETYYDLV 228

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1867 GVLVHSGQASGGHYYSYIiqRNGGDgernrWYKFDDGDVTECKMDDDEEMKNQcfggeymgevfdhmmkrmsyrrqkrww 1946
Cdd:COG5533   229 GFVLHQGSLEGGHYIAYV--KKGGK-----WEKANDSDVTPVSEEEAINEKAK--------------------------- 274


                  ....*....
gi 145309311 1947 NAYILFYER 1955
Cdd:COG5533   275 NAYLYFYER 283
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1683-1923 1.72e-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: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1683 QHDALEFFNSLVDSLDEALKALGHPAMLSK--------VLGGSFADQKICQGcpHRYECEESFTTLNVDIRNHQNLLDSL 1754
Cdd:cd02665    22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEksknpmvqLFYGTFLTEGVLEG--KPFCNCETFGQYPLQVNGYGNLHECL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1755 E-QYVKGDLlEGANAYHCEKCNKkvdtvkRLLIKKLPPVLAIQLKRFDYDWERECaiKFNDYFEFPRELDMEPYtvagva 1833
Cdd:cd02665   100 EaAMFEGEV-ELLPSDHSVKSGQ------ERWFTELPPVLTFELSRFEFNQGRPE--KIHDKLEFPQIIQQVPY------ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1834 klegdnvnpesqliqqseqsesetagstkyRLVGVLVHSGQASGGHYYSYIIQRNggdgeRNRWYKFDDGDVTECkmdDD 1913
Cdd:cd02665   165 ------------------------------ELHAVLVHEGQANAGHYWAYIYKQS-----RQEWEKYNDISVTES---SW 206

                         250
                  ....*....|
gi 145309311 1914 EEMKNQCFGG 1923
Cdd:cd02665   207 EEVERDSFGG 216
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1669-1912 1.93e-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: 78.18  E-value: 1.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1669 KQFRLWGEpvNLREQHDALEFFNSLVDSLDEALKalgHPamlskvLGGSFADQKICQGCPH----RYECeESFTTLNV-- 1742
Cdd:cd02662    22 PSLIEYLE--EFLEQQDAHELFQVLLETLEQLLK---FP------FDGLLASRIVCLQCGEsskvRYES-FTMLSLPVpn 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1743 -DIRNHQNLLDSLEQYVKGDLLEGanaYHCEKCnkkvdtvkRLLIKKLPPVLAIQLKRFDYDwERECAIKFNDYFEFPRE 1821
Cdd:cd02662    90 qSSGSGTTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPER 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1822 LDmepytvagvaklegdnvnpesqliqqseqsesetagSTKYRLVGVLVHSGQASGGHYYSY----IIQRNGGDGE---- 1893
Cdd:cd02662   158 LP------------------------------------KVLYRLRAVVVHYGSHSSGHYVCYrrkpLFSKDKEPGSfvrm 201

                         250       260
                  ....*....|....*....|....*.
gi 145309311 1894 -------RNRWYKFDDGDVTECKMDD 1912
Cdd:cd02662   202 regpsstSHPWWRISDTTVKEVSESE 227
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1750-1955 4.34e-12

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 71.84  E-value: 4.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1750 LLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDweRECAIKFNDYFEFP-RELDMEPYT 1828
Cdd:COG5560   677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSV--RSFRDKIDDLVEYPiDDLDLSGVE 754

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1829 VAgvaklegdnvNPESQLIqqseqsesetagstkYRLVGVLVHSGQASGGHYYSYIiqRNGGDgerNRWYKFDDGDVTEc 1908
Cdd:COG5560   755 YM----------VDDPRLI---------------YDLYAVDNHYGGLSGGHYTAYA--RNFAN---NGWYLFDDSRITE- 803

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 145309311 1909 kMDDDEEMKNqcfggeymgevfdhmmkrmsyrrqkrwwNAYILFYER 1955
Cdd:COG5560   804 -VDPEDSVTS----------------------------SAYVLFYRR 821
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
1557-1902 4.77e-11

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 66.53  E-value: 4.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  1557 VGLKNAGATCYMNSVIQQLYMIPSIRNgiLAIEGTGSDVDD------------DMSGDEKQDN--ESNvdprddvfgypq 1622
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRN--LALSHLATECLKehcllcelgflfDMLEKAKGKNcqASN------------ 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  1623 qFEDkpALSKTEDRKeyNIGVLRHLQVIFGHLAASRL-QYyvprgfWKQFRLwgepvnlrEQ--HDALEFFNSLVDSlde 1699
Cdd:pfam13423   67 -FLR--ALSSIPEAS--ALGLLDEDRETNSAISLSSLiQS------FNRFLL--------DQlsSEENSTPPNPSPA--- 124

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  1700 alkalghPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLN------VDIRNHQNLLDSLEQYVKGDLL-EGANAYHCE 1772
Cdd:pfam13423  125 -------ESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDliyprkPSSNNKKPPNQTFSSILKSSLErETTTKAWCE 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311  1773 KCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWEREcaIKFNDYfeFPRELDMepytvagvaklegdnvnpesqliqQSEQ 1852
Cdd:pfam13423  198 KCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL--WKTPGW--LPPEIGL------------------------TLSD 249

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 145309311  1853 SESETAGSTKYRLVGVLVH-SGQASGGHYYSYI--IQRNGGDGERNRWYKFDD 1902
Cdd:pfam13423  250 DLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVkvADSELEDPTESQWYLFND 302
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1543-1908 2.87e-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: 65.03  E-value: 2.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1543 EYLPpvgprppkGFVGLKNAGATCYMNSVIQQLYMIPSIRNGILaiegtgsdvdddmSGDEKQDNESNVDPRDDVFGypq 1622
Cdd:cd02669   114 PYLP--------GFVGLNNIKNNDYANVIIQALSHVKPIRNFFL-------------LYENYENIKDRKSELVKRLS--- 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1623 qfedkpALSktedRKEYNIGVLRhlqvifGHLAASRLQYYVPRGFWKQFRLwgepvnlREQHDALEFFNSLVDSLdealk 1702
Cdd:cd02669   170 ------ELI----RKIWNPRNFK------GHVSPHELLQAVSKVSKKKFSI-------TEQSDPVEFLSWLLNTL----- 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1703 algHPAmlskvLGGSFAD-----QKICQG---------CPHRYECEES----------------FTTLNVDIRN-----H 1747
Cdd:cd02669   222 ---HKD-----LGGSKKPnssiiHDCFQGkvqietqkiKPHAEEEGSKdkffkdsrvkktsvspFLLLTLDLPPpplfkD 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1748 QNLLDSLEQYVKGDLLEGANAYHCEKCNKKVdtvKRLLIKKLPPVLAIQLKRFDYdwerecaikfNDYF--------EFP 1819
Cdd:cd02669   294 GNEENIIPQVPLKQLLKKYDGKTETELKDSL---KRYLISRLPKYLIFHIKRFSK----------NNFFkeknptivNFP 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1820 RELDMEPYTVAGVAKLEGDnvnpesqliqqseqsesetagSTKYRLVGVLVHSGQASGGHYYSYIIQRNGgdgeRNRWYK 1899
Cdd:cd02669   361 IKNLDLSDYVHFDKPSLNL---------------------STKYNLVANIVHEGTPQEDGTWRVQLRHKS----TNKWFE 415


                  ....*....
gi 145309311 1900 FDDGDVTEC 1908
Cdd:cd02669   416 IQDLNVKEV 424
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1682-1954 3.70e-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: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1682 EQHDALEFFNSLVDSLDealkalgHPAMLSKVlggsfadqKICQGcPHRYECEESFttlnVDIRNHQNLLDSLEQyVKGD 1761
Cdd:cd02670    22 EQQDPEEFFNFITDKLL-------MPLLEPKV--------DIIHG-GKKDQDDDKL----VNERLLQIPVPDDDD-GGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1762 LLEganayHCEKC--NKKVdtvkrllIKKLPPVLAIQLKRfdYDWERECAIKFNDYFEFPRELDMePYTVAGvAKLEGDN 1839
Cdd:cd02670    81 TLE-----QCLEQyfNNSV-------FAKAPSCLIICLKR--YGKTEGKAQKMFKKILIPDEIDI-PDFVAD-DPRACSK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1840 VNPESQlIQQSEQSESETAGSTKYRLVGVLVHSGQA-SGGHYYSYI------IQRNGGDGERNRWYKFDDgdvteckMDD 1912
Cdd:cd02670   145 CQLECR-VCYDDKDFSPTCGKFKLSLCSAVCHRGTSlETGHYVAFVrygsysLTETDNEAYNAQWVFFDD-------MAD 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 145309311 1913 DEemknqcfGGEYmgeVFDHMMKRmsyrrqkRWWNAYILFYE 1954
Cdd:cd02670   217 RD-------GVSN---GFNIPAAR-------LLEDPYMLFYQ 241
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
 900-964 1.02e-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: 45.76  E-value: 1.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309311  900 DDLEVWSHTNDTIGSVRRCILNRIKANVAHtkIELFVGGELIDPADDRKLIGQLNLKDKSLITAK 964
Cdd:cd17065    17 QEFTLEVHSNETLGSVRQKIAERLNCPVDQ--VQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1721-1907 2.47e-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: 45.58  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1721 QKICQGCPHRYECEESFTTLNVDIRNHQNL-----LDSLEQYVKGDL-LEGANAYHCEKCNKKVDTVKRLLIKKLPP--- 1791
Cdd:cd02672    81 SQDQLGTPFSCGTSRNSVSLLYTLSLPLGStktskESTFLQLLKRSLdLEKVTKAWCDTCCKYQPLEQTTSIRHLPDill 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309311 1792 -VLAIQLKRFDydweRECAIKFNDYFEFpreLDMEPytvaGVAKLEGDNVNPESQLIQQSeqsesetagSTKYRLVGVLV 1870
Cdd:cd02672   161 lVLVINLSVTN----GEFDDINVVLPSG---KVMQN----KVSPKAIDHDKLVKNRGQES---------IYKYELVGYVC 220

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 145309311 1871 H-SGQASGGHYYSYIIQRNgGDGERNRWYKFDDGDVTE 1907
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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