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Conserved domains on  [gi|386766827|ref|NP_001247387|]
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fat facets, isoform D [Drosophila melanogaster]

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 ...
 1666-2064 2.02e-146

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: 459.03  E-value: 2.02e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1666 GFCGLKNAGATCYMNSVLQQLYMVPAVRVGILRAhgaattdgedfsgdsdltggglgsalfsgpasalvslpsssstieD 1745
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI---------------------------------------------P 35

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1746 GLHDVRKNYHVVILKHVQAIFAHLGHSALQYYVPRglWTHFKLLGEPVNLREQQDAVEFFMSLLESLDEGLKALGQPQLM 1825
Cdd:cd02659    36 PTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELT--DKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLI 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1826 NATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLP 1905
Cdd:cd02659   114 KNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLP 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1906 PVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEgevvevGDNCQTNVETTKYELTGIVVHSGQASGG 1985
Cdd:cd02659   194 PVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKE------GDSEKKDSESYIYELHGVLVHSGDAHGG 267

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386766827 1986 HYFSYILSKNpangKCQWYKFDDGEVTECKMHEDEEmkaECFGGEYMGETYDNNlkrmqYRRQKRWWNAYMLFYTRCDQ 2064
Cdd:cd02659   268 HYYSYIKDRD----DGKWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYERKSP 334
DUF3517 pfam12030
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ...
 2198-2566 1.41e-95

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: 316.16  E-value: 1.41e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2198 PSRLGEYILMAPSPDVRTVFVKLVVFFCH-----FAINDEPLTGYDGA----NLCEQVLISVLRLL---KSEAADYGKHL 2265
Cdd:pfam12030    1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCDPDDLEeewrSLSDSVLEAVVALLdhlWKEFHTHLRSW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2266 PHYFSLFSMYVGLGTREKQQLLRLN-VPLQFIQVALDDGPGPAIKYQYPE------------FSKLHQVVSHLIRCSDVS 2332
Cdd:pfam12030   81 DEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARmlrlvekrrppsYEKLIQLLSVLLRCCDLS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2333 EKCQSSNQNARPLsnpfkdPNVAHEELTPLSTECMDLL--FNRTG---YIKKVIEDTNVGDEGLKLLQYCSWENPHFSRA 2407
Cdd:pfam12030  161 LPPQSINEGAEPL------PNSLPDGPFPLTSEEADLLrpLGRTNgsiFVKKLLEIDQNPEATRKILRFLLWENPELSDS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2408 VLTELLWQCGFAYCHDMRHhTDLLLNILLIDDSWQHHRIHNALNGVAEEREGLLETIQRAKTHYQKRAYQIIKCLTqLFH 2487
Cdd:pfam12030  235 ILKTLLWGIRGAPAHLLRD-PFLRAAIVFCEDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQCINCRL-GFD 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2488 KSPIALQMLHT------------NSNITRHwsiAVEWLQGELdrqrgigcqyNSYSWSPPAQSNDNTNG----------- 2544
Cdd:pfam12030  313 KEWFASQVLENipdwappllsypDSNVRSE---TEDFLQEEL----------FSHEMGPDPQFRLREAArrlgiacleyl 379

                          410       420
                   ....*....|....*....|....*...
gi 386766827  2545 ---YMLERSQ---SAKNTWSMAFELCPD 2566
Cdd:pfam12030  380 rgtYVLRRSQverSAVETLQRVIELCPE 407
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
 994-1060 6.69e-04

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: 40.76  E-value: 6.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386766827  994 DDMEIVTHSNETMAAFKRNLLKRIKgTSTANIKvdlFYANDEMIGVSDEINPLYQYTIRDKMNLTAK 1060
Cdd:cd17065    17 QEFTLEVHSNETLGSVRQKIAERLN-CPVDQVQ---IFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
 
Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1666-2064 2.02e-146

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: 459.03  E-value: 2.02e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1666 GFCGLKNAGATCYMNSVLQQLYMVPAVRVGILRAhgaattdgedfsgdsdltggglgsalfsgpasalvslpsssstieD 1745
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI---------------------------------------------P 35

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1746 GLHDVRKNYHVVILKHVQAIFAHLGHSALQYYVPRglWTHFKLLGEPVNLREQQDAVEFFMSLLESLDEGLKALGQPQLM 1825
Cdd:cd02659    36 PTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELT--DKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLI 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1826 NATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLP 1905
Cdd:cd02659   114 KNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLP 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1906 PVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEgevvevGDNCQTNVETTKYELTGIVVHSGQASGG 1985
Cdd:cd02659   194 PVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKE------GDSEKKDSESYIYELHGVLVHSGDAHGG 267

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386766827 1986 HYFSYILSKNpangKCQWYKFDDGEVTECKMHEDEEmkaECFGGEYMGETYDNNlkrmqYRRQKRWWNAYMLFYTRCDQ 2064
Cdd:cd02659   268 HYYSYIKDRD----DGKWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYERKSP 334
DUF3517 pfam12030
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ...
 2198-2566 1.41e-95

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: 316.16  E-value: 1.41e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2198 PSRLGEYILMAPSPDVRTVFVKLVVFFCH-----FAINDEPLTGYDGA----NLCEQVLISVLRLL---KSEAADYGKHL 2265
Cdd:pfam12030    1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCDPDDLEeewrSLSDSVLEAVVALLdhlWKEFHTHLRSW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2266 PHYFSLFSMYVGLGTREKQQLLRLN-VPLQFIQVALDDGPGPAIKYQYPE------------FSKLHQVVSHLIRCSDVS 2332
Cdd:pfam12030   81 DEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARmlrlvekrrppsYEKLIQLLSVLLRCCDLS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2333 EKCQSSNQNARPLsnpfkdPNVAHEELTPLSTECMDLL--FNRTG---YIKKVIEDTNVGDEGLKLLQYCSWENPHFSRA 2407
Cdd:pfam12030  161 LPPQSINEGAEPL------PNSLPDGPFPLTSEEADLLrpLGRTNgsiFVKKLLEIDQNPEATRKILRFLLWENPELSDS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2408 VLTELLWQCGFAYCHDMRHhTDLLLNILLIDDSWQHHRIHNALNGVAEEREGLLETIQRAKTHYQKRAYQIIKCLTqLFH 2487
Cdd:pfam12030  235 ILKTLLWGIRGAPAHLLRD-PFLRAAIVFCEDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQCINCRL-GFD 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2488 KSPIALQMLHT------------NSNITRHwsiAVEWLQGELdrqrgigcqyNSYSWSPPAQSNDNTNG----------- 2544
Cdd:pfam12030  313 KEWFASQVLENipdwappllsypDSNVRSE---TEDFLQEEL----------FSHEMGPDPQFRLREAArrlgiacleyl 379

                          410       420
                   ....*....|....*....|....*...
gi 386766827  2545 ---YMLERSQ---SAKNTWSMAFELCPD 2566
Cdd:pfam12030  380 rgtYVLRRSQverSAVETLQRVIELCPE 407
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1668-2059 1.98e-78

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 262.76  E-value: 1.98e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  1668 CGLKNAGATCYMNSVLQQLYMVPAVRVGILRAHGAATTDGEDFSGDsdltggglgsalfsgpasalvslpsssstiedgl 1747
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------------------------------- 46

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  1748 hdvrknyhvvILKHVQAIFAHL-GHSALQYYVPRGLWTHFKLLGEPVNLREQQDAVEFFMSLLESLDEGLKA---LGQPQ 1823
Cdd:pfam00443   47 ----------LLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENES 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  1824 LMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLT------ESLEQYVKGELLEGADAYHCDKCDKKVVTVK 1897
Cdd:pfam00443  117 LITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIK 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  1898 RVCVKKLPPVLAIQLKRFEYDYErvCAIKFNDYFEFPRILDMEPYTVSGLAKLEGEVVevgdncqtnvettKYELTGIVV 1977
Cdd:pfam00443  197 QLKISRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ-------------DYRLVAVVV 261

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  1978 HSGQASGGHYFSYIlsKNPANGKcqWYKFDDGEVTECKMHEDEEMkaecfggeymgetydnnlkrmqyrrqkrwWNAYML 2057
Cdd:pfam00443  262 HSGSLSSGHYIAYI--KAYENNR--WYKFDDEKVTEVDEETAVLS-----------------------------SSAYIL 308


                   ..
gi 386766827  2058 FY 2059
Cdd:pfam00443  309 FY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 1666-2117 5.12e-37

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 153.87  E-value: 5.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1666 GFCGLKNAGATCYMNSVLQQLYMVPAVRVGILRAhgaaTTDGEDfsgdsdltggglgsalfsGPASALVSLPSSSSTIED 1745
Cdd:COG5077   192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI----PTDHPR------------------GRDSVALALQRLFYNLQT 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1746 GLHDVrknyhvvilkhvqaifahlghSALQYYVPRGlWTHFKLLgepvnlrEQQDAVEFFMSLLESLDEGLKALGQPQLM 1825
Cdd:COG5077   250 GEEPV---------------------DTTELTRSFG-WDSDDSF-------MQHDIQEFNRVLQDNLEKSMRGTVVENAL 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1826 NATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDK---CDKKvvtvKRVCVK 1902
Cdd:COG5077   301 NGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEKhglQDAK----KGVIFE 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1903 KLPPVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEGEVVEvgdncqtnvettkYELTGIVVHSGQA 1982
Cdd:COG5077   377 SLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRDADKSENSDAV-------------YVLYGVLVHSGDL 443

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1983 SGGHYFSYIlsKNPANGkcQWYKFDDGEVTECKMHEDEEmkaECFGGEYMgetYDNNLKRMQyrRQKRWWNAYMLFYTRC 2062
Cdd:COG5077   444 HEGHYYALL--KPEKDG--RWYKFDDTRVTRATEKEVLE---ENFGGDHP---YKDKIRDHS--GIKRFMSAYMLVYLRK 511

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386766827 2063 DQ-----TPVQYE---PSVEQlSLAESRNMVLPLPKPIERSVRHQNIRFLHSRSIFSVEFFNF 2117
Cdd:COG5077   512 SMlddllNPVAAVdipPHVEE-VLSEEIDKTEVRCKEIDEIHLYRGVRLYTIDSFIHYHGFDY 573
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
 994-1060 6.69e-04

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: 40.76  E-value: 6.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386766827  994 DDMEIVTHSNETMAAFKRNLLKRIKgTSTANIKvdlFYANDEMIGVSDEINPLYQYTIRDKMNLTAK 1060
Cdd:cd17065    17 QEFTLEVHSNETLGSVRQKIAERLN-CPVDQVQ---IFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
 
Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1666-2064 2.02e-146

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: 459.03  E-value: 2.02e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1666 GFCGLKNAGATCYMNSVLQQLYMVPAVRVGILRAhgaattdgedfsgdsdltggglgsalfsgpasalvslpsssstieD 1745
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI---------------------------------------------P 35

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1746 GLHDVRKNYHVVILKHVQAIFAHLGHSALQYYVPRglWTHFKLLGEPVNLREQQDAVEFFMSLLESLDEGLKALGQPQLM 1825
Cdd:cd02659    36 PTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELT--DKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLI 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1826 NATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLP 1905
Cdd:cd02659   114 KNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLP 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1906 PVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEgevvevGDNCQTNVETTKYELTGIVVHSGQASGG 1985
Cdd:cd02659   194 PVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKE------GDSEKKDSESYIYELHGVLVHSGDAHGG 267

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386766827 1986 HYFSYILSKNpangKCQWYKFDDGEVTECKMHEDEEmkaECFGGEYMGETYDNNlkrmqYRRQKRWWNAYMLFYTRCDQ 2064
Cdd:cd02659   268 HYYSYIKDRD----DGKWYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYERKSP 334
DUF3517 pfam12030
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ...
 2198-2566 1.41e-95

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: 316.16  E-value: 1.41e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2198 PSRLGEYILMAPSPDVRTVFVKLVVFFCH-----FAINDEPLTGYDGA----NLCEQVLISVLRLL---KSEAADYGKHL 2265
Cdd:pfam12030    1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCDPDDLEeewrSLSDSVLEAVVALLdhlWKEFHTHLRSW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2266 PHYFSLFSMYVGLGTREKQQLLRLN-VPLQFIQVALDDGPGPAIKYQYPE------------FSKLHQVVSHLIRCSDVS 2332
Cdd:pfam12030   81 DEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARmlrlvekrrppsYEKLIQLLSVLLRCCDLS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2333 EKCQSSNQNARPLsnpfkdPNVAHEELTPLSTECMDLL--FNRTG---YIKKVIEDTNVGDEGLKLLQYCSWENPHFSRA 2407
Cdd:pfam12030  161 LPPQSINEGAEPL------PNSLPDGPFPLTSEEADLLrpLGRTNgsiFVKKLLEIDQNPEATRKILRFLLWENPELSDS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2408 VLTELLWQCGFAYCHDMRHhTDLLLNILLIDDSWQHHRIHNALNGVAEEREGLLETIQRAKTHYQKRAYQIIKCLTqLFH 2487
Cdd:pfam12030  235 ILKTLLWGIRGAPAHLLRD-PFLRAAIVFCEDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQCINCRL-GFD 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  2488 KSPIALQMLHT------------NSNITRHwsiAVEWLQGELdrqrgigcqyNSYSWSPPAQSNDNTNG----------- 2544
Cdd:pfam12030  313 KEWFASQVLENipdwappllsypDSNVRSE---TEDFLQEEL----------FSHEMGPDPQFRLREAArrlgiacleyl 379

                          410       420
                   ....*....|....*....|....*...
gi 386766827  2545 ---YMLERSQ---SAKNTWSMAFELCPD 2566
Cdd:pfam12030  380 rgtYVLRRSQverSAVETLQRVIELCPE 407
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1668-2059 1.98e-78

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 262.76  E-value: 1.98e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  1668 CGLKNAGATCYMNSVLQQLYMVPAVRVGILRAHGAATTDGEDFSGDsdltggglgsalfsgpasalvslpsssstiedgl 1747
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------------------------------- 46

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  1748 hdvrknyhvvILKHVQAIFAHL-GHSALQYYVPRGLWTHFKLLGEPVNLREQQDAVEFFMSLLESLDEGLKA---LGQPQ 1823
Cdd:pfam00443   47 ----------LLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENES 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  1824 LMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLT------ESLEQYVKGELLEGADAYHCDKCDKKVVTVK 1897
Cdd:pfam00443  117 LITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIK 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  1898 RVCVKKLPPVLAIQLKRFEYDYErvCAIKFNDYFEFPRILDMEPYTVSGLAKLEGEVVevgdncqtnvettKYELTGIVV 1977
Cdd:pfam00443  197 QLKISRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ-------------DYRLVAVVV 261

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  1978 HSGQASGGHYFSYIlsKNPANGKcqWYKFDDGEVTECKMHEDEEMkaecfggeymgetydnnlkrmqyrrqkrwWNAYML 2057
Cdd:pfam00443  262 HSGSLSSGHYIAYI--KAYENNR--WYKFDDEKVTEVDEETAVLS-----------------------------SSAYIL 308


                   ..
gi 386766827  2058 FY 2059
Cdd:pfam00443  309 FY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 1795-2059 5.64e-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: 5.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1795 LREQQDAVEFFMSLLESLDEGLKALG--------QPQLMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDI----RNH 1862
Cdd:cd02257    19 FSEQQDAHEFLLFLLDKLHEELKKSSkrtsdsssLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1863 SSLTESLEQYVKGELLEGADAYHCDKCdKKVVTVKRVCVKKLPPVLAIQLKRFEYDyERVCAIKFNDYFEFPRILDMEPY 1942
Cdd:cd02257    99 VSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPY 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1943 TVSGlaklegevvevGDNCQTNVETTKYELTGIVVHSGQ-ASGGHYFSYILSKNpangKCQWYKFDDGEVTECKMHEDEE 2021
Cdd:cd02257   177 LSEG-----------EKDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPS----DGKWYKFNDDKVTEVSEEEVLE 241

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 386766827 2022 MkaecfggeymgetydnnlkrmqyrrQKRWWNAYMLFY 2059
Cdd:cd02257   242 F-------------------------GSLSSSAYILFY 254
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1669-2060 2.22e-50

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: 182.62  E-value: 2.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1669 GLKNAGATCYMNSVLQQLYMVPAVRvgilrahgaattdgedfsgdsdltggglgsalfsgpaSALVSLPSSSSTIEDGLH 1748
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFR-------------------------------------KAVYECNSTEDAELKNMP 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1749 DVRKNYHVVILKHVQAIFAHLGHSALQYYVPRGLwthFKLLGepVNLREQQDAVEF---FMSLLESLDEGLKALGQPQLM 1825
Cdd:cd02668    44 PDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGF---VKALG--LDTGQQQDAQEFsklFLSLLEAKLSKSKNPDLKNIV 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1826 NATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLP 1905
Cdd:cd02668   119 QDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLP 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1906 PVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYtvsglaklegevvevGDNCQTNVETtkYELTGIVVHSGQ-ASG 1984
Cdd:cd02668   199 PTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEY---------------LAESDEGSYV--YELSGVLIHQGVsAYS 261

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1985 GHYFSYIlsKNPANGKcqWYKFDDGEVTEC--KMHED--EEMKAECFGGEYMGETYDNNlkrmqyrrqkrwwNAYMLFYT 2060
Cdd:cd02668   262 GHYIAHI--KDEQTGE--WYKFNDEDVEEMpgKPLKLgnSEDPAKPRKSEIKKGTHSSR-------------TAYMLVYK 324
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1668-2018 2.74e-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: 164.37  E-value: 2.74e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1668 CGLKNAGATCYMNSVLQQLYMVPAVrvgilrahgaattdgedfsgdsdltggglgsalfsgpASALVSlpsssstiedGL 1747
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPL-------------------------------------ANYLLS----------RE 34

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1748 HDVRKNYHVV-----ILKHVQAIFAHLGHSalqyYVPRGLWTHFKLLGEPVNLREQQDAVEFFMSLLES-----LDEGLK 1817
Cdd:cd02661    35 HSKDCCNEGFcmmcaLEAHVERALASSGPG----SAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAmqkacLDRFKK 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1818 ALGQPQLMNAT------LGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDK 1891
Cdd:cd02661   111 LKAVDPSSQETtlvqqiFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKK 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1892 KVVTVKRVCVKKLPPVLAIQLKRFEYDYERvcaiKFNDYFEFPRILDMEPYTVsglaklegevvevgdncQTNVETTKYE 1971
Cdd:cd02661   191 KVKASKQLTIHRAPNVLTIHLKRFSNFRGG----KINKQISFPETLDLSPYMS-----------------QPNDGPLKYK 249

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 386766827 1972 LTGIVVHSG-QASGGHYFSYILSknpANGkcQWYKFDDGEVTECKMHE 2018
Cdd:cd02661   250 LYAVLVHSGfSPHSGHYYCYVKS---SNG--KWYNMDDSKVSPVSIET 292
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1797-2060 7.38e-39

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: 145.89  E-value: 7.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1797 EQQDAVEFFMSLLESLDEGLKALGQPQLMNATlggsfsdqkICQECPHRYSKEEPFSVFSVDI------RNHSSLTESLE 1870
Cdd:cd02674    21 DQQDAQEFLLFLLDGLHSIIVDLFQGQLKSRL---------TCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLEDCLR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1871 QYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERvcAIKFNDYFEFP-RILDMEPYTVSGlak 1949
Cdd:cd02674    92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGS--TRKLTTPVTFPlNDLDLTPYVDTR--- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1950 legevvevgdnCQTNVetTKYELTGIVVHSGQASGGHYFSYIlsKNPANGkcQWYKFDDGEVTecKMHEDEEMKAecfgg 2029
Cdd:cd02674   167 -----------SFTGP--FKYDLYAVVNHYGSLNGGHYTAYC--KNNETN--DWYKFDDSRVT--KVSESSVVSS----- 222

                         250       260       270
                  ....*....|....*....|....*....|.
gi 386766827 2030 eymgetydnnlkrmqyrrqkrwwNAYMLFYT 2060
Cdd:cd02674   223 -----------------------SAYILFYE 230
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1669-2027 1.83e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 148.29  E-value: 1.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1669 GLKNAGATCYMNSVLQQLYMVPavrvgILRAHgaattdgedfsgdsdltggglgsaLFSGPASALVSLPSSSSTIEDGLH 1748
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNP-----LLRNY------------------------FLSDRHSCTCLSCSPNSCLSCAMD 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1749 DVRKNYHVViLKHVQAIFAHLGHSAlqyyvprglWTHFKLLGEpvnlREQQDAVEFFMSLLESLDEG-LKALGQPQLMNA 1827
Cdd:cd02660    53 EIFQEFYYS-GDRSPYGPINLLYLS---------WKHSRNLAG----YSQQDAHEFFQFLLDQLHTHyGGDKNEANDESH 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1828 -------TLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHS---------------SLTESLEQYVKGELLeGADAYH 1885
Cdd:cd02660   119 cnciihqTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKStpswalgesgvsgtpTLSDCLDRFTRPEKL-GDFAYK 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1886 CDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVCAiKFNDYFEFPRILDMEPYTVSGLAKLEGEVVEVGDNcqtnv 1965
Cdd:cd02660   198 CSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSR-KIDTYVQFPLELNMTPYTSSSIGDTQDSNSLDPDY----- 271

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386766827 1966 ettKYELTGIVVHSGQASGGHYFSYIlsknpANGKCQWYKFDDGEVTECKmhEDEEMKAECF 2027
Cdd:cd02660   272 ---TYDLFAVVVHKGTLDTGHYTAYC-----RQGDGQWFKFDDAMITRVS--EEEVLKSQAY 323
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 1666-2117 5.12e-37

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 153.87  E-value: 5.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1666 GFCGLKNAGATCYMNSVLQQLYMVPAVRVGILRAhgaaTTDGEDfsgdsdltggglgsalfsGPASALVSLPSSSSTIED 1745
Cdd:COG5077   192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI----PTDHPR------------------GRDSVALALQRLFYNLQT 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1746 GLHDVrknyhvvilkhvqaifahlghSALQYYVPRGlWTHFKLLgepvnlrEQQDAVEFFMSLLESLDEGLKALGQPQLM 1825
Cdd:COG5077   250 GEEPV---------------------DTTELTRSFG-WDSDDSF-------MQHDIQEFNRVLQDNLEKSMRGTVVENAL 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1826 NATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDK---CDKKvvtvKRVCVK 1902
Cdd:COG5077   301 NGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEKhglQDAK----KGVIFE 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1903 KLPPVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEGEVVEvgdncqtnvettkYELTGIVVHSGQA 1982
Cdd:COG5077   377 SLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRDADKSENSDAV-------------YVLYGVLVHSGDL 443

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1983 SGGHYFSYIlsKNPANGkcQWYKFDDGEVTECKMHEDEEmkaECFGGEYMgetYDNNLKRMQyrRQKRWWNAYMLFYTRC 2062
Cdd:COG5077   444 HEGHYYALL--KPEKDG--RWYKFDDTRVTRATEKEVLE---ENFGGDHP---YKDKIRDHS--GIKRFMSAYMLVYLRK 511

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386766827 2063 DQ-----TPVQYE---PSVEQlSLAESRNMVLPLPKPIERSVRHQNIRFLHSRSIFSVEFFNF 2117
Cdd:COG5077   512 SMlddllNPVAAVdipPHVEE-VLSEEIDKTEVRCKEIDEIHLYRGVRLYTIDSFIHYHGFDY 573
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1798-2060 1.53e-31

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 127.04  E-value: 1.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1798 QQDAVEFFMSLLESLDEGLKALGQPQL--------MNATLG---------GSFSDQKICQECPHRYSKEEPFSVFSVDIR 1860
Cdd:cd02663    65 HQDAHEFLNFLLNEIAEILDAERKAEKanrklnnnNNAEPQptwvheifqGILTNETRCLTCETVSSRDETFLDLSIDVE 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1861 NHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVCAIKFNDYFEFPriLDME 1940
Cdd:cd02663   145 QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFP--LELR 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1941 PYTVSGLAKlegevvevgDNCQTnvettkYELTGIVVHSGQ-ASGGHYFSYILSKNpangkcQWYKFDDGEVTECkmheD 2019
Cdd:cd02663   223 LFNTTDDAE---------NPDRL------YELVAVVVHIGGgPNHGHYVSIVKSHG------GWLLFDDETVEKI----D 277

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 386766827 2020 EEMKAECFGGEymgetydNNLKrmqyrrqkrwwNAYMLFYT 2060
Cdd:cd02663   278 ENAVEEFFGDS-------PNQA-----------TAYVLFYQ 300
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1669-2015 4.26e-30

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 123.76  E-value: 4.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1669 GLKNAGATCYMNSVLQQLYMVPAVRVGILRahgaattdgedfsgdsdltggglgsalfsgpasalvslpsssstiedgLH 1748
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS------------------------------------------------LN 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1749 DVRKNYHVVILKHVQAIFAHLGHSALQYYVPRGLWTHfKLLGEPVNLREQQDAVEFFMSLLESLDeglkalgqpQLMNAT 1828
Cdd:cd02664    33 LPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLE-ASRPPWFTPGSQQDCSEYLRYLLDRLH---------TLIEKM 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1829 LGGSFSDQKICQECPHRYSKEEPFSVFSVDIrnhSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLPPVL 1908
Cdd:cd02664   103 FGGKLSTTIRCLNCNSTSARTERFRDLDLSF---PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYL 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1909 AIQLKRFEYDYERVCAIKFNDYFEFPRILDMePYTV------SGLAKLEGEVVEVGDNCqtnVETTKYELTGIVVHSGQA 1982
Cdd:cd02664   180 ILTLLRFSYDQKTHVREKIMDNVSINEVLSL-PVRVesksseSPLEKKEEESGDDGELV---TRQVHYRLYAVVVHSGYS 255

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 386766827 1983 S-GGHYFSYILSKNPANGKCQ----------------WYKFDDGEVTECK 2015
Cdd:cd02664   256 SeSGHYFTYARDQTDADSTGQecpepkdaeendesknWYLFNDSRVTFSS 305
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1798-2059 5.41e-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: 113.25  E-value: 5.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1798 QQDAVEFFMSLLESLDEGLKALgqpqlmnatLGGSFSDQKICQECPHRYSKEEPFSVFS----VDIRNHSSLTESLEQYV 1873
Cdd:cd02667    51 QQDSHELLRYLLDGLRTFIDSI---------FGGELTSTIMCESCGTVSLVYEPFLDLSlprsDEIKSECSIESCLKQFT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1874 KGELLEGADAYHCDKCDKkvvTVKRVCVKKLPPVLAIQLKRFEYDyERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEGE 1953
Cdd:cd02667   122 EVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPFCDPKCNSSEDK 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1954 vvevgdncqtnvETTKYELTGIVVHSGQASGGHYFSYILSKNP-----------------ANGKCQWYKFDDGEVTEckM 2016
Cdd:cd02667   198 ------------SSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPqqrlsdltkskpaadeaGPGSGQWYYISDSDVRE--V 263

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 386766827 2017 HEDEEMKAEcfggeymgetydnnlkrmqyrrqkrwwnAYMLFY 2059
Cdd:cd02667   264 SLEEVLKSE----------------------------AYLLFY 278
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1669-2023 1.06e-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 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: 98.55  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1669 GLKNAGATCYMNSVLQQLYMVPAV--RVGILRAHGAATTDGEDFSGDSDLTGggLGSALFSGPASALVSLPSSSSTIEDG 1746
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFqwRYDDLENKFPSDVVDPANDLNCQLIK--LADGLLSGRYSKPASLKSENDPYQVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1747 LHdvrknyhvvilkhvqaifahlghsalqyyvPRGlwthFK-LLGEpvNLRE-----QQDAVEFFMSLLESLDEGLKALG 1820
Cdd:cd02658    79 IK------------------------------PSM----FKaLIGK--GHPEfstmrQQDALEFLLHLIDKLDRESFKNL 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1821 QPQLMNatLGGSFSDQKI-CQECPHRYSKEEPFSVFSVDIRNHS--------------SLTESLEQYVKGELLEgadaYH 1885
Cdd:cd02658   123 GLNPND--LFKFMIEDRLeCLSCKKVKYTSELSEILSLPVPKDEatekeegelvyepvPLEDCLKAYFAPETIE----DF 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1886 CDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVcaikfndyfefPRILDMEpytvsglaklegevVEVGDncqtNV 1965
Cdd:cd02658   197 CSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWV-----------PKKLDVP--------------IDVPE----EL 247

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386766827 1966 ETTKYELTGIVVHSG-QASGGHYFSYIlsKNPANGKCQWYKFDDGEVTECKmhEDEEMK 2023
Cdd:cd02658   248 GPGKYELIAFISHKGtSVHSGHYVAHI--KKEIDGEGKWVLFNDEKVVASQ--DPPEMK 302
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1669-2031 1.23e-19

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: 92.39  E-value: 1.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1669 GLKNAGATCYMNSVLQQLYMVPAVRvGILRAHGAATTDGEDFSGDsdltggglgsaLFSGPASALVSLPSSSSTIedglh 1748
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELR-DALKNYNPARRGANQSSDN-----------LTNALRDLFDTMDKKQEPV----- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1749 dvrknyhvvilkhVQAIFAHLGHSALQYYVPRGLWTHFKllgepvnlreQQDAVEFFMSLLESLDEGLK-ALGQPQLMNA 1827
Cdd:cd02657    64 -------------PPIEFLQLLRMAFPQFAEKQNQGGYA----------QQDAEECWSQLLSVLSQKLPgAGSKGSFIDQ 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1828 TLGGSFSDQKICQECPHRYSKE-EPFSVFSVDIrNHSSLTESLEQYVKgELLEGADAYHCDKCDKKVVTVKRVCVKKLPP 1906
Cdd:cd02657   121 LFGIELETKMKCTESPDEEEVStESEYKLQCHI-SITTEVNYLQDGLK-KGLEEEIEKHSPTLGRDAIYTKTSRISRLPK 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1907 VLAIQLKRFEYDYERVCAIKFNDYFEFPRILDM-EPYTVSGLaklegevvevgdncqtnvettkYELTGIVVHSGQ-ASG 1984
Cdd:cd02657   199 YLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLyELCTPSGY----------------------YELVAVITHQGRsADS 256

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 386766827 1985 GHYFSYILSKNPAngkcQWYKFDDGEVTEckmHEDEEMKAECFGGEY 2031
Cdd:cd02657   257 GHYVAWVRRKNDG----KWIKFDDDKVSE---VTEEDILKLSGGGDW 296
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1667-2021 8.96e-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: 84.17  E-value: 8.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1667 FCGLKNAGATCYMNSVLQQLYMVPAVRVGIlrahgaattdgedfsgdsdltggglgsalfsgpaSALVSLPSSSSTIEDG 1746
Cdd:cd02671    24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGL----------------------------------KHLVSLISSVEQLQSS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1747 LHDVRKNYHvvilkhvqaifahlghSALQYYVPRGLWTHFKLLGEPVNLREQQDAVEFFMSLLESLDEGLKALGQPQLMN 1826
Cdd:cd02671    70 FLLNPEKYN----------------DELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEKDFQGQLVL 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1827 ATLggsfsdqkiCQECPHRYSKEEPFSVFSVDIR--NHSSLTESLE-----------------QYVKGELLEGADAYHCD 1887
Cdd:cd02671   134 RTR---------CLECETFTERREDFQDISVPVQesELSKSEESSEispdpktemktlkwaisQFASVERIVGEDKYFCE 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1888 KCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVCAI----KFNDYFEFPRILDMEpytvsglaklegevvEVGDNCQT 1963
Cdd:cd02671   205 NCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVNTPLLTPLKLSLE---------------EWSTKPKN 269

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386766827 1964 NVettkYELTGIVVHSG-QASGGHYFSYIlsknpangkcQWYKFDDGEVtecKMHEDEE 2021
Cdd:cd02671   270 DV----YRLFAVVMHSGaTISSGHYTAYV----------RWLLFDDSEV---KVTEEKD 311
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1794-2015 3.85e-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: 77.41  E-value: 3.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1794 NLREQQDAVEFFMSLLESLDEGLKalgQPqlmnatLGGSFSDQKICQECPHRYS-KEEPFSVFSVDIRNHS-----SLTE 1867
Cdd:cd02662    30 EFLEQQDAHELFQVLLETLEQLLK---FP------FDGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSsgsgtTLEH 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1868 SLEQYVKGELLEGadaYHCDKCDKKVVtvkrvcvkKLPPVLAIQLKRFEYDyERVCAIKFNDYFEFPRILDmepytvsgl 1947
Cdd:cd02662   101 CLDDFLSTEIIDD---YKCDRCQTVIV--------RLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPERLP--------- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1948 aklegevvevgdncqtnveTTKYELTGIVVHSGQASGGHYFSY----------------ILSKNPANGKCQWYKFDDGEV 2011
Cdd:cd02662   160 -------------------KVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvRMREGPSSTSHPWWRISDTTV 220


                  ....
gi 386766827 2012 TECK 2015
Cdd:cd02662   221 KEVS 224
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1853-2062 3.00e-14

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 79.16  E-value: 3.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1853 SVFSVD-------IRNHS---SLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERv 1922
Cdd:COG5560   655 SLFSYDplwtireIGAAErtiTLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF- 733

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1923 cAIKFNDYFEFPRI-LDMEPYTVSGLAKLEGevvevgdncqtnvettkYELTGIVVHSGQASGGHYFSYIlsKNPANGkc 2001
Cdd:COG5560   734 -RDKIDDLVEYPIDdLDLSGVEYMVDDPRLI-----------------YDLYAVDNHYGGLSGGHYTAYA--RNFANN-- 791

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386766827 2002 QWYKFDDGEVTECkmhEDEEMKAEcfggeymgetydnnlkrmqyrrqkrwwNAYMLFYTRC 2062
Cdd:COG5560   792 GWYLFDDSRITEV---DPEDSVTS---------------------------SAYVLFYRRK 822
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1669-2061 7.20e-14

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 74.84  E-value: 7.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1669 GLKNAGATCYMNSVLQQLYMvpavrvgilrahgaattdgedfsgdsdltggglgsalfsgpasalvSLPSSSSTIEDGLh 1748
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAL----------------------------------------------YLPKLDELLDDLS- 33

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1749 dvrKNYHVVILKHVQaifahlGHSALQY----YVPRGLWTHFKLLGEPVNLRE-QQDAVEFFMSLLESLdeglkalgqpq 1823
Cdd:COG5533    34 ---KELKVLKNVIRK------PEPDLNQeealKLFTALWSSKEHKVGWIPPMGsQEDAHELLGKLLDEL----------- 93

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1824 lmNATLGGSFSDQ--KICQECPHRYSKeepfSVFSVDIrnhsSLTEslEQYVKG-----ELLEGADAYHCDKCDKKVVT- 1895
Cdd:COG5533    94 --KLDLVNSFTIRifKTTKDKKKTSTG----DWFDIII----ELPD--QTWVNNlktlqEFIDNMEELVDDETGVKAKEn 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1896 -----VKR----VCVKKLPPVLAIQLKRFEYDyervcaikfndyfefprildmepytvSGLAKLEGEVVE------VGDN 1960
Cdd:COG5533   162 eelevQAKqeyeVSFVKLPKILTIQLKRFANL--------------------------GGNQKIDTEVDEkfelpvKHDQ 215

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1961 CQTNVETTKYELTGIVVHSGQASGGHYFSYILSKNpangkcQWYKFDDGEVTECKMHEDEEMKAEcfggeymgetydnnl 2040
Cdd:COG5533   216 ILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKKGG------KWEKANDSDVTPVSEEEAINEKAK--------------- 274

                         410       420
                  ....*....|....*....|.
gi 386766827 2041 krmqyrrqkrwwNAYMLFYTR 2061
Cdd:COG5533   275 ------------NAYLYFYER 283
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1798-2029 2.50e-13

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 71.82  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1798 QQDAVEFFMSLLESLDEGLK-ALGQPQLMNATLG-------GSFSDQKICQEcpHRYSKEEPFSVFSVDIRNHSSLTESL 1869
Cdd:cd02665    22 QQDVSEFTHLLLDWLEDAFQaAAEAISPGEKSKNpmvqlfyGTFLTEGVLEG--KPFCNCETFGQYPLQVNGYGNLHECL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1870 EqyvkGELLEG-ADAyhcDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVCaiKFNDYFEFPRILDMEPytvsgla 1948
Cdd:cd02665   100 E----AAMFEGeVEL---LPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPE--KIHDKLEFPQIIQQVP------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1949 klegevvevgdncqtnvettkYELTGIVVHSGQASGGHYFSYILSKNpangKCQWYKFDDGEVTECKMhedEEMKAECFG 2028
Cdd:cd02665   164 ---------------------YELHAVLVHEGQANAGHYWAYIYKQS----RQEWEKYNDISVTESSW---EEVERDSFG 215


                  .
gi 386766827 2029 G 2029
Cdd:cd02665   216 G 216
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
1669-2008 1.09e-09

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 62.29  E-value: 1.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  1669 GLKNAGATCYMNSVLQQLYMVPAVRVGILrAHgAATTDGEDFSGDSDLtggGLgsaLFsgpasalvslpsssstieDGLH 1748
Cdd:pfam13423    2 GLETHIPNSYTNSLLQLLRFIPPLRNLAL-SH-LATECLKEHCLLCEL---GF---LF------------------DMLE 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  1749 DVRKnyhvvilKHVQA-----IFAHL-GHSALqyyvprGLWTHFKLLGEPVNLREQQDAVEFFmsLLESL-DEGLKALGQ 1821
Cdd:pfam13423   56 KAKG-------KNCQAsnflrALSSIpEASAL------GLLDEDRETNSAISLSSLIQSFNRF--LLDQLsSEENSTPPN 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  1822 PQ----LMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTES----------LEQYVKGELLEGAdayHCD 1887
Cdd:pfam13423  121 PSpaesPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYPRKPSSNNKkppnqtfssiLKSSLERETTTKA---WCE 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827  1888 KCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVCAikfndyfefprildmepyTVSGLAKlegEV-VEVGDNCQTNVE 1966
Cdd:pfam13423  198 KCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWK------------------TPGWLPP---EIgLTLSDDLQGDNE 256

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 386766827  1967 TTKYELTGIVVH-SGQASGGHYFSYI---LSKNPANGKCQWYKFDD 2008
Cdd:pfam13423  257 IVKYELRGVVVHiGDSGTSGHLVSFVkvaDSELEDPTESQWYLFND 302
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1669-2021 1.16e-09

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: 62.89  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1669 GLKNAGATCYMNSVLQQLYMVPAVRVGILRAHGaattDGEDFSGDSDLTggglgsALFSGPASALVSLPSSSSTIedglH 1748
Cdd:cd02666     3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDE----SKAELASDYPTE------RRIGGREVSRSELQRSNQFV----Y 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1749 DVRKnyhvvilkhvqaIFAHLGHSALQYYVPRGLWTHFKLLgepvnlreQQDAVEFFMSLLESLDEGLKALGQPQLMNAT 1828
Cdd:cd02666    69 ELRS------------LFNDLIHSNTRSVTPSKELAYLALR--------QQDVTECIDNVLFQLEVALEPISNAFAGPDT 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1829 -LGGSFSDQ-------KICQ--------ECPHRYSKEEPFSVFSVDIR---------NHS-SLTESLEQYVKGELLEgad 1882
Cdd:cd02666   129 eDDKEQSDLikrlfsgKTKQqlvpesmgNQPSVRTKTERFLSLLVDVGkkgreivvlLEPkDLYDALDRYFDYDSLT--- 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1883 ayhcdkcdkkvvtvkrvcvkKLPPVLAIQLKrfeydyervcaikfNDYFEFPRILDMEPYT----VSGLAKLEGEVVEVG 1958
Cdd:cd02666   206 --------------------KLPQRSQVQAQ--------------LAQPLQRELISMDRYElpssIDDIDELIREAIQSE 251

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1959 DNCQTNVETTK------------------YELTGIVVHSGQASGGHYFSYIlsKNPANGkcQWYKFDDGEVTEckmHEDE 2020
Cdd:cd02666   252 SSLVRQAQNELaelkheiekqfddlksygYRLHAVFIHRGEASSGHYWVYI--KDFEEN--VWRKYNDETVTV---VPAS 324


                  .
gi 386766827 2021 E 2021
Cdd:cd02666   325 E 325
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1654-2014 8.00e-08

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 57.71  E-value: 8.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1654 DYLPpvgarptkGFCGLKNAGATCYMNSVLQQLYMVPAVRvgilrahgaattdgeDF--SGDSDLTGGGLgsalfsgpAS 1731
Cdd:cd02669   114 PYLP--------GFVGLNNIKNNDYANVIIQALSHVKPIR---------------NFflLYENYENIKDR--------KS 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1732 ALVSLPSSSstiedglhdVRKNYHVVILK-HVQAifahlgHSALQYYVprglwthfKLLGEPVNLREQQDAVEFFMSLLE 1810
Cdd:cd02669   163 ELVKRLSEL---------IRKIWNPRNFKgHVSP------HELLQAVS--------KVSKKKFSITEQSDPVEFLSWLLN 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1811 SLdegLKALGqpqlmnatlGGSFSDQKICQEC-------------PHRYSKEEPFSVFSVDIRNHSSLT----------- 1866
Cdd:cd02669   220 TL---HKDLG---------GSKKPNSSIIHDCfqgkvqietqkikPHAEEEGSKDKFFKDSRVKKTSVSpfllltldlpp 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1867 ----------ESLEQYVKGELLegadayhcDKCDKKVVT-----VKRVCVKKLPPVLAIQLKRFEYdyervcaikfNDYF 1931
Cdd:cd02669   288 pplfkdgneeNIIPQVPLKQLL--------KKYDGKTETelkdsLKRYLISRLPKYLIFHIKRFSK----------NNFF 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1932 --------EFP-RILDMEPYtvsglaklegevveVGDNCQTNVETTKYELTGIVVHSGQASGGHYFSYILSKNPANgkcQ 2002
Cdd:cd02669   350 keknptivNFPiKNLDLSDY--------------VHFDKPSLNLSTKYNLVANIVHEGTPQEDGTWRVQLRHKSTN---K 412

                         410
                  ....*....|..
gi 386766827 2003 WYKFDDGEVTEC 2014
Cdd:cd02669   413 WFEIQDLNVKEV 424
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1902-2008 1.87e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 45.60  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1902 KKLPPVLAIQLKRFEYDYERvcAIKFNDYFEFPRILDMEPY---TVSGLAKLEGEVVEVGDNCQTNVETTKYELT--GIV 1976
Cdd:cd02670    96 AKAPSCLIICLKRYGKTEGK--AQKMFKKILIPDEIDIPDFvadDPRACSKCQLECRVCYDDKDFSPTCGKFKLSlcSAV 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 386766827 1977 VHSGQA-SGGHYFSYI--------LSKNPANGKcQWYKFDD 2008
Cdd:cd02670   174 CHRGTSlETGHYVAFVrygsysltETDNEAYNA-QWVFFDD 213
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
 994-1060 6.69e-04

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: 40.76  E-value: 6.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386766827  994 DDMEIVTHSNETMAAFKRNLLKRIKgTSTANIKvdlFYANDEMIGVSDEINPLYQYTIRDKMNLTAK 1060
Cdd:cd17065    17 QEFTLEVHSNETLGSVRQKIAERLN-CPVDQVQ---IFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1827-2013 2.46e-03

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


Pssm-ID: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 42.50  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1827 ATLGGSFSdqKICQECPHRYSKEEPFSV----------FSVDIRNHSSLTESL---EQYVK-GELLEGADAYHCDKCDKK 1892
Cdd:cd02672    66 STLIQNFT--RFLLETISQDQLGTPFSCgtsrnsvsllYTLSLPLGSTKTSKEstfLQLLKrSLDLEKVTKAWCDTCCKY 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766827 1893 VVTVKRVCVKKLPPVLAIQLKRfeydYERVCAIKFNDYF-EFPRILDMEPYTVSGLAKLEGEVVEVGDNcqtnvETTKYE 1971
Cdd:cd02672   144 QPLEQTTSIRHLPDILLLVLVI----NLSVTNGEFDDINvVLPSGKVMQNKVSPKAIDHDKLVKNRGQE-----SIYKYE 214

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 386766827 1972 LTGIVVH-SGQASGGHYFSYILSKNPANGKCQWYKFDDGEVTE 2013
Cdd:cd02672   215 LVGYVCEiNDSSRGQHNVVFVIKVNEESTHGRWYLFNDFLVTP 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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