NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2108519807|ref|XP_044054134|]
View 

ubiquitin carboxyl-terminal hydrolase 8 [Siniperca chuatsi]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 756-1085 2.24e-112

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: 347.74  E-value: 2.24e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLCNtpamaeyfnnnyyledinrsnilghkgevaeefgvimkalwaglykcisprdfkitigki 835
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  836 ndqfasyDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFKSTVQCM 915
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  916 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEVWKVPPILLVHLKR 991
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  992 FSYEGRWKQKLQTSVDFPLDSLDLGQYVIGP-KQNLKRYNLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSDIS 1070
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 2108519807 1071 TSSVKSSAAYILFYS 1085
Cdd:cd02674    216 ESSVVSSSAYILFYE 230
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
752-934 1.17e-52

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


The actual alignment was detected with superfamily member COG5560:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 199.34  E-value: 1.17e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  752 ASLTGLRNMGNTCYMNSILQCLCNTPAMAEYFNNNYYLEDINRSNILGHKGEVAEEFGVIMKALWAGLYKCISPRDFKIT 831
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  832 IGKINDQFASYDQQDSQELLLFLMDGLHEDLNKAdNRKRYKEE----ENDHLDDQTAADLAWSKHKLLNESIIVALFQGQ 907
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                          170       180
                   ....*....|....*....|....*..
gi 2108519807  908 FKSTVQCMTCHRKSRTFETFMYLSLPL 934
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPL 448
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 8-116 1.54e-31

USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.


:

Pssm-ID: 462647  Cd Length: 113  Bit Score: 119.33  E-value: 1.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807    8 VKELYLSTSLGDLNKKAEIKPD--KTSTRSYVQSACKIFKAAEECRLDRDEEKSYVLYMKYLTVYDIIKKRPDFKQQPEY 85
Cdd:pfam08969    3 LKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVKAT 82

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2108519807   86 YMTMLGPNSFKKAIEEAEKLSESLKLRYEEV 116
Cdd:pfam08969   83 VRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
PTZ00121 super family cl31754
MAEBL; Provisional
 475-606 4.35e-06

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 4.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  475 LSKEEESQIHSEAVAVMEKARQEQEKRIQERRSEEERREKDQKEKQLKEREDSEKRKKEEEGNGHQE-KNKLERQKVEEE 553
Cdd:PTZ00121  1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnKIKAEEAKKEAE 1740

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2108519807  554 EDKKN----KVWEDKEKRGKEQNSDTPSKSMSLDSPAPNHIVSEIKREPLTRARSEE 606
Cdd:PTZ00121  1741 EDKKKaeeaKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 180-310 1.32e-03

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


The actual alignment was detected with superfamily member cd01446:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 132  Bit Score: 39.96  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  180 ITAEKLFHMMKDQAITIIVMDARSHGDFEESHIQVPAQACIS-----------VPEEAISPGITVNqieAKLpevskehw 248
Cdd:cd01446      2 IDCAWLAALLREGGERLLLLDCRPFLEYSSSHIRGAVNVCCPtilrrrlqggkILLQQLLSCPEDR---DRL-------- 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108519807  249 rQRGFVDYIVLLD-----WFSSVTDLTLGTTLQSLKDALFKwdsitilRSEPLILEGGYENWLLFYP 310
Cdd:cd01446     71 -RRGESLAVVVYDesssdRERLREDSTAESVLGKLLRKLQE-------GCSVYLLKGGFEQFSSEFP 129
 
Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 756-1085 2.24e-112

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: 347.74  E-value: 2.24e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLCNtpamaeyfnnnyyledinrsnilghkgevaeefgvimkalwaglykcisprdfkitigki 835
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  836 ndqfasyDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFKSTVQCM 915
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  916 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEVWKVPPILLVHLKR 991
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  992 FSYEGRWKQKLQTSVDFPLDSLDLGQYVIGP-KQNLKRYNLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSDIS 1070
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 2108519807 1071 TSSVKSSAAYILFYS 1085
Cdd:cd02674    216 ESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
755-1084 2.13e-111

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 348.66  E-value: 2.13e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  755 TGLRNMGNTCYMNSILQCLCNTPAMAEYFNNNYYLEDINRSNILGHkgeVAEEFGVIMKALW-AGLYKCISPRDFKITIG 833
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQkNSKSSSVSPKMFKKSLG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  834 KINDQFASYDQQDSQELLLFLMDGLHEDLNkadnrkrykeeendhlddqtaadlawSKHKLLNESIIVALFQGQFKSTVQ 913
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  914 CMTCHRKSRTFETFMYLSLPL----ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEVWKVPPILLVHL 989
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIpgdsAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  990 KRFSYEGRWKQKLQTSVDFPLDsLDLGQYVIGPKQ----NLKRYNLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHE 1065
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKpktnNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290

                          330       340
                   ....*....|....*....|
gi 2108519807 1066 VSDISTS-SVKSSAAYILFY 1084
Cdd:pfam00443  291 VTEVDEEtAVLSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
752-934 1.17e-52

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 199.34  E-value: 1.17e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  752 ASLTGLRNMGNTCYMNSILQCLCNTPAMAEYFNNNYYLEDINRSNILGHKGEVAEEFGVIMKALWAGLYKCISPRDFKIT 831
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  832 IGKINDQFASYDQQDSQELLLFLMDGLHEDLNKAdNRKRYKEE----ENDHLDDQTAADLAWSKHKLLNESIIVALFQGQ 907
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                          170       180
                   ....*....|....*....|....*..
gi 2108519807  908 FKSTVQCMTCHRKSRTFETFMYLSLPL 934
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPL 448
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 8-116 1.54e-31

USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.


Pssm-ID: 462647  Cd Length: 113  Bit Score: 119.33  E-value: 1.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807    8 VKELYLSTSLGDLNKKAEIKPD--KTSTRSYVQSACKIFKAAEECRLDRDEEKSYVLYMKYLTVYDIIKKRPDFKQQPEY 85
Cdd:pfam08969    3 LKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVKAT 82

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2108519807   86 YMTMLGPNSFKKAIEEAEKLSESLKLRYEEV 116
Cdd:pfam08969   83 VRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
756-1085 1.37e-27

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 113.74  E-value: 1.37e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLC-NTPAMaeyfnNNYYLEDINRSNILghKGEVAEEFGVIMKALWAGLYKCISPRDfKITIGK 834
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILAlYLPKL-----DELLDDLSKELKVL--KNVIRKPEPDLNQEEALKLFTALWSSK-EHKVGW 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  835 INDqfaSYDQQDSQELLLFLMDGLHEDLNKADNRKRYK--EEENDHLDDQtaadlaWSkhkllneSIIVALFQGQF---K 909
Cdd:COG5533     73 IPP---MGSQEDAHELLGKLLDELKLDLVNSFTIRIFKttKDKKKTSTGD------WF-------DIIIELPDQTWvnnL 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  910 STVQCmtchrksrTFETFMYLsLPLASTSKcslqdclrlfskeEKLTDNNKVFCRHCKAHRDStkklevwKVPPILLVHL 989
Cdd:COG5533    137 KTLQE--------FIDNMEEL-VDDETGVK-------------AKENEELEVQAKQEYEVSFV-------KLPKILTIQL 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  990 KRFSYEGRwKQKLQTSVDFPLDsLDLGQYVIGPKQNLKRYNLYGVSNHYGGLDGGHYTAYCKNalKQRWYKFDDHEVSDI 1069
Cdd:COG5533    188 KRFANLGG-NQKIDTEVDEKFE-LPVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK--GGKWEKANDSDVTPV 263

                          330
                   ....*....|....*....
gi 2108519807 1070 STS---SVKSSAAYILFYS 1085
Cdd:COG5533    264 SEEeaiNEKAKNAYLYFYE 282
PTZ00121 PTZ00121
MAEBL; Provisional
 475-606 4.35e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 4.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  475 LSKEEESQIHSEAVAVMEKARQEQEKRIQERRSEEERREKDQKEKQLKEREDSEKRKKEEEGNGHQE-KNKLERQKVEEE 553
Cdd:PTZ00121  1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnKIKAEEAKKEAE 1740

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2108519807  554 EDKKN----KVWEDKEKRGKEQNSDTPSKSMSLDSPAPNHIVSEIKREPLTRARSEE 606
Cdd:PTZ00121  1741 EDKKKaeeaKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 477-571 2.51e-04

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 42.75  E-value: 2.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  477 KEEESQIHSEAVAVMEKARQEQEKriqerrseeerreKDQKEKQLKEREDSEKRKKEEEGNGHQEKNKLERQKVEEE--- 553
Cdd:pfam11600   35 KEEKERLKEEAKAEKERAKEEARR-------------KKEEEKELKEKERREKKEKDEKEKAEKLRLKEEKRKEKQEale 101

                           90       100
                   ....*....|....*....|.
gi 2108519807  554 ---EDKKNKvweDKEKRGKEQ 571
Cdd:pfam11600  102 aklEEKRKK---EEEKRLKEE 119
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 180-310 1.32e-03

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 39.96  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  180 ITAEKLFHMMKDQAITIIVMDARSHGDFEESHIQVPAQACIS-----------VPEEAISPGITVNqieAKLpevskehw 248
Cdd:cd01446      2 IDCAWLAALLREGGERLLLLDCRPFLEYSSSHIRGAVNVCCPtilrrrlqggkILLQQLLSCPEDR---DRL-------- 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108519807  249 rQRGFVDYIVLLD-----WFSSVTDLTLGTTLQSLKDALFKwdsitilRSEPLILEGGYENWLLFYP 310
Cdd:cd01446     71 -RRGESLAVVVYDesssdRERLREDSTAESVLGKLLRKLQE-------GCSVYLLKGGFEQFSSEFP 129
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 189-305 4.06e-03

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 37.46  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  189 MKDQAITIIvmDARSHGDFEESHIQvpaQAcISVPEEAIS-PGITVNQIEAKLPEVSKEhwrqrgfvDYIVLLDWFSSVT 267
Cdd:pfam00581    1 LEDGKVVLI--DVRPPEEYAKGHIP---GA-VNVPLSSLSlPPLPLLELLEKLLELLKD--------KPIVVYCNSGNRA 66

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2108519807  268 DLtlgtTLQSLKDALFKwdsitilrsEPLILEGGYENW 305
Cdd:pfam00581   67 AA----AAALLKALGYK---------NVYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 196-310 7.07e-03

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 37.05  E-value: 7.07e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807   196 IIVMDARSHGDFEESHIqvpaQACISVPEEAIS--PGITVNQIEAKLPEVSKehwrqRGFVDYIVLLDwFSSVtdlTLGT 273
Cdd:smart00450    5 VVLLDVRSPEEYEGGHI----PGAVNIPLSELLdrRGELDILEFEELLKRLG-----LDKDKPVVVYC-RSGN---RSAK 71

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 2108519807   274 TLQSLKDALFKwdsitilrsEPLILEGGYENWLLFYP 310
Cdd:smart00450   72 AAWLLRELGFK---------NVYLLDGGYKEWSAAGP 99
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 180-246 7.59e-03

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 37.25  E-value: 7.59e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108519807  180 ITAEKLFHMMKDQAITIIvmDARSHGDFEESHIqvpaqacisvpEEAISpgITVNQIEAKLPEVSKE 246
Cdd:COG0607      6 ISPAELAELLESEDAVLL--DVREPEEFAAGHI-----------PGAIN--IPLGELAERLDELPKD 57
 
Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 756-1085 2.24e-112

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: 347.74  E-value: 2.24e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLCNtpamaeyfnnnyyledinrsnilghkgevaeefgvimkalwaglykcisprdfkitigki 835
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  836 ndqfasyDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFKSTVQCM 915
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  916 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEVWKVPPILLVHLKR 991
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  992 FSYEGRWKQKLQTSVDFPLDSLDLGQYVIGP-KQNLKRYNLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSDIS 1070
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 2108519807 1071 TSSVKSSAAYILFYS 1085
Cdd:cd02674    216 ESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
755-1084 2.13e-111

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 348.66  E-value: 2.13e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  755 TGLRNMGNTCYMNSILQCLCNTPAMAEYFNNNYYLEDINRSNILGHkgeVAEEFGVIMKALW-AGLYKCISPRDFKITIG 833
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQkNSKSSSVSPKMFKKSLG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  834 KINDQFASYDQQDSQELLLFLMDGLHEDLNkadnrkrykeeendhlddqtaadlawSKHKLLNESIIVALFQGQFKSTVQ 913
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  914 CMTCHRKSRTFETFMYLSLPL----ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEVWKVPPILLVHL 989
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIpgdsAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  990 KRFSYEGRWKQKLQTSVDFPLDsLDLGQYVIGPKQ----NLKRYNLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHE 1065
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKpktnNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290

                          330       340
                   ....*....|....*....|
gi 2108519807 1066 VSDISTS-SVKSSAAYILFY 1084
Cdd:pfam00443  291 VTEVDEEtAVLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 756-1084 1.13e-73

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: 244.31  E-value: 1.13e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLcntpamaeyfnnnyyledinrsnilghkgevaeefgvimkalwaglykcisprdfkitigki 835
Cdd:cd02257      1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  836 ndqfaSYDQQDSQELLLFLMDGLHEDLNKADNRKRYKEEendhlddqtaadlawskhkllNESIIVALFQGQFKSTVQCM 915
Cdd:cd02257     19 -----FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSS---------------------LKSLIHDLFGGKLESTIVCL 72

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  916 TCHRKSRTFETFMYLSLPL--ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKaHRDSTKKLEVWKVPPILLVHLKRFS 993
Cdd:cd02257     73 ECGHESVSTEPELFLSLPLpvKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFS 151

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  994 YEGRW-KQKLQTSVDFPLdSLDLGQYVI------GPKQNLKRYNLYGVSNHYGGL-DGGHYTAYCKNALKQRWYKFDDHE 1065
Cdd:cd02257    152 FNEDGtKEKLNTKVSFPL-ELDLSPYLSegekdsDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDDK 230

                          330       340
                   ....*....|....*....|....
gi 2108519807 1066 VSDISTSSV-----KSSAAYILFY 1084
Cdd:cd02257    231 VTEVSEEEVlefgsLSSSAYILFY 254
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 755-1085 1.62e-64

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: 220.61  E-value: 1.62e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  755 TGLRNMGNTCYMNSILQCLCNTPAMAEYFNNNYYLEDINRsnilghkgevaEEFGV-------IMKALWAGLYKcISPRD 827
Cdd:cd02661      2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCN-----------EGFCMmcaleahVERALASSGPG-SAPRI 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  828 FKITIGKINDQFASYDQQDSQELLLFLMDGLHedlnKADNRKRYKEEENDHLDDQTaadlawskhkllneSIIVALFQGQ 907
Cdd:cd02661     70 FSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDPSSQET--------------TLVQQIFGGY 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  908 FKSTVQCMTCHRKSRTFETFMYLSLPLASTSkcSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEVWKVPPILLV 987
Cdd:cd02661    132 LRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTI 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  988 HLKRFSYEGRwkQKLQTSVDFPlDSLDLGQYVIGPKQNLKRYNLYGVSNHYGG-LDGGHYTAYCKNALKqRWYKFDDHEV 1066
Cdd:cd02661    210 HLKRFSNFRG--GKINKQISFP-ETLDLSPYMSQPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKSSNG-KWYNMDDSKV 285

                          330
                   ....*....|....*....
gi 2108519807 1067 SDISTSSVKSSAAYILFYS 1085
Cdd:cd02661    286 SPVSIETVLSQKAYILFYI 304
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 756-1084 3.89e-62

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: 214.93  E-value: 3.89e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLCNTPAMAEYF--NNNYYLEDINRSNilghkGEVAEEFGVIMKALWAGLYKC-ISPRDFKITI 832
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFlsDRHSCTCLSCSPN-----SCLSCAMDEIFQEFYYSGDRSpYGPINLLYLS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  833 GKINDQFASYDQQDSQELLLFLMDGLHEDLnkadnrKRYKEEENDHLDDQTaadlawskhkllnesIIVALFQGQFKSTV 912
Cdd:cd02660     77 WKHSRNLAGYSQQDAHEFFQFLLDQLHTHY------GGDKNEANDESHCNC---------------IIHQTFSGSLQSSV 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  913 QCMTCHRKSRTFETFMYLSLPLASTSKCS-------------LQDCLRLFSKEEKLTDNNkVFCRHCKAHRDSTKKLEVW 979
Cdd:cd02660    136 TCQRCGGVSTTVDPFLDLSLDIPNKSTPSwalgesgvsgtptLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIK 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  980 KVPPILLVHLKRFSYE-GRWKQKLQTSVDFPLDsLDLGQYVIG---------PKQNLKRYNLYGVSNHYGGLDGGHYTAY 1049
Cdd:cd02660    215 KLPPVLCFQLKRFEHSlNKTSRKIDTYVQFPLE-LNMTPYTSSsigdtqdsnSLDPDYTYDLFAVVVHKGTLDTGHYTAY 293

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2108519807 1050 CKNALKQrWYKFDDHEVSDISTSSVKSSAAYILFY 1084
Cdd:cd02660    294 CRQGDGQ-WFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 756-1084 1.39e-53

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: 188.75  E-value: 1.39e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLCNTPAMAEYFNNNyyledinrsnilghkgevaeefgvimkalwaglykcisPRDFKITIGKI 835
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  836 NDQFASYDQQDSQELLLFLMDGLhedlnkadnrkrykeeendhlddqtaadlawskhkllnESIIVALFQGQFKSTVQCM 915
Cdd:cd02667     43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  916 TCHRKSRTFETFMYLSLPLA--STSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKahrDSTKKLEVWKVPPILLVHLKRFS 993
Cdd:cd02667     85 SCGTVSLVYEPFLDLSLPRSdeIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQ 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  994 YEGRWK-QKLQTSVDFPlDSLDLGQYViGPKQNLK------RYNLYGVSNHYGGLDGGHYTAYCKNALKQR--------- 1057
Cdd:cd02667    162 QPRSANlRKVSRHVSFP-EILDLAPFC-DPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQrlsdltksk 239

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2108519807 1058 ------------WYKFDDHEVSDISTSSVKSSAAYILFY 1084
Cdd:cd02667    240 paadeagpgsgqWYYISDSDVREVSLEEVLKSEAYLLFY 278
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
752-934 1.17e-52

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 199.34  E-value: 1.17e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  752 ASLTGLRNMGNTCYMNSILQCLCNTPAMAEYFNNNYYLEDINRSNILGHKGEVAEEFGVIMKALWAGLYKCISPRDFKIT 831
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  832 IGKINDQFASYDQQDSQELLLFLMDGLHEDLNKAdNRKRYKEE----ENDHLDDQTAADLAWSKHKLLNESIIVALFQGQ 907
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                          170       180
                   ....*....|....*....|....*..
gi 2108519807  908 FKSTVQCMTCHRKSRTFETFMYLSLPL 934
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPL 448
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 756-1085 2.13e-48

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 174.42  E-value: 2.13e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLcntpamaeYFNNNYY-LEDINRSnILGHKGEVaeefGVImkalwaglykciSPRDFKITIGK 834
Cdd:cd02663      1 GLENFGNTCYCNSVLQAL--------YFENLLTcLKDLFES-ISEQKKRT----GVI------------SPKKFITRLKR 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  835 INDQFASYDQQDSQELLLFLMDGLHEDLNKADNRKRYKEEENdhlddqtaADLAWSKHKllneSIIVALFQGQFKSTVQC 914
Cdd:cd02663     56 ENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLN--------NNNNAEPQP----TWVHEIFQGILTNETRC 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  915 MTCHRKSRTFETFMYLSLPLASTskCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEVWKVPPILLVHLKRFSY 994
Cdd:cd02663    124 LTCETVSSRDETFLDLSIDVEQN--TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKY 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  995 EGRWKQ--KLQTSVDFPL-----DSLDLGQYVIgpkqnlKRYNLYGVSNHYG-GLDGGHYTAYCKNalKQRWYKFDDHEV 1066
Cdd:cd02663    202 DEQLNRyiKLFYRVVFPLelrlfNTTDDAENPD------RLYELVAVVVHIGgGPNHGHYVSIVKS--HGGWLLFDDETV 273

                          330       340
                   ....*....|....*....|....*..
gi 2108519807 1067 SDISTSSV-------KSSA-AYILFYS 1085
Cdd:cd02663    274 EKIDENAVeeffgdsPNQAtAYVLFYQ 300
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 756-1085 1.72e-46

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 169.91  E-value: 1.72e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCL------------CNTPAMAEYFNNNyyledinrSNILGHKGEVAEEFGVIMKALWAGLYKCI 823
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWfmnlefrkavyeCNSTEDAELKNMP--------PDKPHEPQTIIDQLQLIFAQLQFGNRSVV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  824 SPRDFKITIGKINDQfasydQQDSQELLLFLMDGLHEDLNKADNRKrykeeendhlddqtaadlawskhkllNESIIVAL 903
Cdd:cd02668     73 DPSGFVKALGLDTGQ-----QQDAQEFSKLFLSLLEAKLSKSKNPD--------------------------LKNIVQDL 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  904 FQGQFKSTVQCMTCHRKSRTFETFMYLSLPLASTSKcsLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEVWKVPP 983
Cdd:cd02668    122 FRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT--LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPP 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  984 ILLVHLKRFSY--EGRWKQKLQTSVDFPLDsLDLGQYVIGPKQNLKRYNLYGVSNHYG-GLDGGHYTAYCKNALKQRWYK 1060
Cdd:cd02668    200 TLNFQLLRFVFdrKTGAKKKLNASISFPEI-LDMGEYLAESDEGSYVYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYK 278

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2108519807 1061 FDDHEVSDISTSSVK---------------------SSAAYILFYS 1085
Cdd:cd02668    279 FNDEDVEEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVYK 324
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 756-1084 2.86e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 163.58  E-value: 2.86e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLCNTPamaeYFNNNYYledinrsNILGHKGEVAE-----EFGVIMKALWAGLYKCISPRDFKI 830
Cdd:cd02659      4 GLKNQGATCYMNSLLQQLYMTP----EFRNAVY-------SIPPTEDDDDNksvplALQRLFLFLQLSESPVKTTELTDK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  831 TIGKINDQFASYDQQDSQELLLFLMDGLHEDLNKAdnrkrykEEENdhlddqtaadlawskhkllnesIIVALFQGQFKS 910
Cdd:cd02659     73 TRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGT-------GQEG----------------------LIKNLFGGKLVN 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  911 TVQCMTCHRKSRTFETFmyLSLPLASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEVWKVPPILLVHLK 990
Cdd:cd02659    124 YIICKECPHESEREEYF--LDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLK 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  991 RFSYEGR--WKQKLQTSVDFPlDSLDLGQYVI----------GPKQNLK-RYNLYGVSNHYGGLDGGHYTAYCKNALKQR 1057
Cdd:cd02659    202 RFEFDFEtmMRIKINDRFEFP-LELDMEPYTEkglakkegdsEKKDSESyIYELHGVLVHSGDAHGGHYYSYIKDRDDGK 280

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2108519807 1058 WYKFDDHEVSDISTSSV----------------------KSSAAYILFY 1084
Cdd:cd02659    281 WYKFNDDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFY 329
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 756-1084 9.82e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 135.70  E-value: 9.82e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLcntpAMAEYFNNnyyleDINRSNILGHKGEVAEEFGVIM-KALWAglykcISPRDFKITIGK 834
Cdd:cd02664      1 GLINLGNTCYMNSVLQAL----FMAKDFRR-----QVLSLNLPRLGDSQSVMKKLQLlQAHLM-----HTQRRAEAPPDY 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  835 INDQ-----FASYDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFK 909
Cdd:cd02664     67 FLEAsrppwFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLS 108

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  910 STVQCMTCHRKSRTFETFMYLSLplastSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEVWKVPPILLVHL 989
Cdd:cd02664    109 TTIRCLNCNSTSARTERFRDLDL-----SFPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTL 183

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  990 KRFSY--EGRWKQKLQTSVDFPLDsLDLGQYV----IGPKQNLKR---------------YNLYGVSNHYG-GLDGGHYT 1047
Cdd:cd02664    184 LRFSYdqKTHVREKIMDNVSINEV-LSLPVRVesksSESPLEKKEeesgddgelvtrqvhYRLYAVVVHSGySSESGHYF 262

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108519807 1048 AYCKN--------------------ALKQRWYKFDDHEVSDISTSSVK-------SSAAYILFY 1084
Cdd:cd02664    263 TYARDqtdadstgqecpepkdaeenDESKNWYLFNDSRVTFSSFESVQnvtsrfpKDTPYILFY 326
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 8-116 1.54e-31

USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.


Pssm-ID: 462647  Cd Length: 113  Bit Score: 119.33  E-value: 1.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807    8 VKELYLSTSLGDLNKKAEIKPD--KTSTRSYVQSACKIFKAAEECRLDRDEEKSYVLYMKYLTVYDIIKKRPDFKQQPEY 85
Cdd:pfam08969    3 LKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVKAT 82

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2108519807   86 YMTMLGPNSFKKAIEEAEKLSESLKLRYEEV 116
Cdd:pfam08969   83 VRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 756-1084 2.07e-29

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: 119.74  E-value: 2.07e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLCNTPAMAE---YFNNNYYLEDINRSNILghkgevaeefgVIMKALWAGLYKC---ISPRDFK 829
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPARRGANQSSDNLT-----------NALRDLFDTMDKKqepVPPIEFL 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  830 ITIGKINDQFAS------YDQQDSQELLLFLMDGLHEDLNKADnrkrykeEENDHLDDqtaadlawskhkllnesiivaL 903
Cdd:cd02657     70 QLLRMAFPQFAEkqnqggYAQQDAEECWSQLLSVLSQKLPGAG-------SKGSFIDQ---------------------L 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  904 FQGQFKSTVQCM-TCHRKSRTFETFMYLSLPLASTSKCS-LQDCLRLFSKEE--KLTDnnkvfcrhcKAHRDS--TKKLE 977
Cdd:cd02657    122 FGIELETKMKCTeSPDEEEVSTESEYKLQCHISITTEVNyLQDGLKKGLEEEieKHSP---------TLGRDAiyTKTSR 192

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  978 VWKVPPILLVHLKRFSyegrWKQKLQT------SVDFPLDsLDLGQYVigpkQNLKRYNLYGVSNHYG-GLDGGHYTAYC 1050
Cdd:cd02657    193 ISRLPKYLTVQFVRFF----WKRDIQKkakilrKVKFPFE-LDLYELC----TPSGYYELVAVITHQGrSADSGHYVAWV 263

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2108519807 1051 KNALKQRWYKFDDHEVSDISTSSVKSSA-------AYILFY 1084
Cdd:cd02657    264 RRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 735-1084 2.70e-29

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: 120.00  E-value: 2.70e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  735 PSAAKIRNLNPtfgglgasLTGLRNMGNTCYMNSILQCLCNTPAmaeyfnnnyYLEDINRSNILGHKGEVAEEFGVIMKA 814
Cdd:cd02671     13 TSCEKRENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPG---------FKHGLKHLVSLISSVEQLQSSFLLNPE 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  815 LWAGLYKCISPRDFKITIGKINDQFASYDQQDSQELLLFLMDGLHEDLNKadnrkrykeeendhlddqtaadlawskhkl 894
Cdd:cd02671     76 KYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK------------------------------ 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  895 lnesiivaLFQGQFKSTVQCMTCHRKSRTFETFMYLSLPLASTSKCS-----------------LQDCLRLFSKEEKLTD 957
Cdd:cd02671    126 --------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKseesseispdpktemktLKWAISQFASVERIVG 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  958 NNKVFCRHCKAHRDSTKKLEVWKVPPILLVHLKRFSYEGRWK------QKLQTSVDFPLDsLDLGQYVIGPKQNLkrYNL 1031
Cdd:cd02671    198 EDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPLK-LSLEEWSTKPKNDV--YRL 274

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2108519807 1032 YGVSNHYGG-LDGGHYTAYCknalkqRWYKFDDHEV---------SDISTSSVKSSAAYILFY 1084
Cdd:cd02671    275 FAVVMHSGAtISSGHYTAYV------RWLLFDDSEVkvteekdflEALSPNTSSTSTPYLLFY 331
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
756-1085 1.37e-27

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 113.74  E-value: 1.37e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLC-NTPAMaeyfnNNYYLEDINRSNILghKGEVAEEFGVIMKALWAGLYKCISPRDfKITIGK 834
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILAlYLPKL-----DELLDDLSKELKVL--KNVIRKPEPDLNQEEALKLFTALWSSK-EHKVGW 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  835 INDqfaSYDQQDSQELLLFLMDGLHEDLNKADNRKRYK--EEENDHLDDQtaadlaWSkhkllneSIIVALFQGQF---K 909
Cdd:COG5533     73 IPP---MGSQEDAHELLGKLLDELKLDLVNSFTIRIFKttKDKKKTSTGD------WF-------DIIIELPDQTWvnnL 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  910 STVQCmtchrksrTFETFMYLsLPLASTSKcslqdclrlfskeEKLTDNNKVFCRHCKAHRDStkklevwKVPPILLVHL 989
Cdd:COG5533    137 KTLQE--------FIDNMEEL-VDDETGVK-------------AKENEELEVQAKQEYEVSFV-------KLPKILTIQL 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  990 KRFSYEGRwKQKLQTSVDFPLDsLDLGQYVIGPKQNLKRYNLYGVSNHYGGLDGGHYTAYCKNalKQRWYKFDDHEVSDI 1069
Cdd:COG5533    188 KRFANLGG-NQKIDTEVDEKFE-LPVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK--GGKWEKANDSDVTPV 263

                          330
                   ....*....|....*....
gi 2108519807 1070 STS---SVKSSAAYILFYS 1085
Cdd:COG5533    264 SEEeaiNEKAKNAYLYFYE 282
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 756-1084 3.86e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 113.19  E-value: 3.86e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLCNTPAMAEYFNNNYYLEDINRSNI----------LGHkGEVAEEFGVIM--KALWAGLYKCI 823
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPandlncqlikLAD-GLLSGRYSKPAslKSENDPYQVGI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  824 SPRDFKITIGKINDQFASYDQQDSQELLLFLMDglhedlnKADNRKRYKEEENdhlddqtaadlawskhklLNEsiivaL 903
Cdd:cd02658     80 KPSMFKALIGKGHPEFSTMRQQDALEFLLHLID-------KLDRESFKNLGLN------------------PND-----L 129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  904 FQGQFKSTVQCMTCHRKSRTFETFMYLSLPL------------ASTSKCSLQDCLRLFSKEEKLTDnnkvFCRHCKAHRD 971
Cdd:cd02658    130 FKFMIEDRLECLSCKKVKYTSELSEILSLPVpkdeatekeegeLVYEPVPLEDCLKAYFAPETIED----FCSTCKEKTT 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  972 STKKLEVWKVPPILLVHLKRFSYEGRWKQKlqtSVDFPLDsldlGQYVIGPkqnlKRYNLYGVSNHYG-GLDGGHYTAYC 1050
Cdd:cd02658    206 ATKTTGFKTFPDYLVINMKRFQLLENWVPK---KLDVPID----VPEELGP----GKYELIAFISHKGtSVHSGHYVAHI 274

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2108519807 1051 K--NALKQRWYKFDDHEVSDISTSSVKSSAAYILFY 1084
Cdd:cd02658    275 KkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 756-1084 1.71e-23

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 100.52  E-value: 1.71e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLCNTPAMAEYFNNnyYLEdinrsnilghkgevaeefgvimkalwaglykcisprdfkitigki 835
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLIEYLEE--FLE--------------------------------------------- 33

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  836 ndqfasydQQDSQELLLFLMDGLhedlnkadnrkrykeeendhlddqtaadlawskhkllnESIIVALFQGQFKSTVQCM 915
Cdd:cd02662     34 --------QQDAHELFQVLLETL--------------------------------------EQLLKFPFDGLLASRIVCL 67

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  916 TCHRKSR-TFETFMYLSLPL---ASTSKCSLQDCLRLFSKEEKLTDnnkVFCRHCKahrdstkkLEVWKVPPILLVHLKR 991
Cdd:cd02662     68 QCGESSKvRYESFTMLSLPVpnqSSGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSR 136

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  992 FSYEGRWK-QKLQTSVDFPLDsldLGQYvigpkqnlkRYNLYGVSNHYGGLDGGHYTAY--------------------C 1050
Cdd:cd02662    137 SVFDGRGTsTKNSCKVSFPER---LPKV---------LYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreG 204

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2108519807 1051 KNALKQRWYKFDDHEVSDISTSSVK-SSAAYILFY 1084
Cdd:cd02662    205 PSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 756-1067 4.11e-23

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 106.49  E-value: 4.11e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLCNTpamaEYFNNNYY-LEDINRSNilghKGEVAeefgVIMKALWAGLYKCISPRD-FKITIG 833
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFI----AKFRKDVYgIPTDHPRG----RDSVA----LALQRLFYNLQTGEEPVDtTELTRS 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  834 KINDQFASYDQQDSQELLLFLMDGLhedlnkaDNRKRYKEEENdhlddqtaadlawskhkLLNEsiivaLFQGQFKSTVQ 913
Cdd:COG5077    263 FGWDSDDSFMQHDIQEFNRVLQDNL-------EKSMRGTVVEN-----------------ALNG-----IFVGKMKSYIK 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  914 CMTCHRKSRTFETFMYLSLPLASTSkcSLQDCLRLFSKEEKLTDNNKVFCRHcKAHRDSTKKLEVWKVPPILLVHLKRFS 993
Cdd:COG5077    314 CVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFE 390

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  994 YEGRWKQ--KLQTSVDFPlDSLDLGQYV---IGPKQNLK-RYNLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVS 1067
Cdd:COG5077    391 YDFERDMmvKINDRYEFP-LEIDLLPFLdrdADKSENSDaVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVT 469
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 756-1084 1.10e-20

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 96.23  E-value: 1.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  756 GLRNMGNTCYMNSILQCLCNTPAMaeyfnNNYYLEDINRSNILGHKGEVAEEFGVIMKALW-AGLYKC-ISPRDFKITIG 833
Cdd:cd02669    121 GLNNIKNNDYANVIIQALSHVKPI-----RNFFLLYENYENIKDRKSELVKRLSELIRKIWnPRNFKGhVSPHELLQAVS 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  834 KINDQFASYDQQ-DSQELLLFLMDGLHEDLNKadNRKRykeeendhlddqtaadlawskhkllNESIIVALFQGQFKSTV 912
Cdd:cd02669    196 KVSKKKFSITEQsDPVEFLSWLLNTLHKDLGG--SKKP-------------------------NSSIIHDCFQGKVQIET 248

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  913 QCMTCHR---------------KSRTFETFMYLS--LPLASTSKCSLQD-CLRLFSKEEKLTDNNKVfcrHCKAHRDSTK 974
Cdd:cd02669    249 QKIKPHAeeegskdkffkdsrvKKTSVSPFLLLTldLPPPPLFKDGNEEnIIPQVPLKQLLKKYDGK---TETELKDSLK 325

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  975 KLEVWKVPPILLVHLKRFSYEGRWKQKLQTSVDFPLDSLDLGQYVIGPKQNLKR---YNLygVSN--HYGG-LDGGHYTA 1048
Cdd:cd02669    326 RYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLstkYNL--VANivHEGTpQEDGTWRV 403

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2108519807 1049 YCKNALKQRWYKFDDHEVSDISTSSVKSSAAYILFY 1084
Cdd:cd02669    404 QLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 757-1084 2.56e-11

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


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 64.86  E-value: 2.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  757 LRNMGNTCYMNSILQCLCntpamaeyfnnnyyledinrsnilghkgevaeefgvimkalwaglykcisprdfkiTIGKIN 836
Cdd:cd02673      2 LVNTGNSCYFNSTMQALS--------------------------------------------------------SIGKIN 25

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  837 DQFASYDQQDSQELLLFL---MDGLHEdlNKADNRKRYkEEENDHLDDQTAadlawskHKLLNESIIValfqgqfkstvq 913
Cdd:cd02673     26 TEFDNDDQQDAHEFLLTLleaIDDIMQ--VNRTNVPPS-NIEIKRLNPLEA-------FKYTIESSYV------------ 83

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  914 CMTCHRKSRTFETFMYLSLPLASTSKCSLQDclrLFSKEEKLTDNNKVfCRHCKaHRDSTKKLEVWKVPPILLVHLKRFs 993
Cdd:cd02673     84 CIGCSFEENVSDVGNFLDVSMIDNKLDIDEL---LISNFKTWSPIEKD-CSSCK-CESAISSERIMTFPECLSINLKRY- 157

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  994 yegrwkqKLQTSVdfpLDSLDLGQYVIGPKQ-NLKRYNLYGVSNHYG-GLDGGHYTAYCKNALK-QRWYKFDDHEVSDIS 1070
Cdd:cd02673    158 -------KLRIAT---SDYLKKNEEIMKKYCgTDAKYSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIRPVS 227

                          330
                   ....*....|....*..
gi 2108519807 1071 TSSVK---SSAAYILFY 1084
Cdd:cd02673    228 KNDVStnaRSSGYLIFY 244
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
881-1063 1.22e-08

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 57.67  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  881 DQTAADLAWSKHKLL-NESIIVALFQGQFKSTVQCMTC-HRKSRTFETFM----YLSLPLASTSKCSLQD---CLRLFSK 951
Cdd:pfam13423  108 DQLSSEENSTPPNPSpAESPLEQLFGIDAETTIRCSNCgHESVRESSTHVldliYPRKPSSNNKKPPNQTfssILKSSLE 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  952 EEKLTdnnKVFCRHCKAHRDSTKKLEVWKVPPILLVHLKRFSYEgrWKQKLQTSVDFPLD-SLDLGQYVIGPkQNLKRYN 1030
Cdd:pfam13423  188 RETTT---KAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPEiGLTLSDDLQGD-NEIVKYE 261

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2108519807 1031 LYG-VSNHYGGLDGGHYTAYCK-------NALKQRWYKFDD 1063
Cdd:pfam13423  262 LRGvVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 844-1084 3.05e-08

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 55.64  E-value: 3.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  844 QQDSQELLLFLMDGLHEDLNKADNRKRYKEEendhlddqtaadlawSKHKLlnesiiVALFQGQFkSTVqcmTCHRKSRT 923
Cdd:cd02665     22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEK---------------SKNPM------VQLFYGTF-LTE---GVLEGKPF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  924 FETFMYLSLPLASTSKCSLQDCLrlfskeEKLTDNNKVFCRHCKAHRDSTKKLEVWKVPPILLVHLKRFSYEGRWKQKLQ 1003
Cdd:cd02665     77 CNCETFGQYPLQVNGYGNLHECL------EAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPEKIH 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807 1004 TSVDFPldsldlgqyvigpkQNLKR--YNLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSDISTSSVKSSA--- 1078
Cdd:cd02665    151 DKLEFP--------------QIIQQvpYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfgg 216

                          250
                   ....*....|.
gi 2108519807 1079 -----AYILFY 1084
Cdd:cd02665    217 grnpsAYCLMY 227
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 891-1084 3.42e-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: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 52.90  E-value: 3.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  891 KHKLLNE-----SIIVALFQGQFKSTVQCM-----TCHRKSRTFETFMY-LSLPLASTSKCSLQDCLRLFSKEEKLTDNN 959
Cdd:cd02672     54 ESCLLCElgylfSTLIQNFTRFLLETISQDqlgtpFSCGTSRNSVSLLYtLSLPLGSTKTSKESTFLQLLKRSLDLEKVT 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  960 KVFCRHCKAHRDSTKKLEVWKVPPILL----VHLKRFSYEGRWKQ-------KLQTSVDFPLDSLDLGQYVIGPkQNLKR 1028
Cdd:cd02672    134 KAWCDTCCKYQPLEQTTSIRHLPDILLlvlvINLSVTNGEFDDINvvlpsgkVMQNKVSPKAIDHDKLVKNRGQ-ESIYK 212

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108519807 1029 YNLYG-VSNHYGGLDGGHYTA----YCKNALKQRWYKFDDHEVSDISTSsvkssaAYILFY 1084
Cdd:cd02672    213 YELVGyVCEINDSSRGQHNVVfvikVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
PTZ00121 PTZ00121
MAEBL; Provisional
 475-606 4.35e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 4.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  475 LSKEEESQIHSEAVAVMEKARQEQEKRIQERRSEEERREKDQKEKQLKEREDSEKRKKEEEGNGHQE-KNKLERQKVEEE 553
Cdd:PTZ00121  1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnKIKAEEAKKEAE 1740

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2108519807  554 EDKKN----KVWEDKEKRGKEQNSDTPSKSMSLDSPAPNHIVSEIKREPLTRARSEE 606
Cdd:PTZ00121  1741 EDKKKaeeaKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
PTZ00121 PTZ00121
MAEBL; Provisional
 475-571 4.47e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 4.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  475 LSKEEESQIHSEAVAVMEKARQEQEKRIQERRSEEERREKDQKEK--------QLKEREDSEKRKKEEEGNGHQEKNKLE 546
Cdd:PTZ00121  1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEeenkikaaEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691

                           90       100
                   ....*....|....*....|....*....
gi 2108519807  547 RQ-KVEEEEDKKN---KVWEDKEKRGKEQ 571
Cdd:PTZ00121  1692 EAlKKEAEEAKKAeelKKKEAEEKKKAEE 1720
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 755-1074 1.47e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 45.17  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  755 TGLRNMGNTCYMNSILQCL-CNTPA-----MAEYFNNNYYLEDINRSNILGHKGEVAE-----EFGVIMKALWAGLYK-- 821
Cdd:cd02666      2 AGLDNIGNTCYLNSLLQYFfTIKPLrdlvlNFDESKAELASDYPTERRIGGREVSRSElqrsnQFVYELRSLFNDLIHsn 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  822 --CISPRDfkitigkiNDQFASYDQQDSQELLLFLMDglheDLNKADNRKRYKEEENDHLDDQTAADLawskhkllnesi 899
Cdd:cd02666     82 trSVTPSK--------ELAYLALRQQDVTECIDNVLF----QLEVALEPISNAFAGPDTEDDKEQSDL------------ 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  900 IVALFQGQFKSTVQ--CMTCHRKSRT-FETFMYLSLPLAST--------SKCSLQDCL-RLFSKE-------EKLTDNNK 960
Cdd:cd02666    138 IKRLFSGKTKQQLVpeSMGNQPSVRTkTERFLSLLVDVGKKgreivvllEPKDLYDALdRYFDYDsltklpqRSQVQAQL 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  961 VFCRHCKAHRDSTKKLE--VWKVPPILLVHLKRFSYEGRWKQKLQTSVDFPLDSLDlgqyvigpkQNLKR--YNLYGVSN 1036
Cdd:cd02666    218 AQPLQRELISMDRYELPssIDDIDELIREAIQSESSLVRQAQNELAELKHEIEKQF---------DDLKSygYRLHAVFI 288

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2108519807 1037 HYGGLDGGHYTAYCKNALKQRWYKFDDHEVSDISTSSV 1074
Cdd:cd02666    289 HRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEV 326
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 477-571 2.51e-04

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 42.75  E-value: 2.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  477 KEEESQIHSEAVAVMEKARQEQEKriqerrseeerreKDQKEKQLKEREDSEKRKKEEEGNGHQEKNKLERQKVEEE--- 553
Cdd:pfam11600   35 KEEKERLKEEAKAEKERAKEEARR-------------KKEEEKELKEKERREKKEKDEKEKAEKLRLKEEKRKEKQEale 101

                           90       100
                   ....*....|....*....|.
gi 2108519807  554 ---EDKKNKvweDKEKRGKEQ 571
Cdd:pfam11600  102 aklEEKRKK---EEEKRLKEE 119
PTZ00121 PTZ00121
MAEBL; Provisional
 477-607 9.90e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 9.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  477 KEEESQIHSEAVAVMEKARQEQEKRIQERRSEEERREKDQKEKQLKEREDSEKRKKEEEGNGHQEKNKLERQKvEEEEDK 556
Cdd:PTZ00121  1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK-KAEEDK 1576

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2108519807  557 KNKVWEDKEKRGKEQNSdtPSKSMSLDSPAPNHIVSEIKREPLTRARSEEM 607
Cdd:PTZ00121  1577 NMALRKAEEAKKAEEAR--IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 180-310 1.32e-03

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 39.96  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  180 ITAEKLFHMMKDQAITIIVMDARSHGDFEESHIQVPAQACIS-----------VPEEAISPGITVNqieAKLpevskehw 248
Cdd:cd01446      2 IDCAWLAALLREGGERLLLLDCRPFLEYSSSHIRGAVNVCCPtilrrrlqggkILLQQLLSCPEDR---DRL-------- 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108519807  249 rQRGFVDYIVLLD-----WFSSVTDLTLGTTLQSLKDALFKwdsitilRSEPLILEGGYENWLLFYP 310
Cdd:cd01446     71 -RRGESLAVVVYDesssdRERLREDSTAESVLGKLLRKLQE-------GCSVYLLKGGFEQFSSEFP 129
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 491-573 1.59e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 41.95  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  491 MEKARQEQEKRIQerrseeerreKDQKEKQLKEREDSEKRKKEEEGNGHQEknKLERQKVEEEEDKKN-----KVWEDKE 565
Cdd:pfam15558   69 QRKARLGREERRR----------ADRREKQVIEKESRWREQAEDQENQRQE--KLERARQEAEQRKQCqeqrlKEKEEEL 136


                   ....*...
gi 2108519807  566 KRGKEQNS 573
Cdd:pfam15558  137 QALREQNS 144
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 478-571 2.20e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.86  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  478 EEESQIHSEAVAVMEKARQEQEKRIQERRSEeerrekdQKEKQLKEREDSE---KRKKEEE-----------GNGHQEKN 543
Cdd:pfam15709  405 EEERKQRLQLQAAQERARQQQEEFRRKLQEL-------QRKKQQEEAERAEaekQRQKELEmqlaeeqkrlmEMAEEERL 477

                           90       100
                   ....*....|....*....|....*...
gi 2108519807  544 KLERQKVEEEEDKKnkvWEDKEKRGKEQ 571
Cdd:pfam15709  478 EYQRQKQEAEEKAR---LEAEERRQKEE 502
PTZ00121 PTZ00121
MAEBL; Provisional
 474-571 2.36e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  474 SLSKEEEsqihsEAVAVMEKARQEQEKRIQERRSEEERREKDQKEKQLKEREDSEKRKKEEEGNGHQEKNKLERQKvEEE 553
Cdd:PTZ00121  1693 ALKKEAE-----EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK-KEE 1766

                           90
                   ....*....|....*...
gi 2108519807  554 EDKKNKVWEDKEKRGKEQ 571
Cdd:PTZ00121  1767 EKKAEEIRKEKEAVIEEE 1784
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 477-609 2.82e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  477 KEEESQIHSEAVAVMEKARQEQEKRIQERRSEEERREKDQKEKQLKEREDSEKRKKEEEGNGHQEKNKLERQK--VEEE- 553
Cdd:pfam17380  434 QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQamIEEEr 513

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108519807  554 ---------EDKKNKVWEDKEKRGKEQNSDTpsksmSLDSPAPNHIVSEIKREPLTRARSEEMGR 609
Cdd:pfam17380  514 krkllekemEERQKAIYEEERRREAEEERRK-----QQEMEERRRIQEQMRKATEERSRLEAMER 573
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 189-305 4.06e-03

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 37.46  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  189 MKDQAITIIvmDARSHGDFEESHIQvpaQAcISVPEEAIS-PGITVNQIEAKLPEVSKEhwrqrgfvDYIVLLDWFSSVT 267
Cdd:pfam00581    1 LEDGKVVLI--DVRPPEEYAKGHIP---GA-VNVPLSSLSlPPLPLLELLEKLLELLKD--------KPIVVYCNSGNRA 66

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2108519807  268 DLtlgtTLQSLKDALFKwdsitilrsEPLILEGGYENW 305
Cdd:pfam00581   67 AA----AAALLKALGYK---------NVYVLDGGFEAW 91
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 475-571 4.24e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.26  E-value: 4.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  475 LSKEEESQIHSEAVAVMEKARQEQEKriqerrseeerREKDQKEKQLKEREDSEKRKKEEEgngHQEKNKLERQKVEEEE 554
Cdd:pfam17380  406 ILEEERQRKIQQQKVEMEQIRAEQEE-----------ARQREVRRLEEERAREMERVRLEE---QERQQQVERLRQQEEE 471

                           90
                   ....*....|....*..
gi 2108519807  555 DKKNKVWEDKEKRGKEQ 571
Cdd:pfam17380  472 RKRKKLELEKEKRDRKR 488
PTZ00121 PTZ00121
MAEBL; Provisional
 475-571 4.60e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 4.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  475 LSKEEESQIHSEAVAVMEKARQEQEKRIQERRSEEERREKDQK-EKQLKEREDSEKRKKEEEGNGHQEKNKLERQKVEEE 553
Cdd:PTZ00121  1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARiEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630

                           90       100
                   ....*....|....*....|.
gi 2108519807  554 EDKKN---KVWEDKEKRGKEQ 571
Cdd:PTZ00121  1631 EKKKVeqlKKKEAEEKKKAEE 1651
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 196-310 7.07e-03

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 37.05  E-value: 7.07e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807   196 IIVMDARSHGDFEESHIqvpaQACISVPEEAIS--PGITVNQIEAKLPEVSKehwrqRGFVDYIVLLDwFSSVtdlTLGT 273
Cdd:smart00450    5 VVLLDVRSPEEYEGGHI----PGAVNIPLSELLdrRGELDILEFEELLKRLG-----LDKDKPVVVYC-RSGN---RSAK 71

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 2108519807   274 TLQSLKDALFKwdsitilrsEPLILEGGYENWLLFYP 310
Cdd:smart00450   72 AAWLLRELGFK---------NVYLLDGGYKEWSAAGP 99
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 180-246 7.59e-03

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 37.25  E-value: 7.59e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108519807  180 ITAEKLFHMMKDQAITIIvmDARSHGDFEESHIqvpaqacisvpEEAISpgITVNQIEAKLPEVSKE 246
Cdd:COG0607      6 ISPAELAELLESEDAVLL--DVREPEEFAAGHI-----------PGAIN--IPLGELAERLDELPKD 57
Caldesmon pfam02029
Caldesmon;
461-597 8.03e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 40.24  E-value: 8.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108519807  461 PDRSVKP---SIISNTSLSKEEESQIHSEAVAVMEK-ARQEQEKRIQERRSEEERREKDQKEKQLKEREDSEKRKKEEEG 536
Cdd:pfam02029   32 VTESVEPnehNSYEEDSELKPSGQGGLDEEEAFLDRtAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEE 111

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108519807  537 N-----GHQEKNKLERQKVEE-----EEDKKNKvWEDKEKRGKEQNSDTPSKS-MSLDSPAPNHIVSEIKRE 597
Cdd:pfam02029  112 NsswekEEKRDSRLGRYKEEEteireKEYQENK-WSTEVRQAEEEGEEEEDKSeEAEEVPTENFAKEEVKDE 182
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH