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Conserved domains on  [gi|1357729074|ref|XP_024151331|]
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ubiquitin carboxyl-terminal hydrolase 8 [Oryzias melastigma]

Protein Classification

Graphical summary

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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 ...
 749-1078 4.75e-114

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: 351.98  E-value: 4.75e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLCNtpamaeyfnnnyyledinrsnilghkgevaeefgvimkalwaglykfisprdfkitigki 828
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  829 ndqfagyDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFKSTVQCS 908
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  909 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKR 984
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  985 FSYEGRWKQKLQTSVDFPLDNLDLAQYVIGPKQT-LKRYNLYGVSNHYGGLDGGHYTAYCKNAMKQRWYKFDDHEVSDIS 1063
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 1357729074 1064 TSSVKSSAAYILFYS 1078
Cdd:cd02674    216 ESSVVSSSAYILFYE 230
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
745-927 3.44e-54

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: 203.96  E-value: 3.44e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  745 ASLTGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNYYLEDINRSNILGHKGEVAEEFGVIMKALWAGLYKFISPRDFKIT 824
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  825 IGKINDQFAGYDQQDSQELLLFLMDGLHEDLNKAdNRKRYKEE----ENDHLDDQTAADLAWSKHKLLNESIIVALFQGQ 900
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                          170       180
                   ....*....|....*....|....*..
gi 1357729074  901 FKSTVQCSTCHRKSRTFETFMYLSLPL 927
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPL 448
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 6-116 4.81e-32

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: 120.87  E-value: 4.81e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074    6 TEVKELYLSSCLGDLNKKAEIKPD--KTSTRSYVQSACKLFKAAEECRLDRDEEKAYVFYMKYLTVYDIIKKRPDFKQQP 83
Cdd:pfam08969    1 APLKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1357729074   84 DYYITLLGQNSFKKAIEEAEKLSESLKLRYEEV 116
Cdd:pfam08969   81 ATVRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 320-472 1.78e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  320 PPRETTVNTLPQLNFSYPSLEEPKPPVIHPEPVVQPDSQKPPA--PAvvngvAPAEPPTSKTSVIADKLPDTHDSPV--- 394
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAasPA-----GPLPPPTSAQPTAPPPPPGPPPPSLplg 2853

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  395 --ISTGLDLNKQNP---------APNQSPVTSKSFPQFDRTKKPLRDDPKAKENGSTKDSTQngPVVPDRSVKPPLIPSS 463
Cdd:PHA03247  2854 gsVAPGGDVRRRPPsrspaakpaAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPP--PPQPQPQPPPPPQPQP 2931


                   ....*....
gi 1357729074  464 SLSKEEQSQ 472
Cdd:PHA03247  2932 PPPPPPRPQ 2940
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 197-305 5.39e-04

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 pfam00581:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 92  Bit Score: 40.16  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS-PGITVNQIEAKLPSLSKDhwmrrgfvDYIVLLDWFSSVSDLklgtTL 275
Cdd:pfam00581    7 VLIDVRPPEEYAKGHI----PGAVNVPLSSLSlPPLPLLELLEKLLELLKD--------KPIVVYCNSGNRAAA----AA 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 1357729074  276 QSLKDALFKwdsitilrsEPLVLEGGYENW 305
Cdd:pfam00581   71 ALLKALGYK---------NVYVLDGGFEAW 91
 
Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 749-1078 4.75e-114

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: 351.98  E-value: 4.75e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLCNtpamaeyfnnnyyledinrsnilghkgevaeefgvimkalwaglykfisprdfkitigki 828
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  829 ndqfagyDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFKSTVQCS 908
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  909 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKR 984
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  985 FSYEGRWKQKLQTSVDFPLDNLDLAQYVIGPKQT-LKRYNLYGVSNHYGGLDGGHYTAYCKNAMKQRWYKFDDHEVSDIS 1063
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 1357729074 1064 TSSVKSSAAYILFYS 1078
Cdd:cd02674    216 ESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
748-1077 8.86e-112

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 349.43  E-value: 8.86e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  748 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNYYLEDINRSNILGHkgeVAEEFGVIMKALW-AGLYKFISPRDFKITIG 826
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQkNSKSSSVSPKMFKKSLG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  827 KINDQFAGYDQQDSQELLLFLMDGLHEDLNkadnrkrykeeendhlddqtaadlawSKHKLLNESIIVALFQGQFKSTVQ 906
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  907 CSTCHRKSRTFETFMYLSLPL----ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHL 982
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIpgdsAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  983 KRFSYEGRWKQKLQTSVDFPLDnLDLAQYVIGPKQT----LKRYNLYGVSNHYGGLDGGHYTAYCKNAMKQRWYKFDDHE 1058
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPktnnLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290

                          330       340
                   ....*....|....*....|
gi 1357729074 1059 VSDISTS-SVKSSAAYILFY 1077
Cdd:pfam00443  291 VTEVDEEtAVLSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
745-927 3.44e-54

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 203.96  E-value: 3.44e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  745 ASLTGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNYYLEDINRSNILGHKGEVAEEFGVIMKALWAGLYKFISPRDFKIT 824
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  825 IGKINDQFAGYDQQDSQELLLFLMDGLHEDLNKAdNRKRYKEE----ENDHLDDQTAADLAWSKHKLLNESIIVALFQGQ 900
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                          170       180
                   ....*....|....*....|....*..
gi 1357729074  901 FKSTVQCSTCHRKSRTFETFMYLSLPL 927
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPL 448
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 6-116 4.81e-32

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: 120.87  E-value: 4.81e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074    6 TEVKELYLSSCLGDLNKKAEIKPD--KTSTRSYVQSACKLFKAAEECRLDRDEEKAYVFYMKYLTVYDIIKKRPDFKQQP 83
Cdd:pfam08969    1 APLKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1357729074   84 DYYITLLGQNSFKKAIEEAEKLSESLKLRYEEV 116
Cdd:pfam08969   81 ATVRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
749-1078 2.86e-28

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 115.67  E-value: 2.86e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLC-NTPAMaeyfnNNYYLEDINRSNILghKGEVAEEFGVIMKALWAGLYKFISPRDfKITIGK 827
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILAlYLPKL-----DELLDDLSKELKVL--KNVIRKPEPDLNQEEALKLFTALWSSK-EHKVGW 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  828 INDQfagYDQQDSQELLLFLMDGLHEDLNKADNRKRYK--EEENDHLDDQtaadlaWSkhkllneSIIVALFQGQF---K 902
Cdd:COG5533     73 IPPM---GSQEDAHELLGKLLDELKLDLVNSFTIRIFKttKDKKKTSTGD------WF-------DIIIELPDQTWvnnL 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  903 STVQCstchrksrTFETFMYLsLPLASTSKcslqdclrlfskeEKLTDNNKVFCRHCKAHRDStkkleiwKVPPILLVHL 982
Cdd:COG5533    137 KTLQE--------FIDNMEEL-VDDETGVK-------------AKENEELEVQAKQEYEVSFV-------KLPKILTIQL 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  983 KRFSYEGRwKQKLQTSVDFPLDnldlaqYVIGPKQTLK-----RYNLYGVSNHYGGLDGGHYTAYCKnaMKQRWYKFDDH 1057
Cdd:COG5533    188 KRFANLGG-NQKIDTEVDEKFE------LPVKHDQILNivketYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDS 258

                          330       340
                   ....*....|....*....|....
gi 1357729074 1058 EVSDISTS---SVKSSAAYILFYS 1078
Cdd:COG5533    259 DVTPVSEEeaiNEKAKNAYLYFYE 282
PHA03247 PHA03247
large tegument protein UL36; Provisional
 320-472 1.78e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  320 PPRETTVNTLPQLNFSYPSLEEPKPPVIHPEPVVQPDSQKPPA--PAvvngvAPAEPPTSKTSVIADKLPDTHDSPV--- 394
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAasPA-----GPLPPPTSAQPTAPPPPPGPPPPSLplg 2853

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  395 --ISTGLDLNKQNP---------APNQSPVTSKSFPQFDRTKKPLRDDPKAKENGSTKDSTQngPVVPDRSVKPPLIPSS 463
Cdd:PHA03247  2854 gsVAPGGDVRRRPPsrspaakpaAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPP--PPQPQPQPPPPPQPQP 2931


                   ....*....
gi 1357729074  464 SLSKEEQSQ 472
Cdd:PHA03247  2932 PPPPPPRPQ 2940
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 197-305 5.39e-04

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: 40.16  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS-PGITVNQIEAKLPSLSKDhwmrrgfvDYIVLLDWFSSVSDLklgtTL 275
Cdd:pfam00581    7 VLIDVRPPEEYAKGHI----PGAVNVPLSSLSlPPLPLLELLEKLLELLKD--------KPIVVYCNSGNRAAA----AA 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 1357729074  276 QSLKDALFKwdsitilrsEPLVLEGGYENW 305
Cdd:pfam00581   71 ALLKALGYK---------NVYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 197-310 5.84e-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: 37.44  E-value: 5.84e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074   197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS---PGITVNQIEAKLPSLSKDHwmrrgfVDYIVLLDWfssvSDLKLGT 273
Cdd:smart00450    6 VLLDVRSPEEYEGGHI----PGAVNIPLSELLdrrGELDILEFEELLKRLGLDK------DKPVVVYCR----SGNRSAK 71

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 1357729074   274 TLQSLKDALFKwdsitilrsEPLVLEGGYENWLLFYP 310
Cdd:smart00450   72 AAWLLRELGFK---------NVYLLDGGYKEWSAAGP 99
 
Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 749-1078 4.75e-114

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: 351.98  E-value: 4.75e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLCNtpamaeyfnnnyyledinrsnilghkgevaeefgvimkalwaglykfisprdfkitigki 828
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  829 ndqfagyDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFKSTVQCS 908
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  909 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKR 984
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  985 FSYEGRWKQKLQTSVDFPLDNLDLAQYVIGPKQT-LKRYNLYGVSNHYGGLDGGHYTAYCKNAMKQRWYKFDDHEVSDIS 1063
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 1357729074 1064 TSSVKSSAAYILFYS 1078
Cdd:cd02674    216 ESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
748-1077 8.86e-112

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 349.43  E-value: 8.86e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  748 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNYYLEDINRSNILGHkgeVAEEFGVIMKALW-AGLYKFISPRDFKITIG 826
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQkNSKSSSVSPKMFKKSLG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  827 KINDQFAGYDQQDSQELLLFLMDGLHEDLNkadnrkrykeeendhlddqtaadlawSKHKLLNESIIVALFQGQFKSTVQ 906
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  907 CSTCHRKSRTFETFMYLSLPL----ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHL 982
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIpgdsAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  983 KRFSYEGRWKQKLQTSVDFPLDnLDLAQYVIGPKQT----LKRYNLYGVSNHYGGLDGGHYTAYCKNAMKQRWYKFDDHE 1058
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPktnnLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290

                          330       340
                   ....*....|....*....|
gi 1357729074 1059 VSDISTS-SVKSSAAYILFY 1077
Cdd:pfam00443  291 VTEVDEEtAVLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 749-1077 3.01e-74

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: 245.86  E-value: 3.01e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLCNtpamaeyfnnnyyledinrsnilghkgevaeefgvimkalwaglykfisprdfkitigki 828
Cdd:cd02257      1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  829 ndqfagyDQQDSQELLLFLMDGLHEDLNKADNRKRYKEEendhlddqtaadlawskhkllNESIIVALFQGQFKSTVQCS 908
Cdd:cd02257     21 -------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSS---------------------LKSLIHDLFGGKLESTIVCL 72

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  909 TCHRKSRTFETFMYLSLPL--ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKaHRDSTKKLEIWKVPPILLVHLKRFS 986
Cdd:cd02257     73 ECGHESVSTEPELFLSLPLpvKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFS 151

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  987 YEGRW-KQKLQTSVDFPLDNLDLAQYVIGPKQTLK-----RYNLYGVSNHYGGL-DGGHYTAYCKNAMKQRWYKFDDHEV 1059
Cdd:cd02257    152 FNEDGtKEKLNTKVSFPLELDLSPYLSEGEKDSDSdngsyKYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDDKV 231

                          330       340
                   ....*....|....*....|...
gi 1357729074 1060 SDISTSSV-----KSSAAYILFY 1077
Cdd:cd02257    232 TEVSEEEVlefgsLSSSAYILFY 254
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 748-1078 2.32e-65

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: 222.92  E-value: 2.32e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  748 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNYYLEDINRsnilghkgevaEEFGV-------IMKALWAGLyKFISPRD 820
Cdd:cd02661      2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCN-----------EGFCMmcaleahVERALASSG-PGSAPRI 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  821 FKITIGKINDQFAGYDQQDSQELLLFLMDGLHedlnKADNRKRYKEEENDHLDDQTaadlawskhkllneSIIVALFQGQ 900
Cdd:cd02661     70 FSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDPSSQET--------------TLVQQIFGGY 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  901 FKSTVQCSTCHRKSRTFETFMYLSLPLASTSkcSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLV 980
Cdd:cd02661    132 LRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTI 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  981 HLKRFSYEGRwkQKLQTSVDFPlDNLDLAQYVIGPKQTLKRYNLYGVSNHYGG-LDGGHYTAYCKnAMKQRWYKFDDHEV 1059
Cdd:cd02661    210 HLKRFSNFRG--GKINKQISFP-ETLDLSPYMSQPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVK-SSNGKWYNMDDSKV 285

                          330
                   ....*....|....*....
gi 1357729074 1060 SDISTSSVKSSAAYILFYS 1078
Cdd:cd02661    286 SPVSIETVLSQKAYILFYI 304
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 749-1077 1.16e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 221.86  E-value: 1.16e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLCNTPAMAEYF--NNNYYLEDINRSNilghkGEVAEEFGVIMKALWAGLYK-FISPRDFKITI 825
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFlsDRHSCTCLSCSPN-----SCLSCAMDEIFQEFYYSGDRsPYGPINLLYLS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  826 GKINDQFAGYDQQDSQELLLFLMDGLHEDLnkadnrKRYKEEENDHLDDQTaadlawskhkllnesIIVALFQGQFKSTV 905
Cdd:cd02660     77 WKHSRNLAGYSQQDAHEFFQFLLDQLHTHY------GGDKNEANDESHCNC---------------IIHQTFSGSLQSSV 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  906 QCSTCHRKSRTFETFMYLSLPLASTSKCS-------------LQDCLRLFSKEEKLTDNNkVFCRHCKAHRDSTKKLEIW 972
Cdd:cd02660    136 TCQRCGGVSTTVDPFLDLSLDIPNKSTPSwalgesgvsgtptLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIK 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  973 KVPPILLVHLKRFSYE-GRWKQKLQTSVDFPLDnLDLAQYVIGPKQTLK---------RYNLYGVSNHYGGLDGGHYTAY 1042
Cdd:cd02660    215 KLPPVLCFQLKRFEHSlNKTSRKIDTYVQFPLE-LNMTPYTSSSIGDTQdsnsldpdyTYDLFAVVVHKGTLDTGHYTAY 293

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1357729074 1043 CKNAMKQrWYKFDDHEVSDISTSSVKSSAAYILFY 1077
Cdd:cd02660    294 CRQGDGQ-WFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 749-1077 5.02e-55

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: 192.99  E-value: 5.02e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLCNTPAMAEYFNNNyyledinrsnilghkgevaeefgvimkalwaglykfisPRDFKITIGKI 828
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  829 NDQFAGYDQQDSQELLLFLMDGLhedlnkadnrkrykeeendhlddqtaadlawskhkllnESIIVALFQGQFKSTVQCS 908
Cdd:cd02667     43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  909 TCHRKSRTFETFMYLSLPLA--STSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKahrDSTKKLEIWKVPPILLVHLKRFS 986
Cdd:cd02667     85 SCGTVSLVYEPFLDLSLPRSdeIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQ 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  987 YEGRWK-QKLQTSVDFPlDNLDLAQYViGPK------QTLKRYNLYGVSNHYGGLDGGHYTAYCKNAMKQR--------- 1050
Cdd:cd02667    162 QPRSANlRKVSRHVSFP-EILDLAPFC-DPKcnssedKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQrlsdltksk 239

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1357729074 1051 ------------WYKFDDHEVSDISTSSVKSSAAYILFY 1077
Cdd:cd02667    240 paadeagpgsgqWYYISDSDVREVSLEEVLKSEAYLLFY 278
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
745-927 3.44e-54

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 203.96  E-value: 3.44e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  745 ASLTGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNYYLEDINRSNILGHKGEVAEEFGVIMKALWAGLYKFISPRDFKIT 824
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  825 IGKINDQFAGYDQQDSQELLLFLMDGLHEDLNKAdNRKRYKEE----ENDHLDDQTAADLAWSKHKLLNESIIVALFQGQ 900
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                          170       180
                   ....*....|....*....|....*..
gi 1357729074  901 FKSTVQCSTCHRKSRTFETFMYLSLPL 927
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPL 448
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 749-1078 1.49e-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: 174.81  E-value: 1.49e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLcntpamaeYFNNNYY-LEDINRSnILGHKGEVaeefGVImkalwaglykfiSPRDFKITIGK 827
Cdd:cd02663      1 GLENFGNTCYCNSVLQAL--------YFENLLTcLKDLFES-ISEQKKRT----GVI------------SPKKFITRLKR 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  828 INDQFAGYDQQDSQELLLFLMDGLHEDLNKADNRKRYKEEENdhlddqtaADLAWSKHKllneSIIVALFQGQFKSTVQC 907
Cdd:cd02663     56 ENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLN--------NNNNAEPQP----TWVHEIFQGILTNETRC 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  908 STCHRKSRTFETFMYLSLPLASTskCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSY 987
Cdd:cd02663    124 LTCETVSSRDETFLDLSIDVEQN--TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKY 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  988 EGRWKQ--KLQTSVDFPL-----DNLDLAQYvigPKQTlkrYNLYGVSNHYG-GLDGGHYTAYCKNamKQRWYKFDDHEV 1059
Cdd:cd02663    202 DEQLNRyiKLFYRVVFPLelrlfNTTDDAEN---PDRL---YELVAVVVHIGgGPNHGHYVSIVKS--HGGWLLFDDETV 273

                          330       340
                   ....*....|....*....|....*..
gi 1357729074 1060 SDISTSSV-------KSSA-AYILFYS 1078
Cdd:cd02663    274 EKIDENAVeeffgdsPNQAtAYVLFYQ 300
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 749-1078 3.64e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 174.53  E-value: 3.64e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCL------------CNTPAMAEYFNNNyyledinrSNILGHKGEVAEEFGVIMKALWAGLYKFI 816
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWfmnlefrkavyeCNSTEDAELKNMP--------PDKPHEPQTIIDQLQLIFAQLQFGNRSVV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  817 SPRDFKITIGKINDQfagydQQDSQELLLFLMDGLHEDLNKADNRKrykeeendhlddqtaadlawskhkllNESIIVAL 896
Cdd:cd02668     73 DPSGFVKALGLDTGQ-----QQDAQEFSKLFLSLLEAKLSKSKNPD--------------------------LKNIVQDL 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  897 FQGQFKSTVQCSTCHRKSRTFETFMYLSLPLASTSKcsLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPP 976
Cdd:cd02668    122 FRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT--LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPP 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  977 ILLVHLKRFSY--EGRWKQKLQTSVDFPLDnLDLAQYVIGPKQTLKRYNLYGVSNHYG-GLDGGHYTAYCKNAMKQRWYK 1053
Cdd:cd02668    200 TLNFQLLRFVFdrKTGAKKKLNASISFPEI-LDMGEYLAESDEGSYVYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYK 278

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1357729074 1054 FDDHEVSDISTSSVK---------------------SSAAYILFYS 1078
Cdd:cd02668    279 FNDEDVEEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVYK 324
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 749-1077 4.04e-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: 163.20  E-value: 4.04e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLCNTPamaeYFNNNYYledinrsNILGHKGEVAE-----EFGVIMKALWAGLYKFISPRDFKI 823
Cdd:cd02659      4 GLKNQGATCYMNSLLQQLYMTP----EFRNAVY-------SIPPTEDDDDNksvplALQRLFLFLQLSESPVKTTELTDK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  824 TIGKINDQFAGYDQQDSQELLLFLMDGLHEDLNKAdnrkrykEEENdhlddqtaadlawskhkllnesIIVALFQGQFKS 903
Cdd:cd02659     73 TRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGT-------GQEG----------------------LIKNLFGGKLVN 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  904 TVQCSTCHRKSRTFETFmyLSLPLASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLK 983
Cdd:cd02659    124 YIICKECPHESEREEYF--LDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLK 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  984 RFSYEGR--WKQKLQTSVDFPLDnLDLAQYVI----------GPKQTLK-RYNLYGVSNHYGGLDGGHYTAYCKNAMKQR 1050
Cdd:cd02659    202 RFEFDFEtmMRIKINDRFEFPLE-LDMEPYTEkglakkegdsEKKDSESyIYELHGVLVHSGDAHGGHYYSYIKDRDDGK 280

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1357729074 1051 WYKFDDHEVSDISTSSV----------------------KSSAAYILFY 1077
Cdd:cd02659    281 WYKFNDDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFY 329
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 749-1077 6.29e-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: 136.47  E-value: 6.29e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLcntpAMAEYFNNnyyleDINRSNILGHKGEVAEEFGVIM-KALWAglykfISPRDFKITIGK 827
Cdd:cd02664      1 GLINLGNTCYMNSVLQAL----FMAKDFRR-----QVLSLNLPRLGDSQSVMKKLQLlQAHLM-----HTQRRAEAPPDY 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  828 INDQ-----FAGYDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFK 902
Cdd:cd02664     67 FLEAsrppwFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLS 108

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  903 STVQCSTCHRKSRTFETFMYLSLplastSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHL 982
Cdd:cd02664    109 TTIRCLNCNSTSARTERFRDLDL-----SFPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTL 183

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  983 KRFSY--EGRWKQKLQTSVDFPLDnLDLAQYV----IGPKQTLKR---------------YNLYGVSNHYG-GLDGGHYT 1040
Cdd:cd02664    184 LRFSYdqKTHVREKIMDNVSINEV-LSLPVRVesksSESPLEKKEeesgddgelvtrqvhYRLYAVVVHSGySSESGHYF 262

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357729074 1041 AYCKN--------------------AMKQRWYKFDDHEVSDISTSSVK-------SSAAYILFY 1077
Cdd:cd02664    263 TYARDqtdadstgqecpepkdaeenDESKNWYLFNDSRVTFSSFESVQnvtsrfpKDTPYILFY 326
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 6-116 4.81e-32

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: 120.87  E-value: 4.81e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074    6 TEVKELYLSSCLGDLNKKAEIKPD--KTSTRSYVQSACKLFKAAEECRLDRDEEKAYVFYMKYLTVYDIIKKRPDFKQQP 83
Cdd:pfam08969    1 APLKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1357729074   84 DYYITLLGQNSFKKAIEEAEKLSESLKLRYEEV 116
Cdd:pfam08969   81 ATVRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 749-1077 1.26e-31

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 125.91  E-value: 1.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLCNTPAMAE---YFNNNYYLEDINRSNILghkgevaeefgVIMKALWAGLYKF---ISPRDFK 822
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPARRGANQSSDNLT-----------NALRDLFDTMDKKqepVPPIEFL 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  823 ITIGKINDQFA------GYDQQDSQELLLFLMDGLHEDLNKADnrkrykeEENDHLDDqtaadlawskhkllnesiivaL 896
Cdd:cd02657     70 QLLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAG-------SKGSFIDQ---------------------L 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  897 FQGQFKSTVQCS-TCHRKSRTFETFMYLSLPLASTSKCS-LQDCLRLFSKEE--KLTDnnkvfcrhcKAHRDS--TKKLE 970
Cdd:cd02657    122 FGIELETKMKCTeSPDEEEVSTESEYKLQCHISITTEVNyLQDGLKKGLEEEieKHSP---------TLGRDAiyTKTSR 192

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  971 IWKVPPILLVHLKRFSyegrWKQKLQT------SVDFPLdNLDLAQYVIGPKQtlkrYNLYGVSNHYG-GLDGGHYTAYC 1043
Cdd:cd02657    193 ISRLPKYLTVQFVRFF----WKRDIQKkakilrKVKFPF-ELDLYELCTPSGY----YELVAVITHQGrSADSGHYVAWV 263

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1357729074 1044 KNAMKQRWYKFDDHEVSDISTSSVKSSA-------AYILFY 1077
Cdd:cd02657    264 RRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 728-1077 2.66e-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: 2.66e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  728 PSAAKIRSLNPtfgglgasLTGLRNLGNTCYMNSILQCLCNTPAmaeyfnnnyYLEDINRSNILGHKGEVAEEFGVIMKA 807
Cdd:cd02671     13 TSCEKRENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPG---------FKHGLKHLVSLISSVEQLQSSFLLNPE 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  808 LWAGLYKFISPRDFKITIGKINDQFAGYDQQDSQELLLFLMDGLHEDLNKadnrkrykeeendhlddqtaadlawskhkl 887
Cdd:cd02671     76 KYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK------------------------------ 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  888 lnesiivaLFQGQFKSTVQCSTCHRKSRTFETFMYLSLPLASTSKCS-----------------LQDCLRLFSKEEKLTD 950
Cdd:cd02671    126 --------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKseesseispdpktemktLKWAISQFASVERIVG 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  951 NNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRWK------QKLQTSVDFPldnLDLAQYVIGPKQTLKRYNL 1024
Cdd:cd02671    198 EDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTP---LKLSLEEWSTKPKNDVYRL 274

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357729074 1025 YGVSNHYGG-LDGGHYTAYCknamkqRWYKFDDHEV---------SDISTSSVKSSAAYILFY 1077
Cdd:cd02671    275 FAVVMHSGAtISSGHYTAYV------RWLLFDDSEVkvteekdflEALSPNTSSTSTPYLLFY 331
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
749-1078 2.86e-28

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 115.67  E-value: 2.86e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLC-NTPAMaeyfnNNYYLEDINRSNILghKGEVAEEFGVIMKALWAGLYKFISPRDfKITIGK 827
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILAlYLPKL-----DELLDDLSKELKVL--KNVIRKPEPDLNQEEALKLFTALWSSK-EHKVGW 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  828 INDQfagYDQQDSQELLLFLMDGLHEDLNKADNRKRYK--EEENDHLDDQtaadlaWSkhkllneSIIVALFQGQF---K 902
Cdd:COG5533     73 IPPM---GSQEDAHELLGKLLDELKLDLVNSFTIRIFKttKDKKKTSTGD------WF-------DIIIELPDQTWvnnL 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  903 STVQCstchrksrTFETFMYLsLPLASTSKcslqdclrlfskeEKLTDNNKVFCRHCKAHRDStkkleiwKVPPILLVHL 982
Cdd:COG5533    137 KTLQE--------FIDNMEEL-VDDETGVK-------------AKENEELEVQAKQEYEVSFV-------KLPKILTIQL 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  983 KRFSYEGRwKQKLQTSVDFPLDnldlaqYVIGPKQTLK-----RYNLYGVSNHYGGLDGGHYTAYCKnaMKQRWYKFDDH 1057
Cdd:COG5533    188 KRFANLGG-NQKIDTEVDEKFE------LPVKHDQILNivketYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDS 258

                          330       340
                   ....*....|....*....|....
gi 1357729074 1058 EVSDISTS---SVKSSAAYILFYS 1078
Cdd:COG5533    259 DVTPVSEEeaiNEKAKNAYLYFYE 282
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 749-1077 9.72e-28

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: 114.73  E-value: 9.72e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLCNTPAMAEYFNNNYYLEDINRSNI----------LGHkGEVAEEFGVIM--KALWAGLYKFI 816
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPandlncqlikLAD-GLLSGRYSKPAslKSENDPYQVGI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  817 SPRDFKITIGKINDQFAGYDQQDSQELLLFLMDglhedlnKADNRKRYKEEENdhlddqtaadlawskhklLNEsiivaL 896
Cdd:cd02658     80 KPSMFKALIGKGHPEFSTMRQQDALEFLLHLID-------KLDRESFKNLGLN------------------PND-----L 129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  897 FQGQFKSTVQCSTCHRKSRTFETFMYLSLPL------------ASTSKCSLQDCLRLFSKEEKLTDnnkvFCRHCKAHRD 964
Cdd:cd02658    130 FKFMIEDRLECLSCKKVKYTSELSEILSLPVpkdeatekeegeLVYEPVPLEDCLKAYFAPETIED----FCSTCKEKTT 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  965 STKKLEIWKVPPILLVHLKRFSYEGRWKQ-KLQTSVDFPldnldlaqYVIGPkqtlKRYNLYGVSNHYG-GLDGGHYTAY 1042
Cdd:cd02658    206 ATKTTGFKTFPDYLVINMKRFQLLENWVPkKLDVPIDVP--------EELGP----GKYELIAFISHKGtSVHSGHYVAH 273

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1357729074 1043 CK--NAMKQRWYKFDDHEVSDISTSSVKSSAAYILFY 1077
Cdd:cd02658    274 IKkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 749-1077 3.25e-24

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 102.83  E-value: 3.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLCNTPAMAEYFNNnyYLEdinrsnilghkgevaeefgvimkalwaglykfisprdfkitigki 828
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLIEYLEE--FLE--------------------------------------------- 33

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  829 ndqfagydQQDSQELLLFLMDGLhedlnkadnrkrykeeendhlddqtaadlawskhkllnESIIVALFQGQFKSTVQCS 908
Cdd:cd02662     34 --------QQDAHELFQVLLETL--------------------------------------EQLLKFPFDGLLASRIVCL 67

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  909 TCHRKSR-TFETFMYLSLPL---ASTSKCSLQDCLRLFSKEEKLTDnnkVFCRHCKahrdstkkLEIWKVPPILLVHLKR 984
Cdd:cd02662     68 QCGESSKvRYESFTMLSLPVpnqSSGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSR 136

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  985 FSYEGRWK-QKLQTSVDFPLDnldLAQYvigpkqtlkRYNLYGVSNHYGGLDGGHYTAY--------------------C 1043
Cdd:cd02662    137 SVFDGRGTsTKNSCKVSFPER---LPKV---------LYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreG 204

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1357729074 1044 KNAMKQRWYKFDDHEVSDISTSSVK-SSAAYILFY 1077
Cdd:cd02662    205 PSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 749-1060 5.30e-22

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 103.03  E-value: 5.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  749 GLRNLGNTCYMNSILQCLCNTpamaEYFNNNYY-LEDINRSNilghKGEVAeefgVIMKALWAGLYKFISPRD-FKITIG 826
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFI----AKFRKDVYgIPTDHPRG----RDSVA----LALQRLFYNLQTGEEPVDtTELTRS 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  827 KINDQFAGYDQQDSQELLLFLMDGLhedlnkaDNRKRYKEEENdhlddqtaadlawskhkLLNEsiivaLFQGQFKSTVQ 906
Cdd:COG5077    263 FGWDSDDSFMQHDIQEFNRVLQDNL-------EKSMRGTVVEN-----------------ALNG-----IFVGKMKSYIK 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  907 CSTCHRKSRTFETFMYLSLPLASTSkcSLQDCLRLFSKEEKLTDNNKVFCRHcKAHRDSTKKLEIWKVPPILLVHLKRFS 986
Cdd:COG5077    314 CVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFE 390

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  987 YEGRWKQ--KLQTSVDFPlDNLDLAQYVigPKQTLKR------YNLYGVSNHYGGLDGGHYTAYCKNAMKQRWYKFDDHE 1058
Cdd:COG5077    391 YDFERDMmvKINDRYEFP-LEIDLLPFL--DRDADKSensdavYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTR 467


                   ..
gi 1357729074 1059 VS 1060
Cdd:COG5077    468 VT 469
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 711-1077 1.56e-21

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 98.93  E-value: 1.56e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  711 DTKPVTSKVYSKVEIAR--PSAAKIRSLN-----PTFgglgaslTGLRNLGNTCYMNSILQCLCNTPAMaeyfnNNYYLE 783
Cdd:cd02669     83 DIKYVLNPTYTKEQISDldRDPKLSRDLDgkpylPGF-------VGLNNIKNNDYANVIIQALSHVKPI-----RNFFLL 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  784 DINRSNILGHKGEVAEEFGVIMKALW-AGLYK-FISPRDFKITIGKI-NDQFAGYDQQDSQELLLFLMDGLHEDLNKADN 860
Cdd:cd02669    151 YENYENIKDRKSELVKRLSELIRKIWnPRNFKgHVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKK 230

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  861 RkrykeeendhlddqtaadlawskhkllNESIIVALFQG--------------QFKSTVQCSTCHR-KSRTFETFMYLS- 924
Cdd:cd02669    231 P---------------------------NSSIIHDCFQGkvqietqkikphaeEEGSKDKFFKDSRvKKTSVSPFLLLTl 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  925 -LPLASTSKCSLQD-CLRLFSKEEKLTDNNKVfcrHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRWKQKLQTSVDFP 1002
Cdd:cd02669    284 dLPPPPLFKDGNEEnIIPQVPLKQLLKKYDGK---TETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFP 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074 1003 LDNLDLAQYVIGPKQTLKR---YNLygVSN--HYGG-LDGGHYTAYCKNAMKQRWYKFDDHEVSDISTSSVKSSAAYILF 1076
Cdd:cd02669    361 IKNLDLSDYVHFDKPSLNLstkYNL--VANivHEGTpQEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQI 438


                   .
gi 1357729074 1077 Y 1077
Cdd:cd02669    439 W 439
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 750-1077 3.65e-12

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


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 67.55  E-value: 3.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  750 LRNLGNTCYMNSILQCLCntpamaeyfnnnyyledinrsnilghkgevaeefgvimkalwaglykfisprdfkiTIGKIN 829
Cdd:cd02673      2 LVNTGNSCYFNSTMQALS--------------------------------------------------------SIGKIN 25

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  830 DQFAGYDQQDSQELLLFL---MDGLHEdlNKADNRKRYkEEENDHLDDQTAadlawskHKLLNESIIValfqgqfkstvq 906
Cdd:cd02673     26 TEFDNDDQQDAHEFLLTLleaIDDIMQ--VNRTNVPPS-NIEIKRLNPLEA-------FKYTIESSYV------------ 83

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  907 CSTCHRKSRTFETFMYLSLPLASTSKCSLQDclrLFSKEEKLTDNNKVfCRHCKaHRDSTKKLEIWKVPPILLVHLKRFs 986
Cdd:cd02673     84 CIGCSFEENVSDVGNFLDVSMIDNKLDIDEL---LISNFKTWSPIEKD-CSSCK-CESAISSERIMTFPECLSINLKRY- 157

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  987 yegrwkqKLQTSVdfpLDNLDLAQYVIGPKQ-TLKRYNLYGVSNHYG-GLDGGHYTAYCKNAMK-QRWYKFDDHEVSDIS 1063
Cdd:cd02673    158 -------KLRIAT---SDYLKKNEEIMKKYCgTDAKYSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIRPVS 227

                          330
                   ....*....|....*..
gi 1357729074 1064 TSSVK---SSAAYILFY 1077
Cdd:cd02673    228 KNDVStnaRSSGYLIFY 244
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 837-1077 8.79e-09

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 57.18  E-value: 8.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  837 QQDSQELLLFLMDGLHEDLNKADNRKRYKEEendhlddqtaadlawSKHKLlnesiiVALFQGQFkSTVqcsTCHRKSRT 916
Cdd:cd02665     22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEK---------------SKNPM------VQLFYGTF-LTE---GVLEGKPF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  917 FETFMYLSLPLASTSKCSLQDCLrlfskeEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRWKQKLQ 996
Cdd:cd02665     77 CNCETFGQYPLQVNGYGNLHECL------EAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPEKIH 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  997 TSVDFPldnldlaqyvigpkQTLKR--YNLYGVSNHYGGLDGGHYTAYCKNAMKQRWYKFDDHEVSDISTSSVKSSA--- 1071
Cdd:cd02665    151 DKLEFP--------------QIIQQvpYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfgg 216

                          250
                   ....*....|.
gi 1357729074 1072 -----AYILFY 1077
Cdd:cd02665    217 grnpsAYCLMY 227
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
874-1056 5.22e-08

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 55.74  E-value: 5.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  874 DQTAADLAWSKHKLL-NESIIVALFQGQFKSTVQCSTC-HRKSRTFETFM----YLSLPLASTSKCSLQD---CLRLFSK 944
Cdd:pfam13423  108 DQLSSEENSTPPNPSpAESPLEQLFGIDAETTIRCSNCgHESVRESSTHVldliYPRKPSSNNKKPPNQTfssILKSSLE 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  945 EEKLTdnnKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEgrWKQKLQTSVDFPLD-NLDLAQYVIGPKQTLKrYN 1023
Cdd:pfam13423  188 RETTT---KAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPEiGLTLSDDLQGDNEIVK-YE 261

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1357729074 1024 LYG-VSNHYGGLDGGHYTAYCKNAMK-------QRWYKFDD 1056
Cdd:pfam13423  262 LRGvVVHIGDSGTSGHLVSFVKVADSeledpteSQWYLFND 302
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 884-1077 4.93e-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: 52.51  E-value: 4.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  884 KHKLLNE-----SIIVALFQGQFKSTVQC-----STCHRKSRTFETFMY-LSLPLASTSKCSLQDCLRLFSKEEKLTDNN 952
Cdd:cd02672     54 ESCLLCElgylfSTLIQNFTRFLLETISQdqlgtPFSCGTSRNSVSLLYtLSLPLGSTKTSKESTFLQLLKRSLDLEKVT 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  953 KVFCRHCKAHRDSTKKLEIWKVPPILL----VHLKRFSYEGRWKQ-------KLQTSVDFPLDNLDLAQYVIGPKQTLKr 1021
Cdd:cd02672    134 KAWCDTCCKYQPLEQTTSIRHLPDILLlvlvINLSVTNGEFDDINvvlpsgkVMQNKVSPKAIDHDKLVKNRGQESIYK- 212

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357729074 1022 YNLYG-VSNHYGGLDGGHYTA----YCKNAMKQRWYKFDDHEVSDISTSsvkssaAYILFY 1077
Cdd:cd02672    213 YELVGyVCEINDSSRGQHNVVfvikVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
PHA03247 PHA03247
large tegument protein UL36; Provisional
 320-472 1.78e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  320 PPRETTVNTLPQLNFSYPSLEEPKPPVIHPEPVVQPDSQKPPA--PAvvngvAPAEPPTSKTSVIADKLPDTHDSPV--- 394
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAasPA-----GPLPPPTSAQPTAPPPPPGPPPPSLplg 2853

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  395 --ISTGLDLNKQNP---------APNQSPVTSKSFPQFDRTKKPLRDDPKAKENGSTKDSTQngPVVPDRSVKPPLIPSS 463
Cdd:PHA03247  2854 gsVAPGGDVRRRPPsrspaakpaAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPP--PPQPQPQPPPPPQPQP 2931


                   ....*....
gi 1357729074  464 SLSKEEQSQ 472
Cdd:PHA03247  2932 PPPPPPRPQ 2940
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 197-305 5.39e-04

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: 40.16  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS-PGITVNQIEAKLPSLSKDhwmrrgfvDYIVLLDWFSSVSDLklgtTL 275
Cdd:pfam00581    7 VLIDVRPPEEYAKGHI----PGAVNVPLSSLSlPPLPLLELLEKLLELLKD--------KPIVVYCNSGNRAAA----AA 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 1357729074  276 QSLKDALFKwdsitilrsEPLVLEGGYENW 305
Cdd:pfam00581   71 ALLKALGYK---------NVYVLDGGFEAW 91
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 748-1067 5.71e-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: 43.25  E-value: 5.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  748 TGLRNLGNTCYMNSILQCL-CNTPA-----MAEYFNNNYYLEDINRSNILGHKGEVAEEFGVIMKALWAGL--YKFISPR 819
Cdd:cd02666      2 AGLDNIGNTCYLNSLLQYFfTIKPLrdlvlNFDESKAELASDYPTERRIGGREVSRSELQRSNQFVYELRSlfNDLIHSN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  820 DFKITIGKiNDQFAGYDQQDSQELLLFLMDglheDLNKADNRKRYKEEENDHLDDQTAADLawskhkllnesiIVALFQG 899
Cdd:cd02666     82 TRSVTPSK-ELAYLALRQQDVTECIDNVLF----QLEVALEPISNAFAGPDTEDDKEQSDL------------IKRLFSG 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  900 QFK-STVQCSTCHRKSRT--FETFMYLSLPLAST--------SKCSLQDCL----------------RLFSKEEKLTDNN 952
Cdd:cd02666    145 KTKqQLVPESMGNQPSVRtkTERFLSLLVDVGKKgreivvllEPKDLYDALdryfdydsltklpqrsQVQAQLAQPLQRE 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  953 KVFCRHCKAHRDSTKKLEIWK--VPPILLVHLKRFSYEGRWKQKLQTSVDfpldnlDLAQYVigpkqtlkrYNLYGVSNH 1030
Cdd:cd02666    225 LISMDRYELPSSIDDIDELIReaIQSESSLVRQAQNELAELKHEIEKQFD------DLKSYG---------YRLHAVFIH 289

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1357729074 1031 YGGLDGGHYTAYCKNAMKQRWYKFDDHEVSDISTSSV 1067
Cdd:cd02666    290 RGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEV 326
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 337-465 1.30e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.78  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074  337 PSLEEPKPPVIHPEPVVQPDSQKP---PAPAVVNGVAPAEPPTSKTSVIADKLPDTHDSPVISTGLDLNKQNPAPNQSPV 413
Cdd:PRK14951   366 PAAAAEAAAPAEKKTPARPEAAAPaaaPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAV 445

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1357729074  414 TSKSFPqfdrtkkplrDDPKAKENGSTKDSTQNGPVVPDRSVKPPLIPSSSL 465
Cdd:PRK14951   446 ALAPAP----------PAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAAR 487
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 197-310 5.84e-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: 37.44  E-value: 5.84e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357729074   197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS---PGITVNQIEAKLPSLSKDHwmrrgfVDYIVLLDWfssvSDLKLGT 273
Cdd:smart00450    6 VLLDVRSPEEYEGGHI----PGAVNIPLSELLdrrGELDILEFEELLKRLGLDK------DKPVVVYCR----SGNRSAK 71

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 1357729074   274 TLQSLKDALFKwdsitilrsEPLVLEGGYENWLLFYP 310
Cdd:smart00450   72 AAWLLRELGFK---------NVYLLDGGYKEWSAAGP 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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