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Conserved domains on  [gi|1786651895|gb|KAF0043010|]
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hypothetical protein F2P81_004347 [Scophthalmus maximus]

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 ...
 751-1080 9.64e-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: 351.20  E-value: 9.64e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLCNtpamaeyfnnncymadinrynilghkgevaeefgvimkalwaglykfisprdfkvtigki 830
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  831 neqfagyDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddpmaadlawskhkllneSIIVALFQGQFKSTVQCL 910
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  911 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKR 986
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  987 FSYEGRWKQKLQTTVDFPLDSLDLAQYVIGP-KQNQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSEIS 1065
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 1786651895 1066 TSSVKSSAAYILFYS 1080
Cdd:cd02674    216 ESSVVSSSAYILFYE 230
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
749-929 3.34e-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: 197.80  E-value: 3.34e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  749 LTGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNCYMADINRYNILGHKGEVAEEFGVIMKALWAGLYKFISPRDFKVTIG 828
Cdd:COG5560    265 TCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIG 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  829 KINEQFAGYDQQDSQELLLFLMDGLHEDLNKAdNRKRYKEEENDHLDDPMA----ADLAWSKHKLLNESIIVALFQGQFK 904
Cdd:COG5560    345 SFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKPDLSPGDDVVvkkkAKECWWEHLKRNDSIITDLFQGMYK 423

                          170       180
                   ....*....|....*....|....*
gi 1786651895  905 STVQCLTCHRKSRTFETFMYLSLPL 929
Cdd:COG5560    424 STLTCPGCGSVSITFDPFMDLTLPL 448
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 8-116 3.30e-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: 121.25  E-value: 3.30e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895    8 VKELYLSSSLGDLNKKAEIRPD--KTSTRSYVQSACKIFKAAEEFRLDRDEEKAYVLYMKYLTVYEIIKKRPDFKEQPDY 85
Cdd:pfam08969    3 LKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVKAT 82

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1786651895   86 FMTILGPNSFKKAIVEAEKLSDSLKLRYEEV 116
Cdd:pfam08969   83 VRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 316-635 2.92e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.14  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  316 VRPPRQNIISTLPQLNFSYPslieprPPTPTQQEPEVTPKPQETLDPVLANGVTPADPPTSETSMVTDSLQEdtvdfPVK 395
Cdd:pfam03154  429 AQPPVLTQSQSLPPPAASHP------PTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQP-----PSS 497

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  396 VSTSSALDLSKKGSAAAPSSQSPATAKAFPQFDRAKKPSIRvSDEPKPS---QNGSAKDSNPFVP--DR----TAKPSFV 466
Cdd:pfam03154  498 ASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPR-SPSPEPTvvnTPSHASQSARFYKhlDRgynsCARTDLY 576

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  467 pNTSLSKEEQSRIHSEAvagIEKAKQEQEKRiqerrekeqkEKElkerqtgeesEKrkkedeelkhqdkkklERQKAEEV 546
Cdd:pfam03154  577 -FMPLAGSKLAKKREEA---LEKAKREAEQK----------ARE----------EK----------------EREKEKEK 616

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  547 EDKENRPSEEKRRRGKEQSSDAPSKSMSlDSPAPNPNHIVSEIKREPLTRArseemgrSVPGL--PDgwMKFLDTVTGTY 624
Cdd:pfam03154  617 EREREREREREAERAAKASSSSHEGRMG-DPQLAGPAHMRPSFEPPPTTIA-------AVPPYigPD--TPALRTLSEYA 686

                          330
                   ....*....|..
gi 1786651895  625 R-YYHSPTNRVH 635
Cdd:pfam03154  687 RpHVMSPTNRNH 698
 
Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 751-1080 9.64e-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: 351.20  E-value: 9.64e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLCNtpamaeyfnnncymadinrynilghkgevaeefgvimkalwaglykfisprdfkvtigki 830
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  831 neqfagyDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddpmaadlawskhkllneSIIVALFQGQFKSTVQCL 910
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  911 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKR 986
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  987 FSYEGRWKQKLQTTVDFPLDSLDLAQYVIGP-KQNQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSEIS 1065
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 1786651895 1066 TSSVKSSAAYILFYS 1080
Cdd:cd02674    216 ESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
750-1079 3.54e-111

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 347.89  E-value: 3.54e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  750 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNCYMADINRYNILGHkgeVAEEFGVIMKALW-AGLYKFISPRDFKVTIG 828
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQkNSKSSSVSPKMFKKSLG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  829 KINEQFAGYDQQDSQELLLFLMDGLHEDLNkadnrkrykeeendhlddpmaadlawSKHKLLNESIIVALFQGQFKSTVQ 908
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  909 CLTCHRKSRTFETFMYLSLPL----ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHL 984
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIpgdsAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  985 KRFSYEGRWKQKLQTTVDFPLDsLDLAQYVIGPKQ----NQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHE 1060
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKpktnNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290

                          330       340
                   ....*....|....*....|
gi 1786651895 1061 VSEISTS-SVKSSAAYILFY 1079
Cdd:pfam00443  291 VTEVDEEtAVLSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
749-929 3.34e-52

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 197.80  E-value: 3.34e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  749 LTGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNCYMADINRYNILGHKGEVAEEFGVIMKALWAGLYKFISPRDFKVTIG 828
Cdd:COG5560    265 TCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIG 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  829 KINEQFAGYDQQDSQELLLFLMDGLHEDLNKAdNRKRYKEEENDHLDDPMA----ADLAWSKHKLLNESIIVALFQGQFK 904
Cdd:COG5560    345 SFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKPDLSPGDDVVvkkkAKECWWEHLKRNDSIITDLFQGMYK 423

                          170       180
                   ....*....|....*....|....*
gi 1786651895  905 STVQCLTCHRKSRTFETFMYLSLPL 929
Cdd:COG5560    424 STLTCPGCGSVSITFDPFMDLTLPL 448
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
760-1079 4.04e-43

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 169.68  E-value: 4.04e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  760 YMNSILQCLCNTPAMAEYFNNNCYMADINRYNILghkgevaeefgvIMKALWAGLYKFISPRDFKVTIGKINEQFagydq 839
Cdd:COG5560    536 NDNGIEVPVVHLRIEKGYKSKRLFGDPFLQLNVL------------IKASIYDKLVKEFEELLVLVEMKKTDVDL----- 598

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  840 qDSQELLLFLMD---GLHEDLNKADNRKRYK---EEENDHLDDPMAADLAWSKHKLLnesiivALFQGQFKSTVQCLTCH 913
Cdd:COG5560    599 -VSEQVRLLREEsspSSWLKLETEIDTKREEqveEEGQMNFNDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAA 671

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  914 RKSRTfetfmylslplastskcsLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRW 993
Cdd:COG5560    672 ERTIT------------------LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF 733

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  994 KQKLQTTVDFPLDSLDLAQYVIGPKQNQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSEISTSSVKSSA 1073
Cdd:COG5560    734 RDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSS 813


                   ....*.
gi 1786651895 1074 AYILFY 1079
Cdd:COG5560    814 AYVLFY 819
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 8-116 3.30e-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: 121.25  E-value: 3.30e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895    8 VKELYLSSSLGDLNKKAEIRPD--KTSTRSYVQSACKIFKAAEEFRLDRDEEKAYVLYMKYLTVYEIIKKRPDFKEQPDY 85
Cdd:pfam08969    3 LKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVKAT 82

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1786651895   86 FMTILGPNSFKKAIVEAEKLSDSLKLRYEEV 116
Cdd:pfam08969   83 VRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 316-635 2.92e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.14  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  316 VRPPRQNIISTLPQLNFSYPslieprPPTPTQQEPEVTPKPQETLDPVLANGVTPADPPTSETSMVTDSLQEdtvdfPVK 395
Cdd:pfam03154  429 AQPPVLTQSQSLPPPAASHP------PTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQP-----PSS 497

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  396 VSTSSALDLSKKGSAAAPSSQSPATAKAFPQFDRAKKPSIRvSDEPKPS---QNGSAKDSNPFVP--DR----TAKPSFV 466
Cdd:pfam03154  498 ASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPR-SPSPEPTvvnTPSHASQSARFYKhlDRgynsCARTDLY 576

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  467 pNTSLSKEEQSRIHSEAvagIEKAKQEQEKRiqerrekeqkEKElkerqtgeesEKrkkedeelkhqdkkklERQKAEEV 546
Cdd:pfam03154  577 -FMPLAGSKLAKKREEA---LEKAKREAEQK----------ARE----------EK----------------EREKEKEK 616

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  547 EDKENRPSEEKRRRGKEQSSDAPSKSMSlDSPAPNPNHIVSEIKREPLTRArseemgrSVPGL--PDgwMKFLDTVTGTY 624
Cdd:pfam03154  617 EREREREREREAERAAKASSSSHEGRMG-DPQLAGPAHMRPSFEPPPTTIA-------AVPPYigPD--TPALRTLSEYA 686

                          330
                   ....*....|..
gi 1786651895  625 R-YYHSPTNRVH 635
Cdd:pfam03154  687 RpHVMSPTNRNH 698
PTZ00121 PTZ00121
MAEBL; Provisional
 471-568 7.91e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 7.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  471 LSKEEQSRIHSEAVAGIE---------KAKQEQEKRIQERREKEQKEKELKERQTGEESEKRKKEDEELKHQDKKKLERQ 541
Cdd:PTZ00121  1612 AKKAEEAKIKAEELKKAEeekkkveqlKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691

                           90       100
                   ....*....|....*....|....*..
gi 1786651895  542 KAEEVEDKENRPSEEKRRRGKEQSSDA 568
Cdd:PTZ00121  1692 EALKKEAEEAKKAEELKKKEAEEKKKA 1718
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
 344-590 4.42e-03

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 41.23  E-value: 4.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  344 TPTQQEPEVTPKPQETldPVLANGVTPADPPTSETSMVTD--SLQEDTVDFPVKVSTSSALDLSKKGSAAAPS----SQS 417
Cdd:NF033875    38 TDNVQAAELDTQPGTT--TVQPDNPDPQSGSETPKTAVSEeaTVQKDTTSQPTKVEEVASEKNGAEQSSATPNdttnAQQ 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  418 PaTAKAFPQFDRAKKPSIRVSDEP-------KPSQNGSAKDSN-------PFVPDRTAKPSFVPNTSLSK---EEQSRIH 480
Cdd:NF033875   116 P-TVGAEKSAQEQPVVSPETTNEPlgqptevAPAENEANKSTSipkefetPDVDKAVDEAKKDPNITVVEkpaEDLGNVS 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  481 SEAVAGIEKA----KQEQEKRIQERREkeqkekelkerQTGEESEKRKKEDEELKHQDKKKLERQKAEEVEdkenrpsEE 556
Cdd:NF033875   195 SKDLAAKEKEvdqlQKEQAKKIAQQAA-----------ELKAKNEKIAKENAEIAAKNKAEKERYEKEVAE-------YN 256

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1786651895  557 KRRRGKEQSSDAPSKSMSLDSPAPNPNHIVSEIK 590
Cdd:NF033875   257 KHKNENGYVNEAISKNLVFDQSVVTKDTKISSIK 290
 
Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 751-1080 9.64e-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: 351.20  E-value: 9.64e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLCNtpamaeyfnnncymadinrynilghkgevaeefgvimkalwaglykfisprdfkvtigki 830
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  831 neqfagyDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddpmaadlawskhkllneSIIVALFQGQFKSTVQCL 910
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  911 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKR 986
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  987 FSYEGRWKQKLQTTVDFPLDSLDLAQYVIGP-KQNQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSEIS 1065
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 1786651895 1066 TSSVKSSAAYILFYS 1080
Cdd:cd02674    216 ESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
750-1079 3.54e-111

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 347.89  E-value: 3.54e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  750 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNCYMADINRYNILGHkgeVAEEFGVIMKALW-AGLYKFISPRDFKVTIG 828
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQkNSKSSSVSPKMFKKSLG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  829 KINEQFAGYDQQDSQELLLFLMDGLHEDLNkadnrkrykeeendhlddpmaadlawSKHKLLNESIIVALFQGQFKSTVQ 908
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  909 CLTCHRKSRTFETFMYLSLPL----ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHL 984
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIpgdsAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  985 KRFSYEGRWKQKLQTTVDFPLDsLDLAQYVIGPKQ----NQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHE 1060
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKpktnNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290

                          330       340
                   ....*....|....*....|
gi 1786651895 1061 VSEISTS-SVKSSAAYILFY 1079
Cdd:pfam00443  291 VTEVDEEtAVLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 751-1079 3.87e-75

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: 248.55  E-value: 3.87e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLCNtpamaeyfnnncymadinrynilghkgevaeefgvimkalwaglykfisprdfkvtigki 830
Cdd:cd02257      1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  831 neqfagyDQQDSQELLLFLMDGLHEDLNKADNRKRYKEEendhlddpmaadlawskhkllNESIIVALFQGQFKSTVQCL 910
Cdd:cd02257     21 -------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSS---------------------LKSLIHDLFGGKLESTIVCL 72

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  911 TCHRKSRTFETFMYLSLPL--ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKaHRDSTKKLEIWKVPPILLVHLKRFS 988
Cdd:cd02257     73 ECGHESVSTEPELFLSLPLpvKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFS 151

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  989 YEGRW-KQKLQTTVDFPLdSLDLAQYV------IGPKQNQKRYGLYGVSNHYGGL-DGGHYTAYCKNALKQRWYKFDDHE 1060
Cdd:cd02257    152 FNEDGtKEKLNTKVSFPL-ELDLSPYLsegekdSDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDDK 230

                          330       340
                   ....*....|....*....|....
gi 1786651895 1061 VSEISTSSV-----KSSAAYILFY 1079
Cdd:cd02257    231 VTEVSEEEVlefgsLSSSAYILFY 254
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 750-1080 1.45e-67

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: 229.08  E-value: 1.45e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  750 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNCYMADINRynilghkgevaEEFGV-------IMKALWAGLyKFISPRD 822
Cdd:cd02661      2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCN-----------EGFCMmcaleahVERALASSG-PGSAPRI 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  823 FKVTIGKINEQFAGYDQQDSQELLLFLMDGLHedlnKADNRKRYKEEENDHLddpmAADLAWSKHkllnesiivaLFQGQ 902
Cdd:cd02661     70 FSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDPS----SQETTLVQQ----------IFGGY 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  903 FKSTVQCLTCHRKSRTFETFMYLSLPLASTSkcSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLV 982
Cdd:cd02661    132 LRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTI 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  983 HLKRFSYEGRwkQKLQTTVDFPlDSLDLAQYVIGPKQNQKRYGLYGVSNHYGG-LDGGHYTAYCKNALKqRWYKFDDHEV 1061
Cdd:cd02661    210 HLKRFSNFRG--GKINKQISFP-ETLDLSPYMSQPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKSSNG-KWYNMDDSKV 285

                          330
                   ....*....|....*....
gi 1786651895 1062 SEISTSSVKSSAAYILFYS 1080
Cdd:cd02661    286 SPVSIETVLSQKAYILFYI 304
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 751-1079 1.42e-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: 1.42e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLCNTPAMAEYF-----NNNCYMADINrynilghkGEVAEEFGVIMKALWAGLYK-FISPRDFK 824
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFlsdrhSCTCLSCSPN--------SCLSCAMDEIFQEFYYSGDRsPYGPINLL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  825 VTIGKINEQFAGYDQQDSQELLLFLMDGLHEDLnkadnrKRYKEEENDHLDdpmaadlawskhkllNESIIVALFQGQFK 904
Cdd:cd02660     74 YLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHY------GGDKNEANDESH---------------CNCIIHQTFSGSLQ 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  905 STVQCLTCHRKSRTFETFMYLSLPLASTSKCS-------------LQDCLRLFSKEEKLTDNNkVFCRHCKAHRDSTKKL 971
Cdd:cd02660    133 SSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSwalgesgvsgtptLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQL 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  972 EIWKVPPILLVHLKRFSYE-GRWKQKLQTTVDFPLDsLDLAQYVIG---------PKQNQKRYGLYGVSNHYGGLDGGHY 1041
Cdd:cd02660    212 SIKKLPPVLCFQLKRFEHSlNKTSRKIDTYVQFPLE-LNMTPYTSSsigdtqdsnSLDPDYTYDLFAVVVHKGTLDTGHY 290

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1786651895 1042 TAYCKNALKQrWYKFDDHEVSEISTSSVKSSAAYILFY 1079
Cdd:cd02660    291 TAYCRQGDGQ-WFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 751-1079 1.05e-56

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: 197.61  E-value: 1.05e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLCNTPAMAEYFNNNcymadinrynilghkgevaeefgvimkalwaglykfisPRDFKVTIGKI 830
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  831 NEQFAGYDQQDSQELLLFLMDGLhedlnkadnrkrykeeendhlddpmaadlawskhkllnESIIVALFQGQFKSTVQCL 910
Cdd:cd02667     43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  911 TCHRKSRTFETFMYLSLPLA--STSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKahrDSTKKLEIWKVPPILLVHLKRFS 988
Cdd:cd02667     85 SCGTVSLVYEPFLDLSLPRSdeIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQ 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  989 YEGRWK-QKLQTTVDFPlDSLDLAQYViGPKQN------QKRYGLYGVSNHYGGLDGGHYTAYCKNALKQR--------- 1052
Cdd:cd02667    162 QPRSANlRKVSRHVSFP-EILDLAPFC-DPKCNssedksSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQrlsdltksk 239

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1786651895 1053 ------------WYKFDDHEVSEISTSSVKSSAAYILFY 1079
Cdd:cd02667    240 paadeagpgsgqWYYISDSDVREVSLEEVLKSEAYLLFY 278
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
749-929 3.34e-52

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 197.80  E-value: 3.34e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  749 LTGLRNLGNTCYMNSILQCLCNTPAMAEYFNNNCYMADINRYNILGHKGEVAEEFGVIMKALWAGLYKFISPRDFKVTIG 828
Cdd:COG5560    265 TCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIG 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  829 KINEQFAGYDQQDSQELLLFLMDGLHEDLNKAdNRKRYKEEENDHLDDPMA----ADLAWSKHKLLNESIIVALFQGQFK 904
Cdd:COG5560    345 SFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKPDLSPGDDVVvkkkAKECWWEHLKRNDSIITDLFQGMYK 423

                          170       180
                   ....*....|....*....|....*
gi 1786651895  905 STVQCLTCHRKSRTFETFMYLSLPL 929
Cdd:COG5560    424 STLTCPGCGSVSITFDPFMDLTLPL 448
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 751-1080 5.79e-51

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: 182.12  E-value: 5.79e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLcntpamaeYFNNNCY-MADInRYNILGHKGEVaeefGVImkalwaglykfiSPRDFKVTIGK 829
Cdd:cd02663      1 GLENFGNTCYCNSVLQAL--------YFENLLTcLKDL-FESISEQKKRT----GVI------------SPKKFITRLKR 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  830 INEQFAGYDQQDSQELLLFLMDGLHEDLNKADNRKRYKEEENDHLDDPMAADlaWskhkllnesiIVALFQGQFKSTVQC 909
Cdd:cd02663     56 ENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPT--W----------VHEIFQGILTNETRC 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  910 LTCHRKSRTFETFMYLSLPLASTskCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSY 989
Cdd:cd02663    124 LTCETVSSRDETFLDLSIDVEQN--TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKY 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  990 EGRWKQ--KLQTTVDFPL-----DSLDLAQYVigpkqnQKRYGLYGVSNHYG-GLDGGHYTAYCKNalKQRWYKFDDHEV 1061
Cdd:cd02663    202 DEQLNRyiKLFYRVVFPLelrlfNTTDDAENP------DRLYELVAVVVHIGgGPNHGHYVSIVKS--HGGWLLFDDETV 273

                          330       340
                   ....*....|....*....|....*..
gi 1786651895 1062 SEISTSSV-------KSSA-AYILFYS 1080
Cdd:cd02663    274 EKIDENAVeeffgdsPNQAtAYVLFYQ 300
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 751-1080 1.32e-47

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: 172.99  E-value: 1.32e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCL------------CNTPAMAEYFNNNCymadinryNILGHKGEVAEEFGVIMKALWAGLYKFI 818
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWfmnlefrkavyeCNSTEDAELKNMPP--------DKPHEPQTIIDQLQLIFAQLQFGNRSVV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  819 SPRDFKVTIGKINEQfagydQQDSQELLLFLMDGLHEDLNKADNRKrykeeendhlddpmaadlawskhkllNESIIVAL 898
Cdd:cd02668     73 DPSGFVKALGLDTGQ-----QQDAQEFSKLFLSLLEAKLSKSKNPD--------------------------LKNIVQDL 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  899 FQGQFKSTVQCLTCHRKSRTFETFMYLSLPLASTSKcsLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPP 978
Cdd:cd02668    122 FRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT--LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPP 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  979 ILLVHLKRFSY--EGRWKQKLQTTVDFPLDsLDLAQYVIGPKQNQKRYGLYGVSNHYG-GLDGGHYTAYCKNALKQRWYK 1055
Cdd:cd02668    200 TLNFQLLRFVFdrKTGAKKKLNASISFPEI-LDMGEYLAESDEGSYVYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYK 278

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1786651895 1056 FDDHEVSEISTSSVK---------------------SSAAYILFYS 1080
Cdd:cd02668    279 FNDEDVEEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVYK 324
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 751-1079 4.96e-47

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: 171.67  E-value: 4.96e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLCNTPamaeYFNNNCYMADINRYNIlGHKGEVAEeFGVIMKALWAGLYKFISPRDFKVTIGKI 830
Cdd:cd02659      4 GLKNQGATCYMNSLLQQLYMTP----EFRNAVYSIPPTEDDD-DNKSVPLA-LQRLFLFLQLSESPVKTTELTDKTRSFG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  831 NEQFAGYDQQDSQELLLFLMDGLHEDLNKAdnrkrykEEENdhlddpmaadlawskhkllnesIIVALFQGQFKSTVQCL 910
Cdd:cd02659     78 WDSLNTFEQHDVQEFFRVLFDKLEEKLKGT-------GQEG----------------------LIKNLFGGKLVNYIICK 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  911 TCHRKSRTFETFmyLSLPLASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYE 990
Cdd:cd02659    129 ECPHESEREEYF--LDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFD 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  991 GR--WKQKLQTTVDFPlDSLDLAQYVI----------GPKQNQK-RYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFD 1057
Cdd:cd02659    207 FEtmMRIKINDRFEFP-LELDMEPYTEkglakkegdsEKKDSESyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFN 285

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1786651895 1058 DHEVSEISTSSV----------------------KSSAAYILFY 1079
Cdd:cd02659    286 DDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFY 329
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
760-1079 4.04e-43

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 169.68  E-value: 4.04e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  760 YMNSILQCLCNTPAMAEYFNNNCYMADINRYNILghkgevaeefgvIMKALWAGLYKFISPRDFKVTIGKINEQFagydq 839
Cdd:COG5560    536 NDNGIEVPVVHLRIEKGYKSKRLFGDPFLQLNVL------------IKASIYDKLVKEFEELLVLVEMKKTDVDL----- 598

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  840 qDSQELLLFLMD---GLHEDLNKADNRKRYK---EEENDHLDDPMAADLAWSKHKLLnesiivALFQGQFKSTVQCLTCH 913
Cdd:COG5560    599 -VSEQVRLLREEsspSSWLKLETEIDTKREEqveEEGQMNFNDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAA 671

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  914 RKSRTfetfmylslplastskcsLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRW 993
Cdd:COG5560    672 ERTIT------------------LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF 733

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  994 KQKLQTTVDFPLDSLDLAQYVIGPKQNQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSEISTSSVKSSA 1073
Cdd:COG5560    734 RDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSS 813


                   ....*.
gi 1786651895 1074 AYILFY 1079
Cdd:COG5560    814 AYVLFY 819
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 751-1079 1.17e-36

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: 141.48  E-value: 1.17e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLcntpAMAEYFNNncymaDINRYNILGHKGEVAEEFGVIM-KALWAglykfISPRDFKVTIGK 829
Cdd:cd02664      1 GLINLGNTCYMNSVLQAL----FMAKDFRR-----QVLSLNLPRLGDSQSVMKKLQLlQAHLM-----HTQRRAEAPPDY 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  830 INEQ-----FAGYDQQDSQELLLFLMDGLHedlnkadnrkrykeeendhlddpmaadlawskhkllneSIIVALFQGQFK 904
Cdd:cd02664     67 FLEAsrppwFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLS 108

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  905 STVQCLTCHRKSRTFETFMYLSLplastSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHL 984
Cdd:cd02664    109 TTIRCLNCNSTSARTERFRDLDL-----SFPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTL 183

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  985 KRFSY--EGRWKQKLQTTVDFPLDsLDLAQYV----IGPKQNQKR---------------YGLYGVSNHYG-GLDGGHYT 1042
Cdd:cd02664    184 LRFSYdqKTHVREKIMDNVSINEV-LSLPVRVesksSESPLEKKEeesgddgelvtrqvhYRLYAVVVHSGySSESGHYF 262

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786651895 1043 AYCKN--------------------ALKQRWYKFDDHEVSEISTSSVK-------SSAAYILFY 1079
Cdd:cd02664    263 TYARDqtdadstgqecpepkdaeenDESKNWYLFNDSRVTFSSFESVQnvtsrfpKDTPYILFY 326
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 8-116 3.30e-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: 121.25  E-value: 3.30e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895    8 VKELYLSSSLGDLNKKAEIRPD--KTSTRSYVQSACKIFKAAEEFRLDRDEEKAYVLYMKYLTVYEIIKKRPDFKEQPDY 85
Cdd:pfam08969    3 LKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVKAT 82

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1786651895   86 FMTILGPNSFKKAIVEAEKLSDSLKLRYEEV 116
Cdd:pfam08969   83 VRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 751-1079 1.04e-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: 126.29  E-value: 1.04e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLCNTPAMAE---YFNNNCYMADINRYNILghkgevaeefgVIMKALWAGLYKF---ISPRDFK 824
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPARRGANQSSDNLT-----------NALRDLFDTMDKKqepVPPIEFL 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  825 VTIGKINEQFA------GYDQQDSQELLLFLMDGLHEDLNKADnrkrykeEENDHLDDpmaadlawskhkllnesiivaL 898
Cdd:cd02657     70 QLLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAG-------SKGSFIDQ---------------------L 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  899 FQGQFKSTVQCL-TCHRKSRTFETFMYLSLPLASTSKCS-LQDCLRLFSKEE--KLTDnnkvfcrhcKAHRDS--TKKLE 972
Cdd:cd02657    122 FGIELETKMKCTeSPDEEEVSTESEYKLQCHISITTEVNyLQDGLKKGLEEEieKHSP---------TLGRDAiyTKTSR 192

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  973 IWKVPPILLVHLKRFSyegrWKQKLQT------TVDFPLDsLDLAQYVigpkQNQKRYGLYGVSNHYG-GLDGGHYTAYC 1045
Cdd:cd02657    193 ISRLPKYLTVQFVRFF----WKRDIQKkakilrKVKFPFE-LDLYELC----TPSGYYELVAVITHQGrSADSGHYVAWV 263

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1786651895 1046 KNALKQRWYKFDDHEVSEISTSSVKSSA-------AYILFY 1079
Cdd:cd02657    264 RRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 730-1079 1.27e-30

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 123.85  E-value: 1.27e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  730 PSAAKIRNLNPtfgglgqsLTGLRNLGNTCYMNSILQCLCNTPAmaeyfnnncYMADINRYNILGHKGEVAEEFGVIMKA 809
Cdd:cd02671     13 TSCEKRENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPG---------FKHGLKHLVSLISSVEQLQSSFLLNPE 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  810 LWAGLYKFISPRDFKVTIGKINEQFAGYDQQDSQELLLFLMDGLHEDLNKadnrkrykeeendhlddpmaadlawskhkl 889
Cdd:cd02671     76 KYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK------------------------------ 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  890 lnesiivaLFQGQFKSTVQCLTCHRKSRTFETFMYLSLPLASTSKCS-----------------LQDCLRLFSKEEKLTD 952
Cdd:cd02671    126 --------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKseesseispdpktemktLKWAISQFASVERIVG 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  953 NNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRWK------QKLQTTVDFPLDsLDLAQYVIGPKQNQkrYGL 1026
Cdd:cd02671    198 EDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPLK-LSLEEWSTKPKNDV--YRL 274

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786651895 1027 YGVSNHYGG-LDGGHYTAYCknalkqRWYKFDDHEV---------SEISTSSVKSSAAYILFY 1079
Cdd:cd02671    275 FAVVMHSGAtISSGHYTAYV------RWLLFDDSEVkvteekdflEALSPNTSSTSTPYLLFY 331
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
751-1080 3.01e-28

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 115.67  E-value: 3.01e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLC-NTPAMAEYFNNNC--YMADINRYNiLGHKGEVAEEFGVIMKALWAglykfisprDFKVTI 827
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSkeLKVLKNVIR-KPEPDLNQEEALKLFTALWS---------SKEHKV 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  828 GKINEQfagYDQQDSQELLLFLMDGLHEDLNKADNRKRYK--EEENDHLDDPMAadlawskhkllneSIIVALFQGQF-- 903
Cdd:COG5533     71 GWIPPM---GSQEDAHELLGKLLDELKLDLVNSFTIRIFKttKDKKKTSTGDWF-------------DIIIELPDQTWvn 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  904 -KSTVQCltchrksrTFETFMYLsLPLASTSKcslqdclrlfskeEKLTDNNKVFCRHCKAHRDStkkleiwKVPPILLV 982
Cdd:COG5533    135 nLKTLQE--------FIDNMEEL-VDDETGVK-------------AKENEELEVQAKQEYEVSFV-------KLPKILTI 185

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  983 HLKRFSYEGRwKQKLQTTVDFPLDsLDLAQYVIGPKQNQKRYGLYGVSNHYGGLDGGHYTAYCKNalKQRWYKFDDHEVS 1062
Cdd:COG5533    186 QLKRFANLGG-NQKIDTEVDEKFE-LPVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK--GGKWEKANDSDVT 261

                          330       340
                   ....*....|....*....|.
gi 1786651895 1063 EISTS---SVKSSAAYILFYS 1080
Cdd:COG5533    262 PVSEEeaiNEKAKNAYLYFYE 282
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 751-1079 3.67e-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: 116.27  E-value: 3.67e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLCNTPAMAEYFNN--NCYMADIN--RYNI------LGHkGEVAEEFGVIM--KALWAGLYKFI 818
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDleNKFPSDVVdpANDLncqlikLAD-GLLSGRYSKPAslKSENDPYQVGI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  819 SPRDFKVTIGKINEQFAGYDQQDSQELLLFLMDglhedlnKADNRKRYKEEENdhlddpmaadlawskhklLNEsiivaL 898
Cdd:cd02658     80 KPSMFKALIGKGHPEFSTMRQQDALEFLLHLID-------KLDRESFKNLGLN------------------PND-----L 129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  899 FQGQFKSTVQCLTCHRKSRTFETFMYLSLPL------------ASTSKCSLQDCLRLFSKEEKLTDnnkvFCRHCKAHRD 966
Cdd:cd02658    130 FKFMIEDRLECLSCKKVKYTSELSEILSLPVpkdeatekeegeLVYEPVPLEDCLKAYFAPETIED----FCSTCKEKTT 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  967 STKKLEIWKVPPILLVHLKRFSYEGRWKQKlqtTVDFPLDSLDlaqyVIGPkqnqKRYGLYGVSNHYG-GLDGGHYTAYC 1045
Cdd:cd02658    206 ATKTTGFKTFPDYLVINMKRFQLLENWVPK---KLDVPIDVPE----ELGP----GKYELIAFISHKGtSVHSGHYVAHI 274

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1786651895 1046 K--NALKQRWYKFDDHEVSEISTSSVKSSAAYILFY 1079
Cdd:cd02658    275 KkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 751-1079 2.05e-26

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: 108.99  E-value: 2.05e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLCNTPAMAEYfnnncymadINRYNilghkgevaeefgvimkalwaglykfisprdfkvtigki 830
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLIEY---------LEEFL--------------------------------------- 32

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  831 neqfagyDQQDSQELLLFLMDGLhedlnkadnrkrykeeendhlddpmaadlawskhkllnESIIVALFQGQFKSTVQCL 910
Cdd:cd02662     33 -------EQQDAHELFQVLLETL--------------------------------------EQLLKFPFDGLLASRIVCL 67

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  911 TCHRKSR-TFETFMYLSLPL---ASTSKCSLQDCLRLFSKEEKLTDnnkVFCRHCKahrdstkkLEIWKVPPILLVHLKR 986
Cdd:cd02662     68 QCGESSKvRYESFTMLSLPVpnqSSGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSR 136

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  987 FSYEGRWK-QKLQTTVDFPlDSLdlaqyvigpkqNQKRYGLYGVSNHYGGLDGGHYTAY--------------------C 1045
Cdd:cd02662    137 SVFDGRGTsTKNSCKVSFP-ERL-----------PKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreG 204

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1786651895 1046 KNALKQRWYKFDDHEVSEISTSSVK-SSAAYILFY 1079
Cdd:cd02662    205 PSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 751-1069 1.08e-21

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 101.87  E-value: 1.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLCNTpamaEYFNNNCYmaDINRYNILGhKGEVAeefgVIMKALWAGLYKFISPRD-FKVTIGK 829
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFI----AKFRKDVY--GIPTDHPRG-RDSVA----LALQRLFYNLQTGEEPVDtTELTRSF 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  830 INEQFAGYDQQDSQELLLFLMDGLhedlnkadnrkrykeeENDHLDDPMaadlawskhkllnESIIVALFQGQFKSTVQC 909
Cdd:COG5077    264 GWDSDDSFMQHDIQEFNRVLQDNL----------------EKSMRGTVV-------------ENALNGIFVGKMKSYIKC 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  910 LTCHRKSRTFETFMYLSLPLASTSkcSLQDCLRLFSKEEKLTDNNKVFCRHcKAHRDSTKKLEIWKVPPILLVHLKRFSY 989
Cdd:COG5077    315 VNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEY 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  990 EGRWKQ--KLQTTVDFPlDSLDLAQYV---IGPKQNQK-RYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSE 1063
Cdd:COG5077    392 DFERDMmvKINDRYEFP-LEIDLLPFLdrdADKSENSDaVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTR 470


                   ....*.
gi 1786651895 1064 ISTSSV 1069
Cdd:COG5077    471 ATEKEV 476
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 751-1079 2.10e-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: 95.46  E-value: 2.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  751 GLRNLGNTCYMNSILQCLCNTPAMAEYF-NNNCYMADINRynilghKGEVAEEFGVIMKALW-AGLYK-FISPRDFKVTI 827
Cdd:cd02669    121 GLNNIKNNDYANVIIQALSHVKPIRNFFlLYENYENIKDR------KSELVKRLSELIRKIWnPRNFKgHVSPHELLQAV 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  828 GKI-NEQFAGYDQQDSQELLLFLMDGLHEDLNKadNRKRykeeendhlddpmaadlawskhkllNESIIVALFQGQFKST 906
Cdd:cd02669    195 SKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGG--SKKP-------------------------NSSIIHDCFQGKVQIE 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  907 VQCLTCHR---------------KSRTFETFMYLS--LPLASTSKCSLQD-CLRLFSKEEKLTDNNKVfcrHCKAHRDST 968
Cdd:cd02669    248 TQKIKPHAeeegskdkffkdsrvKKTSVSPFLLLTldLPPPPLFKDGNEEnIIPQVPLKQLLKKYDGK---TETELKDSL 324

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  969 KKLEIWKVPPILLVHLKRFSYEGRWKQKLQTTVDFPLDSLDLAQYVIGPKQNQKRYGLYG-VSN--HYGG-LDGGHYTAY 1044
Cdd:cd02669    325 KRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNlVANivHEGTpQEDGTWRVQ 404

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1786651895 1045 CKNALKQRWYKFDDHEVSEISTSSVKSSAAYILFY 1079
Cdd:cd02669    405 LRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 826-1079 2.35e-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: 65.24  E-value: 2.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  826 TIGKINEQFAGYDQQDSQELLLFL---MDGLHEdlNKADNRKRYkEEENDHLdDPMAAdlawskHKLLNESIIValfqgq 902
Cdd:cd02673     20 SIGKINTEFDNDDQQDAHEFLLTLleaIDDIMQ--VNRTNVPPS-NIEIKRL-NPLEA------FKYTIESSYV------ 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  903 fkstvqCLTCHRKSRTFETFMYLSLPLASTSKCSLQDclrLFSKEEKLTDNNKVfCRHCKaHRDSTKKLEIWKVPPILLV 982
Cdd:cd02673     84 ------CIGCSFEENVSDVGNFLDVSMIDNKLDIDEL---LISNFKTWSPIEKD-CSSCK-CESAISSERIMTFPECLSI 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  983 HLKRFsyegrwkqKLQTTVdfpLDSLDLAQYVIGPKQNQ-KRYGLYGVSNHYG-GLDGGHYTAYCKNALK-QRWYKFDDH 1059
Cdd:cd02673    153 NLKRY--------KLRIAT---SDYLKKNEEIMKKYCGTdAKYSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDD 221

                          250       260
                   ....*....|....*....|...
gi 1786651895 1060 EVSEISTSSVK---SSAAYILFY 1079
Cdd:cd02673    222 EIRPVSKNDVStnaRSSGYLIFY 244
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 839-1079 1.73e-10

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 62.19  E-value: 1.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  839 QQDSQELLLFLMDGLhEDlnkADNRKRYKEEENDHLDDPMaadlawskhkllnesiiVALFQGQFkSTVqclTCHRKSRT 918
Cdd:cd02665     22 QQDVSEFTHLLLDWL-ED---AFQAAAEAISPGEKSKNPM-----------------VQLFYGTF-LTE---GVLEGKPF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  919 FETFMYLSLPLASTSKCSLQDCLrlfskeEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRWKQKLQ 998
Cdd:cd02665     77 CNCETFGQYPLQVNGYGNLHECL------EAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPEKIH 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  999 TTVDFPldsldlaqyvigPKQNQKRYGLYGVSNHYGGLDGGHYTAYCKNALKQRWYKFDDHEVSEISTSSVKSSA----- 1073
Cdd:cd02665    151 DKLEFP------------QIIQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfgggr 218


                   ....*....
gi 1786651895 1074 ---AYILFY 1079
Cdd:cd02665    219 npsAYCLMY 227
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 886-1079 4.64e-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: 4.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  886 KHKLLNE-----SIIVALFQGQFKSTVQC-----LTCHRKSRTFETFMY-LSLPLASTSKCSLQDCLRLFSKEEKLTDNN 954
Cdd:cd02672     54 ESCLLCElgylfSTLIQNFTRFLLETISQdqlgtPFSCGTSRNSVSLLYtLSLPLGSTKTSKESTFLQLLKRSLDLEKVT 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  955 KVFCRHCKAHRDSTKKLEIWKVPPILL----VHLKRFSYEGRWKQ-------KLQTTVDFPLDSLDLAQYVIGPKQNQKr 1023
Cdd:cd02672    134 KAWCDTCCKYQPLEQTTSIRHLPDILLlvlvINLSVTNGEFDDINvvlpsgkVMQNKVSPKAIDHDKLVKNRGQESIYK- 212

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786651895 1024 YGLYG-VSNHYGGLDGGHYTA----YCKNALKQRWYKFDDHEVSEISTSsvkssaAYILFY 1079
Cdd:cd02672    213 YELVGyVCEINDSSRGQHNVVfvikVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
878-1058 8.71e-07

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 51.89  E-value: 8.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  878 MAADLAWSKHKLL-NESIIVALFQGQFKSTVQCLTC-HRKSRTFETFM----YLSLPLASTSKCSLQD---CLRLFSKEE 948
Cdd:pfam13423  110 LSSEENSTPPNPSpAESPLEQLFGIDAETTIRCSNCgHESVRESSTHVldliYPRKPSSNNKKPPNQTfssILKSSLERE 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  949 KLTdnnKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEgrWKQKLQTTVDFPLD-SLDLAQYVIGPkQNQKRYGLY 1027
Cdd:pfam13423  190 TTT---KAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPEiGLTLSDDLQGD-NEIVKYELR 263

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1786651895 1028 G-VSNHYGGLDGGHYTAYCK-------NALKQRWYKFDD 1058
Cdd:pfam13423  264 GvVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 750-1069 1.25e-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: 45.56  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  750 TGLRNLGNTCYMNSILQCL-CNTP---AMAEYFNNNCYMAD--INRYNILGHKGEVAEEFGVIMKALWAGL--YKFISPR 821
Cdd:cd02666      2 AGLDNIGNTCYLNSLLQYFfTIKPlrdLVLNFDESKAELASdyPTERRIGGREVSRSELQRSNQFVYELRSlfNDLIHSN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  822 DFKVTIGKiNEQFAGYDQQDSQELLLFLMDglheDLNKADNRKRYKEEENDHLDDPMAADLawskhkllnesiIVALFQG 901
Cdd:cd02666     82 TRSVTPSK-ELAYLALRQQDVTECIDNVLF----QLEVALEPISNAFAGPDTEDDKEQSDL------------IKRLFSG 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  902 QFK-STVQCLTCHRKSRT--FETFMYLSLPLAST--------SKCSLQDCL----------------RLFSKEEKLTDNN 954
Cdd:cd02666    145 KTKqQLVPESMGNQPSVRtkTERFLSLLVDVGKKgreivvllEPKDLYDALdryfdydsltklpqrsQVQAQLAQPLQRE 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  955 KVFCRHCKAHRDSTKKLEIWK--VPPILLVHLKRFSYEGRWKQKLQTTVDfpldslDLAQYVigpkqnqkrYGLYGVSNH 1032
Cdd:cd02666    225 LISMDRYELPSSIDDIDELIReaIQSESSLVRQAQNELAELKHEIEKQFD------DLKSYG---------YRLHAVFIH 289

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1786651895 1033 YGGLDGGHYTAYCKNALKQRWYKFDDHEVSEISTSSV 1069
Cdd:cd02666    290 RGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEV 326
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 316-635 2.92e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.14  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  316 VRPPRQNIISTLPQLNFSYPslieprPPTPTQQEPEVTPKPQETLDPVLANGVTPADPPTSETSMVTDSLQEdtvdfPVK 395
Cdd:pfam03154  429 AQPPVLTQSQSLPPPAASHP------PTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQP-----PSS 497

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  396 VSTSSALDLSKKGSAAAPSSQSPATAKAFPQFDRAKKPSIRvSDEPKPS---QNGSAKDSNPFVP--DR----TAKPSFV 466
Cdd:pfam03154  498 ASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPR-SPSPEPTvvnTPSHASQSARFYKhlDRgynsCARTDLY 576

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  467 pNTSLSKEEQSRIHSEAvagIEKAKQEQEKRiqerrekeqkEKElkerqtgeesEKrkkedeelkhqdkkklERQKAEEV 546
Cdd:pfam03154  577 -FMPLAGSKLAKKREEA---LEKAKREAEQK----------ARE----------EK----------------EREKEKEK 616

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  547 EDKENRPSEEKRRRGKEQSSDAPSKSMSlDSPAPNPNHIVSEIKREPLTRArseemgrSVPGL--PDgwMKFLDTVTGTY 624
Cdd:pfam03154  617 EREREREREREAERAAKASSSSHEGRMG-DPQLAGPAHMRPSFEPPPTTIA-------AVPPYigPD--TPALRTLSEYA 686

                          330
                   ....*....|..
gi 1786651895  625 R-YYHSPTNRVH 635
Cdd:pfam03154  687 RpHVMSPTNRNH 698
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 975-1079 3.90e-04

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


Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 43.28  E-value: 3.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  975 KVPPILLVHLKRFSYEGRWKQKLQTTVDfPLDSLDLAQYV----------------------IGPKQNQKRYGLYGVSNH 1032
Cdd:cd02670     97 KAPSCLIICLKRYGKTEGKAQKMFKKIL-IPDEIDIPDFVaddpracskcqlecrvcyddkdFSPTCGKFKLSLCSAVCH 175

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786651895 1033 YG-GLDGGHYTAYCK-----------NALKQRWYKFDD-------HEVSEISTSSVKSSaAYILFY 1079
Cdd:cd02670    176 RGtSLETGHYVAFVRygsysltetdnEAYNAQWVFFDDmadrdgvSNGFNIPAARLLED-PYMLFY 240
PTZ00121 PTZ00121
MAEBL; Provisional
 471-568 7.91e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 7.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  471 LSKEEQSRIHSEAVAGIE---------KAKQEQEKRIQERREKEQKEKELKERQTGEESEKRKKEDEELKHQDKKKLERQ 541
Cdd:PTZ00121  1612 AKKAEEAKIKAEELKKAEeekkkveqlKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691

                           90       100
                   ....*....|....*....|....*..
gi 1786651895  542 KAEEVEDKENRPSEEKRRRGKEQSSDA 568
Cdd:PTZ00121  1692 EALKKEAEEAKKAEELKKKEAEEKKKA 1718
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
 344-590 4.42e-03

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 41.23  E-value: 4.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  344 TPTQQEPEVTPKPQETldPVLANGVTPADPPTSETSMVTD--SLQEDTVDFPVKVSTSSALDLSKKGSAAAPS----SQS 417
Cdd:NF033875    38 TDNVQAAELDTQPGTT--TVQPDNPDPQSGSETPKTAVSEeaTVQKDTTSQPTKVEEVASEKNGAEQSSATPNdttnAQQ 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  418 PaTAKAFPQFDRAKKPSIRVSDEP-------KPSQNGSAKDSN-------PFVPDRTAKPSFVPNTSLSK---EEQSRIH 480
Cdd:NF033875   116 P-TVGAEKSAQEQPVVSPETTNEPlgqptevAPAENEANKSTSipkefetPDVDKAVDEAKKDPNITVVEkpaEDLGNVS 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  481 SEAVAGIEKA----KQEQEKRIQERREkeqkekelkerQTGEESEKRKKEDEELKHQDKKKLERQKAEEVEdkenrpsEE 556
Cdd:NF033875   195 SKDLAAKEKEvdqlQKEQAKKIAQQAA-----------ELKAKNEKIAKENAEIAAKNKAEKERYEKEVAE-------YN 256

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1786651895  557 KRRRGKEQSSDAPSKSMSLDSPAPNPNHIVSEIK 590
Cdd:NF033875   257 KHKNENGYVNEAISKNLVFDQSVVTKDTKISSIK 290
PTZ00121 PTZ00121
MAEBL; Provisional
 431-564 5.94e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 5.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  431 KKPSIRVSDEPKPSQNGSAKDSNPFVPDRTAKPSFVPNTSLSKEEQSRIHSEAVAGIEKAKQEQEKRIQERREKEQKEKE 510
Cdd:PTZ00121  1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786651895  511 LKERQTGEESEKRKKEDEELKHQD-----KKKLERQKAEEVEDK--ENRPSEEKRRRGKEQ 564
Cdd:PTZ00121  1633 KKVEQLKKKEAEEKKKAEELKKAEeenkiKAAEEAKKAEEDKKKaeEAKKAEEDEKKAAEA 1693
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 313-684 8.88e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 8.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  313 NAKVRPPRQNIISTLPQLNFsYPSLIEPRPPTPTQQEPEVTPKPQETLDPVLANGVTPADP------------------- 373
Cdd:PRK10263   445 NAWQAEEQQSTFAPQSTYQT-EQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPplyyfeeveekrarereql 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  374 ---------PTSETSMVTDSLQEDTVDF--PVK-VSTSSALDLSKKGSAAAPSSQSPATAKAF-PQFDRAKKPSIRVSDE 440
Cdd:PRK10263   524 aawyqpipePVKEPEPIKSSLKAPSVAAvpPVEaAAAVSPLASGVKKATLATGAAATVAAPVFsLANSGGPRPQVKEGIG 603

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  441 PKPSQNGSAKdsnpfVPDRTAKPSF---VPNTSLSKE---EQSRIHSEAVAG-----IEKAKQEQEKRiqerrekeqkek 509
Cdd:PRK10263   604 PQLPRPKRIR-----VPTRRELASYgikLPSQRAAEEkarEAQRNQYDSGDQynddeIDAMQQDELAR------------ 666

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  510 elkerQTGEESEKRKKEDEELKHQDKKKlERQKAEEVEDKENRPSEEKRRRGKEQSSDApsKSMSLDSPAPNP-NHIVSE 588
Cdd:PRK10263   667 -----QFAQTQQQRYGEQYQHDVPVNAE-DADAAAEAELARQFAQTQQQRYSGEQPAGA--NPFSLDDFEFSPmKALLDD 738

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786651895  589 IKREPL-TRARSEEMGRSVPGLPDGWMKFLDTVTGTYRYYHSPTNRVHlyPPEVPVPQTPPSTPPTVKQKPSRPAEPDAN 667
Cdd:PRK10263   739 GPHEPLfTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVA--PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQ 816

                          410
                   ....*....|....*..
gi 1786651895  668 CEQEREQSKLKRSYSSP 684
Cdd:PRK10263   817 YQQPQQPVAPQPQYQQP 833
 
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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