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Conserved domains on  [gi|765114864|ref|XP_011486858|]
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ubiquitin carboxyl-terminal hydrolase 8 [Oryzias latipes]

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 ...
 747-1076 2.83e-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: 352.75  E-value: 2.83e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCLCNtpamaeyfnsnyyledinrsnilghkgefaeefgvimkalwaglykcisprdfkitigki 826
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  827 ndqfagyDQQDSQELLLFLMDGLHedlnkadnkkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFKSTVQCS 906
Cdd:cd02674    21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  907 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKR 982
Cdd:cd02674    56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  983 FSYEGRWKQKLQTTVDFPLDNLDLTQYVIGPKQT-LKRYYLYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHEVSEIS 1061
Cdd:cd02674   136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                         330
                  ....*....|....*
gi 765114864 1062 TSSVKSSAAYILFYS 1076
Cdd:cd02674   216 ESSVVSSSAYILFYE 230
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
743-925 1.18e-54

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


The actual alignment was detected with superfamily member COG5560:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 205.50  E-value: 1.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  743 ASLTGLRNLGNTCYMNSILQCLCNTPAMAEYFNSNYYLEDINRSNILGHKGEFAEEFGVIMKALWAGLYKCISPRDFKIT 822
Cdd:COG5560   263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  823 IGKINDQFAGYDQQDSQELLLFLMDGLHEDLNKAdNKKRYKEE----ENDHLDDQTAADLAWSKHKLLNESIIVALFQGQ 898
Cdd:COG5560   343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                         170       180
                  ....*....|....*....|....*..
gi 765114864  899 FKSTVQCSTCHRKSRTFETFMYLSLPL 925
Cdd:COG5560   422 YKSTLTCPGCGSVSITFDPFMDLTLPL 448
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 6-116 2.25e-31

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


:

Pssm-ID: 462647  Cd Length: 113  Bit Score: 118.94  E-value: 2.25e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864     6 TEVKELYLSTSLGELNKKAEIKPD--KTSTRSYVQSACKLFKAAEECRLDRDEEKAYVLYMKYLTVYDIIKKRPDFKQQP 83
Cdd:pfam08969    1 APLKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 765114864    84 EYYITLLGQNSFKKAIEEAEKLSESLKLRYEEA 116
Cdd:pfam08969   81 ATVRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 197-305 7.07e-04

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


The actual alignment was detected with superfamily member pfam00581:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 92  Bit Score: 39.77  E-value: 7.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864   197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS-PGITVNQIEAKLPSMSKDhwmkrgfvDYIILLDWFSSVSDLklgtTL 275
Cdd:pfam00581    7 VLIDVRPPEEYAKGHI----PGAVNVPLSSLSlPPLPLLELLEKLLELLKD--------KPIVVYCNSGNRAAA----AA 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 765114864   276 QSLKDALFKwdsmtilrsEPLVLEGGYENW 305
Cdd:pfam00581   71 ALLKALGYK---------NVYVLDGGFEAW 91
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 358-620 5.02e-03

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.83  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  358 QKPPAPAVANGVAPAEPPTSKTSviaDKLPDTHDSPvrspastgldlnkKSPAPNQSPATAKAFPQFDRTKKPVRDEpKP 437
Cdd:PTZ00449  589 KDPEEPKKPKRPRSAQRPTRPKS---PKLPELLDIP-------------KSPKRPESPKSPKRPPPPQRPSSPERPE-GP 651

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  438 KEDGSTKdstqngpvvPDRSVKPPLIPSTslsKEEQNQIHLEAVAVMEKAKQEQEKRMQERRLEEEKREKELKDRLEREE 517
Cdd:PTZ00449  652 KIIKSPK---------PPKSPKPPFDPKF---KEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPR 719

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  518 SERRSKQEEEKRHLErkRLERQKAEEEEDKENKTWDERER-RGKEPNADTpsksmsldsPVPNHLVSEIKREPL---TRA 593
Cdd:PTZ00449  720 PLPPKLPRDEEFPFE--PIGDPDAEQPDDIEFFTPPEEERtFFHETPADT---------PLPDILAEEFKEEDIhaeTGE 788

                         250       260
                  ....*....|....*....|....*..
gi 765114864  594 RSEEMGRtvpglPDGWMKFLDTVTGTY 620
Cdd:PTZ00449  789 PDEAMKR-----PDSPSEHEDKPPGDH 810
 
Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 747-1076 2.83e-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: 352.75  E-value: 2.83e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCLCNtpamaeyfnsnyyledinrsnilghkgefaeefgvimkalwaglykcisprdfkitigki 826
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  827 ndqfagyDQQDSQELLLFLMDGLHedlnkadnkkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFKSTVQCS 906
Cdd:cd02674    21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  907 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKR 982
Cdd:cd02674    56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  983 FSYEGRWKQKLQTTVDFPLDNLDLTQYVIGPKQT-LKRYYLYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHEVSEIS 1061
Cdd:cd02674   136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                         330
                  ....*....|....*
gi 765114864 1062 TSSVKSSAAYILFYS 1076
Cdd:cd02674   216 ESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
746-1075 1.39e-111

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 348.66  E-value: 1.39e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864   746 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNSNYYLEDINRSNILGHkgeFAEEFGVIMKALW-AGLYKCISPRDFKITIG 824
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQkNSKSSSVSPKMFKKSLG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864   825 KINDQFAGYDQQDSQELLLFLMDGLHEDLNkadnkkrykeeendhlddqtaadlawSKHKLLNESIIVALFQGQFKSTVQ 904
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864   905 CSTCHRKSRTFETFMYLSLPL----ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHL 980
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIpgdsAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864   981 KRFSYEGRWKQKLQTTVDFPLDnLDLTQYVIG---PKQTLKRYY-LYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHE 1056
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEelkPKTNNLQDYrLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290

                          330       340
                   ....*....|....*....|
gi 765114864  1057 VSEISTS-SVKSSAAYILFY 1075
Cdd:pfam00443  291 VTEVDEEtAVLSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
743-925 1.18e-54

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 205.50  E-value: 1.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  743 ASLTGLRNLGNTCYMNSILQCLCNTPAMAEYFNSNYYLEDINRSNILGHKGEFAEEFGVIMKALWAGLYKCISPRDFKIT 822
Cdd:COG5560   263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  823 IGKINDQFAGYDQQDSQELLLFLMDGLHEDLNKAdNKKRYKEE----ENDHLDDQTAADLAWSKHKLLNESIIVALFQGQ 898
Cdd:COG5560   343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                         170       180
                  ....*....|....*....|....*..
gi 765114864  899 FKSTVQCSTCHRKSRTFETFMYLSLPL 925
Cdd:COG5560   422 YKSTLTCPGCGSVSITFDPFMDLTLPL 448
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 6-116 2.25e-31

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


Pssm-ID: 462647  Cd Length: 113  Bit Score: 118.94  E-value: 2.25e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864     6 TEVKELYLSTSLGELNKKAEIKPD--KTSTRSYVQSACKLFKAAEECRLDRDEEKAYVLYMKYLTVYDIIKKRPDFKQQP 83
Cdd:pfam08969    1 APLKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 765114864    84 EYYITLLGQNSFKKAIEEAEKLSESLKLRYEEA 116
Cdd:pfam08969   81 ATVRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
747-1076 7.52e-28

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 114.51  E-value: 7.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCLC-NTPAMaeyfnSNYYLEDINRSNILghKGEFAEEFGVIMKALWAGLYKCISPRDfKITIGK 825
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKL-----DELLDDLSKELKVL--KNVIRKPEPDLNQEEALKLFTALWSSK-EHKVGW 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  826 INDQfagYDQQDSQELLLFLMDGLHEDLNKA--DNKKRYKEEENDHLDDQtaadlaWSkhkllneSIIVALFQGQF---K 900
Cdd:COG5533    73 IPPM---GSQEDAHELLGKLLDELKLDLVNSftIRIFKTTKDKKKTSTGD------WF-------DIIIELPDQTWvnnL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  901 STVQCstchrksrTFETFMYLsLPLASTSKcslqdclrlfskeEKLTDNNKVFCRHCKAHRDStkkleiwKVPPILLVHL 980
Cdd:COG5533   137 KTLQE--------FIDNMEEL-VDDETGVK-------------AKENEELEVQAKQEYEVSFV-------KLPKILTIQL 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  981 KRFSYEGRwKQKLQTTVDfplDNLDLTqyvIGPKQTLK-----RYYLYGVSNHYGGLDGGHYTAYCKnaTKQRWYKFDDH 1055
Cdd:COG5533   188 KRFANLGG-NQKIDTEVD---EKFELP---VKHDQILNivketYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDS 258

                         330       340
                  ....*....|....*....|....
gi 765114864 1056 EVSEISTS---SVKSSAAYILFYS 1076
Cdd:COG5533   259 DVTPVSEEeaiNEKAKNAYLYFYE 282
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 197-305 7.07e-04

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


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 39.77  E-value: 7.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864   197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS-PGITVNQIEAKLPSMSKDhwmkrgfvDYIILLDWFSSVSDLklgtTL 275
Cdd:pfam00581    7 VLIDVRPPEEYAKGHI----PGAVNVPLSSLSlPPLPLLELLEKLLELLKD--------KPIVVYCNSGNRAAA----AA 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 765114864   276 QSLKDALFKwdsmtilrsEPLVLEGGYENW 305
Cdd:pfam00581   71 ALLKALGYK---------NVYVLDGGFEAW 91
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 358-620 5.02e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.83  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  358 QKPPAPAVANGVAPAEPPTSKTSviaDKLPDTHDSPvrspastgldlnkKSPAPNQSPATAKAFPQFDRTKKPVRDEpKP 437
Cdd:PTZ00449  589 KDPEEPKKPKRPRSAQRPTRPKS---PKLPELLDIP-------------KSPKRPESPKSPKRPPPPQRPSSPERPE-GP 651

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  438 KEDGSTKdstqngpvvPDRSVKPPLIPSTslsKEEQNQIHLEAVAVMEKAKQEQEKRMQERRLEEEKREKELKDRLEREE 517
Cdd:PTZ00449  652 KIIKSPK---------PPKSPKPPFDPKF---KEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPR 719

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  518 SERRSKQEEEKRHLErkRLERQKAEEEEDKENKTWDERER-RGKEPNADTpsksmsldsPVPNHLVSEIKREPL---TRA 593
Cdd:PTZ00449  720 PLPPKLPRDEEFPFE--PIGDPDAEQPDDIEFFTPPEEERtFFHETPADT---------PLPDILAEEFKEEDIhaeTGE 788

                         250       260
                  ....*....|....*....|....*..
gi 765114864  594 RSEEMGRtvpglPDGWMKFLDTVTGTY 620
Cdd:PTZ00449  789 PDEAMKR-----PDSPSEHEDKPPGDH 810
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 197-310 5.24e-03

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


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 37.44  E-value: 5.24e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864    197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS--PGITVNQIEAKLPSMSkdhwmKRGFVDYIILLDWfssvSDLKLGTT 274
Cdd:smart00450    6 VLLDVRSPEEYEGGHI----PGAVNIPLSELLdrRGELDILEFEELLKRL-----GLDKDKPVVVYCR----SGNRSAKA 72

                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 765114864    275 LQSLKDALFKwdsmtilrsEPLVLEGGYENWLLFYP 310
Cdd:smart00450   73 AWLLRELGFK---------NVYLLDGGYKEWSAAGP 99
 
Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 747-1076 2.83e-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: 352.75  E-value: 2.83e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCLCNtpamaeyfnsnyyledinrsnilghkgefaeefgvimkalwaglykcisprdfkitigki 826
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  827 ndqfagyDQQDSQELLLFLMDGLHedlnkadnkkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFKSTVQCS 906
Cdd:cd02674    21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  907 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKR 982
Cdd:cd02674    56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  983 FSYEGRWKQKLQTTVDFPLDNLDLTQYVIGPKQT-LKRYYLYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHEVSEIS 1061
Cdd:cd02674   136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                         330
                  ....*....|....*
gi 765114864 1062 TSSVKSSAAYILFYS 1076
Cdd:cd02674   216 ESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
746-1075 1.39e-111

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 348.66  E-value: 1.39e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864   746 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNSNYYLEDINRSNILGHkgeFAEEFGVIMKALW-AGLYKCISPRDFKITIG 824
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQkNSKSSSVSPKMFKKSLG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864   825 KINDQFAGYDQQDSQELLLFLMDGLHEDLNkadnkkrykeeendhlddqtaadlawSKHKLLNESIIVALFQGQFKSTVQ 904
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864   905 CSTCHRKSRTFETFMYLSLPL----ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHL 980
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIpgdsAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864   981 KRFSYEGRWKQKLQTTVDFPLDnLDLTQYVIG---PKQTLKRYY-LYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHE 1056
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEelkPKTNNLQDYrLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290

                          330       340
                   ....*....|....*....|
gi 765114864  1057 VSEISTS-SVKSSAAYILFY 1075
Cdd:pfam00443  291 VTEVDEEtAVLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 747-1075 1.10e-74

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


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 247.01  E-value: 1.10e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCLCNtpamaeyfnsnyyledinrsnilghkgefaeefgvimkalwaglykcisprdfkitigki 826
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  827 ndqfagyDQQDSQELLLFLMDGLHEDLNKADNKKRYKEEendhlddqtaadlawskhkllNESIIVALFQGQFKSTVQCS 906
Cdd:cd02257    21 -------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSS---------------------LKSLIHDLFGGKLESTIVCL 72

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  907 TCHRKSRTFETFMYLSLPL--ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKaHRDSTKKLEIWKVPPILLVHLKRFS 984
Cdd:cd02257    73 ECGHESVSTEPELFLSLPLpvKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFS 151

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  985 YEGRW-KQKLQTTVDFPLdNLDLTQYVI------GPKQTLKRYYLYGVSNHYGGL-DGGHYTAYCKNATKQRWYKFDDHE 1056
Cdd:cd02257   152 FNEDGtKEKLNTKVSFPL-ELDLSPYLSegekdsDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDDK 230

                         330       340
                  ....*....|....*....|....
gi 765114864 1057 VSEISTSSV-----KSSAAYILFY 1075
Cdd:cd02257   231 VTEVSEEEVlefgsLSSSAYILFY 254
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 747-1075 1.68e-65

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 224.17  E-value: 1.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCLCNTPAMAEYFNSN--YYLEDINRSNilghkGEFAEEFGVIMKALWAGLYKC-ISPRDFKITI 823
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSDrhSCTCLSCSPN-----SCLSCAMDEIFQEFYYSGDRSpYGPINLLYLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  824 GKINDQFAGYDQQDSQELLLFLMDGLHEDLnkadnkKRYKEEENDHLDDQTaadlawskhkllnesIIVALFQGQFKSTV 903
Cdd:cd02660    77 WKHSRNLAGYSQQDAHEFFQFLLDQLHTHY------GGDKNEANDESHCNC---------------IIHQTFSGSLQSSV 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  904 QCSTCHRKSRTFETFMYLSLPLASTSKCS-------------LQDCLRLFSKEEKLTDNNkVFCRHCKAHRDSTKKLEIW 970
Cdd:cd02660   136 TCQRCGGVSTTVDPFLDLSLDIPNKSTPSwalgesgvsgtptLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIK 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  971 KVPPILLVHLKRFSYE-GRWKQKLQTTVDFPLDnLDLTQYVIGPKQTLK---------RYYLYGVSNHYGGLDGGHYTAY 1040
Cdd:cd02660   215 KLPPVLCFQLKRFEHSlNKTSRKIDTYVQFPLE-LNMTPYTSSSIGDTQdsnsldpdyTYDLFAVVVHKGTLDTGHYTAY 293

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 765114864 1041 CKNATKQrWYKFDDHEVSEISTSSVKSSAAYILFY 1075
Cdd:cd02660   294 CRQGDGQ-WFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 746-1076 2.06e-65

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 223.31  E-value: 2.06e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  746 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNSNYYLEDINRsnilghkgefaEEFGV-------IMKALWAGLYKcISPRD 818
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCN-----------EGFCMmcaleahVERALASSGPG-SAPRI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  819 FKITIGKINDQFAGYDQQDSQELLLFLMDGLHedlnKADNKKRYKEEENDHLDDQTaadlawskhkllneSIIVALFQGQ 898
Cdd:cd02661    70 FSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDPSSQET--------------TLVQQIFGGY 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  899 FKSTVQCSTCHRKSRTFETFMYLSLPLASTSkcSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLV 978
Cdd:cd02661   132 LRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTI 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  979 HLKRFSYEGRwkQKLQTTVDFPlDNLDLTQYVIGPKQTLKRYYLYGVSNHYGG-LDGGHYTAYCKNATKqRWYKFDDHEV 1057
Cdd:cd02661   210 HLKRFSNFRG--GKINKQISFP-ETLDLSPYMSQPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKSSNG-KWYNMDDSKV 285

                         330
                  ....*....|....*....
gi 765114864 1058 SEISTSSVKSSAAYILFYS 1076
Cdd:cd02661   286 SPVSIETVLSQKAYILFYI 304
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 747-1075 4.59e-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: 195.68  E-value: 4.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCLCNTPAMAEYFNSNyyledinrsnilghkgefaeefgvimkalwaglykcisPRDFKITIGKI 826
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  827 NDQFAGYDQQDSQELLLFLMDGLhedlnkadnkkrykeeendhlddqtaadlawskhkllnESIIVALFQGQFKSTVQCS 906
Cdd:cd02667    43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  907 TCHRKSRTFETFMYLSLPLA--STSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKahrDSTKKLEIWKVPPILLVHLKRFS 984
Cdd:cd02667    85 SCGTVSLVYEPFLDLSLPRSdeIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQ 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  985 YEGRWK-QKLQTTVDFPlDNLDLTQYV-----IGPKQTLKRYYLYGVSNHYGGLDGGHYTAYCKNATKQR---------- 1048
Cdd:cd02667   162 QPRSANlRKVSRHVSFP-EILDLAPFCdpkcnSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQrlsdltkskp 240

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 765114864 1049 -----------WYKFDDHEVSEISTSSVKSSAAYILFY 1075
Cdd:cd02667   241 aadeagpgsgqWYYISDSDVREVSLEEVLKSEAYLLFY 278
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
743-925 1.18e-54

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 205.50  E-value: 1.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  743 ASLTGLRNLGNTCYMNSILQCLCNTPAMAEYFNSNYYLEDINRSNILGHKGEFAEEFGVIMKALWAGLYKCISPRDFKIT 822
Cdd:COG5560   263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  823 IGKINDQFAGYDQQDSQELLLFLMDGLHEDLNKAdNKKRYKEE----ENDHLDDQTAADLAWSKHKLLNESIIVALFQGQ 898
Cdd:COG5560   343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                         170       180
                  ....*....|....*....|....*..
gi 765114864  899 FKSTVQCSTCHRKSRTFETFMYLSLPL 925
Cdd:COG5560   422 YKSTLTCPGCGSVSITFDPFMDLTLPL 448
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 747-1076 1.66e-48

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 174.81  E-value: 1.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCLcntpamaeYFNSNYY-LEDINRSnILGHKgefaEEFGVimkalwaglykcISPRDFKITIGK 825
Cdd:cd02663     1 GLENFGNTCYCNSVLQAL--------YFENLLTcLKDLFES-ISEQK----KRTGV------------ISPKKFITRLKR 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  826 INDQFAGYDQQDSQELLLFLMDGLHEDLNKADNKKRYKEEENdhlddqtaADLAWSKHKllneSIIVALFQGQFKSTVQC 905
Cdd:cd02663    56 ENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLN--------NNNNAEPQP----TWVHEIFQGILTNETRC 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  906 STCHRKSRTFETFMYLSLPLAstSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSY 985
Cdd:cd02663   124 LTCETVSSRDETFLDLSIDVE--QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKY 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  986 EGRWKQ--KLQTTVDFPLDNLDLTQYVIGPKQTlKRYYLYGVSNHYG-GLDGGHYTAYCKnaTKQRWYKFDDHEVSEIST 1062
Cdd:cd02663   202 DEQLNRyiKLFYRVVFPLELRLFNTTDDAENPD-RLYELVAVVVHIGgGPNHGHYVSIVK--SHGGWLLFDDETVEKIDE 278

                         330       340
                  ....*....|....*....|..
gi 765114864 1063 SSV-------KSSA-AYILFYS 1076
Cdd:cd02663   279 NAVeeffgdsPNQAtAYVLFYQ 300
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 747-1076 1.03e-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: 173.38  E-value: 1.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCL------------CNTPAMAEYFNSNYYlEDINRSNILGHkgefaeeFGVIMKALWAGLYKCI 814
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWfmnlefrkavyeCNSTEDAELKNMPPD-KPHEPQTIIDQ-------LQLIFAQLQFGNRSVV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  815 SPRDFKITIGKINDQfagydQQDSQELLLFLMDGLHEDLNKADNKKrykeeendhlddqtaadlawskhkllNESIIVAL 894
Cdd:cd02668    73 DPSGFVKALGLDTGQ-----QQDAQEFSKLFLSLLEAKLSKSKNPD--------------------------LKNIVQDL 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  895 FQGQFKSTVQCSTCHRKSRTFETFMYLSLPLASTSKcsLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPP 974
Cdd:cd02668   122 FRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT--LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPP 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  975 ILLVHLKRFSY--EGRWKQKLQTTVDFPLDnLDLTQYVIGPKQTLKRYYLYGVSNHYG-GLDGGHYTAYCKNATKQRWYK 1051
Cdd:cd02668   200 TLNFQLLRFVFdrKTGAKKKLNASISFPEI-LDMGEYLAESDEGSYVYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYK 278

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 765114864 1052 FDDHEVSEISTSSVK---------------------SSAAYILFYS 1076
Cdd:cd02668   279 FNDEDVEEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVYK 324
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 747-1075 4.92e-45

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: 165.89  E-value: 4.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCLCNTPAMAEYFNSNYYLE-DINRSNILghkgefaEEFGVIMKALWAGLYKCISPRDFKITIGK 825
Cdd:cd02659     4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEdDDDNKSVP-------LALQRLFLFLQLSESPVKTTELTDKTRSF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  826 INDQFAGYDQQDSQELLLFLMDGLHEDLNKADNKKrykeeendhlddqtaadlawskhkllnesIIVALFQGQFKSTVQC 905
Cdd:cd02659    77 GWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEG-----------------------------LIKNLFGGKLVNYIIC 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  906 STCHRKSRTFETFmyLSLPLASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSY 985
Cdd:cd02659   128 KECPHESEREEYF--LDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEF 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  986 EGR--WKQKLQTTVDFPLDnLDLTQYVI----------GPKQTLK-RYYLYGVSNHYGGLDGGHYTAYCKNATKQRWYKF 1052
Cdd:cd02659   206 DFEtmMRIKINDRFEFPLE-LDMEPYTEkglakkegdsEKKDSESyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKF 284

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 765114864 1053 DDHEVSEISTSSV----------------------KSSAAYILFY 1075
Cdd:cd02659   285 NDDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFY 329
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 747-1075 2.93e-35

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 137.24  E-value: 2.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCLcntpAMAEYFNsnyyledinRSNILGHKGEFAEEFGVIMKALWAGLYKCISPRDFKITIGKI 826
Cdd:cd02664     1 GLINLGNTCYMNSVLQAL----FMAKDFR---------RQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  827 NDQ-----FAGYDQQDSQELLLFLMDGLHedlnkadnkkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFKS 901
Cdd:cd02664    68 LEAsrppwFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLST 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  902 TVQCSTCHRKSRTFETFMYLSLplastSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLK 981
Cdd:cd02664   110 TIRCLNCNSTSARTERFRDLDL-----SFPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLL 184

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  982 RFSY--EGRWKQKLQTTVDFPLDnLDLTQYV----IGPKQTLKR---------------YYLYGVSNHYG-GLDGGHYTA 1039
Cdd:cd02664   185 RFSYdqKTHVREKIMDNVSINEV-LSLPVRVesksSESPLEKKEeesgddgelvtrqvhYRLYAVVVHSGySSESGHYFT 263

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 765114864 1040 YCKNAT--------------------KQRWYKFDDHEVSEISTSSVK-------SSAAYILFY 1075
Cdd:cd02664   264 YARDQTdadstgqecpepkdaeendeSKNWYLFNDSRVTFSSFESVQnvtsrfpKDTPYILFY 326
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 747-1075 6.18e-32

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 127.06  E-value: 6.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCLCNTPAMAE---YFNSNYYLEDINRSNILghkgefaeefgVIMKALWAGLYK---CISPRDFK 820
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPARRGANQSSDNLT-----------NALRDLFDTMDKkqePVPPIEFL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  821 ITIGKINDQFA------GYDQQDSQELLLFLMDGLHEDLNKADNKKrykeeendhlddqtaadlawskhkllneSIIVAL 894
Cdd:cd02657    70 QLLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKG----------------------------SFIDQL 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  895 FQGQFKSTVQCS-TCHRKSRTFETFMYLSLPLASTSKCS-LQDCLRLFSKEE--KLTDnnkvfcrhcKAHRDS--TKKLE 968
Cdd:cd02657   122 FGIELETKMKCTeSPDEEEVSTESEYKLQCHISITTEVNyLQDGLKKGLEEEieKHSP---------TLGRDAiyTKTSR 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  969 IWKVPPILLVHLKRFSyegrWKQKLQT------TVDFPLdNLDLTQYVigpkqTLKRYY-LYGVSNHYG-GLDGGHYTAY 1040
Cdd:cd02657   193 ISRLPKYLTVQFVRFF----WKRDIQKkakilrKVKFPF-ELDLYELC-----TPSGYYeLVAVITHQGrSADSGHYVAW 262

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 765114864 1041 CKNATKQRWYKFDDHEVSEISTSSVKSSA-------AYILFY 1075
Cdd:cd02657   263 VRRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 6-116 2.25e-31

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


Pssm-ID: 462647  Cd Length: 113  Bit Score: 118.94  E-value: 2.25e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864     6 TEVKELYLSTSLGELNKKAEIKPD--KTSTRSYVQSACKLFKAAEECRLDRDEEKAYVLYMKYLTVYDIIKKRPDFKQQP 83
Cdd:pfam08969    1 APLKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 765114864    84 EYYITLLGQNSFKKAIEEAEKLSESLKLRYEEA 116
Cdd:pfam08969   81 ATVRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 726-1075 1.25e-29

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 121.15  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  726 PSAAKIRSLNPtfggmgasLTGLRNLGNTCYMNSILQCLCNTP----AMAEYFNSNYYLEDINRSNILGHKgefaeefgv 801
Cdd:cd02671    13 TSCEKRENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPgfkhGLKHLVSLISSVEQLQSSFLLNPE--------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  802 imkaLWAGLYKCISPRDFKITIGKINDQFAGYDQQDSQELLLFLMDGLHEDLNKadnkkrykeeendhlddqtaadlaws 881
Cdd:cd02671    76 ----KYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK-------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  882 khkllnesiivaLFQGQFKSTVQCSTCHRKSRTFETFMYLSLPLASTSKCS-----------------LQDCLRLFSKEE 944
Cdd:cd02671   126 ------------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKseesseispdpktemktLKWAISQFASVE 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  945 KLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRWK------QKLQTTVDFPldnLDLTQYVIGPKQTLK 1018
Cdd:cd02671   194 RIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTP---LKLSLEEWSTKPKND 270

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 765114864 1019 RYYLYGVSNHYGG-LDGGHYTAYCknatkqRWYKFDDHEV---------SEISTSSVKSSAAYILFY 1075
Cdd:cd02671   271 VYRLFAVVMHSGAtISSGHYTAYV------RWLLFDDSEVkvteekdflEALSPNTSSTSTPYLLFY 331
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 747-1075 1.47e-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: 117.42  E-value: 1.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCLCNTPAmaeyFNSNYY-LEDINRSNILGHKGEFAEEFGVIMKALWAGLYKC------------ 813
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPS----FQWRYDdLENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKpaslksendpyq 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  814 --ISPRDFKITIGKINDQFAGYDQQDSQELLLFLMDglhedlnKADNKKRYKEEENdhlddqtaadlawskhklLNEsii 891
Cdd:cd02658    77 vgIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLID-------KLDRESFKNLGLN------------------PND--- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  892 vaLFQGQFKSTVQCSTCHRKSRTFETFMYLSLPL------------ASTSKCSLQDCLRLFSKEEKLTDnnkvFCRHCKA 959
Cdd:cd02658   129 --LFKFMIEDRLECLSCKKVKYTSELSEILSLPVpkdeatekeegeLVYEPVPLEDCLKAYFAPETIED----FCSTCKE 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  960 HRDSTKKLEIWKVPPILLVHLKRFSYEGRWKQKlqtTVDFPLDnldlTQYVIGPkqtlKRYYLYGVSNHYG-GLDGGHYT 1038
Cdd:cd02658   203 KTTATKTTGFKTFPDYLVINMKRFQLLENWVPK---KLDVPID----VPEELGP----GKYELIAFISHKGtSVHSGHYV 271

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 765114864 1039 AYCK--NATKQRWYKFDDHEVSEISTSSVKSSAAYILFY 1075
Cdd:cd02658   272 AHIKkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
747-1076 7.52e-28

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 114.51  E-value: 7.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCLC-NTPAMaeyfnSNYYLEDINRSNILghKGEFAEEFGVIMKALWAGLYKCISPRDfKITIGK 825
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKL-----DELLDDLSKELKVL--KNVIRKPEPDLNQEEALKLFTALWSSK-EHKVGW 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  826 INDQfagYDQQDSQELLLFLMDGLHEDLNKA--DNKKRYKEEENDHLDDQtaadlaWSkhkllneSIIVALFQGQF---K 900
Cdd:COG5533    73 IPPM---GSQEDAHELLGKLLDELKLDLVNSftIRIFKTTKDKKKTSTGD------WF-------DIIIELPDQTWvnnL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  901 STVQCstchrksrTFETFMYLsLPLASTSKcslqdclrlfskeEKLTDNNKVFCRHCKAHRDStkkleiwKVPPILLVHL 980
Cdd:COG5533   137 KTLQE--------FIDNMEEL-VDDETGVK-------------AKENEELEVQAKQEYEVSFV-------KLPKILTIQL 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  981 KRFSYEGRwKQKLQTTVDfplDNLDLTqyvIGPKQTLK-----RYYLYGVSNHYGGLDGGHYTAYCKnaTKQRWYKFDDH 1055
Cdd:COG5533   188 KRFANLGG-NQKIDTEVD---EKFELP---VKHDQILNivketYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDS 258

                         330       340
                  ....*....|....*....|....
gi 765114864 1056 EVSEISTS---SVKSSAAYILFYS 1076
Cdd:COG5533   259 DVTPVSEEeaiNEKAKNAYLYFYE 282
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 747-1075 1.64e-25

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: 106.30  E-value: 1.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQCLCNTPAMAEYfnsnyyLEDINrsnilghkgefaeefgvimkalwaglykcisprdfkitigki 826
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEY------LEEFL------------------------------------------ 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  827 ndqfagyDQQDSQELLLFLMDGLhedlnkadnkkrykeeendhlddqtaadlawskhkllnESIIVALFQGQFKSTVQCS 906
Cdd:cd02662    33 -------EQQDAHELFQVLLETL--------------------------------------EQLLKFPFDGLLASRIVCL 67

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  907 TCHRKSR-TFETFMYLSLPL---ASTSKCSLQDCLRLFSKEEKLTDnnkVFCRHCKahrdstkkLEIWKVPPILLVHLKR 982
Cdd:cd02662    68 QCGESSKvRYESFTMLSLPVpnqSSGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSR 136

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  983 FSYEGRWK-QKLQTTVDFPLDnldLTQYvigpkqtlkRYYLYGVSNHYGGLDGGHYTAY--------------------C 1041
Cdd:cd02662   137 SVFDGRGTsTKNSCKVSFPER---LPKV---------LYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreG 204

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 765114864 1042 KNATKQRWYKFDDHEVSEISTSSVK-SSAAYILFY 1075
Cdd:cd02662   205 PSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 709-1075 1.12e-23

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 105.48  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  709 DTKPVTAKVYSKVEIAR--PSAAKIRSLN--PTFGGMgaslTGLRNLGNTCYMNSILQCLCNTPAMaeyfnSNYYLEDIN 784
Cdd:cd02669    83 DIKYVLNPTYTKEQISDldRDPKLSRDLDgkPYLPGF----VGLNNIKNNDYANVIIQALSHVKPI-----RNFFLLYEN 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  785 RSNILGHKGEFAEEFGVIMKALW-AGLYKC-ISPRDFKITIGKI-NDQFAGYDQQDSQELLLFLMDGLHEDLNKadNKKR 861
Cdd:cd02669   154 YENIKDRKSELVKRLSELIRKIWnPRNFKGhVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGG--SKKP 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  862 ykeeendhlddqtaadlawskhkllNESIIVALFQG--------------QFKSTVQCSTCHRKSRTFET-FMYLS--LP 924
Cdd:cd02669   232 -------------------------NSSIIHDCFQGkvqietqkikphaeEEGSKDKFFKDSRVKKTSVSpFLLLTldLP 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  925 LASTSKCSLQD-CLRLFSKEEKLTDNNKVfcrHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRWKQKLQTTVDFPLDN 1003
Cdd:cd02669   287 PPPLFKDGNEEnIIPQVPLKQLLKKYDGK---TETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKN 363

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 765114864 1004 LDLTQYVIGPKQTLKRYYLYG-VSN--HYGG-LDGGHYTAYCKNATKQRWYKFDDHEVSEISTSSVKSSAAYILFY 1075
Cdd:cd02669   364 LDLSDYVHFDKPSLNLSTKYNlVANivHEGTpQEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 747-1065 2.12e-21

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 101.10  E-value: 2.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  747 GLRNLGNTCYMNSILQclcntpamaEYFNSNYYLEDINRSNILGHKGEfaEEFGVIMKALWAGLYKCISPRD-FKITIGK 825
Cdd:COG5077   195 GLRNQGATCYMNSLLQ---------SLFFIAKFRKDVYGIPTDHPRGR--DSVALALQRLFYNLQTGEEPVDtTELTRSF 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  826 INDQFAGYDQQDSQELLLFLMDGLhedlnkaDNKKRYKEEENdhlddqtaadlawskhkLLNEsiivaLFQGQFKSTVQC 905
Cdd:COG5077   264 GWDSDDSFMQHDIQEFNRVLQDNL-------EKSMRGTVVEN-----------------ALNG-----IFVGKMKSYIKC 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  906 STCHRKSRTFETFMYLSLPLASTSkcSLQDCLRLFSKEEKLTDNNKVFCRHcKAHRDSTKKLEIWKVPPILLVHLKRFSY 985
Cdd:COG5077   315 VNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEY 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  986 EGRWKQ--KLQTTVDFPlDNLDLTQYVigPKQTLKR------YYLYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHEV 1057
Cdd:COG5077   392 DFERDMmvKINDRYEFP-LEIDLLPFL--DRDADKSensdavYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRV 468


                  ....*...
gi 765114864 1058 SEISTSSV 1065
Cdd:COG5077   469 TRATEKEV 476
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 748-1075 1.29e-12

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


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 68.71  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  748 LRNLGNTCYMNSILQCLCntpamaeyfnsnyyledinrsnilghkgefaeefgvimkalwaglykcisprdfkiTIGKIN 827
Cdd:cd02673     2 LVNTGNSCYFNSTMQALS--------------------------------------------------------SIGKIN 25

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  828 DQFAGYDQQDSQELLLFL---MDGLHEdlNKADNKKRYkEEENDHLDDQTAadlawskHKLLNESIIValfqgqfkstvq 904
Cdd:cd02673    26 TEFDNDDQQDAHEFLLTLleaIDDIMQ--VNRTNVPPS-NIEIKRLNPLEA-------FKYTIESSYV------------ 83

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  905 CSTCHRKSRTFETFMYLSLPLASTSKCSLQDclrLFSKEEKLTDNNKVfCRHCKaHRDSTKKLEIWKVPPILLVHLKRFs 984
Cdd:cd02673    84 CIGCSFEENVSDVGNFLDVSMIDNKLDIDEL---LISNFKTWSPIEKD-CSSCK-CESAISSERIMTFPECLSINLKRY- 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  985 yegrwkqKLQT-TVDFPLDNLDLTQYVIGpkqTLKRYYLYGVSNHYG-GLDGGHYTAYCKNATK-QRWYKFDDHEVSEIS 1061
Cdd:cd02673   158 -------KLRIaTSDYLKKNEEIMKKYCG---TDAKYSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIRPVS 227

                         330
                  ....*....|....*..
gi 765114864 1062 TSSVK---SSAAYILFY 1075
Cdd:cd02673   228 KNDVStnaRSSGYLIFY 244
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 835-1075 1.83e-09

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 59.11  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  835 QQDSQELLLFLMDGLHEDLNKADNKKRYKEEendhlddqtaadlawSKHKLlnesiiVALFQGQFkSTVqcsTCHRKSRT 914
Cdd:cd02665    22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEK---------------SKNPM------VQLFYGTF-LTE---GVLEGKPF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  915 FETFMYLSLPLASTSKCSLQDCLrlfskeEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRWKQKLQ 994
Cdd:cd02665    77 CNCETFGQYPLQVNGYGNLHECL------EAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPEKIH 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  995 TTVDFPldnldltqyvigpkQTLKR--YYLYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHEVSEISTSSVKSSA--- 1069
Cdd:cd02665   151 DKLEFP--------------QIIQQvpYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfgg 216

                         250
                  ....*....|.
gi 765114864 1070 -----AYILFY 1075
Cdd:cd02665   217 grnpsAYCLMY 227
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
872-1054 5.30e-08

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 55.74  E-value: 5.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864   872 DQTAADLAWSKHKLL-NESIIVALFQGQFKSTVQCSTC-HRKSRTFETFM----YLSLPLASTSKCSLQD---CLRLFSK 942
Cdd:pfam13423  108 DQLSSEENSTPPNPSpAESPLEQLFGIDAETTIRCSNCgHESVRESSTHVldliYPRKPSSNNKKPPNQTfssILKSSLE 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864   943 EEKLTdnnKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEgrWKQKLQTTVDFPLD-NLDLTQYVIGPKQTLKrYY 1021
Cdd:pfam13423  188 RETTT---KAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPEiGLTLSDDLQGDNEIVK-YE 261

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 765114864  1022 LYG-VSNHYGGLDGGHYTAYCK-------NATKQRWYKFDD 1054
Cdd:pfam13423  262 LRGvVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 882-1075 8.59e-08

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


Pssm-ID: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 54.83  E-value: 8.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  882 KHKLLNE-----SIIVALFQGQFKSTVQC-----STCHRKSRTFETFMY-LSLPLASTSKCSLQDCLRLFSKEEKLTDNN 950
Cdd:cd02672    54 ESCLLCElgylfSTLIQNFTRFLLETISQdqlgtPFSCGTSRNSVSLLYtLSLPLGSTKTSKESTFLQLLKRSLDLEKVT 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  951 KVFCRHCKAHRDSTKKLEIWKVPPILL----VHLKRFSYEGRWKQ-------KLQTTVDFPLDNLDLTQYVIGPKQTLKr 1019
Cdd:cd02672   134 KAWCDTCCKYQPLEQTTSIRHLPDILLlvlvINLSVTNGEFDDINvvlpsgkVMQNKVSPKAIDHDKLVKNRGQESIYK- 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 765114864 1020 YYLYG-VSNHYGGLDGGHYTA----YCKNATKQRWYKFDDHEVSEISTSsvkssaAYILFY 1075
Cdd:cd02672   213 YELVGyVCEINDSSRGQHNVVfvikVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 746-1065 2.18e-06

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: 50.95  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  746 TGLRNLGNTCYMNSILQCL-CNTPA-----MAEYFNSNYYLEDINRSNILGHKGEFAE-----EFGVIMKALWAGLYK-- 812
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFfTIKPLrdlvlNFDESKAELASDYPTERRIGGREVSRSElqrsnQFVYELRSLFNDLIHsn 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  813 --CISPRDfkitigkiNDQFAGYDQQDSQELLLFLMDglheDLNKADNKKRYKEEENDHLDDQTAADLawskhkllnesi 890
Cdd:cd02666    82 trSVTPSK--------ELAYLALRQQDVTECIDNVLF----QLEVALEPISNAFAGPDTEDDKEQSDL------------ 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  891 IVALFQGQFK-STVQCSTCHRKSRT--FETFMYLSLPLAST--------SKCSLQDCL----------------RLFSKE 943
Cdd:cd02666   138 IKRLFSGKTKqQLVPESMGNQPSVRtkTERFLSLLVDVGKKgreivvllEPKDLYDALdryfdydsltklpqrsQVQAQL 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  944 EKLTDNNKVFCRHCKAHRDSTKKLEIWK--VPPILLVHLKRFSYEGRWKQKLQTTVDfpldnlDLTQYVigpkqtlkrYY 1021
Cdd:cd02666   218 AQPLQRELISMDRYELPSSIDDIDELIReaIQSESSLVRQAQNELAELKHEIEKQFD------DLKSYG---------YR 282

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 765114864 1022 LYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHEVSEISTSSV 1065
Cdd:cd02666   283 LHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEV 326
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 971-1075 5.24e-05

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


Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 45.98  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  971 KVPPILLVHLKRFSYEGRWKQKLQTTVDfPLDNLDLTQYVIG-PKQTLKRYYLYGVSN---------------------H 1028
Cdd:cd02670    97 KAPSCLIICLKRYGKTEGKAQKMFKKIL-IPDEIDIPDFVADdPRACSKCQLECRVCYddkdfsptcgkfklslcsavcH 175

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 765114864 1029 YG-GLDGGHYTAYCK-----------NATKQRWYKFDD-------HEVSEISTSSVKSSaAYILFY 1075
Cdd:cd02670   176 RGtSLETGHYVAFVRygsysltetdnEAYNAQWVFFDDmadrdgvSNGFNIPAARLLED-PYMLFY 240
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 197-305 7.07e-04

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


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 39.77  E-value: 7.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864   197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS-PGITVNQIEAKLPSMSKDhwmkrgfvDYIILLDWFSSVSDLklgtTL 275
Cdd:pfam00581    7 VLIDVRPPEEYAKGHI----PGAVNVPLSSLSlPPLPLLELLEKLLELLKD--------KPIVVYCNSGNRAAA----AA 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 765114864   276 QSLKDALFKwdsmtilrsEPLVLEGGYENW 305
Cdd:pfam00581   71 ALLKALGYK---------NVYVLDGGFEAW 91
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 358-620 5.02e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.83  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  358 QKPPAPAVANGVAPAEPPTSKTSviaDKLPDTHDSPvrspastgldlnkKSPAPNQSPATAKAFPQFDRTKKPVRDEpKP 437
Cdd:PTZ00449  589 KDPEEPKKPKRPRSAQRPTRPKS---PKLPELLDIP-------------KSPKRPESPKSPKRPPPPQRPSSPERPE-GP 651

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  438 KEDGSTKdstqngpvvPDRSVKPPLIPSTslsKEEQNQIHLEAVAVMEKAKQEQEKRMQERRLEEEKREKELKDRLEREE 517
Cdd:PTZ00449  652 KIIKSPK---------PPKSPKPPFDPKF---KEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPR 719

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864  518 SERRSKQEEEKRHLErkRLERQKAEEEEDKENKTWDERER-RGKEPNADTpsksmsldsPVPNHLVSEIKREPL---TRA 593
Cdd:PTZ00449  720 PLPPKLPRDEEFPFE--PIGDPDAEQPDDIEFFTPPEEERtFFHETPADT---------PLPDILAEEFKEEDIhaeTGE 788

                         250       260
                  ....*....|....*....|....*..
gi 765114864  594 RSEEMGRtvpglPDGWMKFLDTVTGTY 620
Cdd:PTZ00449  789 PDEAMKR-----PDSPSEHEDKPPGDH 810
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 197-310 5.24e-03

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


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 37.44  E-value: 5.24e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765114864    197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS--PGITVNQIEAKLPSMSkdhwmKRGFVDYIILLDWfssvSDLKLGTT 274
Cdd:smart00450    6 VLLDVRSPEEYEGGHI----PGAVNIPLSELLdrRGELDILEFEELLKRL-----GLDKDKPVVVYCR----SGNRSAKA 72

                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 765114864    275 LQSLKDALFKwdsmtilrsEPLVLEGGYENWLLFYP 310
Cdd:smart00450   73 AWLLRELGFK---------NVYLLDGGYKEWSAAGP 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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