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Conserved domains on  [gi|1174681693|ref|XP_020568266|]
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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 1174681693  747 GLRNLGNTCYMNSILQCLCNtpamaeyfnsnyyledinrsnilghkgefaeefgvimkalwaglykcisprdfkitigki 826
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  827 ndqfagyDQQDSQELLLFLMDGLHedlnkadnkkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFKSTVQCS 906
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  907 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKR 982
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  983 FSYEGRWKQKLQTTVDFPLDNLDLTQYVIGPKQT-LKRYYLYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHEVSEIS 1061
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 1174681693 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 1174681693  743 ASLTGLRNLGNTCYMNSILQCLCNTPAMAEYFNSNYYLEDINRSNILGHKGEFAEEFGVIMKALWAGLYKCISPRDFKIT 822
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  823 IGKINDQFAGYDQQDSQELLLFLMDGLHEDLNKAdNKKRYKEE----ENDHLDDQTAADLAWSKHKLLNESIIVALFQGQ 898
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                          170       180
                   ....*....|....*....|....*..
gi 1174681693  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 1174681693    6 TEVKELYLSTSLGELNKKAEIKPD--KTSTRSYVQSACKLFKAAEECRLDRDEEKAYVLYMKYLTVYDIIKKRPDFKQQP 83
Cdd:pfam08969    1 APLKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1174681693   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 1174681693  197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS-PGITVNQIEAKLPSMSKDhwmkrgfvDYIILLDWFSSVSDLklgtTL 275
Cdd:pfam00581    7 VLIDVRPPEEYAKGHI----PGAVNVPLSSLSlPPLPLLELLEKLLELLKD--------KPIVVYCNSGNRAAA----AA 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 1174681693  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 1174681693  358 QKPPAPAVANGVAPAEPPTSKTSviaDKLPDTHDSPvrspastgldlnkKSPAPNQSPATAKAFPQFDRTKKPVRDEpKP 437
Cdd:PTZ00449   589 KDPEEPKKPKRPRSAQRPTRPKS---PKLPELLDIP-------------KSPKRPESPKSPKRPPPPQRPSSPERPE-GP 651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  438 KEDGSTKdstqngpvvPDRSVKPPLIPSTslsKEEQNQIHLEAVAVMEKAKQEQEKRMQERRLEEEKREKELKDRLEREE 517
Cdd:PTZ00449   652 KIIKSPK---------PPKSPKPPFDPKF---KEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPR 719

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  518 SERRSKQEEEKRHLErkRLERQKAEEEEDKENKTWDERER-RGKEPNADTpsksmsldsPVPNHLVSEIKREPL---TRA 593
Cdd:PTZ00449   720 PLPPKLPRDEEFPFE--PIGDPDAEQPDDIEFFTPPEEERtFFHETPADT---------PLPDILAEEFKEEDIhaeTGE 788

                          250       260
                   ....*....|....*....|....*..
gi 1174681693  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 1174681693  747 GLRNLGNTCYMNSILQCLCNtpamaeyfnsnyyledinrsnilghkgefaeefgvimkalwaglykcisprdfkitigki 826
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  827 ndqfagyDQQDSQELLLFLMDGLHedlnkadnkkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFKSTVQCS 906
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  907 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKR 982
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  983 FSYEGRWKQKLQTTVDFPLDNLDLTQYVIGPKQT-LKRYYLYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHEVSEIS 1061
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 1174681693 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 1174681693  746 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNSNYYLEDINRSNILGHkgeFAEEFGVIMKALW-AGLYKCISPRDFKITIG 824
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQkNSKSSSVSPKMFKKSLG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  825 KINDQFAGYDQQDSQELLLFLMDGLHEDLNkadnkkrykeeendhlddqtaadlawSKHKLLNESIIVALFQGQFKSTVQ 904
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  905 CSTCHRKSRTFETFMYLSLPL----ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHL 980
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIpgdsAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  981 KRFSYEGRWKQKLQTTVDFPLDnLDLTQYVIG---PKQTLKRYY-LYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHE 1056
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEelkPKTNNLQDYrLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290

                          330       340
                   ....*....|....*....|
gi 1174681693 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 1174681693  743 ASLTGLRNLGNTCYMNSILQCLCNTPAMAEYFNSNYYLEDINRSNILGHKGEFAEEFGVIMKALWAGLYKCISPRDFKIT 822
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  823 IGKINDQFAGYDQQDSQELLLFLMDGLHEDLNKAdNKKRYKEE----ENDHLDDQTAADLAWSKHKLLNESIIVALFQGQ 898
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                          170       180
                   ....*....|....*....|....*..
gi 1174681693  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 1174681693    6 TEVKELYLSTSLGELNKKAEIKPD--KTSTRSYVQSACKLFKAAEECRLDRDEEKAYVLYMKYLTVYDIIKKRPDFKQQP 83
Cdd:pfam08969    1 APLKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1174681693   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 1174681693  747 GLRNLGNTCYMNSILQCLC-NTPAMaeyfnSNYYLEDINRSNILghKGEFAEEFGVIMKALWAGLYKCISPRDfKITIGK 825
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILAlYLPKL-----DELLDDLSKELKVL--KNVIRKPEPDLNQEEALKLFTALWSSK-EHKVGW 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  826 INDQfagYDQQDSQELLLFLMDGLHEDLNKA--DNKKRYKEEENDHLDDQtaadlaWSkhkllneSIIVALFQGQF---K 900
Cdd:COG5533     73 IPPM---GSQEDAHELLGKLLDELKLDLVNSftIRIFKTTKDKKKTSTGD------WF-------DIIIELPDQTWvnnL 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  901 STVQCstchrksrTFETFMYLsLPLASTSKcslqdclrlfskeEKLTDNNKVFCRHCKAHRDStkkleiwKVPPILLVHL 980
Cdd:COG5533    137 KTLQE--------FIDNMEEL-VDDETGVK-------------AKENEELEVQAKQEYEVSFV-------KLPKILTIQL 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  981 KRFSYEGRwKQKLQTTVDfplDNLDLTqyvIGPKQTLK-----RYYLYGVSNHYGGLDGGHYTAYCKnaTKQRWYKFDDH 1055
Cdd:COG5533    188 KRFANLGG-NQKIDTEVD---EKFELP---VKHDQILNivketYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDS 258

                          330       340
                   ....*....|....*....|....
gi 1174681693 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 1174681693  197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS-PGITVNQIEAKLPSMSKDhwmkrgfvDYIILLDWFSSVSDLklgtTL 275
Cdd:pfam00581    7 VLIDVRPPEEYAKGHI----PGAVNVPLSSLSlPPLPLLELLEKLLELLKD--------KPIVVYCNSGNRAAA----AA 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 1174681693  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 1174681693  358 QKPPAPAVANGVAPAEPPTSKTSviaDKLPDTHDSPvrspastgldlnkKSPAPNQSPATAKAFPQFDRTKKPVRDEpKP 437
Cdd:PTZ00449   589 KDPEEPKKPKRPRSAQRPTRPKS---PKLPELLDIP-------------KSPKRPESPKSPKRPPPPQRPSSPERPE-GP 651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  438 KEDGSTKdstqngpvvPDRSVKPPLIPSTslsKEEQNQIHLEAVAVMEKAKQEQEKRMQERRLEEEKREKELKDRLEREE 517
Cdd:PTZ00449   652 KIIKSPK---------PPKSPKPPFDPKF---KEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPR 719

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  518 SERRSKQEEEKRHLErkRLERQKAEEEEDKENKTWDERER-RGKEPNADTpsksmsldsPVPNHLVSEIKREPL---TRA 593
Cdd:PTZ00449   720 PLPPKLPRDEEFPFE--PIGDPDAEQPDDIEFFTPPEEERtFFHETPADT---------PLPDILAEEFKEEDIhaeTGE 788

                          250       260
                   ....*....|....*....|....*..
gi 1174681693  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 1174681693   197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS--PGITVNQIEAKLPSMSkdhwmKRGFVDYIILLDWfssvSDLKLGTT 274
Cdd:smart00450    6 VLLDVRSPEEYEGGHI----PGAVNIPLSELLdrRGELDILEFEELLKRL-----GLDKDKPVVVYCR----SGNRSAKA 72

                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 1174681693   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 1174681693  747 GLRNLGNTCYMNSILQCLCNtpamaeyfnsnyyledinrsnilghkgefaeefgvimkalwaglykcisprdfkitigki 826
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  827 ndqfagyDQQDSQELLLFLMDGLHedlnkadnkkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFKSTVQCS 906
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  907 TCHRKSRTFETFMYLSLPLASTS----KCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKR 982
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  983 FSYEGRWKQKLQTTVDFPLDNLDLTQYVIGPKQT-LKRYYLYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHEVSEIS 1061
Cdd:cd02674    136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215

                          330
                   ....*....|....*
gi 1174681693 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 1174681693  746 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNSNYYLEDINRSNILGHkgeFAEEFGVIMKALW-AGLYKCISPRDFKITIG 824
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQkNSKSSSVSPKMFKKSLG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  825 KINDQFAGYDQQDSQELLLFLMDGLHEDLNkadnkkrykeeendhlddqtaadlawSKHKLLNESIIVALFQGQFKSTVQ 904
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  905 CSTCHRKSRTFETFMYLSLPL----ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHL 980
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIpgdsAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  981 KRFSYEGRWKQKLQTTVDFPLDnLDLTQYVIG---PKQTLKRYY-LYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHE 1056
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEelkPKTNNLQDYrLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290

                          330       340
                   ....*....|....*....|
gi 1174681693 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 1174681693  747 GLRNLGNTCYMNSILQCLCNtpamaeyfnsnyyledinrsnilghkgefaeefgvimkalwaglykcisprdfkitigki 826
Cdd:cd02257      1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  827 ndqfagyDQQDSQELLLFLMDGLHEDLNKADNKKRYKEEendhlddqtaadlawskhkllNESIIVALFQGQFKSTVQCS 906
Cdd:cd02257     21 -------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSS---------------------LKSLIHDLFGGKLESTIVCL 72

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  907 TCHRKSRTFETFMYLSLPL--ASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKaHRDSTKKLEIWKVPPILLVHLKRFS 984
Cdd:cd02257     73 ECGHESVSTEPELFLSLPLpvKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFS 151

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  985 YEGRW-KQKLQTTVDFPLdNLDLTQYVI------GPKQTLKRYYLYGVSNHYGGL-DGGHYTAYCKNATKQRWYKFDDHE 1056
Cdd:cd02257    152 FNEDGtKEKLNTKVSFPL-ELDLSPYLSegekdsDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDDK 230

                          330       340
                   ....*....|....*....|....
gi 1174681693 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 1174681693  747 GLRNLGNTCYMNSILQCLCNTPAMAEYFNSN--YYLEDINRSNilghkGEFAEEFGVIMKALWAGLYKC-ISPRDFKITI 823
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFLSDrhSCTCLSCSPN-----SCLSCAMDEIFQEFYYSGDRSpYGPINLLYLS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  824 GKINDQFAGYDQQDSQELLLFLMDGLHEDLnkadnkKRYKEEENDHLDDQTaadlawskhkllnesIIVALFQGQFKSTV 903
Cdd:cd02660     77 WKHSRNLAGYSQQDAHEFFQFLLDQLHTHY------GGDKNEANDESHCNC---------------IIHQTFSGSLQSSV 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  904 QCSTCHRKSRTFETFMYLSLPLASTSKCS-------------LQDCLRLFSKEEKLTDNNkVFCRHCKAHRDSTKKLEIW 970
Cdd:cd02660    136 TCQRCGGVSTTVDPFLDLSLDIPNKSTPSwalgesgvsgtptLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIK 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  971 KVPPILLVHLKRFSYE-GRWKQKLQTTVDFPLDnLDLTQYVIGPKQTLK---------RYYLYGVSNHYGGLDGGHYTAY 1040
Cdd:cd02660    215 KLPPVLCFQLKRFEHSlNKTSRKIDTYVQFPLE-LNMTPYTSSSIGDTQdsnsldpdyTYDLFAVVVHKGTLDTGHYTAY 293

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1174681693 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 1174681693  746 TGLRNLGNTCYMNSILQCLCNTPAMAEYFNSNYYLEDINRsnilghkgefaEEFGV-------IMKALWAGLYKcISPRD 818
Cdd:cd02661      2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCN-----------EGFCMmcaleahVERALASSGPG-SAPRI 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  819 FKITIGKINDQFAGYDQQDSQELLLFLMDGLHedlnKADNKKRYKEEENDHLDDQTaadlawskhkllneSIIVALFQGQ 898
Cdd:cd02661     70 FSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDPSSQET--------------TLVQQIFGGY 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  899 FKSTVQCSTCHRKSRTFETFMYLSLPLASTSkcSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLV 978
Cdd:cd02661    132 LRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTI 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  979 HLKRFSYEGRwkQKLQTTVDFPlDNLDLTQYVIGPKQTLKRYYLYGVSNHYGG-LDGGHYTAYCKNATKqRWYKFDDHEV 1057
Cdd:cd02661    210 HLKRFSNFRG--GKINKQISFP-ETLDLSPYMSQPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKSSNG-KWYNMDDSKV 285

                          330
                   ....*....|....*....
gi 1174681693 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 1174681693  747 GLRNLGNTCYMNSILQCLCNTPAMAEYFNSNyyledinrsnilghkgefaeefgvimkalwaglykcisPRDFKITIGKI 826
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  827 NDQFAGYDQQDSQELLLFLMDGLhedlnkadnkkrykeeendhlddqtaadlawskhkllnESIIVALFQGQFKSTVQCS 906
Cdd:cd02667     43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  907 TCHRKSRTFETFMYLSLPLA--STSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKahrDSTKKLEIWKVPPILLVHLKRFS 984
Cdd:cd02667     85 SCGTVSLVYEPFLDLSLPRSdeIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQ 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  985 YEGRWK-QKLQTTVDFPlDNLDLTQYV-----IGPKQTLKRYYLYGVSNHYGGLDGGHYTAYCKNATKQR---------- 1048
Cdd:cd02667    162 QPRSANlRKVSRHVSFP-EILDLAPFCdpkcnSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQrlsdltkskp 240

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1174681693 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 1174681693  743 ASLTGLRNLGNTCYMNSILQCLCNTPAMAEYFNSNYYLEDINRSNILGHKGEFAEEFGVIMKALWAGLYKCISPRDFKIT 822
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  823 IGKINDQFAGYDQQDSQELLLFLMDGLHEDLNKAdNKKRYKEE----ENDHLDDQTAADLAWSKHKLLNESIIVALFQGQ 898
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGM 421

                          170       180
                   ....*....|....*....|....*..
gi 1174681693  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 1174681693  747 GLRNLGNTCYMNSILQCLcntpamaeYFNSNYY-LEDINRSnILGHKgefaEEFGVimkalwaglykcISPRDFKITIGK 825
Cdd:cd02663      1 GLENFGNTCYCNSVLQAL--------YFENLLTcLKDLFES-ISEQK----KRTGV------------ISPKKFITRLKR 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  826 INDQFAGYDQQDSQELLLFLMDGLHEDLNKADNKKRYKEEENdhlddqtaADLAWSKHKllneSIIVALFQGQFKSTVQC 905
Cdd:cd02663     56 ENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLN--------NNNNAEPQP----TWVHEIFQGILTNETRC 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  906 STCHRKSRTFETFMYLSLPLAstSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSY 985
Cdd:cd02663    124 LTCETVSSRDETFLDLSIDVE--QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKY 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  986 EGRWKQ--KLQTTVDFPLDNLDLTQYVIGPKQTlKRYYLYGVSNHYG-GLDGGHYTAYCKnaTKQRWYKFDDHEVSEIST 1062
Cdd:cd02663    202 DEQLNRyiKLFYRVVFPLELRLFNTTDDAENPD-RLYELVAVVVHIGgGPNHGHYVSIVK--SHGGWLLFDDETVEKIDE 278

                          330       340
                   ....*....|....*....|..
gi 1174681693 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 1174681693  747 GLRNLGNTCYMNSILQCL------------CNTPAMAEYFNSNYYlEDINRSNILGHkgefaeeFGVIMKALWAGLYKCI 814
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWfmnlefrkavyeCNSTEDAELKNMPPD-KPHEPQTIIDQ-------LQLIFAQLQFGNRSVV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  815 SPRDFKITIGKINDQfagydQQDSQELLLFLMDGLHEDLNKADNKKrykeeendhlddqtaadlawskhkllNESIIVAL 894
Cdd:cd02668     73 DPSGFVKALGLDTGQ-----QQDAQEFSKLFLSLLEAKLSKSKNPD--------------------------LKNIVQDL 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  895 FQGQFKSTVQCSTCHRKSRTFETFMYLSLPLASTSKcsLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPP 974
Cdd:cd02668    122 FRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT--LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPP 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  975 ILLVHLKRFSY--EGRWKQKLQTTVDFPLDnLDLTQYVIGPKQTLKRYYLYGVSNHYG-GLDGGHYTAYCKNATKQRWYK 1051
Cdd:cd02668    200 TLNFQLLRFVFdrKTGAKKKLNASISFPEI-LDMGEYLAESDEGSYVYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYK 278

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1174681693 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 1174681693  747 GLRNLGNTCYMNSILQCLCNTPAMAEYFNSNYYLE-DINRSNILghkgefaEEFGVIMKALWAGLYKCISPRDFKITIGK 825
Cdd:cd02659      4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEdDDDNKSVP-------LALQRLFLFLQLSESPVKTTELTDKTRSF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  826 INDQFAGYDQQDSQELLLFLMDGLHEDLNKADNKKrykeeendhlddqtaadlawskhkllnesIIVALFQGQFKSTVQC 905
Cdd:cd02659     77 GWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEG-----------------------------LIKNLFGGKLVNYIIC 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  906 STCHRKSRTFETFmyLSLPLASTSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSY 985
Cdd:cd02659    128 KECPHESEREEYF--LDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEF 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  986 EGR--WKQKLQTTVDFPLDnLDLTQYVI----------GPKQTLK-RYYLYGVSNHYGGLDGGHYTAYCKNATKQRWYKF 1052
Cdd:cd02659    206 DFEtmMRIKINDRFEFPLE-LDMEPYTEkglakkegdsEKKDSESyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKF 284

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1174681693 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 1174681693  747 GLRNLGNTCYMNSILQCLcntpAMAEYFNsnyyledinRSNILGHKGEFAEEFGVIMKALWAGLYKCISPRDFKITIGKI 826
Cdd:cd02664      1 GLINLGNTCYMNSVLQAL----FMAKDFR---------RQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYF 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  827 NDQ-----FAGYDQQDSQELLLFLMDGLHedlnkadnkkrykeeendhlddqtaadlawskhkllneSIIVALFQGQFKS 901
Cdd:cd02664     68 LEAsrppwFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLST 109

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  902 TVQCSTCHRKSRTFETFMYLSLplastSKCSLQDCLRLFSKEEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLK 981
Cdd:cd02664    110 TIRCLNCNSTSARTERFRDLDL-----SFPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLL 184

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  982 RFSY--EGRWKQKLQTTVDFPLDnLDLTQYV----IGPKQTLKR---------------YYLYGVSNHYG-GLDGGHYTA 1039
Cdd:cd02664    185 RFSYdqKTHVREKIMDNVSINEV-LSLPVRVesksSESPLEKKEeesgddgelvtrqvhYRLYAVVVHSGySSESGHYFT 263

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1174681693 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 1174681693  747 GLRNLGNTCYMNSILQCLCNTPAMAE---YFNSNYYLEDINRSNILghkgefaeefgVIMKALWAGLYK---CISPRDFK 820
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPARRGANQSSDNLT-----------NALRDLFDTMDKkqePVPPIEFL 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  821 ITIGKINDQFA------GYDQQDSQELLLFLMDGLHEDLNKADNKKrykeeendhlddqtaadlawskhkllneSIIVAL 894
Cdd:cd02657     70 QLLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKG----------------------------SFIDQL 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  895 FQGQFKSTVQCS-TCHRKSRTFETFMYLSLPLASTSKCS-LQDCLRLFSKEE--KLTDnnkvfcrhcKAHRDS--TKKLE 968
Cdd:cd02657    122 FGIELETKMKCTeSPDEEEVSTESEYKLQCHISITTEVNyLQDGLKKGLEEEieKHSP---------TLGRDAiyTKTSR 192

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  969 IWKVPPILLVHLKRFSyegrWKQKLQT------TVDFPLdNLDLTQYVigpkqTLKRYY-LYGVSNHYG-GLDGGHYTAY 1040
Cdd:cd02657    193 ISRLPKYLTVQFVRFF----WKRDIQKkakilrKVKFPF-ELDLYELC-----TPSGYYeLVAVITHQGrSADSGHYVAW 262

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1174681693 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 1174681693    6 TEVKELYLSTSLGELNKKAEIKPD--KTSTRSYVQSACKLFKAAEECRLDRDEEKAYVLYMKYLTVYDIIKKRPDFKQQP 83
Cdd:pfam08969    1 APLKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1174681693   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 1174681693  726 PSAAKIRSLNPtfggmgasLTGLRNLGNTCYMNSILQCLCNTP----AMAEYFNSNYYLEDINRSNILGHKgefaeefgv 801
Cdd:cd02671     13 TSCEKRENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPgfkhGLKHLVSLISSVEQLQSSFLLNPE--------- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  802 imkaLWAGLYKCISPRDFKITIGKINDQFAGYDQQDSQELLLFLMDGLHEDLNKadnkkrykeeendhlddqtaadlaws 881
Cdd:cd02671     76 ----KYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK-------------------------- 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  882 khkllnesiivaLFQGQFKSTVQCSTCHRKSRTFETFMYLSLPLASTSKCS-----------------LQDCLRLFSKEE 944
Cdd:cd02671    126 ------------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKseesseispdpktemktLKWAISQFASVE 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  945 KLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRWK------QKLQTTVDFPldnLDLTQYVIGPKQTLK 1018
Cdd:cd02671    194 RIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTP---LKLSLEEWSTKPKND 270

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1174681693 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 1174681693  747 GLRNLGNTCYMNSILQCLCNTPAmaeyFNSNYY-LEDINRSNILGHKGEFAEEFGVIMKALWAGLYKC------------ 813
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPS----FQWRYDdLENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKpaslksendpyq 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  814 --ISPRDFKITIGKINDQFAGYDQQDSQELLLFLMDglhedlnKADNKKRYKEEENdhlddqtaadlawskhklLNEsii 891
Cdd:cd02658     77 vgIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLID-------KLDRESFKNLGLN------------------PND--- 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  892 vaLFQGQFKSTVQCSTCHRKSRTFETFMYLSLPL------------ASTSKCSLQDCLRLFSKEEKLTDnnkvFCRHCKA 959
Cdd:cd02658    129 --LFKFMIEDRLECLSCKKVKYTSELSEILSLPVpkdeatekeegeLVYEPVPLEDCLKAYFAPETIED----FCSTCKE 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  960 HRDSTKKLEIWKVPPILLVHLKRFSYEGRWKQKlqtTVDFPLDnldlTQYVIGPkqtlKRYYLYGVSNHYG-GLDGGHYT 1038
Cdd:cd02658    203 KTTATKTTGFKTFPDYLVINMKRFQLLENWVPK---KLDVPID----VPEELGP----GKYELIAFISHKGtSVHSGHYV 271

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1174681693 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 1174681693  747 GLRNLGNTCYMNSILQCLC-NTPAMaeyfnSNYYLEDINRSNILghKGEFAEEFGVIMKALWAGLYKCISPRDfKITIGK 825
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILAlYLPKL-----DELLDDLSKELKVL--KNVIRKPEPDLNQEEALKLFTALWSSK-EHKVGW 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  826 INDQfagYDQQDSQELLLFLMDGLHEDLNKA--DNKKRYKEEENDHLDDQtaadlaWSkhkllneSIIVALFQGQF---K 900
Cdd:COG5533     73 IPPM---GSQEDAHELLGKLLDELKLDLVNSftIRIFKTTKDKKKTSTGD------WF-------DIIIELPDQTWvnnL 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  901 STVQCstchrksrTFETFMYLsLPLASTSKcslqdclrlfskeEKLTDNNKVFCRHCKAHRDStkkleiwKVPPILLVHL 980
Cdd:COG5533    137 KTLQE--------FIDNMEEL-VDDETGVK-------------AKENEELEVQAKQEYEVSFV-------KLPKILTIQL 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  981 KRFSYEGRwKQKLQTTVDfplDNLDLTqyvIGPKQTLK-----RYYLYGVSNHYGGLDGGHYTAYCKnaTKQRWYKFDDH 1055
Cdd:COG5533    188 KRFANLGG-NQKIDTEVD---EKFELP---VKHDQILNivketYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDS 258

                          330       340
                   ....*....|....*....|....
gi 1174681693 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 1174681693  747 GLRNLGNTCYMNSILQCLCNTPAMAEYfnsnyyLEDINrsnilghkgefaeefgvimkalwaglykcisprdfkitigki 826
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLIEY------LEEFL------------------------------------------ 32

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  827 ndqfagyDQQDSQELLLFLMDGLhedlnkadnkkrykeeendhlddqtaadlawskhkllnESIIVALFQGQFKSTVQCS 906
Cdd:cd02662     33 -------EQQDAHELFQVLLETL--------------------------------------EQLLKFPFDGLLASRIVCL 67

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  907 TCHRKSR-TFETFMYLSLPL---ASTSKCSLQDCLRLFSKEEKLTDnnkVFCRHCKahrdstkkLEIWKVPPILLVHLKR 982
Cdd:cd02662     68 QCGESSKvRYESFTMLSLPVpnqSSGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSR 136

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  983 FSYEGRWK-QKLQTTVDFPLDnldLTQYvigpkqtlkRYYLYGVSNHYGGLDGGHYTAY--------------------C 1041
Cdd:cd02662    137 SVFDGRGTsTKNSCKVSFPER---LPKV---------LYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreG 204

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1174681693 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 1174681693  709 DTKPVTAKVYSKVEIAR--PSAAKIRSLN--PTFGGMgaslTGLRNLGNTCYMNSILQCLCNTPAMaeyfnSNYYLEDIN 784
Cdd:cd02669     83 DIKYVLNPTYTKEQISDldRDPKLSRDLDgkPYLPGF----VGLNNIKNNDYANVIIQALSHVKPI-----RNFFLLYEN 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  785 RSNILGHKGEFAEEFGVIMKALW-AGLYKC-ISPRDFKITIGKI-NDQFAGYDQQDSQELLLFLMDGLHEDLNKadNKKR 861
Cdd:cd02669    154 YENIKDRKSELVKRLSELIRKIWnPRNFKGhVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGG--SKKP 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  862 ykeeendhlddqtaadlawskhkllNESIIVALFQG--------------QFKSTVQCSTCHRKSRTFET-FMYLS--LP 924
Cdd:cd02669    232 -------------------------NSSIIHDCFQGkvqietqkikphaeEEGSKDKFFKDSRVKKTSVSpFLLLTldLP 286

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  925 LASTSKCSLQD-CLRLFSKEEKLTDNNKVfcrHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRWKQKLQTTVDFPLDN 1003
Cdd:cd02669    287 PPPLFKDGNEEnIIPQVPLKQLLKKYDGK---TETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKN 363

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1174681693 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 1174681693  747 GLRNLGNTCYMNSILQclcntpamaEYFNSNYYLEDINRSNILGHKGEfaEEFGVIMKALWAGLYKCISPRD-FKITIGK 825
Cdd:COG5077    195 GLRNQGATCYMNSLLQ---------SLFFIAKFRKDVYGIPTDHPRGR--DSVALALQRLFYNLQTGEEPVDtTELTRSF 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  826 INDQFAGYDQQDSQELLLFLMDGLhedlnkaDNKKRYKEEENdhlddqtaadlawskhkLLNEsiivaLFQGQFKSTVQC 905
Cdd:COG5077    264 GWDSDDSFMQHDIQEFNRVLQDNL-------EKSMRGTVVEN-----------------ALNG-----IFVGKMKSYIKC 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  906 STCHRKSRTFETFMYLSLPLASTSkcSLQDCLRLFSKEEKLTDNNKVFCRHcKAHRDSTKKLEIWKVPPILLVHLKRFSY 985
Cdd:COG5077    315 VNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEY 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  986 EGRWKQ--KLQTTVDFPlDNLDLTQYVigPKQTLKR------YYLYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHEV 1057
Cdd:COG5077    392 DFERDMmvKINDRYEFP-LEIDLLPFL--DRDADKSensdavYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRV 468


                   ....*...
gi 1174681693 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 1174681693  748 LRNLGNTCYMNSILQCLCntpamaeyfnsnyyledinrsnilghkgefaeefgvimkalwaglykcisprdfkiTIGKIN 827
Cdd:cd02673      2 LVNTGNSCYFNSTMQALS--------------------------------------------------------SIGKIN 25

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  828 DQFAGYDQQDSQELLLFL---MDGLHEdlNKADNKKRYkEEENDHLDDQTAadlawskHKLLNESIIValfqgqfkstvq 904
Cdd:cd02673     26 TEFDNDDQQDAHEFLLTLleaIDDIMQ--VNRTNVPPS-NIEIKRLNPLEA-------FKYTIESSYV------------ 83

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  905 CSTCHRKSRTFETFMYLSLPLASTSKCSLQDclrLFSKEEKLTDNNKVfCRHCKaHRDSTKKLEIWKVPPILLVHLKRFs 984
Cdd:cd02673     84 CIGCSFEENVSDVGNFLDVSMIDNKLDIDEL---LISNFKTWSPIEKD-CSSCK-CESAISSERIMTFPECLSINLKRY- 157

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  985 yegrwkqKLQT-TVDFPLDNLDLTQYVIGpkqTLKRYYLYGVSNHYG-GLDGGHYTAYCKNATK-QRWYKFDDHEVSEIS 1061
Cdd:cd02673    158 -------KLRIaTSDYLKKNEEIMKKYCG---TDAKYSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIRPVS 227

                          330
                   ....*....|....*..
gi 1174681693 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 1174681693  835 QQDSQELLLFLMDGLHEDLNKADNKKRYKEEendhlddqtaadlawSKHKLlnesiiVALFQGQFkSTVqcsTCHRKSRT 914
Cdd:cd02665     22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEK---------------SKNPM------VQLFYGTF-LTE---GVLEGKPF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  915 FETFMYLSLPLASTSKCSLQDCLrlfskeEKLTDNNKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEGRWKQKLQ 994
Cdd:cd02665     77 CNCETFGQYPLQVNGYGNLHECL------EAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPEKIH 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  995 TTVDFPldnldltqyvigpkQTLKR--YYLYGVSNHYGGLDGGHYTAYCKNATKQRWYKFDDHEVSEISTSSVKSSA--- 1069
Cdd:cd02665    151 DKLEFP--------------QIIQQvpYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfgg 216

                          250
                   ....*....|.
gi 1174681693 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 1174681693  872 DQTAADLAWSKHKLL-NESIIVALFQGQFKSTVQCSTC-HRKSRTFETFM----YLSLPLASTSKCSLQD---CLRLFSK 942
Cdd:pfam13423  108 DQLSSEENSTPPNPSpAESPLEQLFGIDAETTIRCSNCgHESVRESSTHVldliYPRKPSSNNKKPPNQTfssILKSSLE 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  943 EEKLTdnnKVFCRHCKAHRDSTKKLEIWKVPPILLVHLKRFSYEgrWKQKLQTTVDFPLD-NLDLTQYVIGPKQTLKrYY 1021
Cdd:pfam13423  188 RETTT---KAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPEiGLTLSDDLQGDNEIVK-YE 261

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1174681693 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 1174681693  882 KHKLLNE-----SIIVALFQGQFKSTVQC-----STCHRKSRTFETFMY-LSLPLASTSKCSLQDCLRLFSKEEKLTDNN 950
Cdd:cd02672     54 ESCLLCElgylfSTLIQNFTRFLLETISQdqlgtPFSCGTSRNSVSLLYtLSLPLGSTKTSKESTFLQLLKRSLDLEKVT 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  951 KVFCRHCKAHRDSTKKLEIWKVPPILL----VHLKRFSYEGRWKQ-------KLQTTVDFPLDNLDLTQYVIGPKQTLKr 1019
Cdd:cd02672    134 KAWCDTCCKYQPLEQTTSIRHLPDILLlvlvINLSVTNGEFDDINvvlpsgkVMQNKVSPKAIDHDKLVKNRGQESIYK- 212

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1174681693 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 1174681693  746 TGLRNLGNTCYMNSILQCL-CNTPA-----MAEYFNSNYYLEDINRSNILGHKGEFAE-----EFGVIMKALWAGLYK-- 812
Cdd:cd02666      2 AGLDNIGNTCYLNSLLQYFfTIKPLrdlvlNFDESKAELASDYPTERRIGGREVSRSElqrsnQFVYELRSLFNDLIHsn 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  813 --CISPRDfkitigkiNDQFAGYDQQDSQELLLFLMDglheDLNKADNKKRYKEEENDHLDDQTAADLawskhkllnesi 890
Cdd:cd02666     82 trSVTPSK--------ELAYLALRQQDVTECIDNVLF----QLEVALEPISNAFAGPDTEDDKEQSDL------------ 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  891 IVALFQGQFK-STVQCSTCHRKSRT--FETFMYLSLPLAST--------SKCSLQDCL----------------RLFSKE 943
Cdd:cd02666    138 IKRLFSGKTKqQLVPESMGNQPSVRtkTERFLSLLVDVGKKgreivvllEPKDLYDALdryfdydsltklpqrsQVQAQL 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  944 EKLTDNNKVFCRHCKAHRDSTKKLEIWK--VPPILLVHLKRFSYEGRWKQKLQTTVDfpldnlDLTQYVigpkqtlkrYY 1021
Cdd:cd02666    218 AQPLQRELISMDRYELPSSIDDIDELIReaIQSESSLVRQAQNELAELKHEIEKQFD------DLKSYG---------YR 282

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1174681693 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 1174681693  971 KVPPILLVHLKRFSYEGRWKQKLQTTVDfPLDNLDLTQYVIG-PKQTLKRYYLYGVSN---------------------H 1028
Cdd:cd02670     97 KAPSCLIICLKRYGKTEGKAQKMFKKIL-IPDEIDIPDFVADdPRACSKCQLECRVCYddkdfsptcgkfklslcsavcH 175

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1174681693 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 1174681693  197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS-PGITVNQIEAKLPSMSKDhwmkrgfvDYIILLDWFSSVSDLklgtTL 275
Cdd:pfam00581    7 VLIDVRPPEEYAKGHI----PGAVNVPLSSLSlPPLPLLELLEKLLELLKD--------KPIVVYCNSGNRAAA----AA 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 1174681693  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 1174681693  358 QKPPAPAVANGVAPAEPPTSKTSviaDKLPDTHDSPvrspastgldlnkKSPAPNQSPATAKAFPQFDRTKKPVRDEpKP 437
Cdd:PTZ00449   589 KDPEEPKKPKRPRSAQRPTRPKS---PKLPELLDIP-------------KSPKRPESPKSPKRPPPPQRPSSPERPE-GP 651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  438 KEDGSTKdstqngpvvPDRSVKPPLIPSTslsKEEQNQIHLEAVAVMEKAKQEQEKRMQERRLEEEKREKELKDRLEREE 517
Cdd:PTZ00449   652 KIIKSPK---------PPKSPKPPFDPKF---KEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPR 719

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174681693  518 SERRSKQEEEKRHLErkRLERQKAEEEEDKENKTWDERER-RGKEPNADTpsksmsldsPVPNHLVSEIKREPL---TRA 593
Cdd:PTZ00449   720 PLPPKLPRDEEFPFE--PIGDPDAEQPDDIEFFTPPEEERtFFHETPADT---------PLPDILAEEFKEEDIhaeTGE 788

                          250       260
                   ....*....|....*....|....*..
gi 1174681693  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 1174681693   197 VVMDARSLKDYEESHIqvpaQTCISVPEEAIS--PGITVNQIEAKLPSMSkdhwmKRGFVDYIILLDWfssvSDLKLGTT 274
Cdd:smart00450    6 VLLDVRSPEEYEGGHI----PGAVNIPLSELLdrRGELDILEFEELLKRL-----GLDKDKPVVVYCR----SGNRSAKA 72

                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 1174681693   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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