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Conserved domains on  [gi|74138825|dbj|BAE27219|]
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unnamed protein product [Mus musculus]

Protein Classification

ubiquitin specific protease( domain architecture ID 12950362)

ubiquitin specific protease (such as USP19) regulates cell cycle progression and is involved in the cellular response to different types of stress, including the unfolded protein response (UPR), hypoxia and muscle atrophy.

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
535-1257 4.21e-119

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: 391.94  E-value: 4.21e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  535 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHQAFQPSKLKA 614
Cdd:COG5560  262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  615 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 691
Cdd:COG5560  342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  692 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpifyfarepHSKPIKFLVSVSKENSSASEVLDSLSqsvhvkpenlr 771
Cdd:COG5560  422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVFPESGRRQPLKIELDASST----------- 479
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  772 lAEVIKNRfhrvflpshsLDAVSptDVLLCFELLSPELAKERVVVlEVQQRPQVPSIPISKCAACQRKQQSEEEklkrct 851
Cdd:COG5560  480 -IRGLKKL----------VDAEY--GKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG------ 539
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  852 rcyrVGYCnqfcqKTHWPDHKGLCRPENIGYPFL---VSVPASRLTyarlaQLLEGYARYSVSVFQPPfqpgrmalesqs 928
Cdd:COG5560  540 ----IEVP-----VVHLRIEKGYKSKRLFGDPFLqlnVLIKASIYD-----KLVKEFEELLVLVEMKK------------ 593
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  929 pgctTLLSTSSLEAGDSEREPIQPSELQLVTpvaEGDTgahrvwppadrgpvPSTSGLSSEmlasgpiegcpllagERVS 1008
Cdd:COG5560  594 ----TDVDLVSEQVRLLREESSPSSWLKLET---EIDT--------------KREEQVEEE---------------GQMN 637
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1009 RPEAAVPGYQHSSESVNthtpqfFIYKIDASNREQRLEDKGETPlelgddcslalvwrnnerlqefvlvaskelecaedp 1088
Cdd:COG5560  638 FNDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------------ 675
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1089 gsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDKINDLV 1167
Cdd:COG5560  676 ------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDKIDDLV 741
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1168 EFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQVVTRY 1247
Cdd:COG5560  742 EYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPEDSVTSS 813
                        730
                 ....*....|
gi 74138825 1248 AYVLFYRRRN 1257
Cdd:COG5560  814 AYVLFYRRKS 823
USP19_linker pfam16602
Linker region of USP19 deubiquitinase; This region is generally located between a CS domain ...
415-537 5.51e-61

Linker region of USP19 deubiquitinase; This region is generally located between a CS domain pfam04969 and the enzymatic UCH domain pfam00582 of USP19 deubiquitinases. This region is predicted to be natively unstructured. Its precise functional role is not known.


:

Pssm-ID: 465191  Cd Length: 121  Bit Score: 203.99  E-value: 5.51e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825    415 RQSQRWGGLEAPATRGAVGGAKVAVPTGPTPLDSTPPGGGPHPLTGQEEARAVEKEKPKARSEDSGLDGVVARTPLEHVA 494
Cdd:pfam16602    1 RHSQRWGGLEAPATQGAVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 74138825    495 PKPDPHLASPKPTCMVPPMPHSPVSGDSVeeDEEEEKKVCLPG 537
Cdd:pfam16602   81 IKQEPLLTSPKPTCMVPPMTHSPVSSESV--EEEEEKKVCLPG 121
p23_CS_SGT1_like cd06466
p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 ...
328-424 3.60e-20

p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 allele of Skp1). Sgt1 interacts with multiple protein complexes and has the features of a cochaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. ScSgt1 is needed for the G1/S and G2/M cell-cycle transitions, and for assembly of the core kinetochore complex (CBF3) via activation of Ctf13, the F-box protein. Binding of Hsp82 (a yeast Hsp90 homologue) to ScSgt1, promotes the binding of Sgt1 to Skp1 and of Skp1 to Ctf13. Some proteins in this group have an SGT1-specific (SGS) domain at the extreme C-terminus. The ScSgt1-SGS domain binds adenylate cyclase. The hSgt1-SGS domain interacts with some S100 family proteins, and studies suggest that the interaction of hSgt1 with Hsp90 and Hsp70 may be regulated by S100A6 in a Ca2+ dependent fashion. This group also includes the p23_like domains of Melusin and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). Melusin is a vertebrate protein which interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


:

Pssm-ID: 107223  Cd Length: 84  Bit Score: 86.10  E-value: 3.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  328 DSYEKgPDSVVVHVYVKEIRRDSSRVLFREQDFTLIFQTRDGNflrlhpgcgphtIFRWQVKLRNLIEPEQCTFCFTASR 407
Cdd:cd06466    1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                         90
                 ....*....|....*..
gi 74138825  408 IDICLRKRQSQRWGGLE 424
Cdd:cd06466   68 VEITLKKAEPGSWPSLE 84
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
58-140 5.43e-05

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


:

Pssm-ID: 107220  Cd Length: 84  Bit Score: 43.04  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825   58 WRQSADEVIVKLRVGTGPVRLEDVDAAFTDTDCVVRLPDGR--QWGGVFFAEIQSSCTKVQArKGGLLQLVLPKKVPLLT 135
Cdd:cd06463    1 WYQTLDEVTITIPLKDVTKKDVKVEFTPKSLTVSVKGGGGKeyLLEGELFGPIDPEESKWTV-EDRKIEITLKKKEPGEW 79

                 ....*
gi 74138825  136 WPSLL 140
Cdd:cd06463   80 WPRLE 84
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
535-1257 4.21e-119

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 391.94  E-value: 4.21e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  535 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHQAFQPSKLKA 614
Cdd:COG5560  262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  615 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 691
Cdd:COG5560  342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  692 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpifyfarepHSKPIKFLVSVSKENSSASEVLDSLSqsvhvkpenlr 771
Cdd:COG5560  422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVFPESGRRQPLKIELDASST----------- 479
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  772 lAEVIKNRfhrvflpshsLDAVSptDVLLCFELLSPELAKERVVVlEVQQRPQVPSIPISKCAACQRKQQSEEEklkrct 851
Cdd:COG5560  480 -IRGLKKL----------VDAEY--GKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG------ 539
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  852 rcyrVGYCnqfcqKTHWPDHKGLCRPENIGYPFL---VSVPASRLTyarlaQLLEGYARYSVSVFQPPfqpgrmalesqs 928
Cdd:COG5560  540 ----IEVP-----VVHLRIEKGYKSKRLFGDPFLqlnVLIKASIYD-----KLVKEFEELLVLVEMKK------------ 593
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  929 pgctTLLSTSSLEAGDSEREPIQPSELQLVTpvaEGDTgahrvwppadrgpvPSTSGLSSEmlasgpiegcpllagERVS 1008
Cdd:COG5560  594 ----TDVDLVSEQVRLLREESSPSSWLKLET---EIDT--------------KREEQVEEE---------------GQMN 637
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1009 RPEAAVPGYQHSSESVNthtpqfFIYKIDASNREQRLEDKGETPlelgddcslalvwrnnerlqefvlvaskelecaedp 1088
Cdd:COG5560  638 FNDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------------ 675
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1089 gsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDKINDLV 1167
Cdd:COG5560  676 ------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDKIDDLV 741
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1168 EFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQVVTRY 1247
Cdd:COG5560  742 EYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPEDSVTSS 813
                        730
                 ....*....|
gi 74138825 1248 AYVLFYRRRN 1257
Cdd:COG5560  814 AYVLFYRRKS 823
USP19_linker pfam16602
Linker region of USP19 deubiquitinase; This region is generally located between a CS domain ...
415-537 5.51e-61

Linker region of USP19 deubiquitinase; This region is generally located between a CS domain pfam04969 and the enzymatic UCH domain pfam00582 of USP19 deubiquitinases. This region is predicted to be natively unstructured. Its precise functional role is not known.


Pssm-ID: 465191  Cd Length: 121  Bit Score: 203.99  E-value: 5.51e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825    415 RQSQRWGGLEAPATRGAVGGAKVAVPTGPTPLDSTPPGGGPHPLTGQEEARAVEKEKPKARSEDSGLDGVVARTPLEHVA 494
Cdd:pfam16602    1 RHSQRWGGLEAPATQGAVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 74138825    495 PKPDPHLASPKPTCMVPPMPHSPVSGDSVeeDEEEEKKVCLPG 537
Cdd:pfam16602   81 IKQEPLLTSPKPTCMVPPMTHSPVSSESV--EEEEEKKVCLPG 121
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1097-1254 5.85e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 194.04  E-value: 5.85e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1097 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFrSFIWRDKINDLVEFPVRNLDL 1176
Cdd:cd02674   81 APKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSF-SRGSTRKLTTPVTFPLNDLDL 159
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74138825 1177 SKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvGWRLFDDSTVTTVDESQVVTRYAYVLFYR 1254
Cdd:cd02674  160 TPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETN-------DWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
539-726 1.50e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 175.71  E-value: 1.50e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825    539 TGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTggrLAIGFAVLLRALWKGTHQ-AFQPSKLKAIVA 617
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNSKSsSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825    618 SKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQGQYKSKLV 697
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180
                   ....*....|....*....|....*....
gi 74138825    698 CPVCAKVSITFDPFLYLPVPLPQKQKVLP 726
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELK 160
p23_CS_SGT1_like cd06466
p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 ...
328-424 3.60e-20

p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 allele of Skp1). Sgt1 interacts with multiple protein complexes and has the features of a cochaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. ScSgt1 is needed for the G1/S and G2/M cell-cycle transitions, and for assembly of the core kinetochore complex (CBF3) via activation of Ctf13, the F-box protein. Binding of Hsp82 (a yeast Hsp90 homologue) to ScSgt1, promotes the binding of Sgt1 to Skp1 and of Skp1 to Ctf13. Some proteins in this group have an SGT1-specific (SGS) domain at the extreme C-terminus. The ScSgt1-SGS domain binds adenylate cyclase. The hSgt1-SGS domain interacts with some S100 family proteins, and studies suggest that the interaction of hSgt1 with Hsp90 and Hsp70 may be regulated by S100A6 in a Ca2+ dependent fashion. This group also includes the p23_like domains of Melusin and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). Melusin is a vertebrate protein which interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107223  Cd Length: 84  Bit Score: 86.10  E-value: 3.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  328 DSYEKgPDSVVVHVYVKEIRRDSSRVLFREQDFTLIFQTRDGNflrlhpgcgphtIFRWQVKLRNLIEPEQCTFCFTASR 407
Cdd:cd06466    1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                         90
                 ....*....|....*..
gi 74138825  408 IDICLRKRQSQRWGGLE 424
Cdd:cd06466   68 VEITLKKAEPGSWPSLE 84
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
325-414 2.28e-06

CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2.


Pssm-ID: 461503  Cd Length: 76  Bit Score: 46.48  E-value: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825    325 VKNDSYEKgPDSVVVHVYVKEIRRDSSRVLFReqdftliFQTRDgnfLRLHPGCGPHTIfrwQVKLRNLIEPEQCTFCFT 404
Cdd:pfam04969    1 PRYDWYQT-LDEVTITIPVKGAGIKKKDVKVN-------IKPRS---LKVKIKGGYELI---DGELFHPIDPEESSWTIE 66
                           90
                   ....*....|
gi 74138825    405 ASRIDICLRK 414
Cdd:pfam04969   67 GKKVEITLKK 76
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
289-444 1.61e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 48.63  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825   289 RDPEPEQEDQVKEEMALGADPTALVEEPESMVNLAFV-----KNDSYEKgPDSVVVHVYVKEIRRDSSRVLFREQDFTLI 363
Cdd:PLN03088  116 KIAEEEKDLVQPVPSDLPSSVTAPPVEEADATPVVPPskpkyRHEFYQK-PEEVVVTVFAKGVPAENVNVDFGEQILSVV 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825   364 FQTrdgnflrlhPGCGPhtiFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLE-----APATRGAVGGAKVA 438
Cdd:PLN03088  195 IEV---------PGEDA---YHLQPRLFGKIIPDKCKYEVLSTKIEIRLAKAEPITWASLEygkgpAVLPKPNVSSEVSQ 262

                  ....*.
gi 74138825   439 VPTGPT 444
Cdd:PLN03088  263 RPAYPS 268
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
58-140 5.43e-05

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107220  Cd Length: 84  Bit Score: 43.04  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825   58 WRQSADEVIVKLRVGTGPVRLEDVDAAFTDTDCVVRLPDGR--QWGGVFFAEIQSSCTKVQArKGGLLQLVLPKKVPLLT 135
Cdd:cd06463    1 WYQTLDEVTITIPLKDVTKKDVKVEFTPKSLTVSVKGGGGKeyLLEGELFGPIDPEESKWTV-EDRKIEITLKKKEPGEW 79

                 ....*
gi 74138825  136 WPSLL 140
Cdd:cd06463   80 WPRLE 84
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
535-1257 4.21e-119

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 391.94  E-value: 4.21e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  535 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHQAFQPSKLKA 614
Cdd:COG5560  262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  615 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 691
Cdd:COG5560  342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  692 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpifyfarepHSKPIKFLVSVSKENSSASEVLDSLSqsvhvkpenlr 771
Cdd:COG5560  422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVFPESGRRQPLKIELDASST----------- 479
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  772 lAEVIKNRfhrvflpshsLDAVSptDVLLCFELLSPELAKERVVVlEVQQRPQVPSIPISKCAACQRKQQSEEEklkrct 851
Cdd:COG5560  480 -IRGLKKL----------VDAEY--GKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG------ 539
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  852 rcyrVGYCnqfcqKTHWPDHKGLCRPENIGYPFL---VSVPASRLTyarlaQLLEGYARYSVSVFQPPfqpgrmalesqs 928
Cdd:COG5560  540 ----IEVP-----VVHLRIEKGYKSKRLFGDPFLqlnVLIKASIYD-----KLVKEFEELLVLVEMKK------------ 593
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  929 pgctTLLSTSSLEAGDSEREPIQPSELQLVTpvaEGDTgahrvwppadrgpvPSTSGLSSEmlasgpiegcpllagERVS 1008
Cdd:COG5560  594 ----TDVDLVSEQVRLLREESSPSSWLKLET---EIDT--------------KREEQVEEE---------------GQMN 637
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1009 RPEAAVPGYQHSSESVNthtpqfFIYKIDASNREQRLEDKGETPlelgddcslalvwrnnerlqefvlvaskelecaedp 1088
Cdd:COG5560  638 FNDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------------ 675
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1089 gsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDKINDLV 1167
Cdd:COG5560  676 ------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDKIDDLV 741
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1168 EFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQVVTRY 1247
Cdd:COG5560  742 EYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPEDSVTSS 813
                        730
                 ....*....|
gi 74138825 1248 AYVLFYRRRN 1257
Cdd:COG5560  814 AYVLFYRRKS 823
USP19_linker pfam16602
Linker region of USP19 deubiquitinase; This region is generally located between a CS domain ...
415-537 5.51e-61

Linker region of USP19 deubiquitinase; This region is generally located between a CS domain pfam04969 and the enzymatic UCH domain pfam00582 of USP19 deubiquitinases. This region is predicted to be natively unstructured. Its precise functional role is not known.


Pssm-ID: 465191  Cd Length: 121  Bit Score: 203.99  E-value: 5.51e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825    415 RQSQRWGGLEAPATRGAVGGAKVAVPTGPTPLDSTPPGGGPHPLTGQEEARAVEKEKPKARSEDSGLDGVVARTPLEHVA 494
Cdd:pfam16602    1 RHSQRWGGLEAPATQGAVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 74138825    495 PKPDPHLASPKPTCMVPPMPHSPVSGDSVeeDEEEEKKVCLPG 537
Cdd:pfam16602   81 IKQEPLLTSPKPTCMVPPMTHSPVSSESV--EEEEEKKVCLPG 121
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1097-1254 5.85e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 194.04  E-value: 5.85e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1097 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFrSFIWRDKINDLVEFPVRNLDL 1176
Cdd:cd02674   81 APKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSF-SRGSTRKLTTPVTFPLNDLDL 159
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74138825 1177 SKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvGWRLFDDSTVTTVDESQVVTRYAYVLFYR 1254
Cdd:cd02674  160 TPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETN-------DWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
539-726 1.50e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 175.71  E-value: 1.50e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825    539 TGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTggrLAIGFAVLLRALWKGTHQ-AFQPSKLKAIVA 617
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNSKSsSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825    618 SKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQGQYKSKLV 697
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180
                   ....*....|....*....|....*....
gi 74138825    698 CPVCAKVSITFDPFLYLPVPLPQKQKVLP 726
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELK 160
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1102-1253 1.44e-46

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 169.93  E-value: 1.44e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825   1102 LDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWrDKINDLVEFPvRNLDLSKFCI 1181
Cdd:pfam00443  164 LQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTW-EKLNTEVEFP-LELDLSRYLA 241
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74138825   1182 G---QKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSsqrsdvgWRLFDDSTVTTVDES-QVVTRYAYVLFY 1253
Cdd:pfam00443  242 EelkPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNR-------WYKFDDEKVTEVDEEtAVLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1101-1254 1.79e-40

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: 150.33  E-value: 1.79e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1101 TLDQCLNLFTRPEVLAPEEAWYCPqCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPvRNLDLSKFC 1180
Cdd:cd02257  100 SLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFP-LELDLSPYL 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1181 IGQKEEQLPS-----YDLYAVINHYGGMI-GGHYTACARlpnDRSSQRsdvgWRLFDDSTVTTVDESQVVTRY-----AY 1249
Cdd:cd02257  178 SEGEKDSDSDngsykYELVAVVVHSGTSAdSGHYVAYVK---DPSDGK----WYKFNDDKVTEVSEEEVLEFGslsssAY 250

                 ....*
gi 74138825 1250 VLFYR 1254
Cdd:cd02257  251 ILFYE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1089-1253 2.54e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 137.89  E-value: 2.54e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1089 GSAGEAARAGHFTLDQCLNLFTRPEVLAPEeAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVE 1168
Cdd:cd02660  165 WALGESGVSGTPTLSDCLDRFTRPEKLGDF-AYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQ 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1169 FPVRnLDLSKFCIGQKEEQLPS--------YDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvgWRLFDDSTVTTVDE 1240
Cdd:cd02660  244 FPLE-LNMTPYTSSSIGDTQDSnsldpdytYDLFAVVVHKGTLDTGHYTAYCRQGDGQ--------WFKFDDAMITRVSE 314
                        170
                 ....*....|...
gi 74138825 1241 SQVVTRYAYVLFY 1253
Cdd:cd02660  315 EEVLKSQAYLLFY 327
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1101-1253 2.93e-33

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: 131.24  E-value: 2.93e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1101 TLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFsfrSFIWRDKINDLVEFPVRnLDLSKFc 1180
Cdd:cd02661  163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF---SNFRGGKINKQISFPET-LDLSPY- 237
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74138825 1181 IGQKEEQLPSYDLYAVINHYGGMI-GGHYTACARLPNDRssqrsdvgWRLFDDSTVTTVDESQVVTRYAYVLFY 1253
Cdd:cd02661  238 MSQPNDGPLKYKLYAVLVHSGFSPhSGHYYCYVKSSNGK--------WYNMDDSKVSPVSIETVLSQKAYILFY 303
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1100-1254 4.60e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 118.26  E-value: 4.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1100 FTLDQCLNLFTRPEVLAPEEAWYCPQCKqhrEASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRnLDLSKF 1179
Cdd:cd02667  111 CSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEI-LDLAPF 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1180 C----IGQKEEQLPSYDLYAVINHYGGMIGGHYTACARL--PNDRSS-------QRSDVG-----WRLFDDSTVTTVDES 1241
Cdd:cd02667  187 CdpkcNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVrpPQQRLSdltkskpAADEAGpgsgqWYYISDSDVREVSLE 266
                        170
                 ....*....|...
gi 74138825 1242 QVVTRYAYVLFYR 1254
Cdd:cd02667  267 EVLKSEAYLLFYE 279
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
540-726 4.75e-26

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 108.14  E-value: 4.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  540 GLVNLGNTCFMNSVIQSLSNTrelrdffhdrsfeaeinynnplgtggrlaigfavllralwkgthqafqpsklkaivask 619
Cdd:cd02674    1 GLRNLGNTCYMNSILQCLSAD----------------------------------------------------------- 21
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  620 asqftgyaQHDAQEFMAFLLDGLHedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrndSFIVDLFQGQYKSKLVCP 699
Cdd:cd02674   22 --------QQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                        170       180
                 ....*....|....*....|....*..
gi 74138825  700 VCAKVSITFDPFLYLPVPLPQKQKVLP 726
Cdd:cd02674   56 TCGKTSTTFEPFTYLSLPIPSGSGDAP 82
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1106-1257 8.57e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 107.34  E-value: 8.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1106 LNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRsfiW----RDKINDLVEFPVRnLDLSKFCI 1181
Cdd:cd02659  157 LDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFD---FetmmRIKINDRFEFPLE-LDMEPYTE 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1182 ----------GQKEEQLPSYDLYAVINHYGGMIGGHYTACARlpndrssQRSDVGWRLFDDSTVTTVDESQVVTRY---- 1247
Cdd:cd02659  233 kglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYSYIK-------DRDDGKWYKFNDDVVTPFDPNDAEEECfgge 305
                        170       180
                 ....*....|....*....|....*...
gi 74138825 1248 ------------------AYVLFYRRRN 1257
Cdd:cd02659  306 etqktydsgprafkrttnAYMLFYERKS 333
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1099-1253 5.93e-22

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: 98.15  E-value: 5.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1099 HFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWR-DKINDLVEFPvrnLDLS 1177
Cdd:cd02663  146 NTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFP---LELR 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1178 KF-CIGQKEEQLPSYDLYAVINHYGGMIG-GHYTacarlpndrSSQRSDVGWRLFDDSTVTTVDESQVVTRY-------- 1247
Cdd:cd02663  223 LFnTTDDAENPDRLYELVAVVVHIGGGPNhGHYV---------SIVKSHGGWLLFDDETVEKIDENAVEEFFgdspnqat 293

                 ....*.
gi 74138825 1248 AYVLFY 1253
Cdd:cd02663  294 AYVLFY 299
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
540-723 2.41e-21

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: 95.24  E-value: 2.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  540 GLVNLGNTCFMNSVIQSLSNTrelrdffhdrsfeaeinynnplgtggrlaigfavllralwkgthqafqpsklkaivask 619
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  620 asqftgyaQHDAQEFMAFLLDGLHEDLNRIQNKpytetvdsdgrpdevvaeeawQRHKMRNDSFIVDLFQGQYKSKLVCP 699
Cdd:cd02257   22 --------QQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                        170       180
                 ....*....|....*....|....
gi 74138825  700 VCAKVSITFDPFLYLPVPLPQKQK 723
Cdd:cd02257   73 ECGHESVSTEPELFLSLPLPVKGL 96
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
539-716 5.12e-21

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 95.42  E-value: 5.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  539 TGLVNLGNTCFMNSVIQSLSNTRELRDFFhdRSFEAEINYNNPlgtggrlaiGFAVLL-------RALW---KGTHQAFQ 608
Cdd:cd02661    2 AGLQNLGNTCFLNSVLQCLTHTPPLANYL--LSREHSKDCCNE---------GFCMMCaleahveRALAssgPGSAPRIF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  609 PSKLKAIvaskASQFTGYAQHDAQEFMAFLLDGLHED-LNRiqNKPYTETVDSDgrpdevvaeeawqrhkmRNDSFIVDL 687
Cdd:cd02661   71 SSNLKQI----SKHFRIGRQEDAHEFLRYLLDAMQKAcLDR--FKKLKAVDPSS-----------------QETTLVQQI 127
                        170       180
                 ....*....|....*....|....*....
gi 74138825  688 FQGQYKSKLVCPVCAKVSITFDPFLYLPV 716
Cdd:cd02661  128 FGGYLRSQVKCLNCKHVSNTYDPFLDLSL 156
p23_CS_SGT1_like cd06466
p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 ...
328-424 3.60e-20

p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 allele of Skp1). Sgt1 interacts with multiple protein complexes and has the features of a cochaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. ScSgt1 is needed for the G1/S and G2/M cell-cycle transitions, and for assembly of the core kinetochore complex (CBF3) via activation of Ctf13, the F-box protein. Binding of Hsp82 (a yeast Hsp90 homologue) to ScSgt1, promotes the binding of Sgt1 to Skp1 and of Skp1 to Ctf13. Some proteins in this group have an SGT1-specific (SGS) domain at the extreme C-terminus. The ScSgt1-SGS domain binds adenylate cyclase. The hSgt1-SGS domain interacts with some S100 family proteins, and studies suggest that the interaction of hSgt1 with Hsp90 and Hsp70 may be regulated by S100A6 in a Ca2+ dependent fashion. This group also includes the p23_like domains of Melusin and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). Melusin is a vertebrate protein which interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107223  Cd Length: 84  Bit Score: 86.10  E-value: 3.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  328 DSYEKgPDSVVVHVYVKEIRRDSSRVLFREQDFTLIFQTRDGNflrlhpgcgphtIFRWQVKLRNLIEPEQCTFCFTASR 407
Cdd:cd06466    1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                         90
                 ....*....|....*..
gi 74138825  408 IDICLRKRQSQRWGGLE 424
Cdd:cd06466   68 VEITLKKAEPGSWPSLE 84
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
540-721 4.22e-20

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 93.21  E-value: 4.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  540 GLVNLGNTCFMNSVIQSLSNTRELRDFFHdrsfeAEINYNNPLGTGGRLAIGFAV--LLRALW-KGTHQAFQPSKLKAIV 616
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFL-----SDRHSCTCLSCSPNSCLSCAMdeIFQEFYySGDRSPYGPINLLYLS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  617 ASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYtetvdsdgrpdevvaeeawqrHKMRNDSFIVDLFQGQYKSKL 696
Cdd:cd02660   77 WKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEAN---------------------DESHCNCIIHQTFSGSLQSSV 135
                        170       180
                 ....*....|....*....|....*
gi 74138825  697 VCPVCAKVSITFDPFLYLPVPLPQK 721
Cdd:cd02660  136 TCQRCGGVSTTVDPFLDLSLDIPNK 160
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1097-1254 3.05e-19

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: 90.56  E-value: 3.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1097 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFIWRDKINDLVEFPvRNLD 1175
Cdd:cd02668  153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdRKTGAKKKLNASISFP-EILD 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1176 LSKFCIGQKeEQLPSYDLYAVINHYG-GMIGGHYTAcarlpNDRSSQRSDvgWRLFDDSTVTTVDESQV----------- 1243
Cdd:cd02668  232 MGEYLAESD-EGSYVYELSGVLIHQGvSAYSGHYIA-----HIKDEQTGE--WYKFNDEDVEEMPGKPLklgnsedpakp 303
                        170       180
                 ....*....|....*....|.
gi 74138825 1244 ----------VTRYAYVLFYR 1254
Cdd:cd02668  304 rkseikkgthSSRTAYMLVYK 324
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1106-1254 2.00e-16

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: 82.15  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1106 LNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFIWRDK------INDLVEFPVRNLDLSK 1178
Cdd:cd02664  140 LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYdQKTHVREKimdnvsINEVLSLPVRVESKSS 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1179 FCIGQKEE-----------QLPSYDLYAVINHYG-GMIGGHYTACAR-------------LPNDRSSQRSDVGWRLFDDS 1233
Cdd:cd02664  220 ESPLEKKEeesgddgelvtRQVHYRLYAVVVHSGySSESGHYFTYARdqtdadstgqecpEPKDAEENDESKNWYLFNDS 299
                        170       180
                 ....*....|....*....|....*...
gi 74138825 1234 TVTTVD--ESQVVTRY-----AYVLFYR 1254
Cdd:cd02664  300 RVTFSSfeSVQNVTSRfpkdtPYILFYE 327
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
540-725 4.48e-16

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: 80.12  E-value: 4.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  540 GLVNLGNTCFMNSVIQSLSNTRELRDFFHDRsfeaeinynnplgtggrlaigfavllralwkgthqafqPSKLKAIVASK 619
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  620 ASQFTGYAQHDAQEFMAFLLDGLhedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrnDSFIVDLFQGQYKSKLVCP 699
Cdd:cd02667   43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84
                        170       180
                 ....*....|....*....|....*.
gi 74138825  700 VCAKVSITFDPFLYLPVPLPQKQKVL 725
Cdd:cd02667   85 SCGTVSLVYEPFLDLSLPRSDEIKSE 110
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
540-733 9.90e-16

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: 79.84  E-value: 9.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  540 GLVNLGNTCFMNSVIQSLsntrelrdfFHDRSFEAEINYNNPLGTGGRLAIGFA-VLLRALWKGTHQAFQPSKLKAIVAS 618
Cdd:cd02664    1 GLINLGNTCYMNSVLQAL---------FMAKDFRRQVLSLNLPRLGDSQSVMKKlQLLQAHLMHTQRRAEAPPDYFLEAS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  619 KASQFTGYAQHDAQEFMAFLLDGLHedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrndSFIVDLFQGQYKSKLVC 698
Cdd:cd02664   72 RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTIRC 113
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 74138825  699 PVCAKVSITFDPFLYLPVPLPQKQKVLPiFYFARE 733
Cdd:cd02664  114 LNCNSTSARTERFRDLDLSFPSVQDLLN-YFLSPE 147
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1069-1254 5.38e-15

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: 78.01  E-value: 5.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1069 ERLQEF----VLVASKELECAEDPGSAGEAARAGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNV 1144
Cdd:cd02671  145 ERREDFqdisVPVQESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEV 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1145 LIVQLKRFSFRSFIWR-----DKINDLVEFPvrnLDLSKFCIGQKeEQLPSYDLYAVINHYGGMIG-GHYTACARlpndr 1218
Cdd:cd02671  225 ITIHLKCFAANGSEFDcygglSKVNTPLLTP---LKLSLEEWSTK-PKNDVYRLFAVVMHSGATISsGHYTAYVR----- 295
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 74138825 1219 ssqrsdvgWRLFDDSTVTTVDE---------SQVVTRYAYVLFYR 1254
Cdd:cd02671  296 --------WLLFDDSEVKVTEEkdflealspNTSSTSTPYLLFYK 332
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
535-728 5.51e-14

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: 75.82  E-value: 5.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  535 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFhdrsfeaeINYNNPLGTGGR---LAIGFAVLLRALWkgTHQAFQ--- 608
Cdd:cd02669  116 LPGFVGLNNIKNNDYANVIIQALSHVKPIRNFF--------LLYENYENIKDRkseLVKRLSELIRKIW--NPRNFKghv 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  609 -PSK-LKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiQNKPYTETVDS--DG------RPDEVVAEEAWQRHKM 678
Cdd:cd02669  186 sPHElLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGG-SKKPNSSIIHDcfQGkvqietQKIKPHAEEEGSKDKF 264
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 74138825  679 RNDSFivdlfqgQYKSKLVcpvcakvsitfdPFLYLPVPLPQKqkvlPIF 728
Cdd:cd02669  265 FKDSR-------VKKTSVS------------PFLLLTLDLPPP----PLF 291
zf-MYND pfam01753
MYND finger;
833-875 2.34e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 62.44  E-value: 2.34e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 74138825    833 CAACQRkqqsEEEKLKRCTRCYRVGYCNQFCQKTHWPDHKGLC 875
Cdd:pfam01753    1 CAVCGK----EALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1129-1254 3.28e-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 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: 68.90  E-value: 3.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1129 HREA--SKQLLLWRLPNVLIVQLKRFSFRSFI-WRDKINDLVEFPVrNLDLSKFCIgqkeeqlPS--YDLYAVINHYG-G 1202
Cdd:cd02657  182 GRDAiyTKTSRISRLPKYLTVQFVRFFWKRDIqKKAKILRKVKFPF-ELDLYELCT-------PSgyYELVAVITHQGrS 253
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 74138825 1203 MIGGHYTACARLPNDRSsqrsdvgWRLFDDSTVTTVDESQVVT-------RYAYVLFYR 1254
Cdd:cd02657  254 ADSGHYVAWVRRKNDGK-------WIKFDDDKVSEVTEEDILKlsgggdwHIAYILLYK 305
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1101-1255 1.13e-11

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 67.13  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1101 TLDQCLNLFtrpEVLAPE---------EAWYCpQCKQHREASKQlllwRLPNVLIVQLKRFSFRsfIWRDKINDLVEFPV 1171
Cdd:COG5533  138 TLQEFIDNM---EELVDDetgvkakenEELEV-QAKQEYEVSFV----KLPKILTIQLKRFANL--GGNQKIDTEVDEKF 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1172 rNLDLSKFCIGQKEEQLpSYDLYAVINHYGGMIGGHYTACARLPNDrssqrsdvgWRLFDDSTVTTVDESQVVT---RYA 1248
Cdd:COG5533  208 -ELPVKHDQILNIVKET-YYDLVGFVLHQGSLEGGHYIAYVKKGGK---------WEKANDSDVTPVSEEEAINekaKNA 276

                 ....*..
gi 74138825 1249 YVLFYRR 1255
Cdd:COG5533  277 YLYFYER 283
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
1101-1243 1.30e-11

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 69.51  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1101 TLDQCLNLFTRPEVLAPEEAWYCpQCKQHREASKQLLLWRLPNVLIVQLKRFSFRsfIWRD---KINDLVEFPVrNLDLS 1177
Cdd:COG5077  339 NLQESFRRYIQVETLDGDNRYNA-EKHGLQDAKKGVIFESLPPVLHLQLKRFEYD--FERDmmvKINDRYEFPL-EIDLL 414
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74138825 1178 KFC---IGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSsqrsdvgWRLFDDSTVTTVDESQV 1243
Cdd:COG5077  415 PFLdrdADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGR-------WYKFDDTRVTRATEKEV 476
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
540-664 2.22e-11

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 66.36  E-value: 2.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  540 GLVNLGNTCFMNSVIQSLS------NTRELRDFFHDRSFEAEINYNNPLGTgGRLAIGFavlLRALWKGTHQAFqpsklk 613
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlylpklDELLDDLSKELKVLKNVIRKPEPDLN-QEEALKL---FTALWSSKEHKV------ 70
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 74138825  614 aivaskASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRP 664
Cdd:COG5533   71 ------GWIPPMGSQEDAHELLGKLLDELKLDLVNSFTIRIFKTTKDKKKT 115
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
540-698 2.89e-11

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 66.20  E-value: 2.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  540 GLVNLGNTCFMNSVIQSLSNTRELRDffhdrsfeAEINYNNPLGTGGRLAIGFAVLLRALWK---GTHQAFQPSKLKAIV 616
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRD--------ALKNYNPARRGANQSSDNLTNALRDLFDtmdKKQEPVPPIEFLQLL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  617 ASKASQFT------GYAQHDAQEFMAFLLDGLHEDLnriqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQG 690
Cdd:cd02657   73 RMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKL----------------------------PGAGSKGSFIDQLFGI 124

                 ....*...
gi 74138825  691 QYKSKLVC 698
Cdd:cd02657  125 ELETKMKC 132
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
540-720 2.97e-11

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 66.18  E-value: 2.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  540 GLVNLGNTCFMNSVIQSLSNT---RELRDFFHDRSfeaeinyNNPLGTGgrlaigfavllralwkgthqAFQPSKLKAIV 616
Cdd:cd02663    1 GLENFGNTCYCNSVLQALYFEnllTCLKDLFESIS-------EQKKRTG--------------------VISPKKFITRL 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  617 ASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRPDEvvaeeaWQRhkmrndSFIVDLFQGQYKSKL 696
Cdd:cd02663   54 KRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAE------PQP------TWVHEIFQGILTNET 121
                        170       180
                 ....*....|....*....|....
gi 74138825  697 VCPVCAKVSITFDPFLYLPVPLPQ 720
Cdd:cd02663  122 RCLTCETVSSRDETFLDLSIDVEQ 145
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1101-1253 4.87e-11

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 64.31  E-value: 4.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1101 TLDQCLNLFTRPEVLapeEAWYCPQCkqhreaskQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRnldLSKfc 1180
Cdd:cd02662   97 TLEHCLDDFLSTEII---DDYKCDRC--------QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPER---LPK-- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1181 igqkeeqlPSYDLYAVINHYGGMIGGHYTACARLP-----NDRSSQRSDVG---------WRLfDDSTVTTVDESQVVTR 1246
Cdd:cd02662  161 --------VLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdKEPGSFVRMREgpsstshpwWRI-SDTTVKEVSESEVLEQ 231

                 ....*...
gi 74138825 1247 -YAYVLFY 1253
Cdd:cd02662  232 kSAYMLFY 239
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
540-718 3.15e-10

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 63.11  E-value: 3.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  540 GLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNP----------LGTG---GRLAIgfavllRALWKGTHQA 606
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPandlncqlikLADGllsGRYSK------PASLKSENDP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  607 FQ----PSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTetvdsdgrpdevvaeeawqrhkmrnds 682
Cdd:cd02658   75 YQvgikPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPN--------------------------- 127
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 74138825  683 fivDLFQGQYKSKLVCPVCAKVSITFDP--FLYLPVPL 718
Cdd:cd02658  128 ---DLFKFMIEDRLECLSCKKVKYTSELseILSLPVPK 162
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1101-1254 1.18e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 61.18  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1101 TLDQCLNLFTRPEVLapEEawYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFiWRD-KINDLVEFPvrnldlskf 1179
Cdd:cd02658  179 PLEDCLKAYFAPETI--ED--FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLEN-WVPkKLDVPIDVP--------- 244
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74138825 1180 cigqkEEQLPS-YDLYAVINHYGGMI-GGHYTACARLPNDRSSQrsdvgWRLFDDSTVTTVDESQVVTRYAYVLFYR 1254
Cdd:cd02658  245 -----EELGPGkYELIAFISHKGTSVhSGHYVAHIKKEIDGEGK-----WVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
334-424 8.36e-09

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107220  Cd Length: 84  Bit Score: 53.83  E-value: 8.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  334 PDSVVVHVYVKEIRRDSSRVLFREQDFTLIFQTRDGNflrlhpgcgphtIFRWQVKLRNLIEPEQCTFCFTASRIDICLR 413
Cdd:cd06463    5 LDEVTITIPLKDVTKKDVKVEFTPKSLTVSVKGGGGK------------EYLLEGELFGPIDPEESKWTVEDRKIEITLK 72
                         90
                 ....*....|..
gi 74138825  414 KRQ-SQRWGGLE 424
Cdd:cd06463   73 KKEpGEWWPRLE 84
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
511-644 1.77e-07

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 54.90  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  511 PPMPHSPVSgdsveedeeEEKKVCLPGFTGLVNLGNTCFMNSVIQSLsntRELRDFFHDRSFEAEINynnplGTGGRLAI 590
Cdd:cd02671    6 APQPSSATS---------CEKRENLLPFVGLNNLGNTCYLNSVLQVL---YFCPGFKHGLKHLVSLI-----SSVEQLQS 68
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 74138825  591 GFaVLLRALWKGTHQAFQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHE 644
Cdd:cd02671   69 SF-LLNPEKYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
537-716 2.85e-07

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 54.19  E-value: 2.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  537 GFTGLVNLGNTCFMNSVIQSLSNTRELRD----FFHDRSFEAEINYNNPLgtggRLAIGFAvllralwkgthqafQPSKL 612
Cdd:cd02659    1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNavysIPPTEDDDDNKSVPLAL----QRLFLFL--------------QLSES 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  613 KAIVAS-KASQFT-------GYAQHDAQEFMAFLLDGLhedlnriqnkpytetvdsdgrpdevvaEEAWQrhKMRNDSFI 684
Cdd:cd02659   63 PVKTTElTDKTRSfgwdslnTFEQHDVQEFFRVLFDKL---------------------------EEKLK--GTGQEGLI 113
                        170       180       190
                 ....*....|....*....|....*....|..
gi 74138825  685 VDLFQGQYKSKLVCPVCAKVSITFDPFLYLPV 716
Cdd:cd02659  114 KNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
540-566 9.40e-07

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 51.60  E-value: 9.40e-07
                         10        20
                 ....*....|....*....|....*..
gi 74138825  540 GLVNLGNTCFMNSVIQSLSNTRELRDF 566
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEY 27
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
325-414 2.28e-06

CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2.


Pssm-ID: 461503  Cd Length: 76  Bit Score: 46.48  E-value: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825    325 VKNDSYEKgPDSVVVHVYVKEIRRDSSRVLFReqdftliFQTRDgnfLRLHPGCGPHTIfrwQVKLRNLIEPEQCTFCFT 404
Cdd:pfam04969    1 PRYDWYQT-LDEVTITIPVKGAGIKKKDVKVN-------IKPRS---LKVKIKGGYELI---DGELFHPIDPEESSWTIE 66
                           90
                   ....*....|
gi 74138825    405 ASRIDICLRK 414
Cdd:pfam04969   67 GKKVEITLKK 76
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
540-718 7.69e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 49.73  E-value: 7.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  540 GLVNLGNTCFMNSVIQSLSNTRELRDFF-----HDRSFEAEINYNNPLGTGGRLaIGFAVLLRALWKGTHQAFQPSKLka 614
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVyecnsTEDAELKNMPPDKPHEPQTII-DQLQLIFAQLQFGNRSVVDPSGF-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  615 ivaSKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNkpytetvdSDGRpdevvaeeawqrhkmrndSFIVDLFQGQYKS 694
Cdd:cd02668   78 ---VKALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKN--------PDLK------------------NIVQDLFRGEYSY 128
                        170       180
                 ....*....|....*....|....
gi 74138825  695 KLVCPVCAKVSITFDPFLYLPVPL 718
Cdd:cd02668  129 VTQCSKCGRESSLPSKFYELELQL 152
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
289-444 1.61e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 48.63  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825   289 RDPEPEQEDQVKEEMALGADPTALVEEPESMVNLAFV-----KNDSYEKgPDSVVVHVYVKEIRRDSSRVLFREQDFTLI 363
Cdd:PLN03088  116 KIAEEEKDLVQPVPSDLPSSVTAPPVEEADATPVVPPskpkyRHEFYQK-PEEVVVTVFAKGVPAENVNVDFGEQILSVV 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825   364 FQTrdgnflrlhPGCGPhtiFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLE-----APATRGAVGGAKVA 438
Cdd:PLN03088  195 IEV---------PGEDA---YHLQPRLFGKIIPDKCKYEVLSTKIEIRLAKAEPITWASLEygkgpAVLPKPNVSSEVSQ 262

                  ....*.
gi 74138825   439 VPTGPT 444
Cdd:PLN03088  263 RPAYPS 268
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1141-1253 1.98e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 47.55  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1141 LPNVLIVQLKRFSFRSFIwRDKINDLVEFPvrnldlskfcigQKEEQLPsYDLYAVINHYGGMIGGHYTAcarLPNDRSS 1220
Cdd:cd02665  128 LPPVLTFELSRFEFNQGR-PEKIHDKLEFP------------QIIQQVP-YELHAVLVHEGQANAGHYWA---YIYKQSR 190
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 74138825 1221 QRsdvgWRLFDDSTVTTVDESQVVTR--------YAYVLFY 1253
Cdd:cd02665  191 QE----WEKYNDISVTESSWEEVERDsfgggrnpSAYCLMY 227
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
58-140 5.43e-05

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107220  Cd Length: 84  Bit Score: 43.04  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825   58 WRQSADEVIVKLRVGTGPVRLEDVDAAFTDTDCVVRLPDGR--QWGGVFFAEIQSSCTKVQArKGGLLQLVLPKKVPLLT 135
Cdd:cd06463    1 WYQTLDEVTITIPLKDVTKKDVKVEFTPKSLTVSVKGGGGKeyLLEGELFGPIDPEESKWTV-EDRKIEITLKKKEPGEW 79

                 ....*
gi 74138825  136 WPSLL 140
Cdd:cd06463   80 WPRLE 84
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1123-1253 6.07e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 46.37  E-value: 6.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1123 CPQCKqHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRD-KINDLVefpvrnldLSKFCIgqkeeQLPSYDLYAVINHYG 1201
Cdd:cd02673  129 CSSCK-CESAISSERIMTFPECLSINLKRYKLRIATSDYlKKNEEI--------MKKYCG-----TDAKYSLVAVICHLG 194
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 74138825 1202 -GMIGGHYTACARLPNDRSSqrsdvgWRLFDDSTVTTVDESQV---VTRYAYVLFY 1253
Cdd:cd02673  195 eSPYDGHYIAYTKELYNGSS------WLYCSDDEIRPVSKNDVstnARSSGYLIFY 244
p23_CS_hSgt1_like cd06489
p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related ...
337-424 7.04e-05

p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related proteins. hSgt1 is a co-chaperone which has been shown to be elevated in HEp-2 cells as a result of stress conditions such as heat shock. It interacts with the heat shock proteins (HSPs) Hsp70 and Hsp90, and it expression pattern is synchronized with these two Hsps. The interaction with HSP90 has been shown to involve the hSgt1_CS domain, and appears to be required for correct kinetochore assembly and efficient cell division. Some proteins in this subgroup contain a tetratricopeptide repeat (TPR) HSP-binding domain N-terminal to this CS domain, and most proteins in this subgroup contain a Sgt1-specific (SGS) domain C-terminal to the CS domain. The SGS domain interacts with some S100 family proteins. Studies suggest that S100A6 modulates in a Ca2+ dependent manner the interactions of hSgt1 with Hsp90 and Hsp70. The yeast Sgt1 CS domain is not found in this subgroup.


Pssm-ID: 107239  Cd Length: 84  Bit Score: 42.75  E-value: 7.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  337 VVVHVYVKEIRRDSSRVLFREQDFTLIFQTRDGNFLRLhpgcgphtifrwQVKLRNLIEPEQCTFCFTASRIDICLRKRQ 416
Cdd:cd06489    9 VVITILIKNVKPEDVSVEFEKRELSATVKLPSGNDYSL------------KLHLLHPIVPEQSSYKILSTKIEIKLKKTE 76

                 ....*...
gi 74138825  417 SQRWGGLE 424
Cdd:cd06489   77 AIRWSKLE 84
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1131-1202 1.12e-04

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 46.16  E-value: 1.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74138825 1131 EASKQLLLWRLPNVLIVQLKRFSFRSFIwRDKINDLVEFPVRNLDLSKFCIGQKEEQLPS--YDLYAVINHYGG 1202
Cdd:cd02669  322 DSLKRYLISRLPKYLIFHIKRFSKNNFF-KEKNPTIVNFPIKNLDLSDYVHFDKPSLNLStkYNLVANIVHEGT 394
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
537-642 1.74e-04

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 46.02  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  537 GFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHdrsfeaEINYNNPlgtGGRLAIGFAvLLRALWKGTHQAFQPSKLKAIV 616
Cdd:COG5077  192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY------GIPTDHP---RGRDSVALA-LQRLFYNLQTGEEPVDTTELTR 261
                         90       100
                 ....*....|....*....|....*.
gi 74138825  617 ASKASQFTGYAQHDAQEFMAFLLDGL 642
Cdd:COG5077  262 SFGWDSDDSFMQHDIQEFNRVLQDNL 287
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
539-739 5.87e-04

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 43.63  E-value: 5.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  539 TGLVNLGNTCFMNSVIQSLSNTRELRDF---FHDRSFEAEINYNNPLGTGGR--------LAIGFAVLLRALWkgthQAF 607
Cdd:cd02666    2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLvlnFDESKAELASDYPTERRIGGRevsrselqRSNQFVYELRSLF----NDL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  608 QPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGrpdEVVAEeawqrhkmrndsfIVDL 687
Cdd:cd02666   78 IHSNTRSVTPSKELAYLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDK---EQSDL-------------IKRL 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 74138825  688 FQGQYKSKLV---CPVCAKVSITFDPFLYLPVPLPQKQKVLPIfyfarEPHSKPI 739
Cdd:cd02666  142 FSGKTKQQLVpesMGNQPSVRTKTERFLSLLVDVGKKGREIVV-----LLEPKDL 191
p23_melusin_like cd06488
p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related ...
336-424 2.51e-03

p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related proteins. Melusin's tail domain interacts with the cytoplasmic domain of beta1-A and beta1-D isoforms of beta1 integrin, it does not bind other integrin beta subunits. Melusin is a muscle-specific protein expressed in skeletal and cardiac muscles but not in smooth muscle or other tissues. It is needed for heart hypertrophy following mechanical overload. The integrin-binding portion of this domain appears to be sequestered in the full length melusin protein, Ca2+ may modulate the protein's conformation exposing this binding site. This group includes Chordc1, also known as Chp-1, which is conserved from vertebrates to humans. Mammalian Chordc1 interacts with the heat shock protein (HSP) Hsp90 and is implicated in circadian and/or homeostatic mechanisms in the brain. The N-terminal portions of proteins belonging to this group contain two cysteine and histidine rich domain (CHORD) domains.


Pssm-ID: 107238  Cd Length: 87  Bit Score: 38.43  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825  336 SVVVHVYVKEIRRDSSRVLFREQDFT--LIFqtrDGNFlrlhpgcgphtIFRWQVKLRNLIEPEQCTFCFTASRIDICLR 413
Cdd:cd06488   11 HVVVSVYAKNSNPELSVVEANSTVLTihIVF---EGNK-----------EFQLDIELWGVIDVEKSSVNMLPTKVEIKLR 76
                         90
                 ....*....|.
gi 74138825  414 KRQSQRWGGLE 424
Cdd:cd06488   77 KAEPGSWAKLE 87
p23_NUDC_like cd06467
p23_like domain of NUD (nuclear distribution) C and similar proteins. Aspergillus nidulas (An) ...
58-140 3.85e-03

p23_like domain of NUD (nuclear distribution) C and similar proteins. Aspergillus nidulas (An) NUDC is needed for nuclear movement. AnNUDC is localized at the hyphal cortex, and binds NUDF at spindle pole bodies (SPBs) and in the cytoplasm at different stages in the cell cycle. At the SPBs it is part of the dynein molecular motor/NUDF complex that regulates microtubule dynamics. Mammalian(m) NUDC associates both with the dynein complex and also with an anti-inflammatory enzyme, platelet activating factor acetylhydrolase I, PAF-AH(I) complex, through binding mNUDF, the regulatory beta subunit of PAF-AH(I). mNUDC is important for cell proliferation both in normal and tumor tissues. Its expression is elevated in various cell types undergoing mitosis or stimulated to proliferate, with high expression levels observed in leukemic cells and tumors. For a leukemic cell line, human NUDC was shown to activate the thrombopoietin (TPO) receptor (Mpl) by binding to its extracellular domain, and promoting cell proliferation and differentiation. This group also includes the human broadly immunogenic tumor associated antigen, CML66, which is highly expressed in a variety of solid tumors and in leukemias. In normal tissues high expression of CML66 is limited to testis and heart.


Pssm-ID: 107224  Cd Length: 85  Bit Score: 37.91  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825   58 WRQSADEVIVKLRVGTGpVRLEDVDAAFTDTDCVVRLPDGRQW-GGVFFAEIQSSCT--KVQarKGGLLQLVLPKKVPLL 134
Cdd:cd06467    3 WTQTLDEVTVTIPLPEG-TKSKDVKVEITPKHLKVGVKGGEPLlDGELYAKVKVDEStwTLE--DGKLLEITLEKRNEGE 79

                 ....*.
gi 74138825  135 TWPSLL 140
Cdd:cd06467   80 WWPSLV 85
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1104-1253 5.82e-03

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: 40.19  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1104 QCLNLFTRPEVLAPEeawYCPQCKQHREASKQLLLWRLPN----VLIVQLKRF-SFRSFIWRDKI-----NDLVEFPVRN 1173
Cdd:cd02672  121 QLLKRSLDLEKVTKA---WCDTCCKYQPLEQTTSIRHLPDilllVLVINLSVTnGEFDDINVVLPsgkvmQNKVSPKAID 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74138825 1174 LDLSKFCIGQKEeqLPSYDLYAVINHY-GGMIGGHYTACARLPNDRSSQRsdvGWRLFDDSTVTTVDESqvvtryAYVLF 1252
Cdd:cd02672  198 HDKLVKNRGQES--IYKYELVGYVCEInDSSRGQHNVVFVIKVNEESTHG---RWYLFNDFLVTPVSEL------AYILL 266

                 .
gi 74138825 1253 Y 1253
Cdd:cd02672  267 Y 267
 
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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