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Conserved domains on  [gi|270265845|ref|NP_001161844|]
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ubiquitin carboxyl-terminal hydrolase 19 isoform 3 [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 2.45e-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: 2.45e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  535 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHQAFQPSKLKA 614
Cdd:COG5560   262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  615 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 691
Cdd:COG5560   342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  692 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpifyfarepHSKPIKFLVSVSKENSSASEVLDSLSqsvhvkpenlr 771
Cdd:COG5560   422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVFPESGRRQPLKIELDASST----------- 479
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  772 lAEVIKNRfhrvflpshsLDAVSptDVLLCFELLSPELAKERVVVlEVQQRPQVPSIPISKCAACQRKQQSEEEklkrct 851
Cdd:COG5560   480 -IRGLKKL----------VDAEY--GKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG------ 539
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  852 rcyrVGYCnqfcqKTHWPDHKGLCRPENIGYPFL---VSVPASRLTyarlaQLLEGYARYSVSVFQPPfqpgrmalesqs 928
Cdd:COG5560   540 ----IEVP-----VVHLRIEKGYKSKRLFGDPFLqlnVLIKASIYD-----KLVKEFEELLVLVEMKK------------ 593
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  929 pgctTLLSTSSLEAGDSEREPIQPSELQLVTpvaEGDTgahrvwppadrgpvPSTSGLSSEmlasgpiegcpllagERVS 1008
Cdd:COG5560   594 ----TDVDLVSEQVRLLREESSPSSWLKLET---EIDT--------------KREEQVEEE---------------GQMN 637
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1009 RPEAAVPGYQHSSESVNthtpqfFIYKIDASNREQRLEDKGETPlelgddcslalvwrnnerlqefvlvaskelecaedp 1088
Cdd:COG5560   638 FNDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------------ 675
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1089 gsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDKINDLV 1167
Cdd:COG5560   676 ------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDKIDDLV 741
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1168 EFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQVVTRY 1247
Cdd:COG5560   742 EYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPEDSVTSS 813
                         730
                  ....*....|
gi 270265845 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 9.90e-60

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: 200.52  E-value: 9.90e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845   415 RQSQRWGGLEAPATRGAVGGAKVAVPTGPTPLDSTPPGGGPHPLTGQEEARAVEKEKPKARSEDSGLDGVVARTPLEHVA 494
Cdd:pfam16602    1 RHSQRWGGLEAPATQGAVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 270265845   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 3.50e-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: 3.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  328 DSYEKgPDSVVVHVYVKEIRRDSSRVLFREQDFTLIFQTRDGNflrlhpgcgphtIFRWQVKLRNLIEPEQCTFCFTASR 407
Cdd:cd06466     1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                          90
                  ....*....|....*..
gi 270265845  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 5.28e-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: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845   58 WRQSADEVIVKLRVGTGPVRLEDVDAAFTDTDCVVRLPDGR--QWGGVFFAEIQSSCTKVQArKGGLLQLVLPKKVPLLT 135
Cdd:cd06463     1 WYQTLDEVTITIPLKDVTKKDVKVEFTPKSLTVSVKGGGGKeyLLEGELFGPIDPEESKWTV-EDRKIEITLKKKEPGEW 79

                  ....*
gi 270265845  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 2.45e-119

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 391.94  E-value: 2.45e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  535 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHQAFQPSKLKA 614
Cdd:COG5560   262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  615 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 691
Cdd:COG5560   342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  692 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpifyfarepHSKPIKFLVSVSKENSSASEVLDSLSqsvhvkpenlr 771
Cdd:COG5560   422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVFPESGRRQPLKIELDASST----------- 479
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  772 lAEVIKNRfhrvflpshsLDAVSptDVLLCFELLSPELAKERVVVlEVQQRPQVPSIPISKCAACQRKQQSEEEklkrct 851
Cdd:COG5560   480 -IRGLKKL----------VDAEY--GKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG------ 539
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  852 rcyrVGYCnqfcqKTHWPDHKGLCRPENIGYPFL---VSVPASRLTyarlaQLLEGYARYSVSVFQPPfqpgrmalesqs 928
Cdd:COG5560   540 ----IEVP-----VVHLRIEKGYKSKRLFGDPFLqlnVLIKASIYD-----KLVKEFEELLVLVEMKK------------ 593
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  929 pgctTLLSTSSLEAGDSEREPIQPSELQLVTpvaEGDTgahrvwppadrgpvPSTSGLSSEmlasgpiegcpllagERVS 1008
Cdd:COG5560   594 ----TDVDLVSEQVRLLREESSPSSWLKLET---EIDT--------------KREEQVEEE---------------GQMN 637
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1009 RPEAAVPGYQHSSESVNthtpqfFIYKIDASNREQRLEDKGETPlelgddcslalvwrnnerlqefvlvaskelecaedp 1088
Cdd:COG5560   638 FNDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------------ 675
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1089 gsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDKINDLV 1167
Cdd:COG5560   676 ------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDKIDDLV 741
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1168 EFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQVVTRY 1247
Cdd:COG5560   742 EYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPEDSVTSS 813
                         730
                  ....*....|
gi 270265845 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 9.90e-60

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: 200.52  E-value: 9.90e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845   415 RQSQRWGGLEAPATRGAVGGAKVAVPTGPTPLDSTPPGGGPHPLTGQEEARAVEKEKPKARSEDSGLDGVVARTPLEHVA 494
Cdd:pfam16602    1 RHSQRWGGLEAPATQGAVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 270265845   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 5.66e-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: 5.66e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1097 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFrSFIWRDKINDLVEFPVRNLDL 1176
Cdd:cd02674    81 APKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSF-SRGSTRKLTTPVTFPLNDLDL 159
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 270265845 1177 SKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvGWRLFDDSTVTTVDESQVVTRYAYVLFYR 1254
Cdd:cd02674   160 TPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETN-------DWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
539-726 1.45e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 175.71  E-value: 1.45e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845   539 TGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTggrLAIGFAVLLRALWKGTHQ-AFQPSKLKAIVA 617
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNSKSsSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845   618 SKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQGQYKSKLV 697
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180
                   ....*....|....*....|....*....
gi 270265845   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 3.50e-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: 3.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  328 DSYEKgPDSVVVHVYVKEIRRDSSRVLFREQDFTLIFQTRDGNflrlhpgcgphtIFRWQVKLRNLIEPEQCTFCFTASR 407
Cdd:cd06466     1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                          90
                  ....*....|....*..
gi 270265845  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 2.21e-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: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845   325 VKNDSYEKgPDSVVVHVYVKEIRRDSSRVLFReqdftliFQTRDgnfLRLHPGCGPHTIfrwQVKLRNLIEPEQCTFCFT 404
Cdd:pfam04969    1 PRYDWYQT-LDEVTITIPVKGAGIKKKDVKVN-------IKPRS---LKVKIKGGYELI---DGELFHPIDPEESSWTIE 66
                           90
                   ....*....|
gi 270265845   405 ASRIDICLRK 414
Cdd:pfam04969   67 GKKVEITLKK 76
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
289-444 2.03e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 48.24  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  289 RDPEPEQEDQVKEEMALGADPTALVEEPESMVNLAFV-----KNDSYEKgPDSVVVHVYVKEIRRDSSRVLFREQDFTLI 363
Cdd:PLN03088  116 KIAEEEKDLVQPVPSDLPSSVTAPPVEEADATPVVPPskpkyRHEFYQK-PEEVVVTVFAKGVPAENVNVDFGEQILSVV 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  364 FQTrdgnflrlhPGCGPhtiFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLE-----APATRGAVGGAKVA 438
Cdd:PLN03088  195 IEV---------PGEDA---YHLQPRLFGKIIPDKCKYEVLSTKIEIRLAKAEPITWASLEygkgpAVLPKPNVSSEVSQ 262

                  ....*.
gi 270265845  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 5.28e-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: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845   58 WRQSADEVIVKLRVGTGPVRLEDVDAAFTDTDCVVRLPDGR--QWGGVFFAEIQSSCTKVQArKGGLLQLVLPKKVPLLT 135
Cdd:cd06463     1 WYQTLDEVTITIPLKDVTKKDVKVEFTPKSLTVSVKGGGGKeyLLEGELFGPIDPEESKWTV-EDRKIEITLKKKEPGEW 79

                  ....*
gi 270265845  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 2.45e-119

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 391.94  E-value: 2.45e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  535 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHQAFQPSKLKA 614
Cdd:COG5560   262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  615 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 691
Cdd:COG5560   342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  692 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpifyfarepHSKPIKFLVSVSKENSSASEVLDSLSqsvhvkpenlr 771
Cdd:COG5560   422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVFPESGRRQPLKIELDASST----------- 479
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  772 lAEVIKNRfhrvflpshsLDAVSptDVLLCFELLSPELAKERVVVlEVQQRPQVPSIPISKCAACQRKQQSEEEklkrct 851
Cdd:COG5560   480 -IRGLKKL----------VDAEY--GKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG------ 539
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  852 rcyrVGYCnqfcqKTHWPDHKGLCRPENIGYPFL---VSVPASRLTyarlaQLLEGYARYSVSVFQPPfqpgrmalesqs 928
Cdd:COG5560   540 ----IEVP-----VVHLRIEKGYKSKRLFGDPFLqlnVLIKASIYD-----KLVKEFEELLVLVEMKK------------ 593
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  929 pgctTLLSTSSLEAGDSEREPIQPSELQLVTpvaEGDTgahrvwppadrgpvPSTSGLSSEmlasgpiegcpllagERVS 1008
Cdd:COG5560   594 ----TDVDLVSEQVRLLREESSPSSWLKLET---EIDT--------------KREEQVEEE---------------GQMN 637
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1009 RPEAAVPGYQHSSESVNthtpqfFIYKIDASNREQRLEDKGETPlelgddcslalvwrnnerlqefvlvaskelecaedp 1088
Cdd:COG5560   638 FNDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------------ 675
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1089 gsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDKINDLV 1167
Cdd:COG5560   676 ------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDKIDDLV 741
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1168 EFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQVVTRY 1247
Cdd:COG5560   742 EYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPEDSVTSS 813
                         730
                  ....*....|
gi 270265845 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 9.90e-60

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: 200.52  E-value: 9.90e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845   415 RQSQRWGGLEAPATRGAVGGAKVAVPTGPTPLDSTPPGGGPHPLTGQEEARAVEKEKPKARSEDSGLDGVVARTPLEHVA 494
Cdd:pfam16602    1 RHSQRWGGLEAPATQGAVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 270265845   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 5.66e-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: 5.66e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1097 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFrSFIWRDKINDLVEFPVRNLDL 1176
Cdd:cd02674    81 APKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSF-SRGSTRKLTTPVTFPLNDLDL 159
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 270265845 1177 SKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvGWRLFDDSTVTTVDESQVVTRYAYVLFYR 1254
Cdd:cd02674   160 TPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETN-------DWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
539-726 1.45e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 175.71  E-value: 1.45e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845   539 TGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTggrLAIGFAVLLRALWKGTHQ-AFQPSKLKAIVA 617
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNSKSsSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845   618 SKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQGQYKSKLV 697
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180
                   ....*....|....*....|....*....
gi 270265845   698 CPVCAKVSITFDPFLYLPVPLPQKQKVLP 726
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELK 160
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1102-1253 1.39e-46

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 169.93  E-value: 1.39e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  1102 LDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWrDKINDLVEFPvRNLDLSKFCI 1181
Cdd:pfam00443  164 LQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTW-EKLNTEVEFP-LELDLSRYLA 241
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 270265845  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 1.73e-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: 1.73e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1101 TLDQCLNLFTRPEVLAPEEAWYCPqCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPvRNLDLSKFC 1180
Cdd:cd02257   100 SLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFP-LELDLSPYL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1181 IGQKEEQLPS-----YDLYAVINHYGGMI-GGHYTACARlpnDRSSQRsdvgWRLFDDSTVTTVDESQVVTRY-----AY 1249
Cdd:cd02257   178 SEGEKDSDSDngsykYELVAVVVHSGTSAdSGHYVAYVK---DPSDGK----WYKFNDDKVTEVSEEEVLEFGslsssAY 250

                  ....*
gi 270265845 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 2.46e-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: 2.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1089 GSAGEAARAGHFTLDQCLNLFTRPEVLAPEeAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVE 1168
Cdd:cd02660   165 WALGESGVSGTPTLSDCLDRFTRPEKLGDF-AYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQ 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1169 FPVRnLDLSKFCIGQKEEQLPS--------YDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvgWRLFDDSTVTTVDE 1240
Cdd:cd02660   244 FPLE-LNMTPYTSSSIGDTQDSnsldpdytYDLFAVVVHKGTLDTGHYTAYCRQGDGQ--------WFKFDDAMITRVSE 314
                         170
                  ....*....|...
gi 270265845 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 2.84e-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: 2.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1101 TLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFsfrSFIWRDKINDLVEFPVRnLDLSKFc 1180
Cdd:cd02661   163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF---SNFRGGKINKQISFPET-LDLSPY- 237
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 270265845 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 3.35e-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: 118.64  E-value: 3.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1100 FTLDQCLNLFTRPEVLAPEEAWYCPQCKqhrEASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRnLDLSKF 1179
Cdd:cd02667   111 CSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEI-LDLAPF 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1180 C----IGQKEEQLPSYDLYAVINHYGGMIGGHYTACARL--PNDRSS-------QRSDVG-----WRLFDDSTVTTVDES 1241
Cdd:cd02667   187 CdpkcNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVrpPQQRLSdltkskpAADEAGpgsgqWYYISDSDVREVSLE 266
                         170
                  ....*....|...
gi 270265845 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 4.60e-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: 4.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  540 GLVNLGNTCFMNSVIQSLSNTrelrdffhdrsfeaeinynnplgtggrlaigfavllralwkgthqafqpsklkaivask 619
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSAD----------------------------------------------------------- 21
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  620 asqftgyaQHDAQEFMAFLLDGLHedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrndSFIVDLFQGQYKSKLVCP 699
Cdd:cd02674    22 --------QQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                         170       180
                  ....*....|....*....|....*..
gi 270265845  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 8.28e-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: 8.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1106 LNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRsfiW----RDKINDLVEFPVRnLDLSKFCI 1181
Cdd:cd02659   157 LDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFD---FetmmRIKINDRFEFPLE-LDMEPYTE 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1182 ----------GQKEEQLPSYDLYAVINHYGGMIGGHYTACARlpndrssQRSDVGWRLFDDSTVTTVDESQVVTRY---- 1247
Cdd:cd02659   233 kglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYSYIK-------DRDDGKWYKFNDDVVTPFDPNDAEEECfgge 305
                         170       180
                  ....*....|....*....|....*...
gi 270265845 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 5.74e-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: 5.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1099 HFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWR-DKINDLVEFPvrnLDLS 1177
Cdd:cd02663   146 NTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFP---LELR 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1178 KF-CIGQKEEQLPSYDLYAVINHYGGMIG-GHYTacarlpndrSSQRSDVGWRLFDDSTVTTVDESQVVTRY-------- 1247
Cdd:cd02663   223 LFnTTDDAENPDRLYELVAVVVHIGGGPNhGHYV---------SIVKSHGGWLLFDDETVEKIDENAVEEFFgdspnqat 293

                  ....*.
gi 270265845 1248 AYVLFY 1253
Cdd:cd02663   294 AYVLFY 299
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
540-723 2.33e-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: 2.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  540 GLVNLGNTCFMNSVIQSLSNTrelrdffhdrsfeaeinynnplgtggrlaigfavllralwkgthqafqpsklkaivask 619
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  620 asqftgyaQHDAQEFMAFLLDGLHEDLNRIQNKpytetvdsdgrpdevvaeeawQRHKMRNDSFIVDLFQGQYKSKLVCP 699
Cdd:cd02257    22 --------QQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                         170       180
                  ....*....|....*....|....
gi 270265845  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 4.95e-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: 4.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  539 TGLVNLGNTCFMNSVIQSLSNTRELRDFFhdRSFEAEINYNNPlgtggrlaiGFAVLL-------RALW---KGTHQAFQ 608
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPLANYL--LSREHSKDCCNE---------GFCMMCaleahveRALAssgPGSAPRIF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  609 PSKLKAIvaskASQFTGYAQHDAQEFMAFLLDGLHED-LNRiqNKPYTETVDSDgrpdevvaeeawqrhkmRNDSFIVDL 687
Cdd:cd02661    71 SSNLKQI----SKHFRIGRQEDAHEFLRYLLDAMQKAcLDR--FKKLKAVDPSS-----------------QETTLVQQI 127
                         170       180
                  ....*....|....*....|....*....
gi 270265845  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 3.50e-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: 3.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  328 DSYEKgPDSVVVHVYVKEIRRDSSRVLFREQDFTLIFQTRDGNflrlhpgcgphtIFRWQVKLRNLIEPEQCTFCFTASR 407
Cdd:cd06466     1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                          90
                  ....*....|....*..
gi 270265845  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 4.08e-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: 4.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  540 GLVNLGNTCFMNSVIQSLSNTRELRDFFHdrsfeAEINYNNPLGTGGRLAIGFAV--LLRALW-KGTHQAFQPSKLKAIV 616
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFL-----SDRHSCTCLSCSPNSCLSCAMdeIFQEFYySGDRSPYGPINLLYLS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  617 ASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYtetvdsdgrpdevvaeeawqrHKMRNDSFIVDLFQGQYKSKL 696
Cdd:cd02660    77 WKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEAN---------------------DESHCNCIIHQTFSGSLQSSV 135
                         170       180
                  ....*....|....*....|....*
gi 270265845  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 2.95e-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: 2.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1097 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFIWRDKINDLVEFPvRNLD 1175
Cdd:cd02668   153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdRKTGAKKKLNASISFP-EILD 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1176 LSKFCIGQKeEQLPSYDLYAVINHYG-GMIGGHYTAcarlpNDRSSQRSDvgWRLFDDSTVTTVDESQV----------- 1243
Cdd:cd02668   232 MGEYLAESD-EGSYVYELSGVLIHQGvSAYSGHYIA-----HIKDEQTGE--WYKFNDEDVEEMPGKPLklgnsedpakp 303
                         170       180
                  ....*....|....*....|.
gi 270265845 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 1.68e-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: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1106 LNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFIWRDK------INDLVEFPVRNLDLSK 1178
Cdd:cd02664   140 LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYdQKTHVREKimdnvsINEVLSLPVRVESKSS 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1179 FCIGQKEE-----------QLPSYDLYAVINHYG-GMIGGHYTACAR-------------LPNDRSSQRSDVGWRLFDDS 1233
Cdd:cd02664   220 ESPLEKKEeesgddgelvtRQVHYRLYAVVVHSGySSESGHYFTYARdqtdadstgqecpEPKDAEENDESKNWYLFNDS 299
                         170       180
                  ....*....|....*....|....*...
gi 270265845 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 3.37e-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: 80.51  E-value: 3.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  540 GLVNLGNTCFMNSVIQSLSNTRELRDFFHDRsfeaeinynnplgtggrlaigfavllralwkgthqafqPSKLKAIVASK 619
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  620 ASQFTGYAQHDAQEFMAFLLDGLhedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrnDSFIVDLFQGQYKSKLVCP 699
Cdd:cd02667    43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84
                         170       180
                  ....*....|....*....|....*.
gi 270265845  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 9.40e-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: 80.23  E-value: 9.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  540 GLVNLGNTCFMNSVIQSLsntrelrdfFHDRSFEAEINYNNPLGTGGRLAIGFA-VLLRALWKGTHQAFQPSKLKAIVAS 618
Cdd:cd02664     1 GLINLGNTCYMNSVLQAL---------FMAKDFRRQVLSLNLPRLGDSQSVMKKlQLLQAHLMHTQRRAEAPPDYFLEAS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  619 KASQFTGYAQHDAQEFMAFLLDGLHedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrndSFIVDLFQGQYKSKLVC 698
Cdd:cd02664    72 RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTIRC 113
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 270265845  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 5.21e-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: 5.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1069 ERLQEF----VLVASKELECAEDPGSAGEAARAGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNV 1144
Cdd:cd02671   145 ERREDFqdisVPVQESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEV 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1145 LIVQLKRFSFRSFIWR-----DKINDLVEFPvrnLDLSKFCIGQKeEQLPSYDLYAVINHYGGMIG-GHYTACARlpndr 1218
Cdd:cd02671   225 ITIHLKCFAANGSEFDcygglSKVNTPLLTP---LKLSLEEWSTK-PKNDVYRLFAVVMHSGATISsGHYTAYVR----- 295
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 270265845 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 5.32e-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: 5.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  535 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFhdrsfeaeINYNNPLGTGGR---LAIGFAVLLRALWkgTHQAFQ--- 608
Cdd:cd02669   116 LPGFVGLNNIKNNDYANVIIQALSHVKPIRNFF--------LLYENYENIKDRkseLVKRLSELIRKIW--NPRNFKghv 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  609 -PSK-LKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiQNKPYTETVDS--DG------RPDEVVAEEAWQRHKM 678
Cdd:cd02669   186 sPHElLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGG-SKKPNSSIIHDcfQGkvqietQKIKPHAEEEGSKDKF 264
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 270265845  679 RNDSFivdlfqgQYKSKLVcpvcakvsitfdPFLYLPVPLPQKqkvlPIF 728
Cdd:cd02669   265 FKDSR-------VKKTSVS------------PFLLLTLDLPPP----PLF 291
zf-MYND pfam01753
MYND finger;
833-875 1.60e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 62.82  E-value: 1.60e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 270265845   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 3.18e-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: 3.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1129 HREA--SKQLLLWRLPNVLIVQLKRFSFRSFI-WRDKINDLVEFPVrNLDLSKFCIgqkeeqlPS--YDLYAVINHYG-G 1202
Cdd:cd02657   182 GRDAiyTKTSRISRLPKYLTVQFVRFFWKRDIqKKAKILRKVKFPF-ELDLYELCT-------PSgyYELVAVITHQGrS 253
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 270265845 1203 MIGGHYTACARLPNDRSsqrsdvgWRLFDDSTVTTVDESQVVT-------RYAYVLFYR 1254
Cdd:cd02657   254 ADSGHYVAWVRRKNDGK-------WIKFDDDKVSEVTEEDILKlsgggdwHIAYILLYK 305
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1101-1255 1.10e-11

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 67.13  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1101 TLDQCLNLFtrpEVLAPE---------EAWYCpQCKQHREASKQlllwRLPNVLIVQLKRFSFRsfIWRDKINDLVEFPV 1171
Cdd:COG5533   138 TLQEFIDNM---EELVDDetgvkakenEELEV-QAKQEYEVSFV----KLPKILTIQLKRFANL--GGNQKIDTEVDEKF 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1172 rNLDLSKFCIGQKEEQLpSYDLYAVINHYGGMIGGHYTACARLPNDrssqrsdvgWRLFDDSTVTTVDESQVVT---RYA 1248
Cdd:COG5533   208 -ELPVKHDQILNIVKET-YYDLVGFVLHQGSLEGGHYIAYVKKGGK---------WEKANDSDVTPVSEEEAINekaKNA 276

                  ....*..
gi 270265845 1249 YVLFYRR 1255
Cdd:COG5533   277 YLYFYER 283
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
1101-1243 1.26e-11

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 69.51  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1101 TLDQCLNLFTRPEVLAPEEAWYCpQCKQHREASKQLLLWRLPNVLIVQLKRFSFRsfIWRD---KINDLVEFPVrNLDLS 1177
Cdd:COG5077   339 NLQESFRRYIQVETLDGDNRYNA-EKHGLQDAKKGVIFESLPPVLHLQLKRFEYD--FERDmmvKINDRYEFPL-EIDLL 414
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 270265845 1178 KFC---IGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSsqrsdvgWRLFDDSTVTTVDESQV 1243
Cdd:COG5077   415 PFLdrdADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGR-------WYKFDDTRVTRATEKEV 476
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
540-664 2.15e-11

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 66.36  E-value: 2.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  540 GLVNLGNTCFMNSVIQSLS------NTRELRDFFHDRSFEAEINYNNPLGTgGRLAIGFavlLRALWKGTHQAFqpsklk 613
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlylpklDELLDDLSKELKVLKNVIRKPEPDLN-QEEALKL---FTALWSSKEHKV------ 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 270265845  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 2.80e-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: 2.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  540 GLVNLGNTCFMNSVIQSLSNTRELRDffhdrsfeAEINYNNPLGTGGRLAIGFAVLLRALWK---GTHQAFQPSKLKAIV 616
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRD--------ALKNYNPARRGANQSSDNLTNALRDLFDtmdKKQEPVPPIEFLQLL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  617 ASKASQFT------GYAQHDAQEFMAFLLDGLHEDLnriqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQG 690
Cdd:cd02657    73 RMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKL----------------------------PGAGSKGSFIDQLFGI 124

                  ....*...
gi 270265845  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 2.87e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 66.18  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  540 GLVNLGNTCFMNSVIQSLSNT---RELRDFFHDRSfeaeinyNNPLGTGgrlaigfavllralwkgthqAFQPSKLKAIV 616
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYFEnllTCLKDLFESIS-------EQKKRTG--------------------VISPKKFITRL 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  617 ASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRPDEvvaeeaWQRhkmrndSFIVDLFQGQYKSKL 696
Cdd:cd02663    54 KRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAE------PQP------TWVHEIFQGILTNET 121
                         170       180
                  ....*....|....*....|....
gi 270265845  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 4.72e-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: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1101 TLDQCLNLFTRPEVLapeEAWYCPQCkqhreaskQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRnldLSKfc 1180
Cdd:cd02662    97 TLEHCLDDFLSTEII---DDYKCDRC--------QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPER---LPK-- 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1181 igqkeeqlPSYDLYAVINHYGGMIGGHYTACARLP-----NDRSSQRSDVG---------WRLfDDSTVTTVDESQVVTR 1246
Cdd:cd02662   161 --------VLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdKEPGSFVRMREgpsstshpwWRI-SDTTVKEVSESEVLEQ 231

                  ....*...
gi 270265845 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 3.05e-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: 3.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  540 GLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNP----------LGTG---GRLAIgfavllRALWKGTHQA 606
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPandlncqlikLADGllsGRYSK------PASLKSENDP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  607 FQ----PSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTetvdsdgrpdevvaeeawqrhkmrnds 682
Cdd:cd02658    75 YQvgikPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPN--------------------------- 127
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 270265845  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 1.14e-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: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1101 TLDQCLNLFTRPEVLapEEawYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFiWRD-KINDLVEFPvrnldlskf 1179
Cdd:cd02658   179 PLEDCLKAYFAPETI--ED--FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLEN-WVPkKLDVPIDVP--------- 244
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 270265845 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 8.13e-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: 8.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  334 PDSVVVHVYVKEIRRDSSRVLFREQDFTLIFQTRDGNflrlhpgcgphtIFRWQVKLRNLIEPEQCTFCFTASRIDICLR 413
Cdd:cd06463     5 LDEVTITIPLKDVTKKDVKVEFTPKSLTVSVKGGGGK------------EYLLEGELFGPIDPEESKWTVEDRKIEITLK 72
                          90
                  ....*....|..
gi 270265845  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 1.67e-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: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  511 PPMPHSPVSgdsveedeeEEKKVCLPGFTGLVNLGNTCFMNSVIQSLsntRELRDFFHDRSFEAEINynnplGTGGRLAI 590
Cdd:cd02671     6 APQPSSATS---------CEKRENLLPFVGLNNLGNTCYLNSVLQVL---YFCPGFKHGLKHLVSLI-----SSVEQLQS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 270265845  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 2.76e-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: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  537 GFTGLVNLGNTCFMNSVIQSLSNTRELRD----FFHDRSFEAEINYNNPLgtggRLAIGFAvllralwkgthqafQPSKL 612
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNavysIPPTEDDDDNKSVPLAL----QRLFLFL--------------QLSES 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  613 KAIVAS-KASQFT-------GYAQHDAQEFMAFLLDGLhedlnriqnkpytetvdsdgrpdevvaEEAWQrhKMRNDSFI 684
Cdd:cd02659    63 PVKTTElTDKTRSfgwdslnTFEQHDVQEFFRVLFDKL---------------------------EEKLK--GTGQEGLI 113
                         170       180       190
                  ....*....|....*....|....*....|..
gi 270265845  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 9.12e-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: 9.12e-07
                          10        20
                  ....*....|....*....|....*..
gi 270265845  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 2.21e-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: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845   325 VKNDSYEKgPDSVVVHVYVKEIRRDSSRVLFReqdftliFQTRDgnfLRLHPGCGPHTIfrwQVKLRNLIEPEQCTFCFT 404
Cdd:pfam04969    1 PRYDWYQT-LDEVTITIPVKGAGIKKKDVKVN-------IKPRS---LKVKIKGGYELI---DGELFHPIDPEESSWTIE 66
                           90
                   ....*....|
gi 270265845   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 7.45e-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: 7.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  540 GLVNLGNTCFMNSVIQSLSNTRELRDFF-----HDRSFEAEINYNNPLGTGGRLaIGFAVLLRALWKGTHQAFQPSKLka 614
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVyecnsTEDAELKNMPPDKPHEPQTII-DQLQLIFAQLQFGNRSVVDPSGF-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  615 ivaSKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNkpytetvdSDGRpdevvaeeawqrhkmrndSFIVDLFQGQYKS 694
Cdd:cd02668    78 ---VKALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKN--------PDLK------------------NIVQDLFRGEYSY 128
                         170       180
                  ....*....|....*....|....
gi 270265845  695 KLVCPVCAKVSITFDPFLYLPVPL 718
Cdd:cd02668   129 VTQCSKCGRESSLPSKFYELELQL 152
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1141-1253 1.75e-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: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1141 LPNVLIVQLKRFSFRSFIwRDKINDLVEFPvrnldlskfcigQKEEQLPsYDLYAVINHYGGMIGGHYTAcarLPNDRSS 1220
Cdd:cd02665   128 LPPVLTFELSRFEFNQGR-PEKIHDKLEFP------------QIIQQVP-YELHAVLVHEGQANAGHYWA---YIYKQSR 190
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 270265845 1221 QRsdvgWRLFDDSTVTTVDESQVVTR--------YAYVLFY 1253
Cdd:cd02665   191 QE----WEKYNDISVTESSWEEVERDsfgggrnpSAYCLMY 227
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
289-444 2.03e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 48.24  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  289 RDPEPEQEDQVKEEMALGADPTALVEEPESMVNLAFV-----KNDSYEKgPDSVVVHVYVKEIRRDSSRVLFREQDFTLI 363
Cdd:PLN03088  116 KIAEEEKDLVQPVPSDLPSSVTAPPVEEADATPVVPPskpkyRHEFYQK-PEEVVVTVFAKGVPAENVNVDFGEQILSVV 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  364 FQTrdgnflrlhPGCGPhtiFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLE-----APATRGAVGGAKVA 438
Cdd:PLN03088  195 IEV---------PGEDA---YHLQPRLFGKIIPDKCKYEVLSTKIEIRLAKAEPITWASLEygkgpAVLPKPNVSSEVSQ 262

                  ....*.
gi 270265845  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 5.28e-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: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845   58 WRQSADEVIVKLRVGTGPVRLEDVDAAFTDTDCVVRLPDGR--QWGGVFFAEIQSSCTKVQArKGGLLQLVLPKKVPLLT 135
Cdd:cd06463     1 WYQTLDEVTITIPLKDVTKKDVKVEFTPKSLTVSVKGGGGKeyLLEGELFGPIDPEESKWTV-EDRKIEITLKKKEPGEW 79

                  ....*
gi 270265845  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 5.89e-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: 5.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1123 CPQCKqHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRD-KINDLVefpvrnldLSKFCIgqkeeQLPSYDLYAVINHYG 1201
Cdd:cd02673   129 CSSCK-CESAISSERIMTFPECLSINLKRYKLRIATSDYlKKNEEI--------MKKYCG-----TDAKYSLVAVICHLG 194
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 270265845 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 6.85e-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: 6.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  337 VVVHVYVKEIRRDSSRVLFREQDFTLIFQTRDGNFLRLhpgcgphtifrwQVKLRNLIEPEQCTFCFTASRIDICLRKRQ 416
Cdd:cd06489     9 VVITILIKNVKPEDVSVEFEKRELSATVKLPSGNDYSL------------KLHLLHPIVPEQSSYKILSTKIEIKLKKTE 76

                  ....*...
gi 270265845  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 1.09e-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: 1.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 270265845 1131 EASKQLLLWRLPNVLIVQLKRFSFRSFIwRDKINDLVEFPVRNLDLSKFCIGQKEEQLPS--YDLYAVINHYGG 1202
Cdd:cd02669   322 DSLKRYLISRLPKYLIFHIKRFSKNNFF-KEKNPTIVNFPIKNLDLSDYVHFDKPSLNLStkYNLVANIVHEGT 394
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
537-642 1.68e-04

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 46.02  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  537 GFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHdrsfeaEINYNNPlgtGGRLAIGFAvLLRALWKGTHQAFQPSKLKAIV 616
Cdd:COG5077   192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY------GIPTDHP---RGRDSVALA-LQRLFYNLQTGEEPVDTTELTR 261
                          90       100
                  ....*....|....*....|....*.
gi 270265845  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 5.69e-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: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  539 TGLVNLGNTCFMNSVIQSLSNTRELRDF---FHDRSFEAEINYNNPLGTGGR--------LAIGFAVLLRALWkgthQAF 607
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLvlnFDESKAELASDYPTERRIGGRevsrselqRSNQFVYELRSLF----NDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  608 QPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGrpdEVVAEeawqrhkmrndsfIVDL 687
Cdd:cd02666    78 IHSNTRSVTPSKELAYLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDK---EQSDL-------------IKRL 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 270265845  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 2.44e-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: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845  336 SVVVHVYVKEIRRDSSRVLFREQDFT--LIFqtrDGNFlrlhpgcgphtIFRWQVKLRNLIEPEQCTFCFTASRIDICLR 413
Cdd:cd06488    11 HVVVSVYAKNSNPELSVVEANSTVLTihIVF---EGNK-----------EFQLDIELWGVIDVEKSSVNMLPTKVEIKLR 76
                          90
                  ....*....|.
gi 270265845  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 3.74e-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: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845   58 WRQSADEVIVKLRVGTGpVRLEDVDAAFTDTDCVVRLPDGRQW-GGVFFAEIQSSCT--KVQarKGGLLQLVLPKKVPLL 134
Cdd:cd06467     3 WTQTLDEVTVTIPLPEG-TKSKDVKVEITPKHLKVGVKGGEPLlDGELYAKVKVDEStwTLE--DGKLLEITLEKRNEGE 79

                  ....*.
gi 270265845  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 5.65e-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: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1104 QCLNLFTRPEVLAPEeawYCPQCKQHREASKQLLLWRLPN----VLIVQLKRF-SFRSFIWRDKI-----NDLVEFPVRN 1173
Cdd:cd02672   121 QLLKRSLDLEKVTKA---WCDTCCKYQPLEQTTSIRHLPDilllVLVINLSVTnGEFDDINVVLPsgkvmQNKVSPKAID 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265845 1174 LDLSKFCIGQKEeqLPSYDLYAVINHY-GGMIGGHYTACARLPNDRSSQRsdvGWRLFDDSTVTTVDESqvvtryAYVLF 1252
Cdd:cd02672   198 HDKLVKNRGQES--IYKYELVGYVCEInDSSRGQHNVVFVIKVNEESTHG---RWYLFNDFLVTPVSEL------AYILL 266

                  .
gi 270265845 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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