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Conserved domains on  [gi|1189398226|ref|NP_001338031|]
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ubiquitin carboxyl-terminal hydrolase 19 isoform 9 [Homo sapiens]

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];
480-1202 1.31e-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: 391.55  E-value: 1.31e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  480 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHHAFQPSKLKA 559
Cdd:COG5560    262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  560 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 636
Cdd:COG5560    342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  637 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpvfyfarepHSKPIKFLvsvsKENSTASEV-LDSLSQSVHVKPENL 715
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVF----PESGRRQPLkIELDASSTIRGLKKL 486
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  716 RLAEviknrfhrvflpshsldtvspSDTLLCFELLSSELAKERVVVlEVQQRPQVPSVPISKCAACQRKQQSEDEklkrc 795
Cdd:COG5560    487 VDAE---------------------YGKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG----- 539
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  796 trcyrVGYCnqlcqKTHWPDHKGLCRPENIGYPFLvsvpasrltyarlaqllegyarySVSVFQPPFqpGRMALESQSPG 875
Cdd:COG5560    540 -----IEVP-----VVHLRIEKGYKSKRLFGDPFL-----------------------QLNVLIKAS--IYDKLVKEFEE 584
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  876 CTTLLSTGSLEAG-DSERDPIQPPE------LQLVTpmaEGDTglPRVWAAPDRGPVPStsgissemlasgpievgslpa 948
Cdd:COG5560    585 LLVLVEMKKTDVDlVSEQVRLLREEsspsswLKLET---EIDT--KREEQVEEEGQMNF--------------------- 638
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  949 gervsrPEAAVPGYQHPSEAMNahtpqfFIYKIDSSNREQRLEDKGDTPlelgddcslalvwrnnerlqefvlvaskele 1028
Cdd:COG5560    639 ------NDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------- 675
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1029 caedpgsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDK 1107
Cdd:COG5560    676 -----------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDK 736
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1108 INDLVEFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQ 1187
Cdd:COG5560    737 IDDLVEYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPED 808
                          730
                   ....*....|....*
gi 1189398226 1188 VVTRYAYVLFYRRRN 1202
Cdd:COG5560    809 SVTSSAYVLFYRRKS 823
USP19_linker pfam16602
Linker region of USP19 deubiquitinase; This region is generally located between a CS domain ...
360-482 1.66e-58

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: 197.06  E-value: 1.66e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  360 RQSQRWGGLEAPAARGAVGGAKVAVPTGPTPLDSTPPGGAPHPLTGQEEARAVEKDKSKARSEDTGLDSVATRTPMEHVT 439
Cdd:pfam16602    1 RHSQRWGGLEAPATQGAVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1189398226  440 PKPETHLASPKPTCMVPPMPHSPVSGDSVeeEEEEEKKVCLPG 482
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 ...
273-369 4.17e-21

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: 88.80  E-value: 4.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  273 DSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNflrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASR 352
Cdd:cd06466      1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                           90
                   ....*....|....*..
gi 1189398226  353 IDICLRKRQSQRWGGLE 369
Cdd:cd06466     68 VEITLKKAEPGSWPSLE 84
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
105-187 2.53e-06

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: 46.51  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  105 WRQSAEEVIVKLRV-GVGPlqlEDVDAAFTDT--DCVVRFAGGQ--QWGGVFYAEIKSSCAKVqTRKGSLLHLTLPKKVP 179
Cdd:cd06463      1 WYQTLDEVTITIPLkDVTK---KDVKVEFTPKslTVSVKGGGGKeyLLEGELFGPIDPEESKW-TVEDRKIEITLKKKEP 76

                   ....*...
gi 1189398226  180 MLTWPSLL 187
Cdd:cd06463     77 GEWWPRLE 84
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
480-1202 1.31e-119

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 391.55  E-value: 1.31e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  480 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHHAFQPSKLKA 559
Cdd:COG5560    262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  560 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 636
Cdd:COG5560    342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  637 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpvfyfarepHSKPIKFLvsvsKENSTASEV-LDSLSQSVHVKPENL 715
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVF----PESGRRQPLkIELDASSTIRGLKKL 486
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  716 RLAEviknrfhrvflpshsldtvspSDTLLCFELLSSELAKERVVVlEVQQRPQVPSVPISKCAACQRKQQSEDEklkrc 795
Cdd:COG5560    487 VDAE---------------------YGKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG----- 539
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  796 trcyrVGYCnqlcqKTHWPDHKGLCRPENIGYPFLvsvpasrltyarlaqllegyarySVSVFQPPFqpGRMALESQSPG 875
Cdd:COG5560    540 -----IEVP-----VVHLRIEKGYKSKRLFGDPFL-----------------------QLNVLIKAS--IYDKLVKEFEE 584
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  876 CTTLLSTGSLEAG-DSERDPIQPPE------LQLVTpmaEGDTglPRVWAAPDRGPVPStsgissemlasgpievgslpa 948
Cdd:COG5560    585 LLVLVEMKKTDVDlVSEQVRLLREEsspsswLKLET---EIDT--KREEQVEEEGQMNF--------------------- 638
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  949 gervsrPEAAVPGYQHPSEAMNahtpqfFIYKIDSSNREQRLEDKGDTPlelgddcslalvwrnnerlqefvlvaskele 1028
Cdd:COG5560    639 ------NDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------- 675
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1029 caedpgsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDK 1107
Cdd:COG5560    676 -----------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDK 736
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1108 INDLVEFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQ 1187
Cdd:COG5560    737 IDDLVEYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPED 808
                          730
                   ....*....|....*
gi 1189398226 1188 VVTRYAYVLFYRRRN 1202
Cdd:COG5560    809 SVTSSAYVLFYRRKS 823
USP19_linker pfam16602
Linker region of USP19 deubiquitinase; This region is generally located between a CS domain ...
360-482 1.66e-58

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: 197.06  E-value: 1.66e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  360 RQSQRWGGLEAPAARGAVGGAKVAVPTGPTPLDSTPPGGAPHPLTGQEEARAVEKDKSKARSEDTGLDSVATRTPMEHVT 439
Cdd:pfam16602    1 RHSQRWGGLEAPATQGAVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1189398226  440 PKPETHLASPKPTCMVPPMPHSPVSGDSVeeEEEEEKKVCLPG 482
Cdd:pfam16602   81 IKQEPLLTSPKPTCMVPPMTHSPVSSESV--EEEEEKKVCLPG 121
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1042-1199 5.38e-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: 5.38e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1042 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFrSFIWRDKINDLVEFPVRNLDL 1121
Cdd:cd02674     81 APKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSF-SRGSTRKLTTPVTFPLNDLDL 159
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189398226 1122 SKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvGWRLFDDSTVTTVDESQVVTRYAYVLFYR 1199
Cdd:cd02674    160 TPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETN-------DWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
484-671 2.77e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 174.94  E-value: 2.77e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  484 TGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTggrLAIGFAVLLRALWKGTHH-AFQPSKLKAIVA 562
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNSKSsSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  563 SKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQGQYKSKLV 642
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180
                   ....*....|....*....|....*....
gi 1189398226  643 CPVCAKVSITFDPFLYLPVPLPQKQKVLP 671
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 ...
273-369 4.17e-21

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: 88.80  E-value: 4.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  273 DSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNflrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASR 352
Cdd:cd06466      1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                           90
                   ....*....|....*..
gi 1189398226  353 IDICLRKRQSQRWGGLE 369
Cdd:cd06466     68 VEITLKKAEPGSWPSLE 84
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
105-187 2.53e-06

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: 46.51  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  105 WRQSAEEVIVKLRV-GVGPlqlEDVDAAFTDT--DCVVRFAGGQ--QWGGVFYAEIKSSCAKVqTRKGSLLHLTLPKKVP 179
Cdd:cd06463      1 WYQTLDEVTITIPLkDVTK---KDVKVEFTPKslTVSVKGGGGKeyLLEGELFGPIDPEESKW-TVEDRKIEITLKKKEP 76

                   ....*...
gi 1189398226  180 MLTWPSLL 187
Cdd:cd06463     77 GEWWPRLE 84
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
270-359 5.32e-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: 45.33  E-value: 5.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  270 VKNDSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNFLRLHpgcgphttfrwqvKLRNLIEPEQCTFCFT 349
Cdd:pfam04969    1 PRYDWYQT-LDEVTITIPVKGAGIKKKDVKVNIKPRSLKVKIKGGYELIDG-------------ELFHPIDPEESSWTIE 66
                           90
                   ....*....|
gi 1189398226  350 ASRIDICLRK 359
Cdd:pfam04969   67 GKKVEITLKK 76
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
241-419 2.11e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 48.24  E-value: 2.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  241 DDCAKEEM---------AVAADAATLVDEPESMVNLAFV-----KNDSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFT 306
Cdd:PLN03088   114 DEKIAEEEkdlvqpvpsDLPSSVTAPPVEEADATPVVPPskpkyRHEFYQK-PEEVVVTVFAKGVPAENVNVDFGEQILS 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  307 LIFQTrdgnflrlhPGCGPhttFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEApaargavgGAKVAVPT 386
Cdd:PLN03088   193 VVIEV---------PGEDA---YHLQPRLFGKIIPDKCKYEVLSTKIEIRLAKAEPITWASLEY--------GKGPAVLP 252
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1189398226  387 GPTpldsTPPGGAPHPLTGQEEARAVEKDKSKA 419
Cdd:PLN03088   253 KPN----VSSEVSQRPAYPSSKKKKDDWDKLEA 281
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
104-176 6.78e-03

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: 36.85  E-value: 6.78e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189398226  104 DWRQSAEEVIVKLRVGVGPLQLEDVDAAFTDTDCVVRFAGGQQW-GGVFYAEIKSSCAKVqTRKGSLLHLTLPK 176
Cdd:pfam04969    4 DWYQTLDEVTITIPVKGAGIKKKDVKVNIKPRSLKVKIKGGYELiDGELFHPIDPEESSW-TIEGKKVEITLKK 76
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
480-1202 1.31e-119

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 391.55  E-value: 1.31e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  480 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHHAFQPSKLKA 559
Cdd:COG5560    262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  560 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 636
Cdd:COG5560    342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  637 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpvfyfarepHSKPIKFLvsvsKENSTASEV-LDSLSQSVHVKPENL 715
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVF----PESGRRQPLkIELDASSTIRGLKKL 486
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  716 RLAEviknrfhrvflpshsldtvspSDTLLCFELLSSELAKERVVVlEVQQRPQVPSVPISKCAACQRKQQSEDEklkrc 795
Cdd:COG5560    487 VDAE---------------------YGKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG----- 539
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  796 trcyrVGYCnqlcqKTHWPDHKGLCRPENIGYPFLvsvpasrltyarlaqllegyarySVSVFQPPFqpGRMALESQSPG 875
Cdd:COG5560    540 -----IEVP-----VVHLRIEKGYKSKRLFGDPFL-----------------------QLNVLIKAS--IYDKLVKEFEE 584
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  876 CTTLLSTGSLEAG-DSERDPIQPPE------LQLVTpmaEGDTglPRVWAAPDRGPVPStsgissemlasgpievgslpa 948
Cdd:COG5560    585 LLVLVEMKKTDVDlVSEQVRLLREEsspsswLKLET---EIDT--KREEQVEEEGQMNF--------------------- 638
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  949 gervsrPEAAVPGYQHPSEAMNahtpqfFIYKIDSSNREQRLEDKGDTPlelgddcslalvwrnnerlqefvlvaskele 1028
Cdd:COG5560    639 ------NDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------- 675
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1029 caedpgsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDK 1107
Cdd:COG5560    676 -----------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDK 736
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1108 INDLVEFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQ 1187
Cdd:COG5560    737 IDDLVEYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPED 808
                          730
                   ....*....|....*
gi 1189398226 1188 VVTRYAYVLFYRRRN 1202
Cdd:COG5560    809 SVTSSAYVLFYRRKS 823
USP19_linker pfam16602
Linker region of USP19 deubiquitinase; This region is generally located between a CS domain ...
360-482 1.66e-58

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: 197.06  E-value: 1.66e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  360 RQSQRWGGLEAPAARGAVGGAKVAVPTGPTPLDSTPPGGAPHPLTGQEEARAVEKDKSKARSEDTGLDSVATRTPMEHVT 439
Cdd:pfam16602    1 RHSQRWGGLEAPATQGAVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1189398226  440 PKPETHLASPKPTCMVPPMPHSPVSGDSVeeEEEEEKKVCLPG 482
Cdd:pfam16602   81 IKQEPLLTSPKPTCMVPPMTHSPVSSESV--EEEEEKKVCLPG 121
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1042-1199 5.38e-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: 5.38e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1042 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFrSFIWRDKINDLVEFPVRNLDL 1121
Cdd:cd02674     81 APKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSF-SRGSTRKLTTPVTFPLNDLDL 159
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189398226 1122 SKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvGWRLFDDSTVTTVDESQVVTRYAYVLFYR 1199
Cdd:cd02674    160 TPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETN-------DWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
484-671 2.77e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 174.94  E-value: 2.77e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  484 TGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTggrLAIGFAVLLRALWKGTHH-AFQPSKLKAIVA 562
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNSKSsSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  563 SKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQGQYKSKLV 642
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180
                   ....*....|....*....|....*....
gi 1189398226  643 CPVCAKVSITFDPFLYLPVPLPQKQKVLP 671
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELK 160
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1047-1198 1.32e-46

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 169.93  E-value: 1.32e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1047 LDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWrDKINDLVEFPvRNLDLSKFCI 1126
Cdd:pfam00443  164 LQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTW-EKLNTEVEFP-LELDLSRYLA 241
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189398226 1127 G---QKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSsqrsdvgWRLFDDSTVTTVDES-QVVTRYAYVLFY 1198
Cdd:pfam00443  242 EelkPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNR-------WYKFDDEKVTEVDEEtAVLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1046-1199 1.65e-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: 1.65e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1046 TLDQCLNLFTRPEVLAPEEAWYCPqCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPvRNLDLSKFC 1125
Cdd:cd02257    100 SLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFP-LELDLSPYL 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1126 IGQKEEQLPS-----YDLYAVINHYGGMI-GGHYTACARlpnDRSSQRsdvgWRLFDDSTVTTVDESQVVTRY-----AY 1194
Cdd:cd02257    178 SEGEKDSDSDngsykYELVAVVVHSGTSAdSGHYVAYVK---DPSDGK----WYKFNDDKVTEVSEEEVLEFGslsssAY 250

                   ....*
gi 1189398226 1195 VLFYR 1199
Cdd:cd02257    251 ILFYE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1034-1198 2.33e-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: 2.33e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1034 GSAGEAARAGHFTLDQCLNLFTRPEVLAPEeAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVE 1113
Cdd:cd02660    165 WALGESGVSGTPTLSDCLDRFTRPEKLGDF-AYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQ 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1114 FPVRnLDLSKFCIGQKEEQLPS--------YDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvgWRLFDDSTVTTVDE 1185
Cdd:cd02660    244 FPLE-LNMTPYTSSSIGDTQDSnsldpdytYDLFAVVVHKGTLDTGHYTAYCRQGDGQ--------WFKFDDAMITRVSE 314
                          170
                   ....*....|...
gi 1189398226 1186 SQVVTRYAYVLFY 1198
Cdd:cd02660    315 EEVLKSQAYLLFY 327
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1046-1198 3.52e-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: 130.86  E-value: 3.52e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1046 TLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFsfrSFIWRDKINDLVEFPVRnLDLSKFc 1125
Cdd:cd02661    163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF---SNFRGGKINKQISFPET-LDLSPY- 237
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189398226 1126 IGQKEEQLPSYDLYAVINHYGGMI-GGHYTACARLPNDRssqrsdvgWRLFDDSTVTTVDESQVVTRYAYVLFY 1198
Cdd:cd02661    238 MSQPNDGPLKYKLYAVLVHSGFSPhSGHYYCYVKSSNGK--------WYNMDDSKVSPVSIETVLSQKAYILFY 303
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1045-1199 3.18e-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: 3.18e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1045 FTLDQCLNLFTRPEVLAPEEAWYCPQCKqhrEASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRnLDLSKF 1124
Cdd:cd02667    111 CSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEI-LDLAPF 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1125 C----IGQKEEQLPSYDLYAVINHYGGMIGGHYTACARL--PNDRSS-------QRSDVG-----WRLFDDSTVTTVDES 1186
Cdd:cd02667    187 CdpkcNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVrpPQQRLSdltkskpAADEAGpgsgqWYYISDSDVREVSLE 266
                          170
                   ....*....|...
gi 1189398226 1187 QVVTRYAYVLFYR 1199
Cdd:cd02667    267 EVLKSEAYLLFYE 279
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
485-671 4.38e-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: 4.38e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  485 GLVNLGNTCFMNSVIQSLSNTrelrdffhdrsfeaeinynnplgtggrlaigfavllralwkgthhafqpsklkaivask 564
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSAD----------------------------------------------------------- 21
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  565 asqftgyaQHDAQEFMAFLLDGLHedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrndSFIVDLFQGQYKSKLVCP 644
Cdd:cd02674     22 --------QQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                          170       180
                   ....*....|....*....|....*..
gi 1189398226  645 VCAKVSITFDPFLYLPVPLPQKQKVLP 671
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSGDAP 82
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1051-1202 7.86e-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: 7.86e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1051 LNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRsfiW----RDKINDLVEFPVRnLDLSKFCI 1126
Cdd:cd02659    157 LDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFD---FetmmRIKINDRFEFPLE-LDMEPYTE 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1127 ----------GQKEEQLPSYDLYAVINHYGGMIGGHYTACARlpndrssQRSDVGWRLFDDSTVTTVDESQVVTRY---- 1192
Cdd:cd02659    233 kglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYSYIK-------DRDDGKWYKFNDDVVTPFDPNDAEEECfgge 305
                          170       180
                   ....*....|....*....|....*...
gi 1189398226 1193 ------------------AYVLFYRRRN 1202
Cdd:cd02659    306 etqktydsgprafkrttnAYMLFYERKS 333
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1044-1198 5.46e-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: 5.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1044 HFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWR-DKINDLVEFPvrnLDLS 1122
Cdd:cd02663    146 NTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFP---LELR 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1123 KF-CIGQKEEQLPSYDLYAVINHYGGMIG-GHYTacarlpndrSSQRSDVGWRLFDDSTVTTVDESQVVTRY-------- 1192
Cdd:cd02663    223 LFnTTDDAENPDRLYELVAVVVHIGGGPNhGHYV---------SIVKSHGGWLLFDDETVEKIDENAVEEFFgdspnqat 293

                   ....*.
gi 1189398226 1193 AYVLFY 1198
Cdd:cd02663    294 AYVLFY 299
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
485-668 2.22e-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: 2.22e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  485 GLVNLGNTCFMNSVIQSLSNTrelrdffhdrsfeaeinynnplgtggrlaigfavllralwkgthhafqpsklkaivask 564
Cdd:cd02257      1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  565 asqftgyaQHDAQEFMAFLLDGLHEDLNRIQNKpytetvdsdgrpdevvaeeawQRHKMRNDSFIVDLFQGQYKSKLVCP 644
Cdd:cd02257     22 --------QQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                          170       180
                   ....*....|....*....|....
gi 1189398226  645 VCAKVSITFDPFLYLPVPLPQKQK 668
Cdd:cd02257     73 ECGHESVSTEPELFLSLPLPVKGL 96
p23_CS_SGT1_like cd06466
p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 ...
273-369 4.17e-21

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: 88.80  E-value: 4.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  273 DSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNflrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASR 352
Cdd:cd06466      1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                           90
                   ....*....|....*..
gi 1189398226  353 IDICLRKRQSQRWGGLE 369
Cdd:cd06466     68 VEITLKKAEPGSWPSLE 84
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
484-661 8.33e-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: 94.65  E-value: 8.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  484 TGLVNLGNTCFMNSVIQSLSNTRELRDFFhdRSFEAEINYNNPlgtggrlaiGFAVLL-------RALW---KGTHHAFQ 553
Cdd:cd02661      2 AGLQNLGNTCFLNSVLQCLTHTPPLANYL--LSREHSKDCCNE---------GFCMMCaleahveRALAssgPGSAPRIF 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  554 PSKLKAIvaskASQFTGYAQHDAQEFMAFLLDGLHED-LNRiqNKPYTETVDSDgrpdevvaeeawqrhkmRNDSFIVDL 632
Cdd:cd02661     71 SSNLKQI----SKHFRIGRQEDAHEFLRYLLDAMQKAcLDR--FKKLKAVDPSS-----------------QETTLVQQI 127
                          170       180
                   ....*....|....*....|....*....
gi 1189398226  633 FQGQYKSKLVCPVCAKVSITFDPFLYLPV 661
Cdd:cd02661    128 FGGYLRSQVKCLNCKHVSNTYDPFLDLSL 156
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
485-666 3.63e-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: 3.63e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  485 GLVNLGNTCFMNSVIQSLSNTRELRDFF----HDR-----------SFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTH 549
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFlsdrHSCtclscspnsclSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHSR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  550 HafqpsklkaivaskasqFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYtetvdsdgrpdevvaeeawqrHKMRNDSFI 629
Cdd:cd02660     82 N-----------------LAGYSQQDAHEFFQFLLDQLHTHYGGDKNEAN---------------------DESHCNCII 123
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1189398226  630 VDLFQGQYKSKLVCPVCAKVSITFDPFLYLPVPLPQK 666
Cdd:cd02660    124 HQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNK 160
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1042-1199 2.81e-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: 2.81e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1042 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFIWRDKINDLVEFPvRNLD 1120
Cdd:cd02668    153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdRKTGAKKKLNASISFP-EILD 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1121 LSKFCIGQKeEQLPSYDLYAVINHYG-GMIGGHYTAcarlpNDRSSQRSDvgWRLFDDSTVTTVDESQV----------- 1188
Cdd:cd02668    232 MGEYLAESD-EGSYVYELSGVLIHQGvSAYSGHYIA-----HIKDEQTGE--WYKFNDEDVEEMPGKPLklgnsedpakp 303
                          170       180
                   ....*....|....*....|.
gi 1189398226 1189 ----------VTRYAYVLFYR 1199
Cdd:cd02668    304 rkseikkgthSSRTAYMLVYK 324
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1051-1199 1.90e-16

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 82.15  E-value: 1.90e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1051 LNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFIWRDK------INDLVEFPVRNLDLSK 1123
Cdd:cd02664    140 LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYdQKTHVREKimdnvsINEVLSLPVRVESKSS 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1124 FCIGQKEE-----------QLPSYDLYAVINHYG-GMIGGHYTACAR-------------LPNDRSSQRSDVGWRLFDDS 1178
Cdd:cd02664    220 ESPLEKKEeesgddgelvtRQVHYRLYAVVVHSGySSESGHYFTYARdqtdadstgqecpEPKDAEENDESKNWYLFNDS 299
                          170       180
                   ....*....|....*....|....*...
gi 1189398226 1179 TVTTVD--ESQVVTRY-----AYVLFYR 1199
Cdd:cd02664    300 RVTFSSfeSVQNVTSRfpkdtPYILFYE 327
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
485-670 3.21e-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: 3.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  485 GLVNLGNTCFMNSVIQSLSNTRELRDFFHDRsfeaeinynnplgtggrlaigfavllralwkgthhafqPSKLKAIVASK 564
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  565 ASQFTGYAQHDAQEFMAFLLDGLhedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrnDSFIVDLFQGQYKSKLVCP 644
Cdd:cd02667     43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84
                          170       180
                   ....*....|....*....|....*.
gi 1189398226  645 VCAKVSITFDPFLYLPVPLPQKQKVL 670
Cdd:cd02667     85 SCGTVSLVYEPFLDLSLPRSDEIKSE 110
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
485-678 1.43e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 79.46  E-value: 1.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  485 GLVNLGNTCFMNSVIQSLsntrelrdfFHDRSFEAEINYNNPLGTGGRLAIGFA-VLLRALWKGTHHAFQPSKLKAIVAS 563
Cdd:cd02664      1 GLINLGNTCYMNSVLQAL---------FMAKDFRRQVLSLNLPRLGDSQSVMKKlQLLQAHLMHTQRRAEAPPDYFLEAS 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  564 KASQFTGYAQHDAQEFMAFLLDGLHedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrndSFIVDLFQGQYKSKLVC 643
Cdd:cd02664     72 RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTIRC 113
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1189398226  644 PVCAKVSITFDPFLYLPVPLPQKQKVLPvFYFARE 678
Cdd:cd02664    114 LNCNSTSARTERFRDLDLSFPSVQDLLN-YFLSPE 147
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1014-1199 5.67e-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: 77.63  E-value: 5.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1014 ERLQEF----VLVASKELECAEDPGSAGEAARAGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNV 1089
Cdd:cd02671    145 ERREDFqdisVPVQESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEV 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1090 LIVQLKRFSFRSFIWR-----DKINDLVEFPvrnLDLSKFCIGQKeEQLPSYDLYAVINHYGGMIG-GHYTACARlpndr 1163
Cdd:cd02671    225 ITIHLKCFAANGSEFDcygglSKVNTPLLTP---LKLSLEEWSTK-PKNDVYRLFAVVMHSGATISsGHYTAYVR----- 295
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1189398226 1164 ssqrsdvgWRLFDDSTVTTVDE---------SQVVTRYAYVLFYR 1199
Cdd:cd02671    296 --------WLLFDDSEVKVTEEkdflealspNTSSTSTPYLLFYK 332
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
480-666 3.61e-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: 76.59  E-value: 3.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  480 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFhdrsfeaeINYNNPLGTGGR---LAIGFAVLLRALWkgTHHAFQ--- 553
Cdd:cd02669    116 LPGFVGLNNIKNNDYANVIIQALSHVKPIRNFF--------LLYENYENIKDRkseLVKRLSELIRKIW--NPRNFKghv 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  554 -PSK-LKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiQNKPYTETVDS--DG------RPDEVVAEEAWQRHKM 623
Cdd:cd02669    186 sPHElLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGG-SKKPNSSIIHDcfQGkvqietQKIKPHAEEEGSKDKF 264
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1189398226  624 RNDSFivdlfqgQYKSKLVcpvcakvsitfdPFLYLPVPLPQK 666
Cdd:cd02669    265 FKDSR-------VKKTSVS------------PFLLLTLDLPPP 288
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1074-1199 3.02e-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: 3.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1074 HREA--SKQLLLWRLPNVLIVQLKRFSFRSFI-WRDKINDLVEFPVrNLDLSKFCIgqkeeqlPS--YDLYAVINHYG-G 1147
Cdd:cd02657    182 GRDAiyTKTSRISRLPKYLTVQFVRFFWKRDIqKKAKILRKVKFPF-ELDLYELCT-------PSgyYELVAVITHQGrS 253
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1189398226 1148 MIGGHYTACARLPNDRSsqrsdvgWRLFDDSTVTTVDESQVVT-------RYAYVLFYR 1199
Cdd:cd02657    254 ADSGHYVAWVRRKNDGK-------WIKFDDDKVSEVTEEDILKlsgggdwHIAYILLYK 305
zf-MYND pfam01753
MYND finger;
778-820 5.00e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 61.28  E-value: 5.00e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1189398226  778 CAACQRkqqsEDEKLKRCTRCYRVGYCNQLCQKTHWPDHKGLC 820
Cdd:pfam01753    1 CAVCGK----EALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
485-609 7.10e-12

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 67.52  E-value: 7.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  485 GLVNLGNTCFMNSVIQSLS------NTRELRDFFHDRSFEAEINYNNPLGTgGRLAIGFavlLRALWKGTHHAFqpsklk 558
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILAlylpklDELLDDLSKELKVLKNVIRKPEPDLN-QEEALKL---FTALWSSKEHKV------ 70
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1189398226  559 aivaskASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRP 609
Cdd:COG5533     71 ------GWIPPMGSQEDAHELLGKLLDELKLDLVNSFTIRIFKTTKDKKKT 115
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1046-1200 1.05e-11

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 67.13  E-value: 1.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1046 TLDQCLNLFtrpEVLAPE---------EAWYCpQCKQHREASKQlllwRLPNVLIVQLKRFSFRsfIWRDKINDLVEFPV 1116
Cdd:COG5533    138 TLQEFIDNM---EELVDDetgvkakenEELEV-QAKQEYEVSFV----KLPKILTIQLKRFANL--GGNQKIDTEVDEKF 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1117 rNLDLSKFCIGQKEEQLpSYDLYAVINHYGGMIGGHYTACARLPNDrssqrsdvgWRLFDDSTVTTVDESQVVT---RYA 1193
Cdd:COG5533    208 -ELPVKHDQILNIVKET-YYDLVGFVLHQGSLEGGHYIAYVKKGGK---------WEKANDSDVTPVSEEEAINekaKNA 276

                   ....*..
gi 1189398226 1194 YVLFYRR 1200
Cdd:COG5533    277 YLYFYER 283
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
1046-1188 1.19e-11

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 69.51  E-value: 1.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1046 TLDQCLNLFTRPEVLAPEEAWYCpQCKQHREASKQLLLWRLPNVLIVQLKRFSFRsfIWRD---KINDLVEFPVrNLDLS 1122
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNA-EKHGLQDAKKGVIFESLPPVLHLQLKRFEYD--FERDmmvKINDRYEFPL-EIDLL 414
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189398226 1123 KFC---IGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSsqrsdvgWRLFDDSTVTTVDESQV 1188
Cdd:COG5077    415 PFLdrdADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGR-------WYKFDDTRVTRATEKEV 476
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
485-665 2.73e-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: 2.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  485 GLVNLGNTCFMNSVIQSLSNT---RELRDFFHDRSfeaeinyNNPLGTGgrlaigfavllralwkgthhAFQPSKLKAIV 561
Cdd:cd02663      1 GLENFGNTCYCNSVLQALYFEnllTCLKDLFESIS-------EQKKRTG--------------------VISPKKFITRL 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  562 ASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRPDEvvaeeaWQRhkmrndSFIVDLFQGQYKSKL 641
Cdd:cd02663     54 KRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAE------PQP------TWVHEIFQGILTNET 121
                          170       180
                   ....*....|....*....|....
gi 1189398226  642 VCPVCAKVSITFDPFLYLPVPLPQ 665
Cdd:cd02663    122 RCLTCETVSSRDETFLDLSIDVEQ 145
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1046-1198 4.50e-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: 4.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1046 TLDQCLNLFTRPEVLapeEAWYCPQCkqhreaskQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRnldLSKfc 1125
Cdd:cd02662     97 TLEHCLDDFLSTEII---DDYKCDRC--------QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPER---LPK-- 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1126 igqkeeqlPSYDLYAVINHYGGMIGGHYTACARLP-----NDRSSQRSDVG---------WRLfDDSTVTTVDESQVVTR 1191
Cdd:cd02662    161 --------VLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdKEPGSFVRMREgpsstshpwWRI-SDTTVKEVSESEVLEQ 231

                   ....*...
gi 1189398226 1192 -YAYVLFY 1198
Cdd:cd02662    232 kSAYMLFY 239
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
485-643 7.05e-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: 65.04  E-value: 7.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  485 GLVNLGNTCFMNSVIQSLSNTRELRDffhdrsfeAEINYNNPLGTGGRLAIGFAVLLRALWK---GTHHAFQPSKLKAIV 561
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPELRD--------ALKNYNPARRGANQSSDNLTNALRDLFDtmdKKQEPVPPIEFLQLL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  562 ASKASQFT------GYAQHDAQEFMAFLLDGLHEDLnriqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQG 635
Cdd:cd02657     73 RMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKL----------------------------PGAGSKGSFIDQLFGI 124

                   ....*...
gi 1189398226  636 QYKSKLVC 643
Cdd:cd02657    125 ELETKMKC 132
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
485-663 4.40e-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: 62.34  E-value: 4.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  485 GLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNP----------LGTG---GRLAIgfAVLLRALWKGTHHA 551
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPandlncqlikLADGllsGRYSK--PASLKSENDPYQVG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  552 FQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTetvdsdgrpdevvaeeawqrhkmrndsfivD 631
Cdd:cd02658     79 IKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPN------------------------------D 128
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1189398226  632 LFQGQYKSKLVCPVCAKVSITFDP--FLYLPVPL 663
Cdd:cd02658    129 LFKFMIEDRLECLSCKKVKYTSELseILSLPVPK 162
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1046-1199 1.09e-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: 1.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1046 TLDQCLNLFTRPEVLapEEawYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFiWRD-KINDLVEFPvrnldlskf 1124
Cdd:cd02658    179 PLEDCLKAYFAPETI--ED--FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLEN-WVPkKLDVPIDVP--------- 244
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189398226 1125 cigqkEEQLPS-YDLYAVINHYGGMI-GGHYTACARLPNDRSSQrsdvgWRLFDDSTVTTVDESQVVTRYAYVLFYR 1199
Cdd:cd02658    245 -----EELGPGkYELIAFISHKGTSVhSGHYVAHIKKEIDGEGK-----WVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
279-369 2.44e-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: 55.37  E-value: 2.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  279 PDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNflrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASRIDICLR 358
Cdd:cd06463      5 LDEVTITIPLKDVTKKDVKVEFTPKSLTVSVKGGGGK------------EYLLEGELFGPIDPEESKWTVEDRKIEITLK 72
                           90
                   ....*....|..
gi 1189398226  359 KRQ-SQRWGGLE 369
Cdd:cd06463     73 KKEpGEWWPRLE 84
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
456-589 2.34e-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: 54.13  E-value: 2.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  456 PPMPHSPVSgdsveeeeeEEKKVCLPGFTGLVNLGNTCFMNSVIQSLsntRELRDFFHDRSFEAEINynnplGTGGRLAI 535
Cdd:cd02671      6 APQPSSATS---------CEKRENLLPFVGLNNLGNTCYLNSVLQVL---YFCPGFKHGLKHLVSLI-----SSVEQLQS 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1189398226  536 GFaVLLRALWKGTHHAFQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHE 589
Cdd:cd02671     69 SF-LLNPEKYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
482-661 2.62e-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: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  482 GFTGLVNLGNTCFMNSVIQSLSNTRELRD----FFHDRSFEAEINYNNPLgtggRLAIGFAvllralwkgthhafQPSKL 557
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNavysIPPTEDDDDNKSVPLAL----QRLFLFL--------------QLSES 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  558 KAIVAS-KASQFT-------GYAQHDAQEFMAFLLDGLhedlnriqnkpytetvdsdgrpdevvaEEAWQrhKMRNDSFI 629
Cdd:cd02659     63 PVKTTElTDKTRSfgwdslnTFEQHDVQEFFRVLFDKL---------------------------EEKLK--GTGQEGLI 113
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1189398226  630 VDLFQGQYKSKLVCPVCAKVSITFDPFLYLPV 661
Cdd:cd02659    114 KNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
485-511 8.69e-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: 8.69e-07
                           10        20
                   ....*....|....*....|....*..
gi 1189398226  485 GLVNLGNTCFMNSVIQSLSNTRELRDF 511
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLIEY 27
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
105-187 2.53e-06

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: 46.51  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  105 WRQSAEEVIVKLRV-GVGPlqlEDVDAAFTDT--DCVVRFAGGQ--QWGGVFYAEIKSSCAKVqTRKGSLLHLTLPKKVP 179
Cdd:cd06463      1 WYQTLDEVTITIPLkDVTK---KDVKVEFTPKslTVSVKGGGGKeyLLEGELFGPIDPEESKW-TVEDRKIEITLKKKEP 76

                   ....*...
gi 1189398226  180 MLTWPSLL 187
Cdd:cd06463     77 GEWWPRLE 84
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
270-359 5.32e-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: 45.33  E-value: 5.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  270 VKNDSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNFLRLHpgcgphttfrwqvKLRNLIEPEQCTFCFT 349
Cdd:pfam04969    1 PRYDWYQT-LDEVTITIPVKGAGIKKKDVKVNIKPRSLKVKIKGGYELIDG-------------ELFHPIDPEESSWTIE 66
                           90
                   ....*....|
gi 1189398226  350 ASRIDICLRK 359
Cdd:pfam04969   67 GKKVEITLKK 76
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1086-1198 1.67e-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: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1086 LPNVLIVQLKRFSFRSFIwRDKINDLVEFPvrnldlskfcigQKEEQLPsYDLYAVINHYGGMIGGHYTAcarLPNDRSS 1165
Cdd:cd02665    128 LPPVLTFELSRFEFNQGR-PEKIHDKLEFP------------QIIQQVP-YELHAVLVHEGQANAGHYWA---YIYKQSR 190
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1189398226 1166 QRsdvgWRLFDDSTVTTVDESQVVTR--------YAYVLFY 1198
Cdd:cd02665    191 QE----WEKYNDISVTESSWEEVERDsfgggrnpSAYCLMY 227
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
241-419 2.11e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 48.24  E-value: 2.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  241 DDCAKEEM---------AVAADAATLVDEPESMVNLAFV-----KNDSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFT 306
Cdd:PLN03088   114 DEKIAEEEkdlvqpvpsDLPSSVTAPPVEEADATPVVPPskpkyRHEFYQK-PEEVVVTVFAKGVPAENVNVDFGEQILS 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  307 LIFQTrdgnflrlhPGCGPhttFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEApaargavgGAKVAVPT 386
Cdd:PLN03088   193 VVIEV---------PGEDA---YHLQPRLFGKIIPDKCKYEVLSTKIEIRLAKAEPITWASLEY--------GKGPAVLP 252
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1189398226  387 GPTpldsTPPGGAPHPLTGQEEARAVEKDKSKA 419
Cdd:PLN03088   253 KPN----VSSEVSQRPAYPSSKKKKDDWDKLEA 281
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1068-1198 5.61e-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: 5.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1068 CPQCKqHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRD-KINDLVefpvrnldLSKFCIgqkeeQLPSYDLYAVINHYG 1146
Cdd:cd02673    129 CSSCK-CESAISSERIMTFPECLSINLKRYKLRIATSDYlKKNEEI--------MKKYCG-----TDAKYSLVAVICHLG 194
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1189398226 1147 -GMIGGHYTACARLPNDRSSqrsdvgWRLFDDSTVTTVDESQV---VTRYAYVLFY 1198
Cdd:cd02673    195 eSPYDGHYIAYTKELYNGSS------WLYCSDDEIRPVSKNDVstnARSSGYLIFY 244
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1076-1147 1.03e-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: 1.03e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189398226 1076 EASKQLLLWRLPNVLIVQLKRFSFRSFIwRDKINDLVEFPVRNLDLSKFCIGQKEEQLPS--YDLYAVINHYGG 1147
Cdd:cd02669    322 DSLKRYLISRLPKYLIFHIKRFSKNNFF-KEKNPTIVNFPIKNLDLSDYVHFDKPSLNLStkYNLVANIVHEGT 394
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
484-684 1.13e-04

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 45.95  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  484 TGLVNLGNTCFMNSVIQSLSNTRELRDF---FHDRSFEAEINYNNPLGTGGR--------LAIGFAVLLRALWkgthHAF 552
Cdd:cd02666      2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLvlnFDESKAELASDYPTERRIGGRevsrselqRSNQFVYELRSLF----NDL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  553 QPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGrpdEVVAEeawqrhkmrndsfIVDL 632
Cdd:cd02666     78 IHSNTRSVTPSKELAYLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDK---EQSDL-------------IKRL 141
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1189398226  633 FQGQYKSKLV---CPVCAKVSITFDPFLYLPVPLPQKQKVLPVfyfarEPHSKPI 684
Cdd:cd02666    142 FSGKTKQQLVpesMGNQPSVRTKTERFLSLLVDVGKKGREIVV-----LLEPKDL 191
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
482-587 2.78e-04

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 45.25  E-value: 2.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  482 GFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHdrsfeaEINYNNPlgtGGRLAIGFAvlLRALWKGTHHAFQP-SKLKAI 560
Cdd:COG5077    192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY------GIPTDHP---RGRDSVALA--LQRLFYNLQTGEEPvDTTELT 260
                           90       100
                   ....*....|....*....|....*..
gi 1189398226  561 VASKASQFTGYAQHDAQEFMAFLLDGL 587
Cdd:COG5077    261 RSFGWDSDDSFMQHDIQEFNRVLQDNL 287
p23_CS_hSgt1_like cd06489
p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related ...
282-369 3.05e-04

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: 40.82  E-value: 3.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  282 VVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNFLRLhpgcgphttfrwQVKLRNLIEPEQCTFCFTASRIDICLRKRQ 361
Cdd:cd06489      9 VVITILIKNVKPEDVSVEFEKRELSATVKLPSGNDYSL------------KLHLLHPIVPEQSSYKILSTKIEIKLKKTE 76

                   ....*...
gi 1189398226  362 SQRWGGLE 369
Cdd:cd06489     77 AIRWSKLE 84
USP7_C2 pfam14533
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ...
655-744 3.56e-04

Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific proteases has no known function.


Pssm-ID: 464201  Cd Length: 204  Bit Score: 43.24  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  655 PFLY--LPVPLPQKQKVLPV-FYFAREPHSKPIKFLVSVSKeNSTASEVLDSLSQSVHVKPE---NLRLAEVIKNRFHRV 728
Cdd:pfam14533    1 ALYYevLDISLSELENKKSIkVTWLSPGLKKEEELELLVPK-NGTVADLLEELQKKVKLSEEgsgKIRLYEVSNHKIYKE 79
                           90
                   ....*....|....*.
gi 1189398226  729 FLPSHSLDTVSPSDTL 744
Cdd:pfam14533   80 LSEDEPIDSLNDYLTL 95
p23_NUDC_like cd06467
p23_like domain of NUD (nuclear distribution) C and similar proteins. Aspergillus nidulas (An) ...
105-187 4.41e-04

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: 40.22  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  105 WRQSAEEVIVKLRVGVGpLQLEDVDAAFTDTDCVVRFAGGQQW-GGVFYAEIKSSCAkVQTR-KGSLLHLTLPKKVPMLT 182
Cdd:cd06467      3 WTQTLDEVTVTIPLPEG-TKSKDVKVEITPKHLKVGVKGGEPLlDGELYAKVKVDES-TWTLeDGKLLEITLEKRNEGEW 80

                   ....*
gi 1189398226  183 WPSLL 187
Cdd:cd06467     81 WPSLV 85
p23_melusin_like cd06488
p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related ...
281-369 4.89e-04

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: 40.36  E-value: 4.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226  281 SVVVHVYVKEICRDTSRVLFREQDFT--LIFqtrDGNFlrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASRIDICLR 358
Cdd:cd06488     11 HVVVSVYAKNSNPELSVVEANSTVLTihIVF---EGNK-----------EFQLDIELWGVIDVEKSSVNMLPTKVEIKLR 76
                           90
                   ....*....|.
gi 1189398226  359 KRQSQRWGGLE 369
Cdd:cd06488     77 KAEPGSWAKLE 87
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1049-1198 5.39e-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: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1049 QCLNLFTRPEVLAPEeawYCPQCKQHREASKQLLLWRLPN----VLIVQLKRF-SFRSFIWRDKI-----NDLVEFPVRN 1118
Cdd:cd02672    121 QLLKRSLDLEKVTKA---WCDTCCKYQPLEQTTSIRHLPDilllVLVINLSVTnGEFDDINVVLPsgkvmQNKVSPKAID 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398226 1119 LDLSKFCIGQKEeqLPSYDLYAVINHY-GGMIGGHYTACARLPNDRSSQRsdvGWRLFDDSTVTTVDESqvvtryAYVLF 1197
Cdd:cd02672    198 HDKLVKNRGQES--IYKYELVGYVCEInDSSRGQHNVVFVIKVNEESTHG---RWYLFNDFLVTPVSEL------AYILL 266

                   .
gi 1189398226 1198 Y 1198
Cdd:cd02672    267 Y 267
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
104-176 6.78e-03

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: 36.85  E-value: 6.78e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189398226  104 DWRQSAEEVIVKLRVGVGPLQLEDVDAAFTDTDCVVRFAGGQQW-GGVFYAEIKSSCAKVqTRKGSLLHLTLPK 176
Cdd:pfam04969    4 DWYQTLDEVTITIPVKGAGIKKKDVKVNIKPRSLKVKIKGGYELiDGELFHPIDPEESSW-TIEGKKVEITLKK 76
 
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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