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Conserved domains on  [gi|22550104|ref|NP_115971|]
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ubiquitin carboxyl-terminal hydrolase 32 [Homo sapiens]

Protein Classification

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];
518-1316 7.01e-86

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: 300.26  E-value: 7.01e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  518 PQKPGAIDNQPLVTQEPvkatsltlegGRLKrtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 596
Cdd:COG5560   66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  597 LFPrylLFLRQQPATRTQQSNIwvNMGNVPSPNAplkrvlaytgcFSRMQTIKEIHEYLSQRLRIKEEDMRLWLYNSEN- 675
Cdd:COG5560  134 SYP---VVFKLHWLFSINGSLI--NLGHDPVPHS-----------ASSHGTLRDLSERVMNAFVDPSDDFRLWDVVPEIm 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  676 YLTLLDDEDHKLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------EKGATGLSNLGNTCF 744
Cdd:COG5560  198 GLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkEAGTCGLRNLGNTCY 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  745 MNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWTIAKYAPRFNGFQQQ 824
Cdd:COG5560  277 MNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQ 356
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  825 DSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQLRSQVKCKTCGHISV 901
Cdd:COG5560  357 DSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSI 436
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  902 RFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQILLAEVHGSNIKNFPQ 979
Cdd:COG5560  437 TFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIKVMCIYYGGNYNMLE 514
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  980 DNQKVRLSvsgflcafEIPvpvspisassptQTDFSSSPSTNEmftlttngdlprpifipNGMPNTVVPCGTEKNFTNGM 1059
Cdd:COG5560  515 PADKVLLQ--------DIP------------QTDFVYLYETND-----------------NGIEVPVVHLRIEKGYKSKR 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1060 VNGHmPSLP---DSPFTGYIIAVhrKMMRTELYFLSSQKNRPSL--FGMPLIVPCTVHTRKKDLYDAvwIQVSRLASPlp 1134
Cdd:COG5560  558 LFGD-PFLQlnvLIKASIYDKLV--KEFEELLVLVEMKKTDVDLvsEQVRLLREESSPSSWLKLETE--IDTKREEQV-- 630
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1135 pqeasnhaqDCDDSMgyqyPFTLRVVqkdgNSCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwdptalhlryqtsqer 1214
Cdd:COG5560  631 ---------EEEGQM----NFNDAVV----ISCEWE-----------EKRYLSLFSYDP--------------------- 661
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1215 vvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIK 1294
Cdd:COG5560  662 -----LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDK 736
                        810       820
                 ....*....|....*....|..
gi 22550104 1295 SQKIVKFPRESFDPSAFLVPRD 1316
Cdd:COG5560  737 IDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1231-1564 1.30e-25

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.45  E-value: 1.30e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104   1231 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1310
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104   1311 flvprdpalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgtscpss 1390
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104   1391 knsspnssprtlgrskgrlrlpqigsknklssskenLDASkengagqiceladalsrghvlggsqpelvtpqdhevalan 1470
Cdd:pfam00443  234 ------------------------------------LDLS---------------------------------------- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104   1471 gflyeheacgngysngqlgnhseEDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1549
Cdd:pfam00443  238 -----------------------RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 22550104   1550 HPD-EIDTDSAYILFY 1564
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
237-293 3.53e-06

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


:

Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 46.00  E-value: 3.53e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22550104  237 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 293
Cdd:cd00051    6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
270-342 7.04e-04

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 7.04e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22550104    270 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 342
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
518-1316 7.01e-86

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 300.26  E-value: 7.01e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  518 PQKPGAIDNQPLVTQEPvkatsltlegGRLKrtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 596
Cdd:COG5560   66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  597 LFPrylLFLRQQPATRTQQSNIwvNMGNVPSPNAplkrvlaytgcFSRMQTIKEIHEYLSQRLRIKEEDMRLWLYNSEN- 675
Cdd:COG5560  134 SYP---VVFKLHWLFSINGSLI--NLGHDPVPHS-----------ASSHGTLRDLSERVMNAFVDPSDDFRLWDVVPEIm 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  676 YLTLLDDEDHKLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------EKGATGLSNLGNTCF 744
Cdd:COG5560  198 GLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkEAGTCGLRNLGNTCY 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  745 MNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWTIAKYAPRFNGFQQQ 824
Cdd:COG5560  277 MNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQ 356
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  825 DSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQLRSQVKCKTCGHISV 901
Cdd:COG5560  357 DSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSI 436
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  902 RFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQILLAEVHGSNIKNFPQ 979
Cdd:COG5560  437 TFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIKVMCIYYGGNYNMLE 514
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  980 DNQKVRLSvsgflcafEIPvpvspisassptQTDFSSSPSTNEmftlttngdlprpifipNGMPNTVVPCGTEKNFTNGM 1059
Cdd:COG5560  515 PADKVLLQ--------DIP------------QTDFVYLYETND-----------------NGIEVPVVHLRIEKGYKSKR 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1060 VNGHmPSLP---DSPFTGYIIAVhrKMMRTELYFLSSQKNRPSL--FGMPLIVPCTVHTRKKDLYDAvwIQVSRLASPlp 1134
Cdd:COG5560  558 LFGD-PFLQlnvLIKASIYDKLV--KEFEELLVLVEMKKTDVDLvsEQVRLLREESSPSSWLKLETE--IDTKREEQV-- 630
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1135 pqeasnhaqDCDDSMgyqyPFTLRVVqkdgNSCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwdptalhlryqtsqer 1214
Cdd:COG5560  631 ---------EEEGQM----NFNDAVV----ISCEWE-----------EKRYLSLFSYDP--------------------- 661
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1215 vvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIK 1294
Cdd:COG5560  662 -----LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDK 736
                        810       820
                 ....*....|....*....|..
gi 22550104 1295 SQKIVKFPRESFDPSAFLVPRD 1316
Cdd:COG5560  737 IDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
734-927 2.71e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 181.10  E-value: 2.71e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104    734 TGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELWSGTQKN-VAPLKLRWTIA 812
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNSKSSsVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104    813 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVK 892
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 22550104    893 CKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIK 927
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQI 166
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1225-1565 5.46e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 116.62  E-value: 5.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1225 SRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRE 1304
Cdd:cd02674   76 SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLN 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1305 SFDPSAFLVPRDPalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksg 1384
Cdd:cd02674  156 DLDLTPYVDTRSF------------------------------------------------------------------- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1385 tscpssknsspnssprtlgrskgrlrlpqigsknklssskenldaskengagqiceladalsrghvlggsqpelvtpqdh 1464
Cdd:cd02674      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1465 evalANGFLYeheacgngysngqlgnhseedstddqredtrikpiyNLYAISCHSGILGGGHYVTYAKNPNC-KWYCYND 1543
Cdd:cd02674  169 ----TGPFKY------------------------------------DLYAVVNHYGSLNGGHYTAYCKNNETnDWYKFDD 208
                        330       340
                 ....*....|....*....|..
gi 22550104 1544 SSCKELHPDEIDTDSAYILFYE 1565
Cdd:cd02674  209 SRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1231-1564 1.30e-25

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.45  E-value: 1.30e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104   1231 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1310
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104   1311 flvprdpalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgtscpss 1390
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104   1391 knsspnssprtlgrskgrlrlpqigsknklssskenLDASkengagqiceladalsrghvlggsqpelvtpqdhevalan 1470
Cdd:pfam00443  234 ------------------------------------LDLS---------------------------------------- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104   1471 gflyeheacgngysngqlgnhseEDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1549
Cdd:pfam00443  238 -----------------------RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 22550104   1550 HPD-EIDTDSAYILFY 1564
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1508-1564 2.57e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 63.45  E-value: 2.57e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22550104 1508 PIYNLYAISCHSGILG-GGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1564
Cdd:cd02661  246 LKYKLYAVLVHSGFSPhSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
DUSP smart00695
Domain in ubiquitin-specific proteases;
518-585 7.98e-09

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 54.29  E-value: 7.98e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22550104     518 PQKPGAIDNQPLVTQEPvkatsltleGGRLKrtPQLIHGRDYEMVPEPVWRALYHWYGANLA-LPRPVI 585
Cdd:smart00695   28 GKDPGPIDNSGILCSHG---------GPRLK--EHLVEGEDYVLIPEELWNKLVRWYGGGPGpIPRKVV 85
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1499-1566 4.36e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.35  E-value: 4.36e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22550104 1499 DQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNpNCKWYCYNDSSCKELHPDEIDT---DSAYILFYEQ 1566
Cdd:COG5533  214 DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK-GGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
237-293 3.53e-06

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 46.00  E-value: 3.53e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22550104  237 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 293
Cdd:cd00051    6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
236-293 5.98e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 5.98e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22550104    236 LFNAFDENRDNHIDFKEISCGLSACCRG-PL--AERQKFcFKVFDVDRDGVLSRVELRDMV 293
Cdd:pfam13499    7 AFKLLDSDGDGYLDVEELKKLLRKLEEGePLsdEEVEEL-FKEFDLDKDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
234-337 4.48e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  234 EGLFNAFDENRDNHIDFKEISCGLSACCRGPLAERQKFCFKVFDVDRDGVLSRVELRdmvvALLEVWKDNRTDdipelhm 313
Cdd:COG5126   36 ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFR----RLLTALGVSEEE------- 104
                         90       100
                 ....*....|....*....|....
gi 22550104  314 dlsdiVEGILNAHDTTKMGHLTLE 337
Cdd:COG5126  105 -----ADELFARLDTDGDGKISFE 123
EF-hand_7 pfam13499
EF-hand domain pair;
270-342 7.04e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 7.04e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22550104    270 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 342
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
518-1316 7.01e-86

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 300.26  E-value: 7.01e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  518 PQKPGAIDNQPLVTQEPvkatsltlegGRLKrtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 596
Cdd:COG5560   66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  597 LFPrylLFLRQQPATRTQQSNIwvNMGNVPSPNAplkrvlaytgcFSRMQTIKEIHEYLSQRLRIKEEDMRLWLYNSEN- 675
Cdd:COG5560  134 SYP---VVFKLHWLFSINGSLI--NLGHDPVPHS-----------ASSHGTLRDLSERVMNAFVDPSDDFRLWDVVPEIm 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  676 YLTLLDDEDHKLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------EKGATGLSNLGNTCF 744
Cdd:COG5560  198 GLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkEAGTCGLRNLGNTCY 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  745 MNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWTIAKYAPRFNGFQQQ 824
Cdd:COG5560  277 MNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQ 356
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  825 DSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQLRSQVKCKTCGHISV 901
Cdd:COG5560  357 DSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSI 436
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  902 RFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQILLAEVHGSNIKNFPQ 979
Cdd:COG5560  437 TFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIKVMCIYYGGNYNMLE 514
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  980 DNQKVRLSvsgflcafEIPvpvspisassptQTDFSSSPSTNEmftlttngdlprpifipNGMPNTVVPCGTEKNFTNGM 1059
Cdd:COG5560  515 PADKVLLQ--------DIP------------QTDFVYLYETND-----------------NGIEVPVVHLRIEKGYKSKR 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1060 VNGHmPSLP---DSPFTGYIIAVhrKMMRTELYFLSSQKNRPSL--FGMPLIVPCTVHTRKKDLYDAvwIQVSRLASPlp 1134
Cdd:COG5560  558 LFGD-PFLQlnvLIKASIYDKLV--KEFEELLVLVEMKKTDVDLvsEQVRLLREESSPSSWLKLETE--IDTKREEQV-- 630
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1135 pqeasnhaqDCDDSMgyqyPFTLRVVqkdgNSCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwdptalhlryqtsqer 1214
Cdd:COG5560  631 ---------EEEGQM----NFNDAVV----ISCEWE-----------EKRYLSLFSYDP--------------------- 661
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1215 vvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIK 1294
Cdd:COG5560  662 -----LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDK 736
                        810       820
                 ....*....|....*....|..
gi 22550104 1295 SQKIVKFPRESFDPSAFLVPRD 1316
Cdd:COG5560  737 IDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
734-927 2.71e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 181.10  E-value: 2.71e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104    734 TGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELWSGTQKN-VAPLKLRWTIA 812
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNSKSSsVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104    813 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVK 892
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 22550104    893 CKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIK 927
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQI 166
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1225-1565 5.46e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 116.62  E-value: 5.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1225 SRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRE 1304
Cdd:cd02674   76 SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLN 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1305 SFDPSAFLVPRDPalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksg 1384
Cdd:cd02674  156 DLDLTPYVDTRSF------------------------------------------------------------------- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1385 tscpssknsspnssprtlgrskgrlrlpqigsknklssskenldaskengagqiceladalsrghvlggsqpelvtpqdh 1464
Cdd:cd02674      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1465 evalANGFLYeheacgngysngqlgnhseedstddqredtrikpiyNLYAISCHSGILGGGHYVTYAKNPNC-KWYCYND 1543
Cdd:cd02674  169 ----TGPFKY------------------------------------DLYAVVNHYGSLNGGHYTAYCKNNETnDWYKFDD 208
                        330       340
                 ....*....|....*....|..
gi 22550104 1544 SSCKELHPDEIDTDSAYILFYE 1565
Cdd:cd02674  209 SRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1231-1564 1.30e-25

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.45  E-value: 1.30e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104   1231 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1310
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104   1311 flvprdpalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgtscpss 1390
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104   1391 knsspnssprtlgrskgrlrlpqigsknklssskenLDASkengagqiceladalsrghvlggsqpelvtpqdhevalan 1470
Cdd:pfam00443  234 ------------------------------------LDLS---------------------------------------- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104   1471 gflyeheacgngysngqlgnhseEDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1549
Cdd:pfam00443  238 -----------------------RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 22550104   1550 HPD-EIDTDSAYILFY 1564
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-925 8.08e-23

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 98.90  E-value: 8.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  735 GLSNLGNTCFMNSSIQCVSNtqpltqyfisgrhlyelnrtnpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 814
Cdd:cd02674    1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  815 aprfngfQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 894
Cdd:cd02674   21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                        170       180       190
                 ....*....|....*....|....*....|.
gi 22550104  895 TCGHISVRFDPFNFLSLPLPMDSYMHLEITV 925
Cdd:cd02674   56 TCGKTSTTFEPFTYLSLPIPSGSGDAPKVTL 86
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
733-911 2.85e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 99.27  E-value: 2.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  733 ATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIgmkghMAKCYGDLVQELWSGTQKNVAPLKLRWTIA 812
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFC-----MMCALEAHVERALASSGPGSAPRIFSSNLK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  813 KYAPRFNGFQQQDSQELLAFLLDGLHED-LNRvhekpYVELKDSDgrpdwevaaeawdnHLRRNRSIVVDLFHGQLRSQV 891
Cdd:cd02661   76 QISKHFRIGRQEDAHEFLRYLLDAMQKAcLDR-----FKKLKAVD--------------PSSQETTLVQQIFGGYLRSQV 136
                        170       180
                 ....*....|....*....|
gi 22550104  892 KCKTCGHISVRFDPFNFLSL 911
Cdd:cd02661  137 KCLNCKHVSNTYDPFLDLSL 156
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-914 1.83e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 97.44  E-value: 1.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  735 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELW-SGTQKNVAPLKLRWTIAK 813
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSP---NSCLSCAMDEIFQEFYySGDRSPYGPINLLYLSWK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  814 YAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVKC 893
Cdd:cd02660   79 HSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEA---------------------NDESHCNCIIHQTFSGSLQSSVTC 137
                        170       180
                 ....*....|....*....|.
gi 22550104  894 KTCGHISVRFDPFNFLSLPLP 914
Cdd:cd02660  138 QRCGGVSTTVDPFLDLSLDIP 158
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
735-924 4.72e-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: 94.47  E-value: 4.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  735 GLSNLGNTCFMNSSIQCvsntqpltqyfisgrhLYelnrtnpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 814
Cdd:cd02257    1 GLNNLGNTCYLNSVLQA----------------LF--------------------------------------------- 19
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  815 aprfngFQQQDSQELLAFLLDGLHEDLNRVHEKpyvelkdsdgrpdwevaaeawDNHLRRNRSIVVDLFHGQLRSQVKCK 894
Cdd:cd02257   20 ------SEQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                        170       180       190
                 ....*....|....*....|....*....|
gi 22550104  895 TCGHISVRFDPFNFLSLPLPMDSYMHLEIT 924
Cdd:cd02257   73 ECGHESVSTEPELFLSLPLPVKGLPQVSLE 102
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-931 4.07e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 89.37  E-value: 4.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  735 GLSNLGNTCFMNSSIQCVSNTQPLTqyfisgrhlyelnrtnpigmkghmakcygdlvqELWSGTqknvaPLKLRWTIAKY 814
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALR---------------------------------ELLSET-----PKELFSQVCRK 42
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  815 APRFNGFQQQDSQELLAFLLDGLhedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnRSIVVDLFHGQLRSQVKCK 894
Cdd:cd02667   43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 22550104  895 TCGHISVRFDPFNFLSLPLP--------MDSYMHLEITVIKLDGT 931
Cdd:cd02667   85 SCGTVSLVYEPFLDLSLPRSdeiksecsIESCLKQFTEVEILEGN 129
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1231-1324 1.75e-17

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: 84.07  E-value: 1.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1231 EPINLDSCLRAFTSEEELGENEMYYCSKCKtHCLATKKLDLWRLPPILIIHLKRFQFVN-GRWIKSQKIVKFPrESFDPS 1309
Cdd:cd02257   97 PQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFNEdGTKEKLNTKVSFP-LELDLS 174
                         90
                 ....*....|....*
gi 22550104 1310 AFLVPRDPALCQHKP 1324
Cdd:cd02257  175 PYLSEGEKDSDSDNG 189
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-916 7.67e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 77.36  E-value: 7.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  735 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPI-GMKGHMAKcygdLVQELWSG--------------TQ 799
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPAnDLNCQLIK----LADGLLSGryskpaslksendpYQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  800 KNVAPLKLRWTIAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPyvelkdsdgrpdwevaaeawdnhlrrnrsiV 879
Cdd:cd02658   77 VGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLN------------------------------P 126
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 22550104  880 VDLFHGQLRSQVKCKTCGHISVRFDPFNFLSLPLPMD 916
Cdd:cd02658  127 NDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKD 163
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1234-1312 1.78e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 76.16  E-value: 1.78e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22550104 1234 NLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRwiKSQKIVKFPrESFDPSAFL 1312
Cdd:cd02661  163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGG--KINKQISFP-ETLDLSPYM 238
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-914 5.40e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 75.22  E-value: 5.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  735 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISgRHLYELNRTNPIGMKGHMakcygdlVQELWSGTQKNVAPLKLRWTIAKY 814
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS-LNLPRLGDSQSVMKKLQL-------LQAHLMHTQRRAEAPPDYFLEASR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  815 APRFNGFQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 894
Cdd:cd02664   73 PPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTIRCL 114
                        170       180
                 ....*....|....*....|
gi 22550104  895 TCGHISVRFDPFNFLSLPLP 914
Cdd:cd02664  115 NCNSTSARTERFRDLDLSFP 134
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1231-1314 4.25e-13

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: 71.65  E-value: 4.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1231 EPINLDSCLRAFTSEEELGENEMYYCSKCkthCLATKKLDLWRLPPILIIHLKRF-QFVNGRWIKSQKIVKFPrESFDPS 1309
Cdd:cd02667  109 SECSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFqQPRSANLRKVSRHVSFP-EILDLA 184

                 ....*
gi 22550104 1310 AFLVP 1314
Cdd:cd02667  185 PFCDP 189
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1234-1313 1.19e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 68.05  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1234 NLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF--VNGRWIKSQKIVKFPREsFDPSAF 1311
Cdd:cd02659  152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDRFEFPLE-LDMEPY 230

                 ..
gi 22550104 1312 LV 1313
Cdd:cd02659  231 TE 232
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1229-1302 1.20e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 67.78  E-value: 1.20e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22550104 1229 QAEPINLDSCLRAFTSEEELGENEmYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRwiKSQKI---VKFP 1302
Cdd:cd02660  172 VSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNK--TSRKIdtyVQFP 245
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1233-1304 1.79e-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: 66.95  E-value: 1.79e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22550104 1233 INLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVN--GRWIK-SQKIVkFPRE 1304
Cdd:cd02663  147 TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEqlNRYIKlFYRVV-FPLE 220
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-924 5.41e-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: 65.41  E-value: 5.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  735 GLSNLGNTCFMNSSIQCvsntqpltqyfisgrhLYELNrtnpigmkghMAKCYGDLVQELWSGTQKN--VAPLKLRWTIA 812
Cdd:cd02663    1 GLENFGNTCYCNSVLQA----------------LYFEN----------LLTCLKDLFESISEQKKRTgvISPKKFITRLK 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  813 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVELKDSDgrpdwevaaeawDNHLRRNRSIVVDLFHGQLRSQVK 892
Cdd:cd02663   55 RENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNN------------NNNAEPQPTWVHEIFQGILTNETR 122
                        170       180       190
                 ....*....|....*....|....*....|..
gi 22550104  893 CKTCGHISVRFDPFnflsLPLPMDSYMHLEIT 924
Cdd:cd02663  123 CLTCETVSSRDETF----LDLSIDVEQNTSIT 150
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-947 1.53e-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 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: 64.27  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  735 GLSNLGNTCFMNSSIQCVsNTQP-----LTQYFISGRHLYELNRTNPIGMKghmakcygDLVQELwSGTQKNVAPLKLRW 809
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCL-RSVPelrdaLKNYNPARRGANQSSDNLTNALR--------DLFDTM-DKKQEPVPPIEFLQ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  810 TIAKYAPRF------NGFQQQDSQELLAFLLDGLHEDLnrvhekpyvELKDSDGrpdwevaaeawdnhlrrnrSIVVDLF 883
Cdd:cd02657   71 LLRMAFPQFaekqnqGGYAQQDAEECWSQLLSVLSQKL---------PGAGSKG-------------------SFIDQLF 122
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22550104  884 HGQLRSQVKCKTCGHI-SVRFDPFNFLSLPLPMD---SYMH------LEITVIKLDGTtpvryglrLNMDEKYT 947
Cdd:cd02657  123 GIELETKMKCTESPDEeEVSTESEYKLQCHISITtevNYLQdglkkgLEEEIEKHSPT--------LGRDAIYT 188
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1508-1564 2.57e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 63.45  E-value: 2.57e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22550104 1508 PIYNLYAISCHSGILG-GGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1564
Cdd:cd02661  246 LKYKLYAVLVHSGFSPhSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
519-586 2.78e-10

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


Pssm-ID: 399383  Cd Length: 80  Bit Score: 58.15  E-value: 2.78e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22550104    519 QKPGAIDNQPLVTqepvkatslTLEGGRLKrtPQLIHGRDYEMVPEPVWRALYHWYGANLALPRPVIK 586
Cdd:pfam06337   24 NEPGPIDNSDLLD---------DESNGQLK--PNLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRNVVN 80
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-922 1.02e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 61.83  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  735 GLSNLGNTCFMNSSIQcvsntqplTQYFISG-----RHLYELNrtnpIGMKGHMAKCygDLVQELWSGTQKNVAPLKLRW 809
Cdd:cd02671   26 GLNNLGNTCYLNSVLQ--------VLYFCPGfkhglKHLVSLI----SSVEQLQSSF--LLNPEKYNDELANQAPRRLLN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  810 TIAKYAPRFNGFQQQDSQELLAFLLDGLhedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnRSIVVDLFHGQLRS 889
Cdd:cd02671   92 ALREVNPMYEGYLQHDAQEVLQCILGNI--------------------------------------QELVEKDFQGQLVL 133
                        170       180       190
                 ....*....|....*....|....*....|...
gi 22550104  890 QVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLE 922
Cdd:cd02671  134 RTRCLECETFTERREDFQDISVPVQESELSKSE 166
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1490-1567 2.19e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 61.12  E-value: 2.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1490 NHSEEDSTDDQREDTrikpIYNLYAISCHSGILGGGHYVTYAK-NPNCKWYCYNDSSCKELHPDEID------------- 1555
Cdd:cd02659  236 AKKEGDSEKKDSESY----IYELHGVLVHSGDAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEeecfggeetqkty 311
                         90       100
                 ....*....|....*....|.
gi 22550104 1556 ---------TDSAYILFYEQQ 1567
Cdd:cd02659  312 dsgprafkrTTNAYMLFYERK 332
DUSP smart00695
Domain in ubiquitin-specific proteases;
518-585 7.98e-09

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 54.29  E-value: 7.98e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22550104     518 PQKPGAIDNQPLVTQEPvkatsltleGGRLKrtPQLIHGRDYEMVPEPVWRALYHWYGANLA-LPRPVI 585
Cdd:smart00695   28 GKDPGPIDNSGILCSHG---------GPRLK--EHLVEGEDYVLIPEELWNKLVRWYGGGPGpIPRKVV 85
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1499-1566 4.36e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.35  E-value: 4.36e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22550104 1499 DQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNpNCKWYCYNDSSCKELHPDEIDT---DSAYILFYEQ 1566
Cdd:COG5533  214 DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK-GGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1234-1317 7.45e-08

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 56.27  E-value: 7.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1234 NLDSCLRAFTSEEEL-GENEmYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF--VNGRWIKSQKIVKFPrESFDPSA 1310
Cdd:cd02668  157 TLEECIDEFLKEEQLtGDNQ-YFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdrKTGAKKKLNASISFP-EILDMGE 234

                 ....*..
gi 22550104 1311 FLVPRDP 1317
Cdd:cd02668  235 YLAESDE 241
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-911 8.77e-08

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 56.11  E-value: 8.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  735 GLSNLGNTCFMNSSIQcvsntqplTQYFISG--RHLYELNRT-NPIGMKG---HMAKCYGDLvQELwsgtQKNVAPLKLR 808
Cdd:cd02659    4 GLKNQGATCYMNSLLQ--------QLYMTPEfrNAVYSIPPTeDDDDNKSvplALQRLFLFL-QLS----ESPVKTTELT 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  809 WTIAKYAPR-FNGFQQQDSQELLAFLLDGLHEDLnrvhekPYVELKDsdgrpdwevaaeawdnhlrrnrsIVVDLFHGQL 887
Cdd:cd02659   71 DKTRSFGWDsLNTFEQHDVQEFFRVLFDKLEEKL------KGTGQEG-----------------------LIKNLFGGKL 121
                        170       180
                 ....*....|....*....|....
gi 22550104  888 RSQVKCKTCGHISVRFDPFNFLSL 911
Cdd:cd02659  122 VNYIICKECPHESEREEYFLDLQV 145
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-920 1.48e-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: 54.29  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  735 GLSNLGNTCFMNSSIQCVSNTQPLTQYfisgrhlyeLNRTNpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 814
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEY---------LEEFL--------------------------------------- 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  815 aprfngfQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 894
Cdd:cd02662   33 -------EQQDAHELFQVLLETLE--------------------------------------QLLKFPFDGLLASRIVCL 67
                        170       180
                 ....*....|....*....|....*..
gi 22550104  895 TCGHIS-VRFDPFNFLSLPLPMDSYMH 920
Cdd:cd02662   68 QCGESSkVRYESFTMLSLPVPNQSSGS 94
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1507-1565 2.00e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 54.31  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1507 KPIYNLYAISCHSGILGGGHYVTYAK----------------------NPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1564
Cdd:cd02667  199 SVLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278

                 .
gi 22550104 1565 E 1565
Cdd:cd02667  279 E 279
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
735-841 2.91e-07

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 54.04  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  735 GLSNLGNTCFMNSSIQCVS-NTQPLTQYfiSGRHLYELNrtnpiGMKGHMAKCYGDLVQELWSGTQKNVAPLKlrwtIAK 813
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDEL--LDDLSKELK-----VLKNVIRKPEPDLNQEEALKLFTALWSSK----EHK 69
                         90       100
                 ....*....|....*....|....*...
gi 22550104  814 YAPRFNGFQQQDSQELLAFLLDGLHEDL 841
Cdd:COG5533   70 VGWIPPMGSQEDAHELLGKLLDELKLDL 97
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
237-293 3.53e-06

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 46.00  E-value: 3.53e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22550104  237 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 293
Cdd:cd00051    6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1509-1564 9.58e-06

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 49.68  E-value: 9.58e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 22550104 1509 IYNLYAISCHSGILGGGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1564
Cdd:cd02660  272 TYDLFAVVVHKGTLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1231-1287 1.54e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 48.86  E-value: 1.54e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 22550104 1231 EPINLDSCLRAFTSEEELGenemYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF 1287
Cdd:cd02658  176 EPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQL 228
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
732-914 2.14e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 48.85  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  732 GATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGrHLYELNRTNpigmKGHMAKCYGDLVQELWSGT--QKNVAPLKLRW 809
Cdd:cd02669  118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLY-ENYENIKDR----KSELVKRLSELIRKIWNPRnfKGHVSPHELLQ 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  810 TIAKY-APRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdnHLRRNRSIVVDLFHGQLR 888
Cdd:cd02669  193 AVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGG---------------------------SKKPNSSIIHDCFQGKVQ 245
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 22550104  889 --------------SQVKCKTCGH-ISVRFDPFNFLSLPLP 914
Cdd:cd02669  246 ietqkikphaeeegSKDKFFKDSRvKKTSVSPFLLLTLDLP 286
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1509-1565 2.30e-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 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: 48.10  E-value: 2.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22550104 1509 IYNLYAISCHSGILG-GGHYVTYAKNPNC-KWYCYNDSSCKELHPDEI-------DTDSAYILFYE 1565
Cdd:cd02657  240 YYELVAVITHQGRSAdSGHYVAWVRRKNDgKWIKFDDDKVSEVTEEDIlklsgggDWHIAYILLYK 305
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
642-710 3.71e-05

Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin carboxyl-terminal hydrolases and in gametogenetin-binding protein.


Pssm-ID: 405518  Cd Length: 88  Bit Score: 43.69  E-value: 3.71e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22550104    642 FSRMQTIKEIHEYLSQRLRI-KEEDMRLW-LYNSENYlTLLDDEDHKLEYLKIQDEQHLVIEVRNKDMSWP 710
Cdd:pfam14836   18 FSKTDTIDFIEKELRKLFSIpKEKETRLWnRYSSNTR-ELLTDPDITVQEAGLYHGQVLLIEEKNEDGNWP 87
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1507-1565 3.71e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 46.98  E-value: 3.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1507 KPIYNLYAISCHSGILGGGHYVTYAKNPNC---------------------KWYCYNDSSCKELHPDEIDTD-SAYILFY 1564
Cdd:cd02662  160 KVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepgsfvrmregpsstshPWWRISDTTVKEVSESEVLEQkSAYMLFY 239

                 .
gi 22550104 1565 E 1565
Cdd:cd02662  240 E 240
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1491-1565 4.06e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 47.49  E-value: 4.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1491 HSEEDSTDDQREDTRIKpiYNLYAISCHSGI-LGGGHYVTYAKNPNCK---------------------WYCYNDSSCKE 1548
Cdd:cd02664  226 KEEESGDDGELVTRQVH--YRLYAVVVHSGYsSESGHYFTYARDQTDAdstgqecpepkdaeendesknWYLFNDSRVTF 303
                         90       100
                 ....*....|....*....|....
gi 22550104 1549 LHPDEIDT-------DSAYILFYE 1565
Cdd:cd02664  304 SSFESVQNvtsrfpkDTPYILFYE 327
EF-hand_7 pfam13499
EF-hand domain pair;
236-293 5.98e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 5.98e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22550104    236 LFNAFDENRDNHIDFKEISCGLSACCRG-PL--AERQKFcFKVFDVDRDGVLSRVELRDMV 293
Cdd:pfam13499    7 AFKLLDSDGDGYLDVEELKKLLRKLEEGePLsdEEVEEL-FKEFDLDKDGRISFEEFLELY 66
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1507-1564 3.41e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 44.88  E-value: 3.41e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22550104 1507 KPIYNLYAISCHSGI-LGGGHYVTYAknpncKWYCYNDSSCK---------ELHPDEIDTDSAYILFY 1564
Cdd:cd02671  269 NDVYRLFAVVMHSGAtISSGHYTAYV-----RWLLFDDSEVKvteekdfleALSPNTSSTSTPYLLFY 331
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
234-337 4.48e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  234 EGLFNAFDENRDNHIDFKEISCGLSACCRGPLAERQKFCFKVFDVDRDGVLSRVELRdmvvALLEVWKDNRTDdipelhm 313
Cdd:COG5126   36 ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFR----RLLTALGVSEEE------- 104
                         90       100
                 ....*....|....*....|....
gi 22550104  314 dlsdiVEGILNAHDTTKMGHLTLE 337
Cdd:COG5126  105 -----ADELFARLDTDGDGKISFE 123
EF-hand_7 pfam13499
EF-hand domain pair;
270-342 7.04e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 7.04e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22550104    270 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 342
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1242-1288 1.00e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 43.25  E-value: 1.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 22550104 1242 FTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFV 1288
Cdd:cd02664  143 FLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYD 189
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
190-293 1.35e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  190 HLEESDIIDLEKRYW--LLKA--QSRTGRFDLETF----GPLVSPPIRPSLsEGLFNAFDENRDNHIDFKEISCGLSACc 261
Cdd:COG5126   21 VLERDDFEALFRRLWatLFSEadTDGDGRISREEFvagmESLFEATVEPFA-RAAFDLLDTDGDGKISADEFRRLLTAL- 98
                         90       100       110
                 ....*....|....*....|....*....|..
gi 22550104  262 RGPLAERQKFcFKVFDVDRDGVLSRVELRDMV 293
Cdd:COG5126   99 GVSEEEADEL-FARLDTDGDGKISFEEFVAAV 129
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1234-1304 1.39e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 42.35  E-value: 1.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22550104 1234 NLDSCLRAFTSEEELgenEMYYCSKCKThclatkklDLWRLPPILIIHLKRFQF-VNGRWIKSQKIVKFPRE 1304
Cdd:cd02662   97 TLEHCLDDFLSTEII---DDYKCDRCQT--------VIVRLPQILCIHLSRSVFdGRGTSTKNSCKVSFPER 157
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1508-1565 2.20e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 41.75  E-value: 2.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22550104 1508 PIYNLYAISCHSG-ILGGGHYVTYAKN--PNCKW-YCyNDSSCKELHPDEIDTD---SAYILFYE 1565
Cdd:cd02673  182 AKYSLVAVICHLGeSPYDGHYIAYTKElyNGSSWlYC-SDDEIRPVSKNDVSTNarsSGYLIFYD 245
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1510-1553 3.26e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 41.71  E-value: 3.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 22550104 1510 YNLYAISCHSGILGGGHYVTYAKN-PNCKWYCYNDSSCKElHPDE 1553
Cdd:cd02666  281 YRLHAVFIHRGEASSGHYWVYIKDfEENVWRKYNDETVTV-VPAS 324
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1242-1322 3.37e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 41.92  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104 1242 FTSEEELGENEMYYcskckthclatkklDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRDPALCQ 1321
Cdd:cd02669  314 GKTETELKDSLKRY--------------LISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNL 379

                 .
gi 22550104 1322 H 1322
Cdd:cd02669  380 S 380
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1510-1564 3.51e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 41.00  E-value: 3.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22550104 1510 YNLYAISCHSGILGGGHYVTYA-KNPNCKWYCYNDSSCKELHPDEIDTD--------SAYILFY 1564
Cdd:cd02665  164 YELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDsfgggrnpSAYCLMY 227
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
270-308 6.96e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 36.37  E-value: 6.96e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 22550104  270 KFCFKVFDVDRDGVLSRVELRDMVVALLEVWKDNRTDDI 308
Cdd:cd00051    3 REAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEM 41
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
237-340 9.15e-03

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 38.03  E-value: 9.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22550104  237 FNAFDENRDNHIDFKEIS---CGLSACCRGPLAERQkfcFKVFDVDRDGVLSRVELRDMVVALLEvwkdnrtddIPELHM 313
Cdd:cd15898    6 WIKADKDGDGKLSLKEIKkllKRLNIRVSEKELKKL---FKEVDTNGDGTLTFDEFEELYKSLTE---------RPELEP 73
                         90       100
                 ....*....|....*....|....*..
gi 22550104  314 dlsdivegILNAHDTTKMGHLTLEDYQ 340
Cdd:cd15898   74 --------IFKKYAGTNRDYMTLEEFI 92
 
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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