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Conserved domains on  [gi|767996213|ref|XP_011523677|]
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ubiquitin carboxyl-terminal hydrolase 32 isoform X5 [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];
508-1320 3.65e-83

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: 292.56  E-value: 3.65e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  508 PQKPGAIDNQPLVTQEPvkatsltlegGRLKrtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 586
Cdd:COG5560    66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  587 LFPrylLFLRQQPATRTQQSNIWVNMGMMSLRMfpqhlprgnvpspnaplkrvlaytgcfSRMQTIKEIHEYLSQRLRIK 666
Cdd:COG5560   134 SYP---VVFKLHWLFSINGSLINLGHDPVPHSA---------------------------SSHGTLRDLSERVMNAFVDP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  667 EEDMRLWLYNSEN-YLTLLDDEDHKLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------E 734
Cdd:COG5560   184 SDDFRLWDVVPEImGLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkE 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  735 KGATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWT 814
Cdd:COG5560   263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  815 IAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQL 891
Cdd:COG5560   343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMY 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  892 RSQVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQIL 969
Cdd:COG5560   423 KSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIK 500
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  970 LAEVHGSNIKNFPQDNQKVRLSvsgflcafEIPvpvspisassptQTDFSSSPSTNEmftlttngdlprpifipNGMPNT 1049
Cdd:COG5560   501 VMCIYYGGNYNMLEPADKVLLQ--------DIP------------QTDFVYLYETND-----------------NGIEVP 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1050 VVPCGTEKNFTNGMVNGHmPSLP---DSPFTGYIIAVhrKMMRTELYFLSSQKNRPSL--FGMPLIVPCTVHTRKKDLYD 1124
Cdd:COG5560   544 VVHLRIEKGYKSKRLFGD-PFLQlnvLIKASIYDKLV--KEFEELLVLVEMKKTDVDLvsEQVRLLREESSPSSWLKLET 620
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1125 AvwIQVSRLASPlppqeasnhaqDCDDSMgyqyPFTLRVVqkdgNSCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwd 1204
Cdd:COG5560   621 E--IDTKREEQV-----------EEEGQM----NFNDAVV----ISCEWE-----------EKRYLSLFSYDP------- 661
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1205 ptalhlryqtsqervvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILII 1284
Cdd:COG5560   662 -------------------LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILII 722
                         810       820       830
                  ....*....|....*....|....*....|....*.
gi 767996213 1285 HLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRD 1320
Cdd:COG5560   723 HLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1235-1568 1.26e-25

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.45  E-value: 1.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  1235 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1314
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  1315 flvprdpalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgtscpss 1394
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  1395 knsspnssprtlgrskgrlrlpqigsknklssskenLDASkengagqiceladalsrghvlggsqpelvtpqdhevalan 1474
Cdd:pfam00443  234 ------------------------------------LDLS---------------------------------------- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  1475 gflyeheacgngysngqlgnhseEDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1553
Cdd:pfam00443  238 -----------------------RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 767996213  1554 HPD-EIDTDSAYILFY 1568
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
227-283 3.54e-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: 3.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767996213  227 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 283
Cdd:cd00051     6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
260-332 6.39e-04

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 6.39e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767996213   260 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 332
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
508-1320 3.65e-83

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 292.56  E-value: 3.65e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  508 PQKPGAIDNQPLVTQEPvkatsltlegGRLKrtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 586
Cdd:COG5560    66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  587 LFPrylLFLRQQPATRTQQSNIWVNMGMMSLRMfpqhlprgnvpspnaplkrvlaytgcfSRMQTIKEIHEYLSQRLRIK 666
Cdd:COG5560   134 SYP---VVFKLHWLFSINGSLINLGHDPVPHSA---------------------------SSHGTLRDLSERVMNAFVDP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  667 EEDMRLWLYNSEN-YLTLLDDEDHKLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------E 734
Cdd:COG5560   184 SDDFRLWDVVPEImGLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkE 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  735 KGATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWT 814
Cdd:COG5560   263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  815 IAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQL 891
Cdd:COG5560   343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMY 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  892 RSQVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQIL 969
Cdd:COG5560   423 KSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIK 500
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  970 LAEVHGSNIKNFPQDNQKVRLSvsgflcafEIPvpvspisassptQTDFSSSPSTNEmftlttngdlprpifipNGMPNT 1049
Cdd:COG5560   501 VMCIYYGGNYNMLEPADKVLLQ--------DIP------------QTDFVYLYETND-----------------NGIEVP 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1050 VVPCGTEKNFTNGMVNGHmPSLP---DSPFTGYIIAVhrKMMRTELYFLSSQKNRPSL--FGMPLIVPCTVHTRKKDLYD 1124
Cdd:COG5560   544 VVHLRIEKGYKSKRLFGD-PFLQlnvLIKASIYDKLV--KEFEELLVLVEMKKTDVDLvsEQVRLLREESSPSSWLKLET 620
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1125 AvwIQVSRLASPlppqeasnhaqDCDDSMgyqyPFTLRVVqkdgNSCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwd 1204
Cdd:COG5560   621 E--IDTKREEQV-----------EEEGQM----NFNDAVV----ISCEWE-----------EKRYLSLFSYDP------- 661
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1205 ptalhlryqtsqervvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILII 1284
Cdd:COG5560   662 -------------------LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILII 722
                         810       820       830
                  ....*....|....*....|....*....|....*.
gi 767996213 1285 HLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRD 1320
Cdd:COG5560   723 HLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
738-931 2.67e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 181.10  E-value: 2.67e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213   738 TGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELWSGTQKN-VAPLKLRWTIA 816
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNSKSSsVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213   817 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVK 896
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 767996213   897 CKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIK 931
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQI 166
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1229-1569 5.69e-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: 5.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1229 SRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRE 1308
Cdd:cd02674    76 SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLN 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1309 SFDPSAFLVPRDPalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksg 1388
Cdd:cd02674   156 DLDLTPYVDTRSF------------------------------------------------------------------- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1389 tscpssknsspnssprtlgrskgrlrlpqigsknklssskenldaskengagqiceladalsrghvlggsqpelvtpqdh 1468
Cdd:cd02674       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1469 evalANGFLYeheacgngysngqlgnhseedstddqredtrikpiyNLYAISCHSGILGGGHYVTYAKNPNC-KWYCYND 1547
Cdd:cd02674   169 ----TGPFKY------------------------------------DLYAVVNHYGSLNGGHYTAYCKNNETnDWYKFDD 208
                         330       340
                  ....*....|....*....|..
gi 767996213 1548 SSCKELHPDEIDTDSAYILFYE 1569
Cdd:cd02674   209 SRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1235-1568 1.26e-25

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.45  E-value: 1.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  1235 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1314
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  1315 flvprdpalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgtscpss 1394
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  1395 knsspnssprtlgrskgrlrlpqigsknklssskenLDASkengagqiceladalsrghvlggsqpelvtpqdhevalan 1474
Cdd:pfam00443  234 ------------------------------------LDLS---------------------------------------- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  1475 gflyeheacgngysngqlgnhseEDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1553
Cdd:pfam00443  238 -----------------------RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 767996213  1554 HPD-EIDTDSAYILFY 1568
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1512-1568 2.64e-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: 2.64e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767996213 1512 PIYNLYAISCHSGILG-GGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1568
Cdd:cd02661   246 LKYKLYAVLVHSGFSPhSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
DUSP smart00695
Domain in ubiquitin-specific proteases;
508-575 8.16e-09

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 54.29  E-value: 8.16e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996213    508 PQKPGAIDNQPLVTQEPvkatsltleGGRLKrtPQLIHGRDYEMVPEPVWRALYHWYGANLA-LPRPVI 575
Cdd:smart00695   28 GKDPGPIDNSGILCSHG---------GPRLK--EHLVEGEDYVLIPEELWNKLVRWYGGGPGpIPRKVV 85
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1503-1570 4.37e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.35  E-value: 4.37e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767996213 1503 DQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNpNCKWYCYNDSSCKELHPDEIDT---DSAYILFYEQ 1570
Cdd:COG5533   214 DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK-GGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
227-283 3.54e-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: 3.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767996213  227 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 283
Cdd:cd00051     6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
226-283 5.43e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 5.43e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767996213   226 LFNAFDENRDNHIDFKEISCGLSACCRG-PL--AERQKFcFKVFDVDRDGVLSRVELRDMV 283
Cdd:pfam13499    7 AFKLLDSDGDGYLDVEELKKLLRKLEEGePLsdEEVEEL-FKEFDLDKDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
224-327 4.49e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 4.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  224 EGLFNAFDENRDNHIDFKEISCGLSACCRGPLAERQKFCFKVFDVDRDGVLSRVELRdmvvALLEVWKDNRTDdipelhm 303
Cdd:COG5126    36 ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFR----RLLTALGVSEEE------- 104
                          90       100
                  ....*....|....*....|....
gi 767996213  304 dlsdiVEGILNAHDTTKMGHLTLE 327
Cdd:COG5126   105 -----ADELFARLDTDGDGKISFE 123
EF-hand_7 pfam13499
EF-hand domain pair;
260-332 6.39e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 6.39e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767996213   260 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 332
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
508-1320 3.65e-83

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 292.56  E-value: 3.65e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  508 PQKPGAIDNQPLVTQEPvkatsltlegGRLKrtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 586
Cdd:COG5560    66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  587 LFPrylLFLRQQPATRTQQSNIWVNMGMMSLRMfpqhlprgnvpspnaplkrvlaytgcfSRMQTIKEIHEYLSQRLRIK 666
Cdd:COG5560   134 SYP---VVFKLHWLFSINGSLINLGHDPVPHSA---------------------------SSHGTLRDLSERVMNAFVDP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  667 EEDMRLWLYNSEN-YLTLLDDEDHKLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------E 734
Cdd:COG5560   184 SDDFRLWDVVPEImGLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkE 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  735 KGATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWT 814
Cdd:COG5560   263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  815 IAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQL 891
Cdd:COG5560   343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMY 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  892 RSQVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQIL 969
Cdd:COG5560   423 KSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIK 500
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  970 LAEVHGSNIKNFPQDNQKVRLSvsgflcafEIPvpvspisassptQTDFSSSPSTNEmftlttngdlprpifipNGMPNT 1049
Cdd:COG5560   501 VMCIYYGGNYNMLEPADKVLLQ--------DIP------------QTDFVYLYETND-----------------NGIEVP 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1050 VVPCGTEKNFTNGMVNGHmPSLP---DSPFTGYIIAVhrKMMRTELYFLSSQKNRPSL--FGMPLIVPCTVHTRKKDLYD 1124
Cdd:COG5560   544 VVHLRIEKGYKSKRLFGD-PFLQlnvLIKASIYDKLV--KEFEELLVLVEMKKTDVDLvsEQVRLLREESSPSSWLKLET 620
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1125 AvwIQVSRLASPlppqeasnhaqDCDDSMgyqyPFTLRVVqkdgNSCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwd 1204
Cdd:COG5560   621 E--IDTKREEQV-----------EEEGQM----NFNDAVV----ISCEWE-----------EKRYLSLFSYDP------- 661
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1205 ptalhlryqtsqervvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILII 1284
Cdd:COG5560   662 -------------------LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILII 722
                         810       820       830
                  ....*....|....*....|....*....|....*.
gi 767996213 1285 HLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRD 1320
Cdd:COG5560   723 HLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
738-931 2.67e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 181.10  E-value: 2.67e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213   738 TGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELWSGTQKN-VAPLKLRWTIA 816
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNSKSSsVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213   817 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVK 896
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 767996213   897 CKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIK 931
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQI 166
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1229-1569 5.69e-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: 5.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1229 SRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRE 1308
Cdd:cd02674    76 SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLN 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1309 SFDPSAFLVPRDPalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksg 1388
Cdd:cd02674   156 DLDLTPYVDTRSF------------------------------------------------------------------- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1389 tscpssknsspnssprtlgrskgrlrlpqigsknklssskenldaskengagqiceladalsrghvlggsqpelvtpqdh 1468
Cdd:cd02674       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1469 evalANGFLYeheacgngysngqlgnhseedstddqredtrikpiyNLYAISCHSGILGGGHYVTYAKNPNC-KWYCYND 1547
Cdd:cd02674   169 ----TGPFKY------------------------------------DLYAVVNHYGSLNGGHYTAYCKNNETnDWYKFDD 208
                         330       340
                  ....*....|....*....|..
gi 767996213 1548 SSCKELHPDEIDTDSAYILFYE 1569
Cdd:cd02674   209 SRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1235-1568 1.26e-25

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.45  E-value: 1.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  1235 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1314
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  1315 flvprdpalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgtscpss 1394
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  1395 knsspnssprtlgrskgrlrlpqigsknklssskenLDASkengagqiceladalsrghvlggsqpelvtpqdhevalan 1474
Cdd:pfam00443  234 ------------------------------------LDLS---------------------------------------- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  1475 gflyeheacgngysngqlgnhseEDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1553
Cdd:pfam00443  238 -----------------------RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 767996213  1554 HPD-EIDTDSAYILFY 1568
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
739-929 8.34e-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: 8.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  739 GLSNLGNTCFMNSSIQCVSNtqpltqyfisgrhlyelnrtnpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 818
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  819 aprfngfQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 898
Cdd:cd02674    21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                         170       180       190
                  ....*....|....*....|....*....|.
gi 767996213  899 TCGHISVRFDPFNFLSLPLPMDSYMHLEITV 929
Cdd:cd02674    56 TCGKTSTTFEPFTYLSLPIPSGSGDAPKVTL 86
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
737-915 2.89e-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: 2.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  737 ATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIgmkghMAKCYGDLVQELWSGTQKNVAPLKLRWTIA 816
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFC-----MMCALEAHVERALASSGPGSAPRIFSSNLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  817 KYAPRFNGFQQQDSQELLAFLLDGLHED-LNRvhekpYVELKDSDgrpdwevaaeawdnHLRRNRSIVVDLFHGQLRSQV 895
Cdd:cd02661    76 QISKHFRIGRQEDAHEFLRYLLDAMQKAcLDR-----FKKLKAVD--------------PSSQETTLVQQIFGGYLRSQV 136
                         170       180
                  ....*....|....*....|
gi 767996213  896 KCKTCGHISVRFDPFNFLSL 915
Cdd:cd02661   137 KCLNCKHVSNTYDPFLDLSL 156
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
739-918 1.87e-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: 1.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  739 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELW-SGTQKNVAPLKLRWTIAK 817
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSP---NSCLSCAMDEIFQEFYySGDRSPYGPINLLYLSWK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  818 YAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVKC 897
Cdd:cd02660    79 HSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEA---------------------NDESHCNCIIHQTFSGSLQSSVTC 137
                         170       180
                  ....*....|....*....|.
gi 767996213  898 KTCGHISVRFDPFNFLSLPLP 918
Cdd:cd02660   138 QRCGGVSTTVDPFLDLSLDIP 158
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
739-928 4.82e-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: 4.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  739 GLSNLGNTCFMNSSIQCvsntqpltqyfisgrhLYelnrtnpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 818
Cdd:cd02257     1 GLNNLGNTCYLNSVLQA----------------LF--------------------------------------------- 19
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  819 aprfngFQQQDSQELLAFLLDGLHEDLNRVHEKpyvelkdsdgrpdwevaaeawDNHLRRNRSIVVDLFHGQLRSQVKCK 898
Cdd:cd02257    20 ------SEQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                         170       180       190
                  ....*....|....*....|....*....|
gi 767996213  899 TCGHISVRFDPFNFLSLPLPMDSYMHLEIT 928
Cdd:cd02257    73 ECGHESVSTEPELFLSLPLPVKGLPQVSLE 102
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
739-935 3.97e-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: 3.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  739 GLSNLGNTCFMNSSIQCVSNTQPLTqyfisgrhlyelnrtnpigmkghmakcygdlvqELWSGTqknvaPLKLRWTIAKY 818
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALR---------------------------------ELLSET-----PKELFSQVCRK 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  819 APRFNGFQQQDSQELLAFLLDGLhedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnRSIVVDLFHGQLRSQVKCK 898
Cdd:cd02667    43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767996213  899 TCGHISVRFDPFNFLSLPLP--------MDSYMHLEITVIKLDGT 935
Cdd:cd02667    85 SCGTVSLVYEPFLDLSLPRSdeiksecsIESCLKQFTEVEILEGN 129
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1235-1328 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 767996213 1235 EPINLDSCLRAFTSEEELGENEMYYCSKCKtHCLATKKLDLWRLPPILIIHLKRFQFVN-GRWIKSQKIVKFPrESFDPS 1313
Cdd:cd02257    97 PQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFNEdGTKEKLNTKVSFP-LELDLS 174
                          90
                  ....*....|....*
gi 767996213 1314 AFLVPRDPALCQHKP 1328
Cdd:cd02257   175 PYLSEGEKDSDSDNG 189
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
739-920 7.63e-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: 7.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  739 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPI-GMKGHMAKcygdLVQELWSG--------------TQ 803
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPAnDLNCQLIK----LADGLLSGryskpaslksendpYQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  804 KNVAPLKLRWTIAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPyvelkdsdgrpdwevaaeawdnhlrrnrsiV 883
Cdd:cd02658    77 VGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLN------------------------------P 126
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767996213  884 VDLFHGQLRSQVKCKTCGHISVRFDPFNFLSLPLPMD 920
Cdd:cd02658   127 NDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKD 163
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1238-1316 1.82e-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: 1.82e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996213 1238 NLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRwiKSQKIVKFPrESFDPSAFL 1316
Cdd:cd02661   163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGG--KINKQISFP-ETLDLSPYM 238
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
739-918 5.37e-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: 5.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  739 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISgRHLYELNRTNPIGMKGHMakcygdlVQELWSGTQKNVAPLKLRWTIAKY 818
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS-LNLPRLGDSQSVMKKLQL-------LQAHLMHTQRRAEAPPDYFLEASR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  819 APRFNGFQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 898
Cdd:cd02664    73 PPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTIRCL 114
                         170       180
                  ....*....|....*....|
gi 767996213  899 TCGHISVRFDPFNFLSLPLP 918
Cdd:cd02664   115 NCNSTSARTERFRDLDLSFP 134
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1235-1318 4.22e-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: 4.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1235 EPINLDSCLRAFTSEEELGENEMYYCSKCkthCLATKKLDLWRLPPILIIHLKRF-QFVNGRWIKSQKIVKFPrESFDPS 1313
Cdd:cd02667   109 SECSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFqQPRSANLRKVSRHVSFP-EILDLA 184

                  ....*
gi 767996213 1314 AFLVP 1318
Cdd:cd02667   185 PFCDP 189
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1238-1317 1.18e-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: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1238 NLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF--VNGRWIKSQKIVKFPREsFDPSAF 1315
Cdd:cd02659   152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDRFEFPLE-LDMEPY 230

                  ..
gi 767996213 1316 LV 1317
Cdd:cd02659   231 TE 232
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1233-1306 1.21e-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: 1.21e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767996213 1233 QAEPINLDSCLRAFTSEEELGENEmYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRwiKSQKI---VKFP 1306
Cdd:cd02660   172 VSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNK--TSRKIdtyVQFP 245
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1237-1308 1.78e-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: 1.78e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767996213 1237 INLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVN--GRWIK-SQKIVkFPRE 1308
Cdd:cd02663   147 TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEqlNRYIKlFYRVV-FPLE 220
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
739-928 5.18e-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: 5.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  739 GLSNLGNTCFMNSSIQCvsntqpltqyfisgrhLYELNrtnpigmkghMAKCYGDLVQELWSGTQKN--VAPLKLRWTIA 816
Cdd:cd02663     1 GLENFGNTCYCNSVLQA----------------LYFEN----------LLTCLKDLFESISEQKKRTgvISPKKFITRLK 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  817 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVELKDSDgrpdwevaaeawDNHLRRNRSIVVDLFHGQLRSQVK 896
Cdd:cd02663    55 RENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNN------------NNNAEPQPTWVHEIFQGILTNETR 122
                         170       180       190
                  ....*....|....*....|....*....|..
gi 767996213  897 CKTCGHISVRFDPFnflsLPLPMDSYMHLEIT 928
Cdd:cd02663   123 CLTCETVSSRDETF----LDLSIDVEQNTSIT 150
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
739-951 1.50e-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: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  739 GLSNLGNTCFMNSSIQCVsNTQP-----LTQYFISGRHLYELNRTNPIGMKghmakcygDLVQELwSGTQKNVAPLKLRW 813
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCL-RSVPelrdaLKNYNPARRGANQSSDNLTNALR--------DLFDTM-DKKQEPVPPIEFLQ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  814 TIAKYAPRF------NGFQQQDSQELLAFLLDGLHEDLnrvhekpyvELKDSDGrpdwevaaeawdnhlrrnrSIVVDLF 887
Cdd:cd02657    71 LLRMAFPQFaekqnqGGYAQQDAEECWSQLLSVLSQKL---------PGAGSKG-------------------SFIDQLF 122
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767996213  888 HGQLRSQVKCKTCGHI-SVRFDPFNFLSLPLPMD---SYMH------LEITVIKLDGTtpvryglrLNMDEKYT 951
Cdd:cd02657   123 GIELETKMKCTESPDEeEVSTESEYKLQCHISITtevNYLQdglkkgLEEEIEKHSPT--------LGRDAIYT 188
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1512-1568 2.64e-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: 2.64e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767996213 1512 PIYNLYAISCHSGILG-GGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1568
Cdd:cd02661   246 LKYKLYAVLVHSGFSPhSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
509-576 2.81e-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: 2.81e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767996213   509 QKPGAIDNQPLVTqepvkatslTLEGGRLKrtPQLIHGRDYEMVPEPVWRALYHWYGANLALPRPVIK 576
Cdd:pfam06337   24 NEPGPIDNSDLLD---------DESNGQLK--PNLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRNVVN 80
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
739-926 1.03e-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: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  739 GLSNLGNTCFMNSSIQcvsntqplTQYFISG-----RHLYELNrtnpIGMKGHMAKCygDLVQELWSGTQKNVAPLKLRW 813
Cdd:cd02671    26 GLNNLGNTCYLNSVLQ--------VLYFCPGfkhglKHLVSLI----SSVEQLQSSF--LLNPEKYNDELANQAPRRLLN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  814 TIAKYAPRFNGFQQQDSQELLAFLLDGLhedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnRSIVVDLFHGQLRS 893
Cdd:cd02671    92 ALREVNPMYEGYLQHDAQEVLQCILGNI--------------------------------------QELVEKDFQGQLVL 133
                         170       180       190
                  ....*....|....*....|....*....|...
gi 767996213  894 QVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLE 926
Cdd:cd02671   134 RTRCLECETFTERREDFQDISVPVQESELSKSE 166
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1494-1571 2.20e-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: 2.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1494 NHSEEDSTDDQREDTrikpIYNLYAISCHSGILGGGHYVTYAK-NPNCKWYCYNDSSCKELHPDEID------------- 1559
Cdd:cd02659   236 AKKEGDSEKKDSESY----IYELHGVLVHSGDAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEeecfggeetqkty 311
                          90       100
                  ....*....|....*....|.
gi 767996213 1560 ---------TDSAYILFYEQQ 1571
Cdd:cd02659   312 dsgprafkrTTNAYMLFYERK 332
DUSP smart00695
Domain in ubiquitin-specific proteases;
508-575 8.16e-09

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 54.29  E-value: 8.16e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996213    508 PQKPGAIDNQPLVTQEPvkatsltleGGRLKrtPQLIHGRDYEMVPEPVWRALYHWYGANLA-LPRPVI 575
Cdd:smart00695   28 GKDPGPIDNSGILCSHG---------GPRLK--EHLVEGEDYVLIPEELWNKLVRWYGGGPGpIPRKVV 85
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1503-1570 4.37e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.35  E-value: 4.37e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767996213 1503 DQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNpNCKWYCYNDSSCKELHPDEIDT---DSAYILFYEQ 1570
Cdd:COG5533   214 DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK-GGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1238-1321 6.65e-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: 6.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1238 NLDSCLRAFTSEEEL-GENEmYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF--VNGRWIKSQKIVKFPrESFDPSA 1314
Cdd:cd02668   157 TLEECIDEFLKEEQLtGDNQ-YFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdrKTGAKKKLNASISFP-EILDMGE 234

                  ....*..
gi 767996213 1315 FLVPRDP 1321
Cdd:cd02668   235 YLAESDE 241
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
739-915 8.87e-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: 8.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  739 GLSNLGNTCFMNSSIQcvsntqplTQYFISG--RHLYELNRT-NPIGMKG---HMAKCYGDLvQELwsgtQKNVAPLKLR 812
Cdd:cd02659     4 GLKNQGATCYMNSLLQ--------QLYMTPEfrNAVYSIPPTeDDDDNKSvplALQRLFLFL-QLS----ESPVKTTELT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  813 WTIAKYAPR-FNGFQQQDSQELLAFLLDGLHEDLnrvhekPYVELKDsdgrpdwevaaeawdnhlrrnrsIVVDLFHGQL 891
Cdd:cd02659    71 DKTRSFGWDsLNTFEQHDVQEFFRVLFDKLEEKL------KGTGQEG-----------------------LIKNLFGGKL 121
                         170       180
                  ....*....|....*....|....
gi 767996213  892 RSQVKCKTCGHISVRFDPFNFLSL 915
Cdd:cd02659   122 VNYIICKECPHESEREEYFLDLQV 145
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
739-924 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 767996213  739 GLSNLGNTCFMNSSIQCVSNTQPLTQYfisgrhlyeLNRTNpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 818
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEY---------LEEFL--------------------------------------- 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  819 aprfngfQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 898
Cdd:cd02662    33 -------EQQDAHELFQVLLETLE--------------------------------------QLLKFPFDGLLASRIVCL 67
                         170       180
                  ....*....|....*....|....*..
gi 767996213  899 TCGHIS-VRFDPFNFLSLPLPMDSYMH 924
Cdd:cd02662    68 QCGESSkVRYESFTMLSLPVPNQSSGS 94
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1511-1569 2.01e-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: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1511 KPIYNLYAISCHSGILGGGHYVTYAK----------------------NPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1568
Cdd:cd02667   199 SVLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278

                  .
gi 767996213 1569 E 1569
Cdd:cd02667   279 E 279
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
739-845 2.92e-07

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 54.04  E-value: 2.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  739 GLSNLGNTCFMNSSIQCVS-NTQPLTQYfiSGRHLYELNrtnpiGMKGHMAKCYGDLVQELWSGTQKNVAPLKlrwtIAK 817
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKLDEL--LDDLSKELK-----VLKNVIRKPEPDLNQEEALKLFTALWSSK----EHK 69
                          90       100
                  ....*....|....*....|....*...
gi 767996213  818 YAPRFNGFQQQDSQELLAFLLDGLHEDL 845
Cdd:COG5533    70 VGWIPPMGSQEDAHELLGKLLDELKLDL 97
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
227-283 3.54e-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: 3.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767996213  227 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 283
Cdd:cd00051     6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1513-1568 9.86e-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: 9.86e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767996213 1513 IYNLYAISCHSGILGGGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1568
Cdd:cd02660   272 TYDLFAVVVHKGTLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1235-1291 1.56e-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: 1.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767996213 1235 EPINLDSCLRAFTSEEELGenemYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF 1291
Cdd:cd02658   176 EPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQL 228
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
736-918 2.20e-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: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  736 GATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGrHLYELNRTNpigmKGHMAKCYGDLVQELWSGT--QKNVAPLKLRW 813
Cdd:cd02669   118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLY-ENYENIKDR----KSELVKRLSELIRKIWNPRnfKGHVSPHELLQ 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  814 TIAKY-APRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdnHLRRNRSIVVDLFHGQLR 892
Cdd:cd02669   193 AVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGG---------------------------SKKPNSSIIHDCFQGKVQ 245
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767996213  893 --------------SQVKCKTCGH-ISVRFDPFNFLSLPLP 918
Cdd:cd02669   246 ietqkikphaeeegSKDKFFKDSRvKKTSVSPFLLLTLDLP 286
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1513-1569 2.25e-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: 2.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767996213 1513 IYNLYAISCHSGILG-GGHYVTYAKNPNC-KWYCYNDSSCKELHPDEI-------DTDSAYILFYE 1569
Cdd:cd02657   240 YYELVAVITHQGRSAdSGHYVAWVRRKNDgKWIKFDDDKVSEVTEEDIlklsgggDWHIAYILLYK 305
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
646-714 3.57e-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: 3.57e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767996213   646 FSRMQTIKEIHEYLSQRLRI-KEEDMRLW-LYNSENYlTLLDDEDHKLEYLKIQDEQHLVIEVRNKDMSWP 714
Cdd:pfam14836   18 FSKTDTIDFIEKELRKLFSIpKEKETRLWnRYSSNTR-ELLTDPDITVQEAGLYHGQVLLIEEKNEDGNWP 87
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1511-1569 3.72e-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: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1511 KPIYNLYAISCHSGILGGGHYVTYAKNPNC---------------------KWYCYNDSSCKELHPDEIDTD-SAYILFY 1568
Cdd:cd02662   160 KVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepgsfvrmregpsstshPWWRISDTTVKEVSESEVLEQkSAYMLFY 239

                  .
gi 767996213 1569 E 1569
Cdd:cd02662   240 E 240
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1495-1569 4.11e-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: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1495 HSEEDSTDDQREDTRIKpiYNLYAISCHSGI-LGGGHYVTYAKNPNCK---------------------WYCYNDSSCKE 1552
Cdd:cd02664   226 KEEESGDDGELVTRQVH--YRLYAVVVHSGYsSESGHYFTYARDQTDAdstgqecpepkdaeendesknWYLFNDSRVTF 303
                          90       100
                  ....*....|....*....|....
gi 767996213 1553 LHPDEIDT-------DSAYILFYE 1569
Cdd:cd02664   304 SSFESVQNvtsrfpkDTPYILFYE 327
EF-hand_7 pfam13499
EF-hand domain pair;
226-283 5.43e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 5.43e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767996213   226 LFNAFDENRDNHIDFKEISCGLSACCRG-PL--AERQKFcFKVFDVDRDGVLSRVELRDMV 283
Cdd:pfam13499    7 AFKLLDSDGDGYLDVEELKKLLRKLEEGePLsdEEVEEL-FKEFDLDKDGRISFEEFLELY 66
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1511-1568 3.42e-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: 3.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767996213 1511 KPIYNLYAISCHSGI-LGGGHYVTYAknpncKWYCYNDSSCK---------ELHPDEIDTDSAYILFY 1568
Cdd:cd02671   269 NDVYRLFAVVMHSGAtISSGHYTAYV-----RWLLFDDSEVKvteekdfleALSPNTSSTSTPYLLFY 331
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
224-327 4.49e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 4.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  224 EGLFNAFDENRDNHIDFKEISCGLSACCRGPLAERQKFCFKVFDVDRDGVLSRVELRdmvvALLEVWKDNRTDdipelhm 303
Cdd:COG5126    36 ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFR----RLLTALGVSEEE------- 104
                          90       100
                  ....*....|....*....|....
gi 767996213  304 dlsdiVEGILNAHDTTKMGHLTLE 327
Cdd:COG5126   105 -----ADELFARLDTDGDGKISFE 123
EF-hand_7 pfam13499
EF-hand domain pair;
260-332 6.39e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 6.39e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767996213   260 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 332
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1246-1292 1.02e-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: 1.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 767996213 1246 FTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFV 1292
Cdd:cd02664   143 FLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYD 189
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
180-283 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 767996213  180 HLEESDIIDLEKRYW--LLKA--QSRTGRFDLETF----GPLVSPPIRPSLsEGLFNAFDENRDNHIDFKEISCGLSACc 251
Cdd:COG5126    21 VLERDDFEALFRRLWatLFSEadTDGDGRISREEFvagmESLFEATVEPFA-RAAFDLLDTDGDGKISADEFRRLLTAL- 98
                          90       100       110
                  ....*....|....*....|....*....|..
gi 767996213  252 RGPLAERQKFcFKVFDVDRDGVLSRVELRDMV 283
Cdd:COG5126    99 GVSEEEADEL-FARLDTDGDGKISFEEFVAAV 129
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1238-1308 1.43e-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: 41.97  E-value: 1.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767996213 1238 NLDSCLRAFTSEEELgenEMYYCSKCKThclatkklDLWRLPPILIIHLKRFQF-VNGRWIKSQKIVKFPRE 1308
Cdd:cd02662    97 TLEHCLDDFLSTEII---DDYKCDRCQT--------VIVRLPQILCIHLSRSVFdGRGTSTKNSCKVSFPER 157
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1512-1569 2.15e-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: 2.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767996213 1512 PIYNLYAISCHSG-ILGGGHYVTYAKN--PNCKW-YCyNDSSCKELHPDEIDTD---SAYILFYE 1569
Cdd:cd02673   182 AKYSLVAVICHLGeSPYDGHYIAYTKElyNGSSWlYC-SDDEIRPVSKNDVSTNarsSGYLIFYD 245
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1514-1557 3.19e-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: 3.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767996213 1514 YNLYAISCHSGILGGGHYVTYAKN-PNCKWYCYNDSSCKElHPDE 1557
Cdd:cd02666   281 YRLHAVFIHRGEASSGHYWVYIKDfEENVWRKYNDETVTV-VPAS 324
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1246-1326 3.35e-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: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213 1246 FTSEEELGENEMYYcskckthclatkklDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRDPALCQ 1325
Cdd:cd02669   314 GKTETELKDSLKRY--------------LISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNL 379

                  .
gi 767996213 1326 H 1326
Cdd:cd02669   380 S 380
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1514-1568 3.52e-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: 3.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767996213 1514 YNLYAISCHSGILGGGHYVTYA-KNPNCKWYCYNDSSCKELHPDEIDTD--------SAYILFY 1568
Cdd:cd02665   164 YELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDsfgggrnpSAYCLMY 227
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
260-298 6.98e-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: 6.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 767996213  260 KFCFKVFDVDRDGVLSRVELRDMVVALLEVWKDNRTDDI 298
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. ...
227-330 8.75e-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: 38.42  E-value: 8.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996213  227 FNAFDENRDNHIDFKEIS---CGLSACCRGPLAERQkfcFKVFDVDRDGVLSRVELRDMVVALLEvwkdnrtddIPELHM 303
Cdd:cd15898     6 WIKADKDGDGKLSLKEIKkllKRLNIRVSEKELKKL---FKEVDTNGDGTLTFDEFEELYKSLTE---------RPELEP 73
                          90       100
                  ....*....|....*....|....*..
gi 767996213  304 dlsdivegILNAHDTTKMGHLTLEDYQ 330
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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