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Conserved domains on  [gi|767996211|ref|XP_011523676|]
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ubiquitin carboxyl-terminal hydrolase 32 isoform X4 [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];
515-1327 2.98e-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: 2.98e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  515 PQKPGAIDNQPLVTQEPvkatsltlegGRLKrtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 593
Cdd:COG5560    66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  594 LFPrylLFLRQQPATRTQQSNIWVNMGMMSLRMfpqhlprgnvpspnaplkrvlaytgcfSRMQTIKEIHEYLSQRLRIK 673
Cdd:COG5560   134 SYP---VVFKLHWLFSINGSLINLGHDPVPHSA---------------------------SSHGTLRDLSERVMNAFVDP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  674 EEDMRLWLYNSEN-YLTLLDDEDHKLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------E 741
Cdd:COG5560   184 SDDFRLWDVVPEImGLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkE 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  742 KGATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWT 821
Cdd:COG5560   263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  822 IAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQL 898
Cdd:COG5560   343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMY 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  899 RSQVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQIL 976
Cdd:COG5560   423 KSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIK 500
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  977 LAEVHGSNIKNFPQDNQKVRLSvsgflcafEIPvpvspisassptQTDFSSSPSTNEmftlttngdlprpifipNGMPNT 1056
Cdd:COG5560   501 VMCIYYGGNYNMLEPADKVLLQ--------DIP------------QTDFVYLYETND-----------------NGIEVP 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1057 VVPCGTEKNFTNGMVNGHmPSLP---DSPFTGYIIAVhrKMMRTELYFLSSQKNRPSL--FGMPLIVPCTVHTRKKDLYD 1131
Cdd:COG5560   544 VVHLRIEKGYKSKRLFGD-PFLQlnvLIKASIYDKLV--KEFEELLVLVEMKKTDVDLvsEQVRLLREESSPSSWLKLET 620
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1132 AvwIQVSRLASPlppqeasnhaqDCDDSMgyqyPFTLRVVqkdgNSCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwd 1211
Cdd:COG5560   621 E--IDTKREEQV-----------EEEGQM----NFNDAVV----ISCEWE-----------EKRYLSLFSYDP------- 661
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1212 ptalhlryqtsqervvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILII 1291
Cdd:COG5560   662 -------------------LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILII 722
                         810       820       830
                  ....*....|....*....|....*....|....*.
gi 767996211 1292 HLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRD 1327
Cdd:COG5560   723 HLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1242-1575 1.01e-25

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.45  E-value: 1.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  1242 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1321
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  1322 flvprdpalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgtscpss 1401
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  1402 knsspnssprtlgrskgrlrlpqigsknklssskenLDASkengagqiceladalsrghvlggsqpelvtpqdhevalan 1481
Cdd:pfam00443  234 ------------------------------------LDLS---------------------------------------- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  1482 gflyeheacgngysngqlgnhseEDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1560
Cdd:pfam00443  238 -----------------------RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 767996211  1561 HPD-EIDTDSAYILFY 1575
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
234-290 3.56e-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: 3.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767996211  234 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 290
Cdd:cd00051     6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
267-339 5.65e-04

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 5.65e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767996211   267 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 339
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
515-1327 2.98e-83

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 292.56  E-value: 2.98e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  515 PQKPGAIDNQPLVTQEPvkatsltlegGRLKrtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 593
Cdd:COG5560    66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  594 LFPrylLFLRQQPATRTQQSNIWVNMGMMSLRMfpqhlprgnvpspnaplkrvlaytgcfSRMQTIKEIHEYLSQRLRIK 673
Cdd:COG5560   134 SYP---VVFKLHWLFSINGSLINLGHDPVPHSA---------------------------SSHGTLRDLSERVMNAFVDP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  674 EEDMRLWLYNSEN-YLTLLDDEDHKLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------E 741
Cdd:COG5560   184 SDDFRLWDVVPEImGLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkE 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  742 KGATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWT 821
Cdd:COG5560   263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  822 IAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQL 898
Cdd:COG5560   343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMY 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  899 RSQVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQIL 976
Cdd:COG5560   423 KSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIK 500
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  977 LAEVHGSNIKNFPQDNQKVRLSvsgflcafEIPvpvspisassptQTDFSSSPSTNEmftlttngdlprpifipNGMPNT 1056
Cdd:COG5560   501 VMCIYYGGNYNMLEPADKVLLQ--------DIP------------QTDFVYLYETND-----------------NGIEVP 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1057 VVPCGTEKNFTNGMVNGHmPSLP---DSPFTGYIIAVhrKMMRTELYFLSSQKNRPSL--FGMPLIVPCTVHTRKKDLYD 1131
Cdd:COG5560   544 VVHLRIEKGYKSKRLFGD-PFLQlnvLIKASIYDKLV--KEFEELLVLVEMKKTDVDLvsEQVRLLREESSPSSWLKLET 620
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1132 AvwIQVSRLASPlppqeasnhaqDCDDSMgyqyPFTLRVVqkdgNSCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwd 1211
Cdd:COG5560   621 E--IDTKREEQV-----------EEEGQM----NFNDAVV----ISCEWE-----------EKRYLSLFSYDP------- 661
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1212 ptalhlryqtsqervvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILII 1291
Cdd:COG5560   662 -------------------LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILII 722
                         810       820       830
                  ....*....|....*....|....*....|....*.
gi 767996211 1292 HLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRD 1327
Cdd:COG5560   723 HLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
745-938 2.21e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 181.10  E-value: 2.21e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211   745 TGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELWSGTQKN-VAPLKLRWTIA 823
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNSKSSsVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211   824 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVK 903
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 767996211   904 CKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIK 938
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQI 166
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1236-1576 5.30e-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: 5.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1236 SRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRE 1315
Cdd:cd02674    76 SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLN 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1316 SFDPSAFLVPRDPalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksg 1395
Cdd:cd02674   156 DLDLTPYVDTRSF------------------------------------------------------------------- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1396 tscpssknsspnssprtlgrskgrlrlpqigsknklssskenldaskengagqiceladalsrghvlggsqpelvtpqdh 1475
Cdd:cd02674       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1476 evalANGFLYeheacgngysngqlgnhseedstddqredtrikpiyNLYAISCHSGILGGGHYVTYAKNPNC-KWYCYND 1554
Cdd:cd02674   169 ----TGPFKY------------------------------------DLYAVVNHYGSLNGGHYTAYCKNNETnDWYKFDD 208
                         330       340
                  ....*....|....*....|..
gi 767996211 1555 SSCKELHPDEIDTDSAYILFYE 1576
Cdd:cd02674   209 SRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1242-1575 1.01e-25

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.45  E-value: 1.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  1242 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1321
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  1322 flvprdpalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgtscpss 1401
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  1402 knsspnssprtlgrskgrlrlpqigsknklssskenLDASkengagqiceladalsrghvlggsqpelvtpqdhevalan 1481
Cdd:pfam00443  234 ------------------------------------LDLS---------------------------------------- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  1482 gflyeheacgngysngqlgnhseEDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1560
Cdd:pfam00443  238 -----------------------RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 767996211  1561 HPD-EIDTDSAYILFY 1575
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1519-1575 2.68e-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: 2.68e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767996211 1519 PIYNLYAISCHSGILG-GGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1575
Cdd:cd02661   246 LKYKLYAVLVHSGFSPhSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
DUSP smart00695
Domain in ubiquitin-specific proteases;
515-582 8.20e-09

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 54.29  E-value: 8.20e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996211    515 PQKPGAIDNQPLVTQEPvkatsltleGGRLKrtPQLIHGRDYEMVPEPVWRALYHWYGANLA-LPRPVI 582
Cdd:smart00695   28 GKDPGPIDNSGILCSHG---------GPRLK--EHLVEGEDYVLIPEELWNKLVRWYGGGPGpIPRKVV 85
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1510-1577 4.39e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.35  E-value: 4.39e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767996211 1510 DQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNpNCKWYCYNDSSCKELHPDEIDT---DSAYILFYEQ 1577
Cdd:COG5533   214 DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK-GGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
234-290 3.56e-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: 3.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767996211  234 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 290
Cdd:cd00051     6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
233-290 4.76e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 4.76e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767996211   233 LFNAFDENRDNHIDFKEISCGLSACCRG-PL--AERQKFcFKVFDVDRDGVLSRVELRDMV 290
Cdd:pfam13499    7 AFKLLDSDGDGYLDVEELKKLLRKLEEGePLsdEEVEEL-FKEFDLDKDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
231-334 4.51e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  231 EGLFNAFDENRDNHIDFKEISCGLSACCRGPLAERQKFCFKVFDVDRDGVLSRVELRdmvvALLEVWKDNRTDdipelhm 310
Cdd:COG5126    36 ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFR----RLLTALGVSEEE------- 104
                          90       100
                  ....*....|....*....|....
gi 767996211  311 dlsdiVEGILNAHDTTKMGHLTLE 334
Cdd:COG5126   105 -----ADELFARLDTDGDGKISFE 123
EF-hand_7 pfam13499
EF-hand domain pair;
267-339 5.65e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 5.65e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767996211   267 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 339
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
515-1327 2.98e-83

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 292.56  E-value: 2.98e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  515 PQKPGAIDNQPLVTQEPvkatsltlegGRLKrtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 593
Cdd:COG5560    66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  594 LFPrylLFLRQQPATRTQQSNIWVNMGMMSLRMfpqhlprgnvpspnaplkrvlaytgcfSRMQTIKEIHEYLSQRLRIK 673
Cdd:COG5560   134 SYP---VVFKLHWLFSINGSLINLGHDPVPHSA---------------------------SSHGTLRDLSERVMNAFVDP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  674 EEDMRLWLYNSEN-YLTLLDDEDHKLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------E 741
Cdd:COG5560   184 SDDFRLWDVVPEImGLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkE 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  742 KGATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWT 821
Cdd:COG5560   263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  822 IAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQL 898
Cdd:COG5560   343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMY 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  899 RSQVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQIL 976
Cdd:COG5560   423 KSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIK 500
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  977 LAEVHGSNIKNFPQDNQKVRLSvsgflcafEIPvpvspisassptQTDFSSSPSTNEmftlttngdlprpifipNGMPNT 1056
Cdd:COG5560   501 VMCIYYGGNYNMLEPADKVLLQ--------DIP------------QTDFVYLYETND-----------------NGIEVP 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1057 VVPCGTEKNFTNGMVNGHmPSLP---DSPFTGYIIAVhrKMMRTELYFLSSQKNRPSL--FGMPLIVPCTVHTRKKDLYD 1131
Cdd:COG5560   544 VVHLRIEKGYKSKRLFGD-PFLQlnvLIKASIYDKLV--KEFEELLVLVEMKKTDVDLvsEQVRLLREESSPSSWLKLET 620
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1132 AvwIQVSRLASPlppqeasnhaqDCDDSMgyqyPFTLRVVqkdgNSCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwd 1211
Cdd:COG5560   621 E--IDTKREEQV-----------EEEGQM----NFNDAVV----ISCEWE-----------EKRYLSLFSYDP------- 661
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1212 ptalhlryqtsqervvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILII 1291
Cdd:COG5560   662 -------------------LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILII 722
                         810       820       830
                  ....*....|....*....|....*....|....*.
gi 767996211 1292 HLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRD 1327
Cdd:COG5560   723 HLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
745-938 2.21e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 181.10  E-value: 2.21e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211   745 TGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELWSGTQKN-VAPLKLRWTIA 823
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNSKSSsVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211   824 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVK 903
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 767996211   904 CKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIK 938
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQI 166
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1236-1576 5.30e-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: 5.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1236 SRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRE 1315
Cdd:cd02674    76 SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLN 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1316 SFDPSAFLVPRDPalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksg 1395
Cdd:cd02674   156 DLDLTPYVDTRSF------------------------------------------------------------------- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1396 tscpssknsspnssprtlgrskgrlrlpqigsknklssskenldaskengagqiceladalsrghvlggsqpelvtpqdh 1475
Cdd:cd02674       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1476 evalANGFLYeheacgngysngqlgnhseedstddqredtrikpiyNLYAISCHSGILGGGHYVTYAKNPNC-KWYCYND 1554
Cdd:cd02674   169 ----TGPFKY------------------------------------DLYAVVNHYGSLNGGHYTAYCKNNETnDWYKFDD 208
                         330       340
                  ....*....|....*....|..
gi 767996211 1555 SSCKELHPDEIDTDSAYILFYE 1576
Cdd:cd02674   209 SRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1242-1575 1.01e-25

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.45  E-value: 1.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  1242 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1321
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  1322 flvprdpalcqhkpltpqgdelseprilarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgtscpss 1401
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  1402 knsspnssprtlgrskgrlrlpqigsknklssskenLDASkengagqiceladalsrghvlggsqpelvtpqdhevalan 1481
Cdd:pfam00443  234 ------------------------------------LDLS---------------------------------------- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  1482 gflyeheacgngysngqlgnhseEDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1560
Cdd:pfam00443  238 -----------------------RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 767996211  1561 HPD-EIDTDSAYILFY 1575
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
746-936 7.83e-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: 7.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  746 GLSNLGNTCFMNSSIQCVSNtqpltqyfisgrhlyelnrtnpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 825
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  826 aprfngfQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 905
Cdd:cd02674    21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                         170       180       190
                  ....*....|....*....|....*....|.
gi 767996211  906 TCGHISVRFDPFNFLSLPLPMDSYMHLEITV 936
Cdd:cd02674    56 TCGKTSTTFEPFTYLSLPIPSGSGDAPKVTL 86
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
744-922 2.96e-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: 2.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  744 ATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIgmkghMAKCYGDLVQELWSGTQKNVAPLKLRWTIA 823
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFC-----MMCALEAHVERALASSGPGSAPRIFSSNLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  824 KYAPRFNGFQQQDSQELLAFLLDGLHED-LNRvhekpYVELKDSDgrpdwevaaeawdnHLRRNRSIVVDLFHGQLRSQV 902
Cdd:cd02661    76 QISKHFRIGRQEDAHEFLRYLLDAMQKAcLDR-----FKKLKAVD--------------PSSQETTLVQQIFGGYLRSQV 136
                         170       180
                  ....*....|....*....|
gi 767996211  903 KCKTCGHISVRFDPFNFLSL 922
Cdd:cd02661   137 KCLNCKHVSNTYDPFLDLSL 156
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
746-925 1.84e-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: 1.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  746 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELW-SGTQKNVAPLKLRWTIAK 824
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSP---NSCLSCAMDEIFQEFYySGDRSPYGPINLLYLSWK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  825 YAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVKC 904
Cdd:cd02660    79 HSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEA---------------------NDESHCNCIIHQTFSGSLQSSVTC 137
                         170       180
                  ....*....|....*....|.
gi 767996211  905 KTCGHISVRFDPFNFLSLPLP 925
Cdd:cd02660   138 QRCGGVSTTVDPFLDLSLDIP 158
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
746-935 4.01e-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: 94.86  E-value: 4.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  746 GLSNLGNTCFMNSSIQCvsntqpltqyfisgrhLYelnrtnpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 825
Cdd:cd02257     1 GLNNLGNTCYLNSVLQA----------------LF--------------------------------------------- 19
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  826 aprfngFQQQDSQELLAFLLDGLHEDLNRVHEKpyvelkdsdgrpdwevaaeawDNHLRRNRSIVVDLFHGQLRSQVKCK 905
Cdd:cd02257    20 ------SEQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                         170       180       190
                  ....*....|....*....|....*....|
gi 767996211  906 TCGHISVRFDPFNFLSLPLPMDSYMHLEIT 935
Cdd:cd02257    73 ECGHESVSTEPELFLSLPLPVKGLPQVSLE 102
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
746-942 4.07e-19

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 89.37  E-value: 4.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  746 GLSNLGNTCFMNSSIQCVSNTQPLTqyfisgrhlyelnrtnpigmkghmakcygdlvqELWSGTqknvaPLKLRWTIAKY 825
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALR---------------------------------ELLSET-----PKELFSQVCRK 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  826 APRFNGFQQQDSQELLAFLLDGLhedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnRSIVVDLFHGQLRSQVKCK 905
Cdd:cd02667    43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767996211  906 TCGHISVRFDPFNFLSLPLP--------MDSYMHLEITVIKLDGT 942
Cdd:cd02667    85 SCGTVSLVYEPFLDLSLPRSdeiksecsIESCLKQFTEVEILEGN 129
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1242-1335 1.57e-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: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1242 EPINLDSCLRAFTSEEELGENEMYYCSKCKtHCLATKKLDLWRLPPILIIHLKRFQFVN-GRWIKSQKIVKFPrESFDPS 1320
Cdd:cd02257    97 PQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFNEdGTKEKLNTKVSFP-LELDLS 174
                          90
                  ....*....|....*
gi 767996211 1321 AFLVPRDPALCQHKP 1335
Cdd:cd02257   175 PYLSEGEKDSDSDNG 189
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
746-927 7.66e-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: 7.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  746 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPI-GMKGHMAKcygdLVQELWSG--------------TQ 810
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPAnDLNCQLIK----LADGLLSGryskpaslksendpYQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  811 KNVAPLKLRWTIAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPyvelkdsdgrpdwevaaeawdnhlrrnrsiV 890
Cdd:cd02658    77 VGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLN------------------------------P 126
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767996211  891 VDLFHGQLRSQVKCKTCGHISVRFDPFNFLSLPLPMD 927
Cdd:cd02658   127 NDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKD 163
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1245-1323 1.83e-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: 1.83e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996211 1245 NLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRwiKSQKIVKFPrESFDPSAFL 1323
Cdd:cd02661   163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGG--KINKQISFP-ETLDLSPYM 238
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
746-925 5.64e-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: 74.84  E-value: 5.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  746 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISgRHLYELNRTNPIGMKGHMakcygdlVQELWSGTQKNVAPLKLRWTIAKY 825
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS-LNLPRLGDSQSVMKKLQL-------LQAHLMHTQRRAEAPPDYFLEASR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  826 APRFNGFQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 905
Cdd:cd02664    73 PPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTIRCL 114
                         170       180
                  ....*....|....*....|
gi 767996211  906 TCGHISVRFDPFNFLSLPLP 925
Cdd:cd02664   115 NCNSTSARTERFRDLDLSFP 134
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1242-1325 4.28e-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: 4.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1242 EPINLDSCLRAFTSEEELGENEMYYCSKCkthCLATKKLDLWRLPPILIIHLKRF-QFVNGRWIKSQKIVKFPrESFDPS 1320
Cdd:cd02667   109 SECSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFqQPRSANLRKVSRHVSFP-EILDLA 184

                  ....*
gi 767996211 1321 AFLVP 1325
Cdd:cd02667   185 PFCDP 189
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1245-1324 1.12e-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: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1245 NLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF--VNGRWIKSQKIVKFPREsFDPSAF 1322
Cdd:cd02659   152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDRFEFPLE-LDMEPY 230

                  ..
gi 767996211 1323 LV 1324
Cdd:cd02659   231 TE 232
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1240-1313 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 767996211 1240 QAEPINLDSCLRAFTSEEELGENEmYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRwiKSQKI---VKFP 1313
Cdd:cd02660   172 VSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNK--TSRKIdtyVQFP 245
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1244-1315 1.68e-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: 1.68e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767996211 1244 INLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVN--GRWIK-SQKIVkFPRE 1315
Cdd:cd02663   147 TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEqlNRYIKlFYRVV-FPLE 220
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
746-935 4.46e-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: 65.79  E-value: 4.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  746 GLSNLGNTCFMNSSIQCvsntqpltqyfisgrhLYELNrtnpigmkghMAKCYGDLVQELWSGTQKN--VAPLKLRWTIA 823
Cdd:cd02663     1 GLENFGNTCYCNSVLQA----------------LYFEN----------LLTCLKDLFESISEQKKRTgvISPKKFITRLK 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  824 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVELKDSDgrpdwevaaeawDNHLRRNRSIVVDLFHGQLRSQVK 903
Cdd:cd02663    55 RENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNN------------NNNAEPQPTWVHEIFQGILTNETR 122
                         170       180       190
                  ....*....|....*....|....*....|..
gi 767996211  904 CKTCGHISVRFDPFnflsLPLPMDSYMHLEIT 935
Cdd:cd02663   123 CLTCETVSSRDETF----LDLSIDVEQNTSIT 150
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
746-958 1.37e-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: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  746 GLSNLGNTCFMNSSIQCVsNTQP-----LTQYFISGRHLYELNRTNPIGMKghmakcygDLVQELwSGTQKNVAPLKLRW 820
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCL-RSVPelrdaLKNYNPARRGANQSSDNLTNALR--------DLFDTM-DKKQEPVPPIEFLQ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  821 TIAKYAPRF------NGFQQQDSQELLAFLLDGLHEDLnrvhekpyvELKDSDGrpdwevaaeawdnhlrrnrSIVVDLF 894
Cdd:cd02657    71 LLRMAFPQFaekqnqGGYAQQDAEECWSQLLSVLSQKL---------PGAGSKG-------------------SFIDQLF 122
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767996211  895 HGQLRSQVKCKTCGHI-SVRFDPFNFLSLPLPMD---SYMH------LEITVIKLDGTtpvryglrLNMDEKYT 958
Cdd:cd02657   123 GIELETKMKCTESPDEeEVSTESEYKLQCHISITtevNYLQdglkkgLEEEIEKHSPT--------LGRDAIYT 188
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
516-583 2.49e-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: 2.49e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767996211   516 QKPGAIDNQPLVTqepvkatslTLEGGRLKrtPQLIHGRDYEMVPEPVWRALYHWYGANLALPRPVIK 583
Cdd:pfam06337   24 NEPGPIDNSDLLD---------DESNGQLK--PNLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRNVVN 80
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1519-1575 2.68e-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: 2.68e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767996211 1519 PIYNLYAISCHSGILG-GGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1575
Cdd:cd02661   246 LKYKLYAVLVHSGFSPhSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
746-933 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 767996211  746 GLSNLGNTCFMNSSIQcvsntqplTQYFISG-----RHLYELNrtnpIGMKGHMAKCygDLVQELWSGTQKNVAPLKLRW 820
Cdd:cd02671    26 GLNNLGNTCYLNSVLQ--------VLYFCPGfkhglKHLVSLI----SSVEQLQSSF--LLNPEKYNDELANQAPRRLLN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  821 TIAKYAPRFNGFQQQDSQELLAFLLDGLhedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnRSIVVDLFHGQLRS 900
Cdd:cd02671    92 ALREVNPMYEGYLQHDAQEVLQCILGNI--------------------------------------QELVEKDFQGQLVL 133
                         170       180       190
                  ....*....|....*....|....*....|...
gi 767996211  901 QVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLE 933
Cdd:cd02671   134 RTRCLECETFTERREDFQDISVPVQESELSKSE 166
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1501-1578 2.13e-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: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1501 NHSEEDSTDDQREDTrikpIYNLYAISCHSGILGGGHYVTYAK-NPNCKWYCYNDSSCKELHPDEID------------- 1566
Cdd:cd02659   236 AKKEGDSEKKDSESY----IYELHGVLVHSGDAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEeecfggeetqkty 311
                          90       100
                  ....*....|....*....|.
gi 767996211 1567 ---------TDSAYILFYEQQ 1578
Cdd:cd02659   312 dsgprafkrTTNAYMLFYERK 332
DUSP smart00695
Domain in ubiquitin-specific proteases;
515-582 8.20e-09

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 54.29  E-value: 8.20e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996211    515 PQKPGAIDNQPLVTQEPvkatsltleGGRLKrtPQLIHGRDYEMVPEPVWRALYHWYGANLA-LPRPVI 582
Cdd:smart00695   28 GKDPGPIDNSGILCSHG---------GPRLK--EHLVEGEDYVLIPEELWNKLVRWYGGGPGpIPRKVV 85
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1510-1577 4.39e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.35  E-value: 4.39e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767996211 1510 DQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNpNCKWYCYNDSSCKELHPDEIDT---DSAYILFYEQ 1577
Cdd:COG5533   214 DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK-GGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1245-1328 6.57e-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: 6.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1245 NLDSCLRAFTSEEEL-GENEmYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF--VNGRWIKSQKIVKFPrESFDPSA 1321
Cdd:cd02668   157 TLEECIDEFLKEEQLtGDNQ-YFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdrKTGAKKKLNASISFP-EILDMGE 234

                  ....*..
gi 767996211 1322 FLVPRDP 1328
Cdd:cd02668   235 YLAESDE 241
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
746-922 7.80e-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: 7.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  746 GLSNLGNTCFMNSSIQcvsntqplTQYFISG--RHLYELNRT-NPIGMKG---HMAKCYGDLvQELwsgtQKNVAPLKLR 819
Cdd:cd02659     4 GLKNQGATCYMNSLLQ--------QLYMTPEfrNAVYSIPPTeDDDDNKSvplALQRLFLFL-QLS----ESPVKTTELT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  820 WTIAKYAPR-FNGFQQQDSQELLAFLLDGLHEDLnrvhekPYVELKDsdgrpdwevaaeawdnhlrrnrsIVVDLFHGQL 898
Cdd:cd02659    71 DKTRSFGWDsLNTFEQHDVQEFFRVLFDKLEEKL------KGTGQEG-----------------------LIKNLFGGKL 121
                         170       180
                  ....*....|....*....|....
gi 767996211  899 RSQVKCKTCGHISVRFDPFNFLSL 922
Cdd:cd02659   122 VNYIICKECPHESEREEYFLDLQV 145
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
746-931 1.45e-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: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  746 GLSNLGNTCFMNSSIQCVSNTQPLTQYfisgrhlyeLNRTNpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 825
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEY---------LEEFL--------------------------------------- 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  826 aprfngfQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 905
Cdd:cd02662    33 -------EQQDAHELFQVLLETLE--------------------------------------QLLKFPFDGLLASRIVCL 67
                         170       180
                  ....*....|....*....|....*..
gi 767996211  906 TCGHIS-VRFDPFNFLSLPLPMDSYMH 931
Cdd:cd02662    68 QCGESSkVRYESFTMLSLPVPNQSSGS 94
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1518-1576 2.02e-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: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1518 KPIYNLYAISCHSGILGGGHYVTYAK----------------------NPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1575
Cdd:cd02667   199 SVLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278

                  .
gi 767996211 1576 E 1576
Cdd:cd02667   279 E 279
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
746-852 2.93e-07

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 54.04  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  746 GLSNLGNTCFMNSSIQCVS-NTQPLTQYfiSGRHLYELNrtnpiGMKGHMAKCYGDLVQELWSGTQKNVAPLKlrwtIAK 824
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKLDEL--LDDLSKELK-----VLKNVIRKPEPDLNQEEALKLFTALWSSK----EHK 69
                          90       100
                  ....*....|....*....|....*...
gi 767996211  825 YAPRFNGFQQQDSQELLAFLLDGLHEDL 852
Cdd:COG5533    70 VGWIPPMGSQEDAHELLGKLLDELKLDL 97
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
234-290 3.56e-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: 3.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767996211  234 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 290
Cdd:cd00051     6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1520-1575 9.74e-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: 9.74e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767996211 1520 IYNLYAISCHSGILGGGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1575
Cdd:cd02660   272 TYDLFAVVVHKGTLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1242-1298 1.51e-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: 1.51e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767996211 1242 EPINLDSCLRAFTSEEELGenemYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF 1298
Cdd:cd02658   176 EPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQL 228
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
743-925 2.01e-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: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  743 GATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGrHLYELNRTNpigmKGHMAKCYGDLVQELWSGT--QKNVAPLKLRW 820
Cdd:cd02669   118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLY-ENYENIKDR----KSELVKRLSELIRKIWNPRnfKGHVSPHELLQ 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  821 TIAKY-APRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdnHLRRNRSIVVDLFHGQLR 899
Cdd:cd02669   193 AVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGG---------------------------SKKPNSSIIHDCFQGKVQ 245
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767996211  900 --------------SQVKCKTCGH-ISVRFDPFNFLSLPLP 925
Cdd:cd02669   246 ietqkikphaeeegSKDKFFKDSRvKKTSVSPFLLLTLDLP 286
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1520-1576 2.24e-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: 2.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767996211 1520 IYNLYAISCHSGILG-GGHYVTYAKNPNC-KWYCYNDSSCKELHPDEI-------DTDSAYILFYE 1576
Cdd:cd02657   240 YYELVAVITHQGRSAdSGHYVAWVRRKNDgKWIKFDDDKVSEVTEEDIlklsgggDWHIAYILLYK 305
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
653-721 3.52e-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: 3.52e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767996211   653 FSRMQTIKEIHEYLSQRLRI-KEEDMRLW-LYNSENYlTLLDDEDHKLEYLKIQDEQHLVIEVRNKDMSWP 721
Cdd:pfam14836   18 FSKTDTIDFIEKELRKLFSIpKEKETRLWnRYSSNTR-ELLTDPDITVQEAGLYHGQVLLIEEKNEDGNWP 87
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1518-1576 3.73e-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: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1518 KPIYNLYAISCHSGILGGGHYVTYAKNPNC---------------------KWYCYNDSSCKELHPDEIDTD-SAYILFY 1575
Cdd:cd02662   160 KVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepgsfvrmregpsstshPWWRISDTTVKEVSESEVLEQkSAYMLFY 239

                  .
gi 767996211 1576 E 1576
Cdd:cd02662   240 E 240
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1502-1576 4.20e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 47.49  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1502 HSEEDSTDDQREDTRIKpiYNLYAISCHSGI-LGGGHYVTYAKNPNCK---------------------WYCYNDSSCKE 1559
Cdd:cd02664   226 KEEESGDDGELVTRQVH--YRLYAVVVHSGYsSESGHYFTYARDQTDAdstgqecpepkdaeendesknWYLFNDSRVTF 303
                          90       100
                  ....*....|....*....|....
gi 767996211 1560 LHPDEIDT-------DSAYILFYE 1576
Cdd:cd02664   304 SSFESVQNvtsrfpkDTPYILFYE 327
EF-hand_7 pfam13499
EF-hand domain pair;
233-290 4.76e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 4.76e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767996211   233 LFNAFDENRDNHIDFKEISCGLSACCRG-PL--AERQKFcFKVFDVDRDGVLSRVELRDMV 290
Cdd:pfam13499    7 AFKLLDSDGDGYLDVEELKKLLRKLEEGePLsdEEVEEL-FKEFDLDKDGRISFEEFLELY 66
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1518-1575 3.43e-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: 3.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767996211 1518 KPIYNLYAISCHSGI-LGGGHYVTYAknpncKWYCYNDSSCK---------ELHPDEIDTDSAYILFY 1575
Cdd:cd02671   269 NDVYRLFAVVMHSGAtISSGHYTAYV-----RWLLFDDSEVKvteekdfleALSPNTSSTSTPYLLFY 331
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
231-334 4.51e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  231 EGLFNAFDENRDNHIDFKEISCGLSACCRGPLAERQKFCFKVFDVDRDGVLSRVELRdmvvALLEVWKDNRTDdipelhm 310
Cdd:COG5126    36 ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFR----RLLTALGVSEEE------- 104
                          90       100
                  ....*....|....*....|....
gi 767996211  311 dlsdiVEGILNAHDTTKMGHLTLE 334
Cdd:COG5126   105 -----ADELFARLDTDGDGKISFE 123
EF-hand_7 pfam13499
EF-hand domain pair;
267-339 5.65e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 5.65e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767996211   267 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 339
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1253-1299 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 767996211 1253 FTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFV 1299
Cdd:cd02664   143 FLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYD 189
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
187-290 1.36e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  187 HLEESDIIDLEKRYW--LLKA--QSRTGRFDLETF----GPLVSPPIRPSLsEGLFNAFDENRDNHIDFKEISCGLSACc 258
Cdd:COG5126    21 VLERDDFEALFRRLWatLFSEadTDGDGRISREEFvagmESLFEATVEPFA-RAAFDLLDTDGDGKISADEFRRLLTAL- 98
                          90       100       110
                  ....*....|....*....|....*....|..
gi 767996211  259 RGPLAERQKFcFKVFDVDRDGVLSRVELRDMV 290
Cdd:COG5126    99 GVSEEEADEL-FARLDTDGDGKISFEEFVAAV 129
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1245-1315 1.36e-03

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 42.35  E-value: 1.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767996211 1245 NLDSCLRAFTSEEELgenEMYYCSKCKThclatkklDLWRLPPILIIHLKRFQF-VNGRWIKSQKIVKFPRE 1315
Cdd:cd02662    97 TLEHCLDDFLSTEII---DDYKCDRCQT--------VIVRLPQILCIHLSRSVFdGRGTSTKNSCKVSFPER 157
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1519-1576 2.05e-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: 2.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767996211 1519 PIYNLYAISCHSG-ILGGGHYVTYAKN--PNCKW-YCyNDSSCKELHPDEIDTD---SAYILFYE 1576
Cdd:cd02673   182 AKYSLVAVICHLGeSPYDGHYIAYTKElyNGSSWlYC-SDDEIRPVSKNDVSTNarsSGYLIFYD 245
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1521-1575 2.94e-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: 2.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767996211 1521 YNLYAISCHSGILGGGHYVTYAKN-PNCKWYCYNDSSCKElHPDE---IDTDSA----YILFY 1575
Cdd:cd02666   281 YRLHAVFIHRGEASSGHYWVYIKDfEENVWRKYNDETVTV-VPASevfLFTLGNtatpYFLVY 342
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1253-1333 3.34e-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: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211 1253 FTSEEELGENEMYYcskckthclatkklDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRDPALCQ 1332
Cdd:cd02669   314 GKTETELKDSLKRY--------------LISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNL 379

                  .
gi 767996211 1333 H 1333
Cdd:cd02669   380 S 380
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1521-1575 3.51e-03

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 41.00  E-value: 3.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767996211 1521 YNLYAISCHSGILGGGHYVTYA-KNPNCKWYCYNDSSCKELHPDEIDTD--------SAYILFY 1575
Cdd:cd02665   164 YELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDsfgggrnpSAYCLMY 227
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
267-305 7.01e-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: 7.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 767996211  267 KFCFKVFDVDRDGVLSRVELRDMVVALLEVWKDNRTDDI 305
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. ...
234-337 7.69e-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: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996211  234 FNAFDENRDNHIDFKEIS---CGLSACCRGPLAERQkfcFKVFDVDRDGVLSRVELRDMVVALLEvwkdnrtddIPELHM 310
Cdd:cd15898     6 WIKADKDGDGKLSLKEIKkllKRLNIRVSEKELKKL---FKEVDTNGDGTLTFDEFEELYKSLTE---------RPELEP 73
                          90       100
                  ....*....|....*....|....*..
gi 767996211  311 dlsdivegILNAHDTTKMGHLTLEDYQ 337
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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