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Conserved domains on  [gi|1622878589|ref|XP_014975493|]
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ubiquitin carboxyl-terminal hydrolase 32 isoform X5 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
518-1316 8.08e-86

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


The actual alignment was detected with superfamily member COG5560:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 300.26  E-value: 8.08e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  518 PQKPGAIDNQPLVTQEPvkatsltlegGRLKqtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 596
Cdd:COG5560     66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  597 LFPrylLFLRQQPATRTQQSNIwvNMGNVPSPNAplkrvlaytgcFSRMQTIKEIHEYLSQRLRIKEEDMRLWLYNSEN- 675
Cdd:COG5560    134 SYP---VVFKLHWLFSINGSLI--NLGHDPVPHS-----------ASSHGTLRDLSERVMNAFVDPSDDFRLWDVVPEIm 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  676 YLTLLDDEDHRLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------EKGATGLSNLGNTCF 744
Cdd:COG5560    198 GLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkEAGTCGLRNLGNTCY 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  745 MNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWTIAKYAPRFNGFQQQ 824
Cdd:COG5560    277 MNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQ 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  825 DSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQLRSQVKCKTCGHISV 901
Cdd:COG5560    357 DSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSI 436
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  902 RFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQILLAEVHGSNIKNFPQ 979
Cdd:COG5560    437 TFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIKVMCIYYGGNYNMLE 514
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  980 DNQKVRLSvsgflcafEIPvpaspisassptQTDFSSSPSTNgmftlttngdlprpifiPNGMPNTVVPCGTEKNFTNGM 1059
Cdd:COG5560    515 PADKVLLQ--------DIP------------QTDFVYLYETN-----------------DNGIEVPVVHLRIEKGYKSKR 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1060 VNGHmsslpdsPFTGYII----AVHRKMMRTELYFLSSQKNRPSLFGMP-LIVPCTVHTRKKDLYdavwiqVSRLASPLP 1134
Cdd:COG5560    558 LFGD-------PFLQLNVlikaSIYDKLVKEFEELLVLVEMKKTDVDLVsEQVRLLREESSPSSW------LKLETEIDT 624
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1135 PQEASNHAQDcddsmgyQYPFTLRVVqkdgNTCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwdptalhlryqtsqer 1214
Cdd:COG5560    625 KREEQVEEEG-------QMNFNDAVV----ISCEWE-----------EKRYLSLFSYDP--------------------- 661
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1215 vvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIK 1294
Cdd:COG5560    662 -----LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDK 736
                          810       820
                   ....*....|....*....|..
gi 1622878589 1295 SQKIVKFPRESFDPSAFLVPRD 1316
Cdd:COG5560    737 IDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1231-1564 9.50e-26

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.84  E-value: 9.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1231 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1310
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1311 flvprdpalcrrkpltpqgdelseprvlarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgascpss 1390
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1391 knsspsssprtlgrskgrlrlpqigsknklssskenLDASRdngagqiceladalsrghmlggsqpelvtpqdhevalan 1470
Cdd:pfam00443  234 ------------------------------------LDLSR--------------------------------------- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1471 gflyeheacgngysngqlgnhseeDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1549
Cdd:pfam00443  239 ------------------------YLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 1622878589 1550 HPD-EIDTDSAYILFY 1564
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
237-293 3.64e-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: 45.62  E-value: 3.64e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622878589  237 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 293
Cdd:cd00051      6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
270-342 7.10e-04

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 7.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622878589  270 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 342
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
518-1316 8.08e-86

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 300.26  E-value: 8.08e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  518 PQKPGAIDNQPLVTQEPvkatsltlegGRLKqtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 596
Cdd:COG5560     66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  597 LFPrylLFLRQQPATRTQQSNIwvNMGNVPSPNAplkrvlaytgcFSRMQTIKEIHEYLSQRLRIKEEDMRLWLYNSEN- 675
Cdd:COG5560    134 SYP---VVFKLHWLFSINGSLI--NLGHDPVPHS-----------ASSHGTLRDLSERVMNAFVDPSDDFRLWDVVPEIm 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  676 YLTLLDDEDHRLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------EKGATGLSNLGNTCF 744
Cdd:COG5560    198 GLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkEAGTCGLRNLGNTCY 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  745 MNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWTIAKYAPRFNGFQQQ 824
Cdd:COG5560    277 MNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQ 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  825 DSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQLRSQVKCKTCGHISV 901
Cdd:COG5560    357 DSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSI 436
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  902 RFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQILLAEVHGSNIKNFPQ 979
Cdd:COG5560    437 TFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIKVMCIYYGGNYNMLE 514
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  980 DNQKVRLSvsgflcafEIPvpaspisassptQTDFSSSPSTNgmftlttngdlprpifiPNGMPNTVVPCGTEKNFTNGM 1059
Cdd:COG5560    515 PADKVLLQ--------DIP------------QTDFVYLYETN-----------------DNGIEVPVVHLRIEKGYKSKR 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1060 VNGHmsslpdsPFTGYII----AVHRKMMRTELYFLSSQKNRPSLFGMP-LIVPCTVHTRKKDLYdavwiqVSRLASPLP 1134
Cdd:COG5560    558 LFGD-------PFLQLNVlikaSIYDKLVKEFEELLVLVEMKKTDVDLVsEQVRLLREESSPSSW------LKLETEIDT 624
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1135 PQEASNHAQDcddsmgyQYPFTLRVVqkdgNTCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwdptalhlryqtsqer 1214
Cdd:COG5560    625 KREEQVEEEG-------QMNFNDAVV----ISCEWE-----------EKRYLSLFSYDP--------------------- 661
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1215 vvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIK 1294
Cdd:COG5560    662 -----LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDK 736
                          810       820
                   ....*....|....*....|..
gi 1622878589 1295 SQKIVKFPRESFDPSAFLVPRD 1316
Cdd:COG5560    737 IDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
734-927 2.22e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 181.10  E-value: 2.22e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  734 TGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELWSGTQKN-VAPLKLRWTIA 812
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNSKSSsVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  813 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVK 892
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622878589  893 CKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIK 927
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQI 166
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1225-1565 4.51e-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: 117.00  E-value: 4.51e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1225 SRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRE 1304
Cdd:cd02674     76 SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLN 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1305 SFDPSAFLVPRDPalcrrkpltpqgdelseprvlarevkkvdaqssageedvllskspsslsaniisspkgspsssrksg 1384
Cdd:cd02674    156 DLDLTPYVDTRSF------------------------------------------------------------------- 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1385 ascpssknsspsssprtlgrskgrlrlpqigsknklssskenldasrdngagqiceladalsrghmlggsqpelvtpqdh 1464
Cdd:cd02674        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1465 evalANGFLYeheacgngysngqlgnhseedstddqredtrikpiyNLYAISCHSGILGGGHYVTYAKNPNC-KWYCYND 1543
Cdd:cd02674    169 ----TGPFKY------------------------------------DLYAVVNHYGSLNGGHYTAYCKNNETnDWYKFDD 208
                          330       340
                   ....*....|....*....|..
gi 1622878589 1544 SSCKELHPDEIDTDSAYILFYE 1565
Cdd:cd02674    209 SRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1231-1564 9.50e-26

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.84  E-value: 9.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1231 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1310
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1311 flvprdpalcrrkpltpqgdelseprvlarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgascpss 1390
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1391 knsspsssprtlgrskgrlrlpqigsknklssskenLDASRdngagqiceladalsrghmlggsqpelvtpqdhevalan 1470
Cdd:pfam00443  234 ------------------------------------LDLSR--------------------------------------- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1471 gflyeheacgngysngqlgnhseeDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1549
Cdd:pfam00443  239 ------------------------YLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 1622878589 1550 HPD-EIDTDSAYILFY 1564
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1508-1564 2.45e-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: 2.45e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622878589 1508 PIYNLYAISCHSGILG-GGHYVTYAKNPNCKWYCYNDSsckELHPDEIDT---DSAYILFY 1564
Cdd:cd02661    246 LKYKLYAVLVHSGFSPhSGHYYCYVKSSNGKWYNMDDS---KVSPVSIETvlsQKAYILFY 303
DUSP smart00695
Domain in ubiquitin-specific proteases;
518-585 8.38e-09

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 54.29  E-value: 8.38e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622878589   518 PQKPGAIDNQPLVTQEPvkatsltleGGRLKqtPQLIHGRDYEMVPEPVWRALYHWYGANLA-LPRPVI 585
Cdd:smart00695   28 GKDPGPIDNSGILCSHG---------GPRLK--EHLVEGEDYVLIPEELWNKLVRWYGGGPGpIPRKVV 85
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1499-1566 4.36e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.35  E-value: 4.36e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622878589 1499 DQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNpNCKWYCYNDSSCKELHPDEIDT---DSAYILFYEQ 1566
Cdd:COG5533    214 DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK-GGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
237-293 3.64e-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: 45.62  E-value: 3.64e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622878589  237 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 293
Cdd:cd00051      6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
236-293 5.92e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 5.92e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622878589  236 LFNAFDENRDNHIDFKEISCGLSACCRG-PL--AERQKFcFKVFDVDRDGVLSRVELRDMV 293
Cdd:pfam13499    7 AFKLLDSDGDGYLDVEELKKLLRKLEEGePLsdEEVEEL-FKEFDLDKDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
234-337 4.48e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 4.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  234 EGLFNAFDENRDNHIDFKEISCGLSACCRGPLAERQKFCFKVFDVDRDGVLSRVELRdmvvALLEVWKDNRTDdipelhm 313
Cdd:COG5126     36 ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFR----RLLTALGVSEEE------- 104
                           90       100
                   ....*....|....*....|....
gi 1622878589  314 dlsdiVEGILNAHDTTKMGHLTLE 337
Cdd:COG5126    105 -----ADELFARLDTDGDGKISFE 123
EF-hand_7 pfam13499
EF-hand domain pair;
270-342 7.10e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 7.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622878589  270 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 342
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
518-1316 8.08e-86

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 300.26  E-value: 8.08e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  518 PQKPGAIDNQPLVTQEPvkatsltlegGRLKqtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 596
Cdd:COG5560     66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  597 LFPrylLFLRQQPATRTQQSNIwvNMGNVPSPNAplkrvlaytgcFSRMQTIKEIHEYLSQRLRIKEEDMRLWLYNSEN- 675
Cdd:COG5560    134 SYP---VVFKLHWLFSINGSLI--NLGHDPVPHS-----------ASSHGTLRDLSERVMNAFVDPSDDFRLWDVVPEIm 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  676 YLTLLDDEDHRLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------EKGATGLSNLGNTCF 744
Cdd:COG5560    198 GLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkEAGTCGLRNLGNTCY 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  745 MNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWTIAKYAPRFNGFQQQ 824
Cdd:COG5560    277 MNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQ 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  825 DSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQLRSQVKCKTCGHISV 901
Cdd:COG5560    357 DSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSI 436
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  902 RFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQILLAEVHGSNIKNFPQ 979
Cdd:COG5560    437 TFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIKVMCIYYGGNYNMLE 514
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  980 DNQKVRLSvsgflcafEIPvpaspisassptQTDFSSSPSTNgmftlttngdlprpifiPNGMPNTVVPCGTEKNFTNGM 1059
Cdd:COG5560    515 PADKVLLQ--------DIP------------QTDFVYLYETN-----------------DNGIEVPVVHLRIEKGYKSKR 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1060 VNGHmsslpdsPFTGYII----AVHRKMMRTELYFLSSQKNRPSLFGMP-LIVPCTVHTRKKDLYdavwiqVSRLASPLP 1134
Cdd:COG5560    558 LFGD-------PFLQLNVlikaSIYDKLVKEFEELLVLVEMKKTDVDLVsEQVRLLREESSPSSW------LKLETEIDT 624
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1135 PQEASNHAQDcddsmgyQYPFTLRVVqkdgNTCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwdptalhlryqtsqer 1214
Cdd:COG5560    625 KREEQVEEEG-------QMNFNDAVV----ISCEWE-----------EKRYLSLFSYDP--------------------- 661
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1215 vvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIK 1294
Cdd:COG5560    662 -----LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDK 736
                          810       820
                   ....*....|....*....|..
gi 1622878589 1295 SQKIVKFPRESFDPSAFLVPRD 1316
Cdd:COG5560    737 IDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
734-927 2.22e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 181.10  E-value: 2.22e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  734 TGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELWSGTQKN-VAPLKLRWTIA 812
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNSKSSsVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  813 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVK 892
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622878589  893 CKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIK 927
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQI 166
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1225-1565 4.51e-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: 117.00  E-value: 4.51e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1225 SRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRE 1304
Cdd:cd02674     76 SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLN 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1305 SFDPSAFLVPRDPalcrrkpltpqgdelseprvlarevkkvdaqssageedvllskspsslsaniisspkgspsssrksg 1384
Cdd:cd02674    156 DLDLTPYVDTRSF------------------------------------------------------------------- 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1385 ascpssknsspsssprtlgrskgrlrlpqigsknklssskenldasrdngagqiceladalsrghmlggsqpelvtpqdh 1464
Cdd:cd02674        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1465 evalANGFLYeheacgngysngqlgnhseedstddqredtrikpiyNLYAISCHSGILGGGHYVTYAKNPNC-KWYCYND 1543
Cdd:cd02674    169 ----TGPFKY------------------------------------DLYAVVNHYGSLNGGHYTAYCKNNETnDWYKFDD 208
                          330       340
                   ....*....|....*....|..
gi 1622878589 1544 SSCKELHPDEIDTDSAYILFYE 1565
Cdd:cd02674    209 SRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1231-1564 9.50e-26

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.84  E-value: 9.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1231 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1310
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1311 flvprdpalcrrkpltpqgdelseprvlarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgascpss 1390
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1391 knsspsssprtlgrskgrlrlpqigsknklssskenLDASRdngagqiceladalsrghmlggsqpelvtpqdhevalan 1470
Cdd:pfam00443  234 ------------------------------------LDLSR--------------------------------------- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1471 gflyeheacgngysngqlgnhseeDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1549
Cdd:pfam00443  239 ------------------------YLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 1622878589 1550 HPD-EIDTDSAYILFY 1564
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-925 7.41e-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: 7.41e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  735 GLSNLGNTCFMNSSIQCVSNtqpltqyfisgrhlyelnrtnpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 814
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  815 aprfngfQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 894
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1622878589  895 TCGHISVRFDPFNFLSLPLPMDSYMHLEITV 925
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSGDAPKVTL 86
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
733-911 2.62e-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: 2.62e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  733 ATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIgmkghMAKCYGDLVQELWSGTQKNVAPLKLRWTIA 812
Cdd:cd02661      1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFC-----MMCALEAHVERALASSGPGSAPRIFSSNLK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  813 KYAPRFNGFQQQDSQELLAFLLDGLHED-LNRvhekpYVELKDSDgrpdwevaaeawdnHLRRNRSIVVDLFHGQLRSQV 891
Cdd:cd02661     76 QISKHFRIGRQEDAHEFLRYLLDAMQKAcLDR-----FKKLKAVD--------------PSSQETTLVQQIFGGYLRSQV 136
                          170       180
                   ....*....|....*....|
gi 1622878589  892 KCKTCGHISVRFDPFNFLSL 911
Cdd:cd02661    137 KCLNCKHVSNTYDPFLDLSL 156
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-914 1.63e-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: 1.63e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  735 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELW-SGTQKNVAPLKLRWTIAK 813
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSP---NSCLSCAMDEIFQEFYySGDRSPYGPINLLYLSWK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  814 YAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVKC 893
Cdd:cd02660     79 HSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEA---------------------NDESHCNCIIHQTFSGSLQSSVTC 137
                          170       180
                   ....*....|....*....|.
gi 1622878589  894 KTCGHISVRFDPFNFLSLPLP 914
Cdd:cd02660    138 QRCGGVSTTVDPFLDLSLDIP 158
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
735-924 4.02e-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: 4.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  735 GLSNLGNTCFMNSSIQCvsntqpltqyfisgrhLYelnrtnpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 814
Cdd:cd02257      1 GLNNLGNTCYLNSVLQA----------------LF--------------------------------------------- 19
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  815 aprfngFQQQDSQELLAFLLDGLHEDLNRVHEKpyvelkdsdgrpdwevaaeawDNHLRRNRSIVVDLFHGQLRSQVKCK 894
Cdd:cd02257     20 ------SEQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                          170       180       190
                   ....*....|....*....|....*....|
gi 1622878589  895 TCGHISVRFDPFNFLSLPLPMDSYMHLEIT 924
Cdd:cd02257     73 ECGHESVSTEPELFLSLPLPVKGLPQVSLE 102
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-931 3.54e-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: 89.75  E-value: 3.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  735 GLSNLGNTCFMNSSIQCVSNTQPLTqyfisgrhlyelnrtnpigmkghmakcygdlvqELWSGTqknvaPLKLRWTIAKY 814
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALR---------------------------------ELLSET-----PKELFSQVCRK 42
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  815 APRFNGFQQQDSQELLAFLLDGLhedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnRSIVVDLFHGQLRSQVKCK 894
Cdd:cd02667     43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622878589  895 TCGHISVRFDPFNFLSLPLP--------MDSYMHLEITVIKLDGT 931
Cdd:cd02667     85 SCGTVSLVYEPFLDLSLPRSdeiksecsIESCLKQFTEVEILEGN 129
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1231-1317 3.35e-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: 83.30  E-value: 3.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1231 EPINLDSCLRAFTSEEELGENEMYYCSKCKtHCLATKKLDLWRLPPILIIHLKRFQFVN-GRWIKSQKIVKFPrESFDPS 1309
Cdd:cd02257     97 PQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFNEdGTKEKLNTKVSFP-LELDLS 174

                   ....*...
gi 1622878589 1310 AFLVPRDP 1317
Cdd:cd02257    175 PYLSEGEK 182
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-916 7.46e-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: 7.46e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  735 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPI-GMKGHMAKcygdLVQELWSG--------------TQ 799
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPAnDLNCQLIK----LADGLLSGryskpaslksendpYQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  800 KNVAPLKLRWTIAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPyvelkdsdgrpdwevaaeawdnhlrrnrsiV 879
Cdd:cd02658     77 VGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLN------------------------------P 126
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1622878589  880 VDLFHGQLRSQVKCKTCGHISVRFDPFNFLSLPLPMD 916
Cdd:cd02658    127 NDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKD 163
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1234-1312 1.70e-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: 1.70e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622878589 1234 NLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRwiKSQKIVKFPrESFDPSAFL 1312
Cdd:cd02661    163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGG--KINKQISFP-ETLDLSPYM 238
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-914 5.30e-14

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 75.22  E-value: 5.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  735 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISgRHLYELNRTNPIGMKGHMakcygdlVQELWSGTQKNVAPLKLRWTIAKY 814
Cdd:cd02664      1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS-LNLPRLGDSQSVMKKLQL-------LQAHLMHTQRRAEAPPDYFLEASR 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  815 APRFNGFQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 894
Cdd:cd02664     73 PPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTIRCL 114
                          170       180
                   ....*....|....*....|
gi 1622878589  895 TCGHISVRFDPFNFLSLPLP 914
Cdd:cd02664    115 NCNSTSARTERFRDLDLSFP 134
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1231-1314 4.02e-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: 4.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1231 EPINLDSCLRAFTSEEELGENEMYYCSKCkthCLATKKLDLWRLPPILIIHLKRF-QFVNGRWIKSQKIVKFPrESFDPS 1309
Cdd:cd02667    109 SECSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFqQPRSANLRKVSRHVSFP-EILDLA 184

                   ....*
gi 1622878589 1310 AFLVP 1314
Cdd:cd02667    185 PFCDP 189
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1229-1302 1.05e-11

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 68.17  E-value: 1.05e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622878589 1229 QAEPINLDSCLRAFTSEEELGENEmYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRwiKSQKI---VKFP 1302
Cdd:cd02660    172 VSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNK--TSRKIdtyVQFP 245
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1234-1313 1.17e-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: 1.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1234 NLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF--VNGRWIKSQKIVKFPREsFDPSAF 1311
Cdd:cd02659    152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDRFEFPLE-LDMEPY 230

                   ..
gi 1622878589 1312 LV 1313
Cdd:cd02659    231 TE 232
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1233-1304 1.71e-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: 1.71e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622878589 1233 INLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVN--GRWIK-SQKIVkFPRE 1304
Cdd:cd02663    147 TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEqlNRYIKlFYRVV-FPLE 220
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-924 4.63e-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: 4.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  735 GLSNLGNTCFMNSSIQCvsntqpltqyfisgrhLYELNrtnpigmkghMAKCYGDLVQELWSGTQKN--VAPLKLRWTIA 812
Cdd:cd02663      1 GLENFGNTCYCNSVLQA----------------LYFEN----------LLTCLKDLFESISEQKKRTgvISPKKFITRLK 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  813 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVELKDSDgrpdwevaaeawDNHLRRNRSIVVDLFHGQLRSQVK 892
Cdd:cd02663     55 RENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNN------------NNNAEPQPTWVHEIFQGILTNETR 122
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622878589  893 CKTCGHISVRFDPFnflsLPLPMDSYMHLEIT 924
Cdd:cd02663    123 CLTCETVSSRDETF----LDLSIDVEQNTSIT 150
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-947 1.49e-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: 1.49e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  735 GLSNLGNTCFMNSSIQCVsNTQP-----LTQYFISGRHLYELNRTNPIGMKghmakcygDLVQELwSGTQKNVAPLKLRW 809
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCL-RSVPelrdaLKNYNPARRGANQSSDNLTNALR--------DLFDTM-DKKQEPVPPIEFLQ 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  810 TIAKYAPRF------NGFQQQDSQELLAFLLDGLHEDLnrvhekpyvELKDSDGrpdwevaaeawdnhlrrnrSIVVDLF 883
Cdd:cd02657     71 LLRMAFPQFaekqnqGGYAQQDAEECWSQLLSVLSQKL---------PGAGSKG-------------------SFIDQLF 122
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622878589  884 HGQLRSQVKCKTCGHI-SVRFDPFNFLSLPLPMD---SYMH------LEITVIKLDGTtpvryglrLNMDEKYT 947
Cdd:cd02657    123 GIELETKMKCTESPDEeEVSTESEYKLQCHISITtevNYLQdglkkgLEEEIEKHSPT--------LGRDAIYT 188
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1508-1564 2.45e-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: 2.45e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622878589 1508 PIYNLYAISCHSGILG-GGHYVTYAKNPNCKWYCYNDSsckELHPDEIDT---DSAYILFY 1564
Cdd:cd02661    246 LKYKLYAVLVHSGFSPhSGHYYCYVKSSNGKWYNMDDS---KVSPVSIETvlsQKAYILFY 303
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
519-586 2.75e-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: 2.75e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622878589  519 QKPGAIDNQPLVTqepvkatslTLEGGRLKqtPQLIHGRDYEMVPEPVWRALYHWYGANLALPRPVIK 586
Cdd:pfam06337   24 NEPGPIDNSDLLD---------DESNGQLK--PNLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRNVVN 80
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-922 9.11e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 62.22  E-value: 9.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  735 GLSNLGNTCFMNSSIQcvsntqplTQYFISG-----RHLYELNrtnpIGMKGHMAKCygDLVQELWSGTQKNVAPLKLRW 809
Cdd:cd02671     26 GLNNLGNTCYLNSVLQ--------VLYFCPGfkhglKHLVSLI----SSVEQLQSSF--LLNPEKYNDELANQAPRRLLN 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  810 TIAKYAPRFNGFQQQDSQELLAFLLDGLhedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnRSIVVDLFHGQLRS 889
Cdd:cd02671     92 ALREVNPMYEGYLQHDAQEVLQCILGNI--------------------------------------QELVEKDFQGQLVL 133
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1622878589  890 QVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLE 922
Cdd:cd02671    134 RTRCLECETFTERREDFQDISVPVQESELSKSE 166
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1490-1567 2.17e-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: 2.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1490 NHSEEDSTDDQREDTrikpIYNLYAISCHSGILGGGHYVTYAK-NPNCKWYCYNDSSCKELHPDEID------------- 1555
Cdd:cd02659    236 AKKEGDSEKKDSESY----IYELHGVLVHSGDAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEeecfggeetqkty 311
                           90       100
                   ....*....|....*....|.
gi 1622878589 1556 ---------TDSAYILFYEQQ 1567
Cdd:cd02659    312 dsgprafkrTTNAYMLFYERK 332
DUSP smart00695
Domain in ubiquitin-specific proteases;
518-585 8.38e-09

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 54.29  E-value: 8.38e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622878589   518 PQKPGAIDNQPLVTQEPvkatsltleGGRLKqtPQLIHGRDYEMVPEPVWRALYHWYGANLA-LPRPVI 585
Cdd:smart00695   28 GKDPGPIDNSGILCSHG---------GPRLK--EHLVEGEDYVLIPEELWNKLVRWYGGGPGpIPRKVV 85
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1499-1566 4.36e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.35  E-value: 4.36e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622878589 1499 DQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNpNCKWYCYNDSSCKELHPDEIDT---DSAYILFYEQ 1566
Cdd:COG5533    214 DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK-GGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1234-1317 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 1622878589 1234 NLDSCLRAFTSEEEL-GENEmYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF--VNGRWIKSQKIVKFPrESFDPSA 1310
Cdd:cd02668    157 TLEECIDEFLKEEQLtGDNQ-YFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdrKTGAKKKLNASISFP-EILDMGE 234

                   ....*..
gi 1622878589 1311 FLVPRDP 1317
Cdd:cd02668    235 YLAESDE 241
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-911 8.61e-08

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 56.11  E-value: 8.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  735 GLSNLGNTCFMNSSIQcvsntqplTQYFISG--RHLYELNRT-NPIGMKG---HMAKCYGDLvQELwsgtQKNVAPLKLR 808
Cdd:cd02659      4 GLKNQGATCYMNSLLQ--------QLYMTPEfrNAVYSIPPTeDDDDNKSvplALQRLFLFL-QLS----ESPVKTTELT 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  809 WTIAKYAPR-FNGFQQQDSQELLAFLLDGLHEDLnrvhekPYVELKDsdgrpdwevaaeawdnhlrrnrsIVVDLFHGQL 887
Cdd:cd02659     71 DKTRSFGWDsLNTFEQHDVQEFFRVLFDKLEEKL------KGTGQEG-----------------------LIKNLFGGKL 121
                          170       180
                   ....*....|....*....|....
gi 1622878589  888 RSQVKCKTCGHISVRFDPFNFLSL 911
Cdd:cd02659    122 VNYIICKECPHESEREEYFLDLQV 145
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-920 1.35e-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: 1.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  735 GLSNLGNTCFMNSSIQCVSNTQPLTQYfisgrhlyeLNRTNpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 814
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLIEY---------LEEFL--------------------------------------- 32
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  815 aprfngfQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 894
Cdd:cd02662     33 -------EQQDAHELFQVLLETLE--------------------------------------QLLKFPFDGLLASRIVCL 67
                          170       180
                   ....*....|....*....|....*..
gi 1622878589  895 TCGHIS-VRFDPFNFLSLPLPMDSYMH 920
Cdd:cd02662     68 QCGESSkVRYESFTMLSLPVPNQSSGS 94
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1507-1565 1.92e-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: 1.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1507 KPIYNLYAISCHSGILGGGHYVTYAK----------------------NPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1564
Cdd:cd02667    199 SVLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278

                   .
gi 1622878589 1565 E 1565
Cdd:cd02667    279 E 279
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
735-841 2.91e-07

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 54.04  E-value: 2.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  735 GLSNLGNTCFMNSSIQCVS-NTQPLTQYfiSGRHLYELNrtnpiGMKGHMAKCYGDLVQELWSGTQKNVAPLKlrwtIAK 813
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILAlYLPKLDEL--LDDLSKELK-----VLKNVIRKPEPDLNQEEALKLFTALWSSK----EHK 69
                           90       100
                   ....*....|....*....|....*...
gi 1622878589  814 YAPRFNGFQQQDSQELLAFLLDGLHEDL 841
Cdd:COG5533     70 VGWIPPMGSQEDAHELLGKLLDELKLDL 97
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
237-293 3.64e-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: 45.62  E-value: 3.64e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622878589  237 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 293
Cdd:cd00051      6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1509-1564 9.09e-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: 9.09e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622878589 1509 IYNLYAISCHSGILGGGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1564
Cdd:cd02660    272 TYDLFAVVVHKGTLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1231-1287 1.49e-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: 1.49e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622878589 1231 EPINLDSCLRAFTSEEELGenemYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF 1287
Cdd:cd02658    176 EPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQL 228
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
732-914 1.99e-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: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  732 GATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGrHLYELNRTNpigmKGHMAKCYGDLVQELWSGT--QKNVAPLKLRW 809
Cdd:cd02669    118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLY-ENYENIKDR----KSELVKRLSELIRKIWNPRnfKGHVSPHELLQ 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  810 TIAKY-APRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdnHLRRNRSIVVDLFHGQLR 888
Cdd:cd02669    193 AVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGG---------------------------SKKPNSSIIHDCFQGKVQ 245
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1622878589  889 --------------SQVKCKTCGH-ISVRFDPFNFLSLPLP 914
Cdd:cd02669    246 ietqkikphaeeegSKDKFFKDSRvKKTSVSPFLLLTLDLP 286
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1509-1565 2.24e-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 1622878589 1509 IYNLYAISCHSGILG-GGHYVTYAKNPNC-KWYCYNDSSCKELHPDEI-------DTDSAYILFYE 1565
Cdd:cd02657    240 YYELVAVITHQGRSAdSGHYVAWVRRKNDgKWIKFDDDKVSEVTEEDIlklsgggDWHIAYILLYK 305
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1507-1565 3.67e-05

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 46.98  E-value: 3.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1507 KPIYNLYAISCHSGILGGGHYVTYAKNPNC---------------------KWYCYNDSSCKELHPDEIDTD-SAYILFY 1564
Cdd:cd02662    160 KVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepgsfvrmregpsstshPWWRISDTTVKEVSESEVLEQkSAYMLFY 239

                   .
gi 1622878589 1565 E 1565
Cdd:cd02662    240 E 240
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1491-1565 3.96e-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: 3.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1491 HSEEDSTDDQREDTRIKpiYNLYAISCHSGI-LGGGHYVTYAKNPNCK---------------------WYCYNDSSCKE 1548
Cdd:cd02664    226 KEEESGDDGELVTRQVH--YRLYAVVVHSGYsSESGHYFTYARDQTDAdstgqecpepkdaeendesknWYLFNDSRVTF 303
                           90       100
                   ....*....|....*....|....
gi 1622878589 1549 LHPDEIDT-------DSAYILFYE 1565
Cdd:cd02664    304 SSFESVQNvtsrfpkDTPYILFYE 327
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
642-710 4.25e-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: 4.25e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622878589  642 FSRMQTIKEIHEYLSQRLRI-KEEDMRLW-LYNSENYlTLLDDEDHRLEYLKIQDEQHLVIEVRNKDMSWP 710
Cdd:pfam14836   18 FSKTDTIDFIEKELRKLFSIpKEKETRLWnRYSSNTR-ELLTDPDITVQEAGLYHGQVLLIEEKNEDGNWP 87
EF-hand_7 pfam13499
EF-hand domain pair;
236-293 5.92e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 5.92e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622878589  236 LFNAFDENRDNHIDFKEISCGLSACCRG-PL--AERQKFcFKVFDVDRDGVLSRVELRDMV 293
Cdd:pfam13499    7 AFKLLDSDGDGYLDVEELKKLLRKLEEGePLsdEEVEEL-FKEFDLDKDGRISFEEFLELY 66
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1507-1564 3.26e-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: 3.26e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622878589 1507 KPIYNLYAISCHSGI-LGGGHYVTYAknpncKWYCYNDSSCK---------ELHPDEIDTDSAYILFY 1564
Cdd:cd02671    269 NDVYRLFAVVMHSGAtISSGHYTAYV-----RWLLFDDSEVKvteekdfleALSPNTSSTSTPYLLFY 331
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
234-337 4.48e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 4.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  234 EGLFNAFDENRDNHIDFKEISCGLSACCRGPLAERQKFCFKVFDVDRDGVLSRVELRdmvvALLEVWKDNRTDdipelhm 313
Cdd:COG5126     36 ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFR----RLLTALGVSEEE------- 104
                           90       100
                   ....*....|....*....|....
gi 1622878589  314 dlsdiVEGILNAHDTTKMGHLTLE 337
Cdd:COG5126    105 -----ADELFARLDTDGDGKISFE 123
EF-hand_7 pfam13499
EF-hand domain pair;
270-342 7.10e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 7.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622878589  270 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 342
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1242-1288 1.00e-03

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 43.25  E-value: 1.00e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622878589 1242 FTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFV 1288
Cdd:cd02664    143 FLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYD 189
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1234-1304 1.33e-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: 1.33e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622878589 1234 NLDSCLRAFTSEEELgenEMYYCSKCKThclatkklDLWRLPPILIIHLKRFQF-VNGRWIKSQKIVKFPRE 1304
Cdd:cd02662     97 TLEHCLDDFLSTEII---DDYKCDRCQT--------VIVRLPQILCIHLSRSVFdGRGTSTKNSCKVSFPER 157
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
190-293 1.35e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  190 HLEESDIIDLEKRYW--LLKA--QSRTGRFDLETF----GPLVSPPIRPSLsEGLFNAFDENRDNHIDFKEISCGLSACc 261
Cdd:COG5126     21 VLERDDFEALFRRLWatLFSEadTDGDGRISREEFvagmESLFEATVEPFA-RAAFDLLDTDGDGKISADEFRRLLTAL- 98
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622878589  262 RGPLAERQKFcFKVFDVDRDGVLSRVELRDMV 293
Cdd:COG5126     99 GVSEEEADEL-FARLDTDGDGKISFEEFVAAV 129
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1508-1565 2.09e-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: 2.09e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622878589 1508 PIYNLYAISCHSG-ILGGGHYVTYAKN--PNCKW-YCyNDSSCKELHPDEIDTD---SAYILFYE 1565
Cdd:cd02673    182 AKYSLVAVICHLGeSPYDGHYIAYTKElyNGSSWlYC-SDDEIRPVSKNDVSTNarsSGYLIFYD 245
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1510-1553 3.29e-03

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 41.71  E-value: 3.29e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1622878589 1510 YNLYAISCHSGILGGGHYVTYAKN-PNCKWYCYNDSSCKElHPDE 1553
Cdd:cd02666    281 YRLHAVFIHRGEASSGHYWVYIKDfEENVWRKYNDETVTV-VPAS 324
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1242-1321 3.31e-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: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589 1242 FTSEEELGENEMYYcskckthclatkklDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRDPALCR 1321
Cdd:cd02669    314 GKTETELKDSLKRY--------------LISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNL 379
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1510-1564 3.48e-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: 3.48e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622878589 1510 YNLYAISCHSGILGGGHYVTYA-KNPNCKWYCYNDSSCKELHPDEIDTD--------SAYILFY 1564
Cdd:cd02665    164 YELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDsfgggrnpSAYCLMY 227
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
270-308 7.17e-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: 7.17e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622878589  270 KFCFKVFDVDRDGVLSRVELRDMVVALLEVWKDNRTDDI 308
Cdd:cd00051      3 REAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEM 41
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
237-340 9.06e-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: 9.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878589  237 FNAFDENRDNHIDFKEIS---CGLSACCRGPLAERQkfcFKVFDVDRDGVLSRVELRDMVVALLEvwkdnrtddIPELHM 313
Cdd:cd15898      6 WIKADKDGDGKLSLKEIKkllKRLNIRVSEKELKKL---FKEVDTNGDGTLTFDEFEELYKSLTE---------RPELEP 73
                           90       100
                   ....*....|....*....|....*..
gi 1622878589  314 dlsdivegILNAHDTTKMGHLTLEDYQ 340
Cdd:cd15898     74 --------IFKKYAGTNRDYMTLEEFI 92
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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