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Conserved domains on  [gi|1622878581|ref|XP_014975490|]
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ubiquitin carboxyl-terminal hydrolase 32 isoform X1 [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];
535-1347 2.82e-83

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


The actual alignment was detected with superfamily member COG5560:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 292.94  E-value: 2.82e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  535 PQKPGAIDNQPLVTQEPvkatsltlegGRLKqtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 613
Cdd:COG5560     66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  614 LFPrylLFLRQQPATRTQQSNIWVNMGMMSLRMfpqhfprgnvpspnaplkrvlaytgcfSRMQTIKEIHEYLSQRLRIK 693
Cdd:COG5560    134 SYP---VVFKLHWLFSINGSLINLGHDPVPHSA---------------------------SSHGTLRDLSERVMNAFVDP 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  694 EEDMRLWLYNSEN-YLTLLDDEDHRLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------E 761
Cdd:COG5560    184 SDDFRLWDVVPEImGLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkE 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  762 KGATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWT 841
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  842 IAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQL 918
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMY 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  919 RSQVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQIL 996
Cdd:COG5560    423 KSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIK 500
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  997 LAEVHGSNIKNFPQDNQKVRLSvsgflcafEIPvpaspisassptQTDFSSSPSTNgmftlttngdlprpifiPNGMPNT 1076
Cdd:COG5560    501 VMCIYYGGNYNMLEPADKVLLQ--------DIP------------QTDFVYLYETN-----------------DNGIEVP 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1077 VVPCGTEKNFTNGMVNGHmsslpdsPFTGYII----AVHRKMMRTELYFLSSQKNRPSLFGM-PLIVPCTVHTRKKDLYd 1151
Cdd:COG5560    544 VVHLRIEKGYKSKRLFGD-------PFLQLNVlikaSIYDKLVKEFEELLVLVEMKKTDVDLvSEQVRLLREESSPSSW- 615
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1152 avwiqVSRLASPLPPQEASNHAQDcddsmgyQYPFTLRVVqkdgNTCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwd 1231
Cdd:COG5560    616 -----LKLETEIDTKREEQVEEEG-------QMNFNDAVV----ISCEWE-----------EKRYLSLFSYDP------- 661
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1232 ptalhlryqtsqervvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILII 1311
Cdd:COG5560    662 -------------------LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILII 722
                          810       820       830
                   ....*....|....*....|....*....|....*.
gi 1622878581 1312 HLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRD 1347
Cdd:COG5560    723 HLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1262-1595 8.19e-26

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.84  E-value: 8.19e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1262 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1341
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1342 flvprdpalcrrkpltpqgdelseprvlarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgascpss 1421
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1422 knsspsssprtlgrskgrlrlpqigsknklssskenLDASRdngagqiceladalsrghmlggsqpelvtpqdhevalan 1501
Cdd:pfam00443  234 ------------------------------------LDLSR--------------------------------------- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1502 gflyeheacgngysngqlgnhseeDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1580
Cdd:pfam00443  239 ------------------------YLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 1622878581 1581 HPD-EIDTDSAYILFY 1595
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
254-310 3.60e-06

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


:

Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 46.00  E-value: 3.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622878581  254 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 310
Cdd:cd00051      6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
287-359 5.72e-04

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 5.72e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622878581  287 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 359
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
535-1347 2.82e-83

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 292.94  E-value: 2.82e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  535 PQKPGAIDNQPLVTQEPvkatsltlegGRLKqtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 613
Cdd:COG5560     66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  614 LFPrylLFLRQQPATRTQQSNIWVNMGMMSLRMfpqhfprgnvpspnaplkrvlaytgcfSRMQTIKEIHEYLSQRLRIK 693
Cdd:COG5560    134 SYP---VVFKLHWLFSINGSLINLGHDPVPHSA---------------------------SSHGTLRDLSERVMNAFVDP 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  694 EEDMRLWLYNSEN-YLTLLDDEDHRLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------E 761
Cdd:COG5560    184 SDDFRLWDVVPEImGLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkE 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  762 KGATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWT 841
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  842 IAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQL 918
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMY 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  919 RSQVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQIL 996
Cdd:COG5560    423 KSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIK 500
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  997 LAEVHGSNIKNFPQDNQKVRLSvsgflcafEIPvpaspisassptQTDFSSSPSTNgmftlttngdlprpifiPNGMPNT 1076
Cdd:COG5560    501 VMCIYYGGNYNMLEPADKVLLQ--------DIP------------QTDFVYLYETN-----------------DNGIEVP 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1077 VVPCGTEKNFTNGMVNGHmsslpdsPFTGYII----AVHRKMMRTELYFLSSQKNRPSLFGM-PLIVPCTVHTRKKDLYd 1151
Cdd:COG5560    544 VVHLRIEKGYKSKRLFGD-------PFLQLNVlikaSIYDKLVKEFEELLVLVEMKKTDVDLvSEQVRLLREESSPSSW- 615
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1152 avwiqVSRLASPLPPQEASNHAQDcddsmgyQYPFTLRVVqkdgNTCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwd 1231
Cdd:COG5560    616 -----LKLETEIDTKREEQVEEEG-------QMNFNDAVV----ISCEWE-----------EKRYLSLFSYDP------- 661
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1232 ptalhlryqtsqervvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILII 1311
Cdd:COG5560    662 -------------------LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILII 722
                          810       820       830
                   ....*....|....*....|....*....|....*.
gi 1622878581 1312 HLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRD 1347
Cdd:COG5560    723 HLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
765-958 1.80e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 181.49  E-value: 1.80e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  765 TGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELWSGTQKN-VAPLKLRWTIA 843
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNSKSSsVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  844 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVK 923
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622878581  924 CKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIK 958
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQI 166
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1256-1596 5.22e-29

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 116.62  E-value: 5.22e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1256 SRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRE 1335
Cdd:cd02674     76 SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLN 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1336 SFDPSAFLVPRDPalcrrkpltpqgdelseprvlarevkkvdaqssageedvllskspsslsaniisspkgspsssrksg 1415
Cdd:cd02674    156 DLDLTPYVDTRSF------------------------------------------------------------------- 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1416 ascpssknsspsssprtlgrskgrlrlpqigsknklssskenldasrdngagqiceladalsrghmlggsqpelvtpqdh 1495
Cdd:cd02674        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1496 evalANGFLYeheacgngysngqlgnhseedstddqredtrikpiyNLYAISCHSGILGGGHYVTYAKNPNC-KWYCYND 1574
Cdd:cd02674    169 ----TGPFKY------------------------------------DLYAVVNHYGSLNGGHYTAYCKNNETnDWYKFDD 208
                          330       340
                   ....*....|....*....|..
gi 1622878581 1575 SSCKELHPDEIDTDSAYILFYE 1596
Cdd:cd02674    209 SRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1262-1595 8.19e-26

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.84  E-value: 8.19e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1262 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1341
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1342 flvprdpalcrrkpltpqgdelseprvlarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgascpss 1421
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1422 knsspsssprtlgrskgrlrlpqigsknklssskenLDASRdngagqiceladalsrghmlggsqpelvtpqdhevalan 1501
Cdd:pfam00443  234 ------------------------------------LDLSR--------------------------------------- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1502 gflyeheacgngysngqlgnhseeDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1580
Cdd:pfam00443  239 ------------------------YLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 1622878581 1581 HPD-EIDTDSAYILFY 1595
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1539-1595 2.60e-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: 2.60e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622878581 1539 PIYNLYAISCHSGILG-GGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1595
Cdd:cd02661    246 LKYKLYAVLVHSGFSPhSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
DUSP smart00695
Domain in ubiquitin-specific proteases;
535-602 9.15e-09

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 53.90  E-value: 9.15e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622878581   535 PQKPGAIDNQPLVTQEPvkatsltleGGRLKqtPQLIHGRDYEMVPEPVWRALYHWYGANLA-LPRPVI 602
Cdd:smart00695   28 GKDPGPIDNSGILCSHG---------GPRLK--EHLVEGEDYVLIPEELWNKLVRWYGGGPGpIPRKVV 85
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1530-1597 4.45e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.35  E-value: 4.45e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622878581 1530 DQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNpNCKWYCYNDSSCKELHPDEIDT---DSAYILFYEQ 1597
Cdd:COG5533    214 DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK-GGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
254-310 3.60e-06

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 46.00  E-value: 3.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622878581  254 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 310
Cdd:cd00051      6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
253-310 4.82e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 4.82e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622878581  253 LFNAFDENRDNHIDFKEISCGLSACCRG-PL--AERQKFcFKVFDVDRDGVLSRVELRDMV 310
Cdd:pfam13499    7 AFKLLDSDGDGYLDVEELKKLLRKLEEGePLsdEEVEEL-FKEFDLDKDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
251-354 4.57e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 4.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  251 EGLFNAFDENRDNHIDFKEISCGLSACCRGPLAERQKFCFKVFDVDRDGVLSRVELRdmvvALLEVWKDNRTDdipelhm 330
Cdd:COG5126     36 ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFR----RLLTALGVSEEE------- 104
                           90       100
                   ....*....|....*....|....
gi 1622878581  331 dlsdiVEGILNAHDTTKMGHLTLE 354
Cdd:COG5126    105 -----ADELFARLDTDGDGKISFE 123
EF-hand_7 pfam13499
EF-hand domain pair;
287-359 5.72e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 5.72e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622878581  287 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 359
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
535-1347 2.82e-83

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 292.94  E-value: 2.82e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  535 PQKPGAIDNQPLVTQEPvkatsltlegGRLKqtPQLIHGRDYEMVPEPVWRALYHWYG-ANLALPRPVIKNSKTDIPELE 613
Cdd:COG5560     66 GGSPGPIVQGPIVDFEP----------ESLK--KSLREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLPSESAPEVE 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  614 LFPrylLFLRQQPATRTQQSNIWVNMGMMSLRMfpqhfprgnvpspnaplkrvlaytgcfSRMQTIKEIHEYLSQRLRIK 693
Cdd:COG5560    134 SYP---VVFKLHWLFSINGSLINLGHDPVPHSA---------------------------SSHGTLRDLSERVMNAFVDP 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  694 EEDMRLWLYNSEN-YLTLLDDEDHRLEYLKIQDEQHLVIEVR---NKDMSwPEEMSFIAN--SSKIDRHKVPT------E 761
Cdd:COG5560    184 SDDFRLWDVVPEImGLRLGLDSFFRRYRVLASDGRVLHPLTRlelFEDRS-VLLLSKITRnpDWLVDSIVDDHnrsinkE 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  762 KGATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWT 841
Cdd:COG5560    263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  842 IAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVE---LKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQL 918
Cdd:COG5560    343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMY 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  919 RSQVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIKLDGT-TPVRygLRLNMDEKYTGLKKQLSDLCG-LNSEQIL 996
Cdd:COG5560    423 KSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRrQPLK--IELDASSTIRGLKKLVDAEYGkLGCFEIK 500
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  997 LAEVHGSNIKNFPQDNQKVRLSvsgflcafEIPvpaspisassptQTDFSSSPSTNgmftlttngdlprpifiPNGMPNT 1076
Cdd:COG5560    501 VMCIYYGGNYNMLEPADKVLLQ--------DIP------------QTDFVYLYETN-----------------DNGIEVP 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1077 VVPCGTEKNFTNGMVNGHmsslpdsPFTGYII----AVHRKMMRTELYFLSSQKNRPSLFGM-PLIVPCTVHTRKKDLYd 1151
Cdd:COG5560    544 VVHLRIEKGYKSKRLFGD-------PFLQLNVlikaSIYDKLVKEFEELLVLVEMKKTDVDLvSEQVRLLREESSPSSW- 615
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1152 avwiqVSRLASPLPPQEASNHAQDcddsmgyQYPFTLRVVqkdgNTCAWCpwyrfcrgckiDCGEDRAFIGNAyiavdwd 1231
Cdd:COG5560    616 -----LKLETEIDTKREEQVEEEG-------QMNFNDAVV----ISCEWE-----------EKRYLSLFSYDP------- 661
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1232 ptalhlryqtsqervvdehESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILII 1311
Cdd:COG5560    662 -------------------LWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILII 722
                          810       820       830
                   ....*....|....*....|....*....|....*.
gi 1622878581 1312 HLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRD 1347
Cdd:COG5560    723 HLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVD 758
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
765-958 1.80e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 181.49  E-value: 1.80e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  765 TGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELWSGTQKN-VAPLKLRWTIA 843
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNSKSSsVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  844 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVK 923
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622878581  924 CKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIK 958
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQI 166
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1256-1596 5.22e-29

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 116.62  E-value: 5.22e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1256 SRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRE 1335
Cdd:cd02674     76 SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLN 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1336 SFDPSAFLVPRDPalcrrkpltpqgdelseprvlarevkkvdaqssageedvllskspsslsaniisspkgspsssrksg 1415
Cdd:cd02674    156 DLDLTPYVDTRSF------------------------------------------------------------------- 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1416 ascpssknsspsssprtlgrskgrlrlpqigsknklssskenldasrdngagqiceladalsrghmlggsqpelvtpqdh 1495
Cdd:cd02674        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1496 evalANGFLYeheacgngysngqlgnhseedstddqredtrikpiyNLYAISCHSGILGGGHYVTYAKNPNC-KWYCYND 1574
Cdd:cd02674    169 ----TGPFKY------------------------------------DLYAVVNHYGSLNGGHYTAYCKNNETnDWYKFDD 208
                          330       340
                   ....*....|....*....|..
gi 1622878581 1575 SSCKELHPDEIDTDSAYILFYE 1596
Cdd:cd02674    209 SRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1262-1595 8.19e-26

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 109.84  E-value: 8.19e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1262 EPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPREsfdpsa 1341
Cdd:pfam00443  160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE------ 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1342 flvprdpalcrrkpltpqgdelseprvlarevkkvdaqssageedvllskspsslsaniisspkgspsssrksgascpss 1421
Cdd:pfam00443      --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1422 knsspsssprtlgrskgrlrlpqigsknklssskenLDASRdngagqiceladalsrghmlggsqpelvtpqdhevalan 1501
Cdd:pfam00443  234 ------------------------------------LDLSR--------------------------------------- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1502 gflyeheacgngysngqlgnhseeDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNP-NCKWYCYNDSSCKEL 1580
Cdd:pfam00443  239 ------------------------YLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYeNNRWYKFDDEKVTEV 294
                          330
                   ....*....|....*.
gi 1622878581 1581 HPD-EIDTDSAYILFY 1595
Cdd:pfam00443  295 DEEtAVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
766-956 7.87e-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: 7.87e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  766 GLSNLGNTCFMNSSIQCVSNtqpltqyfisgrhlyelnrtnpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 845
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  846 aprfngfQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 925
Cdd:cd02674     21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1622878581  926 TCGHISVRFDPFNFLSLPLPMDSYMHLEITV 956
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSGDAPKVTL 86
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
764-942 2.86e-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: 2.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  764 ATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIgmkghMAKCYGDLVQELWSGTQKNVAPLKLRWTIA 843
Cdd:cd02661      1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFC-----MMCALEAHVERALASSGPGSAPRIFSSNLK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  844 KYAPRFNGFQQQDSQELLAFLLDGLHED-LNRvhekpYVELKDSDgrpdwevaaeawdnHLRRNRSIVVDLFHGQLRSQV 922
Cdd:cd02661     76 QISKHFRIGRQEDAHEFLRYLLDAMQKAcLDR-----FKKLKAVD--------------PSSQETTLVQQIFGGYLRSQV 136
                          170       180
                   ....*....|....*....|
gi 1622878581  923 KCKTCGHISVRFDPFNFLSL 942
Cdd:cd02661    137 KCLNCKHVSNTYDPFLDLSL 156
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
766-945 1.82e-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: 1.82e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  766 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPigmKGHMAKCYGDLVQELW-SGTQKNVAPLKLRWTIAK 844
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSP---NSCLSCAMDEIFQEFYySGDRSPYGPINLLYLSWK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  845 YAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPyvelkdsdgrpdwevaaeawdNHLRRNRSIVVDLFHGQLRSQVKC 924
Cdd:cd02660     79 HSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEA---------------------NDESHCNCIIHQTFSGSLQSSVTC 137
                          170       180
                   ....*....|....*....|.
gi 1622878581  925 KTCGHISVRFDPFNFLSLPLP 945
Cdd:cd02660    138 QRCGGVSTTVDPFLDLSLDIP 158
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
766-955 3.49e-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: 3.49e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  766 GLSNLGNTCFMNSSIQCvsntqpltqyfisgrhLYelnrtnpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 845
Cdd:cd02257      1 GLNNLGNTCYLNSVLQA----------------LF--------------------------------------------- 19
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  846 aprfngFQQQDSQELLAFLLDGLHEDLNRVHEKpyvelkdsdgrpdwevaaeawDNHLRRNRSIVVDLFHGQLRSQVKCK 925
Cdd:cd02257     20 ------SEQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                          170       180       190
                   ....*....|....*....|....*....|
gi 1622878581  926 TCGHISVRFDPFNFLSLPLPMDSYMHLEIT 955
Cdd:cd02257     73 ECGHESVSTEPELFLSLPLPVKGLPQVSLE 102
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
766-962 3.55e-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: 3.55e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  766 GLSNLGNTCFMNSSIQCVSNTQPLTqyfisgrhlyelnrtnpigmkghmakcygdlvqELWSGTqknvaPLKLRWTIAKY 845
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALR---------------------------------ELLSET-----PKELFSQVCRK 42
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  846 APRFNGFQQQDSQELLAFLLDGLhedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnRSIVVDLFHGQLRSQVKCK 925
Cdd:cd02667     43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622878581  926 TCGHISVRFDPFNFLSLPLP--------MDSYMHLEITVIKLDGT 962
Cdd:cd02667     85 SCGTVSLVYEPFLDLSLPRSdeiksecsIESCLKQFTEVEILEGN 129
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1262-1348 3.15e-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: 3.15e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1262 EPINLDSCLRAFTSEEELGENEMYYCSKCKtHCLATKKLDLWRLPPILIIHLKRFQFVN-GRWIKSQKIVKFPrESFDPS 1340
Cdd:cd02257     97 PQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFNEdGTKEKLNTKVSFP-LELDLS 174

                   ....*...
gi 1622878581 1341 AFLVPRDP 1348
Cdd:cd02257    175 PYLSEGEK 182
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
766-947 6.77e-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: 6.77e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  766 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPI-GMKGHMAKcygdLVQELWSG--------------TQ 830
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPAnDLNCQLIK----LADGLLSGryskpaslksendpYQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  831 KNVAPLKLRWTIAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPyvelkdsdgrpdwevaaeawdnhlrrnrsiV 910
Cdd:cd02658     77 VGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLN------------------------------P 126
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1622878581  911 VDLFHGQLRSQVKCKTCGHISVRFDPFNFLSLPLPMD 947
Cdd:cd02658    127 NDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKD 163
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1265-1343 1.82e-14

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 76.16  E-value: 1.82e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622878581 1265 NLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRwiKSQKIVKFPrESFDPSAFL 1343
Cdd:cd02661    163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGG--KINKQISFP-ETLDLSPYM 238
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
766-945 5.52e-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: 5.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  766 GLSNLGNTCFMNSSIQCVSNTQPLTQYFISgRHLYELNRTNPIGMKGHMakcygdlVQELWSGTQKNVAPLKLRWTIAKY 845
Cdd:cd02664      1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS-LNLPRLGDSQSVMKKLQL-------LQAHLMHTQRRAEAPPDYFLEASR 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  846 APRFNGFQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 925
Cdd:cd02664     73 PPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTIRCL 114
                          170       180
                   ....*....|....*....|
gi 1622878581  926 TCGHISVRFDPFNFLSLPLP 945
Cdd:cd02664    115 NCNSTSARTERFRDLDLSFP 134
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1262-1345 4.00e-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: 4.00e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1262 EPINLDSCLRAFTSEEELGENEMYYCSKCkthCLATKKLDLWRLPPILIIHLKRF-QFVNGRWIKSQKIVKFPrESFDPS 1340
Cdd:cd02667    109 SECSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFqQPRSANLRKVSRHVSFP-EILDLA 184

                   ....*
gi 1622878581 1341 AFLVP 1345
Cdd:cd02667    185 PFCDP 189
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1265-1344 1.12e-11

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 68.05  E-value: 1.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1265 NLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF--VNGRWIKSQKIVKFPREsFDPSAF 1342
Cdd:cd02659    152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDRFEFPLE-LDMEPY 230

                   ..
gi 1622878581 1343 LV 1344
Cdd:cd02659    231 TE 232
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1260-1333 1.14e-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: 1.14e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622878581 1260 QAEPINLDSCLRAFTSEEELGENEmYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRwiKSQKI---VKFP 1333
Cdd:cd02660    172 VSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNK--TSRKIdtyVQFP 245
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1264-1335 1.60e-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: 67.33  E-value: 1.60e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622878581 1264 INLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVN--GRWIK-SQKIVkFPRE 1335
Cdd:cd02663    147 TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEqlNRYIKlFYRVV-FPLE 220
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
766-955 4.24e-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: 4.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  766 GLSNLGNTCFMNSSIQCvsntqpltqyfisgrhLYELNrtnpigmkghMAKCYGDLVQELWSGTQKN--VAPLKLRWTIA 843
Cdd:cd02663      1 GLENFGNTCYCNSVLQA----------------LYFEN----------LLTCLKDLFESISEQKKRTgvISPKKFITRLK 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  844 KYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVELKDSDgrpdwevaaeawDNHLRRNRSIVVDLFHGQLRSQVK 923
Cdd:cd02663     55 RENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNN------------NNNAEPQPTWVHEIFQGILTNETR 122
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622878581  924 CKTCGHISVRFDPFnflsLPLPMDSYMHLEIT 955
Cdd:cd02663    123 CLTCETVSSRDETF----LDLSIDVEQNTSIT 150
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
766-978 1.39e-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: 1.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  766 GLSNLGNTCFMNSSIQCVsNTQP-----LTQYFISGRHLYELNRTNPIGMKghmakcygDLVQELwSGTQKNVAPLKLRW 840
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCL-RSVPelrdaLKNYNPARRGANQSSDNLTNALR--------DLFDTM-DKKQEPVPPIEFLQ 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  841 TIAKYAPRF------NGFQQQDSQELLAFLLDGLHEDLnrvhekpyvELKDSDGrpdwevaaeawdnhlrrnrSIVVDLF 914
Cdd:cd02657     71 LLRMAFPQFaekqnqGGYAQQDAEECWSQLLSVLSQKL---------PGAGSKG-------------------SFIDQLF 122
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622878581  915 HGQLRSQVKCKTCGHI-SVRFDPFNFLSLPLPMD---SYMH------LEITVIKLDGTtpvryglrLNMDEKYT 978
Cdd:cd02657    123 GIELETKMKCTESPDEeEVSTESEYKLQCHISITtevNYLQdglkkgLEEEIEKHSPT--------LGRDAIYT 188
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1539-1595 2.60e-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: 2.60e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622878581 1539 PIYNLYAISCHSGILG-GGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1595
Cdd:cd02661    246 LKYKLYAVLVHSGFSPhSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
536-603 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 1622878581  536 QKPGAIDNQPLVTqepvkatslTLEGGRLKqtPQLIHGRDYEMVPEPVWRALYHWYGANLALPRPVIK 603
Cdd:pfam06337   24 NEPGPIDNSDLLD---------DESNGQLK--PNLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRNVVN 80
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
766-953 9.31e-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: 9.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  766 GLSNLGNTCFMNSSIQcvsntqplTQYFISG-----RHLYELNrtnpIGMKGHMAKCygDLVQELWSGTQKNVAPLKLRW 840
Cdd:cd02671     26 GLNNLGNTCYLNSVLQ--------VLYFCPGfkhglKHLVSLI----SSVEQLQSSF--LLNPEKYNDELANQAPRRLLN 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  841 TIAKYAPRFNGFQQQDSQELLAFLLDGLhedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnRSIVVDLFHGQLRS 920
Cdd:cd02671     92 ALREVNPMYEGYLQHDAQEVLQCILGNI--------------------------------------QELVEKDFQGQLVL 133
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1622878581  921 QVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLE 953
Cdd:cd02671    134 RTRCLECETFTERREDFQDISVPVQESELSKSE 166
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1521-1598 2.07e-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: 2.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1521 NHSEEDSTDDQREDTrikpIYNLYAISCHSGILGGGHYVTYAK-NPNCKWYCYNDSSCKELHPDEID------------- 1586
Cdd:cd02659    236 AKKEGDSEKKDSESY----IYELHGVLVHSGDAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEeecfggeetqkty 311
                           90       100
                   ....*....|....*....|.
gi 1622878581 1587 ---------TDSAYILFYEQQ 1598
Cdd:cd02659    312 dsgprafkrTTNAYMLFYERK 332
DUSP smart00695
Domain in ubiquitin-specific proteases;
535-602 9.15e-09

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 53.90  E-value: 9.15e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622878581   535 PQKPGAIDNQPLVTQEPvkatsltleGGRLKqtPQLIHGRDYEMVPEPVWRALYHWYGANLA-LPRPVI 602
Cdd:smart00695   28 GKDPGPIDNSGILCSHG---------GPRLK--EHLVEGEDYVLIPEELWNKLVRWYGGGPGpIPRKVV 85
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1530-1597 4.45e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.35  E-value: 4.45e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622878581 1530 DQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNpNCKWYCYNDSSCKELHPDEIDT---DSAYILFYEQ 1597
Cdd:COG5533    214 DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK-GGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1265-1348 6.60e-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: 6.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1265 NLDSCLRAFTSEEEL-GENEmYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF--VNGRWIKSQKIVKFPrESFDPSA 1341
Cdd:cd02668    157 TLEECIDEFLKEEQLtGDNQ-YFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdrKTGAKKKLNASISFP-EILDMGE 234

                   ....*..
gi 1622878581 1342 FLVPRDP 1348
Cdd:cd02668    235 YLAESDE 241
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
766-942 7.91e-08

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 56.11  E-value: 7.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  766 GLSNLGNTCFMNSSIQcvsntqplTQYFISG--RHLYELNRT-NPIGMKG---HMAKCYGDLvQELwsgtQKNVAPLKLR 839
Cdd:cd02659      4 GLKNQGATCYMNSLLQ--------QLYMTPEfrNAVYSIPPTeDDDDNKSvplALQRLFLFL-QLS----ESPVKTTELT 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  840 WTIAKYAPR-FNGFQQQDSQELLAFLLDGLHEDLnrvhekPYVELKDsdgrpdwevaaeawdnhlrrnrsIVVDLFHGQL 918
Cdd:cd02659     71 DKTRSFGWDsLNTFEQHDVQEFFRVLFDKLEEKL------KGTGQEG-----------------------LIKNLFGGKL 121
                          170       180
                   ....*....|....*....|....
gi 1622878581  919 RSQVKCKTCGHISVRFDPFNFLSL 942
Cdd:cd02659    122 VNYIICKECPHESEREEYFLDLQV 145
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
766-951 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 1622878581  766 GLSNLGNTCFMNSSIQCVSNTQPLTQYfisgrhlyeLNRTNpigmkghmakcygdlvqelwsgtqknvaplklrwtiaky 845
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLIEY---------LEEFL--------------------------------------- 32
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  846 aprfngfQQQDSQELLAFLLDGLHedlnrvhekpyvelkdsdgrpdwevaaeawdnhlrrnrSIVVDLFHGQLRSQVKCK 925
Cdd:cd02662     33 -------EQQDAHELFQVLLETLE--------------------------------------QLLKFPFDGLLASRIVCL 67
                          170       180
                   ....*....|....*....|....*..
gi 1622878581  926 TCGHIS-VRFDPFNFLSLPLPMDSYMH 951
Cdd:cd02662     68 QCGESSkVRYESFTMLSLPVPNQSSGS 94
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1538-1596 1.94e-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: 1.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1538 KPIYNLYAISCHSGILGGGHYVTYAK----------------------NPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1595
Cdd:cd02667    199 SVLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278

                   .
gi 1622878581 1596 E 1596
Cdd:cd02667    279 E 279
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
766-872 2.97e-07

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 54.04  E-value: 2.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  766 GLSNLGNTCFMNSSIQCVS-NTQPLTQYfiSGRHLYELNrtnpiGMKGHMAKCYGDLVQELWSGTQKNVAPLKlrwtIAK 844
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILAlYLPKLDEL--LDDLSKELK-----VLKNVIRKPEPDLNQEEALKLFTALWSSK----EHK 69
                           90       100
                   ....*....|....*....|....*...
gi 1622878581  845 YAPRFNGFQQQDSQELLAFLLDGLHEDL 872
Cdd:COG5533     70 VGWIPPMGSQEDAHELLGKLLDELKLDL 97
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
254-310 3.60e-06

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 46.00  E-value: 3.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622878581  254 FNAFDENRDNHIDFKEISCGLSACCRGPL-AERQKFcFKVFDVDRDGVLSRVELRDMV 310
Cdd:cd00051      6 FRLFDKDGDGTISADELKAALKSLGEGLSeEEIDEM-IREVDKDGDGKIDFEEFLELM 62
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1540-1595 9.70e-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: 9.70e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622878581 1540 IYNLYAISCHSGILGGGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFY 1595
Cdd:cd02660    272 TYDLFAVVVHKGTLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1262-1318 1.48e-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: 1.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622878581 1262 EPINLDSCLRAFTSEEELGenemYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQF 1318
Cdd:cd02658    176 EPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQL 228
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
763-945 1.79e-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: 49.24  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  763 GATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGrHLYELNRTNpigmKGHMAKCYGDLVQELWSGT--QKNVAPLKLRW 840
Cdd:cd02669    118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLY-ENYENIKDR----KSELVKRLSELIRKIWNPRnfKGHVSPHELLQ 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  841 TIAKY-APRFNGFQQQDSQELLAFLLDGLHEDLNRvhekpyvelkdsdgrpdwevaaeawdnHLRRNRSIVVDLFHGQLR 919
Cdd:cd02669    193 AVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGG---------------------------SKKPNSSIIHDCFQGKVQ 245
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1622878581  920 --------------SQVKCKTCGH-ISVRFDPFNFLSLPLP 945
Cdd:cd02669    246 ietqkikphaeeegSKDKFFKDSRvKKTSVSPFLLLTLDLP 286
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1540-1596 2.25e-05

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 48.48  E-value: 2.25e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622878581 1540 IYNLYAISCHSGILG-GGHYVTYAKNPNC-KWYCYNDSSCKELHPDEI-------DTDSAYILFYE 1596
Cdd:cd02657    240 YYELVAVITHQGRSAdSGHYVAWVRRKNDgKWIKFDDDKVSEVTEEDIlklsgggDWHIAYILLYK 305
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1538-1596 3.79e-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: 3.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1538 KPIYNLYAISCHSGILGGGHYVTYAKNPNC---------------------KWYCYNDSSCKELHPDEIDTD-SAYILFY 1595
Cdd:cd02662    160 KVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepgsfvrmregpsstshPWWRISDTTVKEVSESEVLEQkSAYMLFY 239

                   .
gi 1622878581 1596 E 1596
Cdd:cd02662    240 E 240
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1522-1596 4.15e-05

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 47.49  E-value: 4.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1522 HSEEDSTDDQREDTRIKpiYNLYAISCHSGI-LGGGHYVTYAKNPNCK---------------------WYCYNDSSCKE 1579
Cdd:cd02664    226 KEEESGDDGELVTRQVH--YRLYAVVVHSGYsSESGHYFTYARDQTDAdstgqecpepkdaeendesknWYLFNDSRVTF 303
                           90       100
                   ....*....|....*....|....
gi 1622878581 1580 LHPDEIDT-------DSAYILFYE 1596
Cdd:cd02664    304 SSFESVQNvtsrfpkDTPYILFYE 327
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
673-741 4.29e-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: 4.29e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622878581  673 FSRMQTIKEIHEYLSQRLRI-KEEDMRLW-LYNSENYlTLLDDEDHRLEYLKIQDEQHLVIEVRNKDMSWP 741
Cdd:pfam14836   18 FSKTDTIDFIEKELRKLFSIpKEKETRLWnRYSSNTR-ELLTDPDITVQEAGLYHGQVLLIEEKNEDGNWP 87
EF-hand_7 pfam13499
EF-hand domain pair;
253-310 4.82e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 4.82e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622878581  253 LFNAFDENRDNHIDFKEISCGLSACCRG-PL--AERQKFcFKVFDVDRDGVLSRVELRDMV 310
Cdd:pfam13499    7 AFKLLDSDGDGYLDVEELKKLLRKLEEGePLsdEEVEEL-FKEFDLDKDGRISFEEFLELY 66
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1538-1595 3.45e-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: 3.45e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622878581 1538 KPIYNLYAISCHSGI-LGGGHYVTYAknpncKWYCYNDSSCK---------ELHPDEIDTDSAYILFY 1595
Cdd:cd02671    269 NDVYRLFAVVMHSGAtISSGHYTAYV-----RWLLFDDSEVKvteekdfleALSPNTSSTSTPYLLFY 331
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
251-354 4.57e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 4.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  251 EGLFNAFDENRDNHIDFKEISCGLSACCRGPLAERQKFCFKVFDVDRDGVLSRVELRdmvvALLEVWKDNRTDdipelhm 330
Cdd:COG5126     36 ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFR----RLLTALGVSEEE------- 104
                           90       100
                   ....*....|....*....|....
gi 1622878581  331 dlsdiVEGILNAHDTTKMGHLTLE 354
Cdd:COG5126    105 -----ADELFARLDTDGDGKISFE 123
EF-hand_7 pfam13499
EF-hand domain pair;
287-359 5.72e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 5.72e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622878581  287 KFCFKVFDVDRDGVLSRVELRDMVVALlevwkdnrtddipELHMDLSD-IVEGILNAHDTTKMGHLTLEDYQIW 359
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKL-------------EEGEPLSDeEVEELFKEFDLDKDGRISFEEFLEL 65
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1273-1319 1.03e-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: 1.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622878581 1273 FTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFV 1319
Cdd:cd02664    143 FLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYD 189
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1265-1335 1.36e-03

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 42.35  E-value: 1.36e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622878581 1265 NLDSCLRAFTSEEELgenEMYYCSKCKThclatkklDLWRLPPILIIHLKRFQF-VNGRWIKSQKIVKFPRE 1335
Cdd:cd02662     97 TLEHCLDDFLSTEII---DDYKCDRCQT--------VIVRLPQILCIHLSRSVFdGRGTSTKNSCKVSFPER 157
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
207-310 1.37e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  207 HLEESDIIDLEKRYW--LLKA--QSRTGRFDLETF----GPLVSPPIRPSLsEGLFNAFDENRDNHIDFKEISCGLSACc 278
Cdd:COG5126     21 VLERDDFEALFRRLWatLFSEadTDGDGRISREEFvagmESLFEATVEPFA-RAAFDLLDTDGDGKISADEFRRLLTAL- 98
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622878581  279 RGPLAERQKFcFKVFDVDRDGVLSRVELRDMV 310
Cdd:COG5126     99 GVSEEEADEL-FARLDTDGDGKISFEEFVAAV 129
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1539-1596 1.84e-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: 1.84e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622878581 1539 PIYNLYAISCHSG-ILGGGHYVTYAKN--PNCKW-YCyNDSSCKELHPDEIDTD---SAYILFYE 1596
Cdd:cd02673    182 AKYSLVAVICHLGeSPYDGHYIAYTKElyNGSSWlYC-SDDEIRPVSKNDVSTNarsSGYLIFYD 245
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1541-1595 2.95e-03

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 41.71  E-value: 2.95e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622878581 1541 YNLYAISCHSGILGGGHYVTYAKN-PNCKWYCYNDSSCKElHPDE---IDTDSA----YILFY 1595
Cdd:cd02666    281 YRLHAVFIHRGEASSGHYWVYIKDfEENVWRKYNDETVTV-VPASevfLFTLGNtatpYFLVY 342
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1273-1352 3.19e-03

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 41.92  E-value: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581 1273 FTSEEELGENEMYYcskckthclatkklDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRDPALCR 1352
Cdd:cd02669    314 GKTETELKDSLKRY--------------LISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNL 379
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1541-1595 3.65e-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: 3.65e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622878581 1541 YNLYAISCHSGILGGGHYVTYA-KNPNCKWYCYNDSSCKELHPDEIDTD--------SAYILFY 1595
Cdd:cd02665    164 YELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDsfgggrnpSAYCLMY 227
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
287-325 7.10e-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: 7.10e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622878581  287 KFCFKVFDVDRDGVLSRVELRDMVVALLEVWKDNRTDDI 325
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. ...
254-357 8.01e-03

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 38.42  E-value: 8.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878581  254 FNAFDENRDNHIDFKEIS---CGLSACCRGPLAERQkfcFKVFDVDRDGVLSRVELRDMVVALLEvwkdnrtddIPELHM 330
Cdd:cd15898      6 WIKADKDGDGKLSLKEIKkllKRLNIRVSEKELKKL---FKEVDTNGDGTLTFDEFEELYKSLTE---------RPELEP 73
                           90       100
                   ....*....|....*....|....*..
gi 1622878581  331 dlsdivegILNAHDTTKMGHLTLEDYQ 357
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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