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Conserved domains on  [gi|594150411|ref|NP_001277354|]
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ubiquitin carboxyl-terminal hydrolase 45 isoform 2 [Mus musculus]

Protein Classification

zf-UBP and Peptidase_C19K domain-containing protein( domain architecture ID 10489773)

zf-UBP and Peptidase_C19K domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-762 2.77e-91

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: 287.36  E-value: 2.77e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 192 GITNLGNTCFFNAVIQNLAQTYILFELMNEikedgtkfkislssapqleplvvelsspgpltsalflflhsmkeaekgpl 271
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTeetkriqasilkafnnpttktaddetrkkvkaygkegvkmnFI 351
Cdd:cd02667   31 TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLRT-----------------------------------------FI 69
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 352 DRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEERNqlshdrkhlrkwpseeektvvthpkndnleasppastlste 431
Cdd:cd02667   70 DSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK----------------------------------------- 108
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 432 aslnesltdgserdaslessvdadseasepeiaskqpvllrsrgdscghaeqhphlplaselpqakethggeeemaeaia 511
Cdd:cd02667      --------------------------------------------------------------------------------
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 512 elhlsgtvtgnrdfhrekqplnvpnnlcfsegkhtrlhsaqnafqtlsqsyvttsKECSVQSCLYQFTSMELLMGNNKLL 591
Cdd:cd02667  109 -------------------------------------------------------SECSIESCLKQFTEVEILEGNNKFA 133
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 592 CEDCTEkrrkchketssaekkaggvytnARKQLLISAVPAILILHLKRFHQAGL-SLRKVNRHVDFPLTLDLAPFCAATC 670
Cdd:cd02667  134 CENCTK----------------------AKKQYLISKLPPVLVIHLKRFQQPRSaNLRKVSRHVSFPEILDLAPFCDPKC 191
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 671 KNISVGEKVLYGLYGIVEHSGSMRGGHYTAYVKVRVPSRKLSECITGRKTAAGLKEPDGElgghWVHVSDTYVQVVPESR 750
Cdd:cd02667  192 NSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQRLSDLTKSKPAADEAGPGSGQ----WYYISDSDVREVSLEE 267
                        570
                 ....*....|..
gi 594150411 751 ALSAQAYLLFYE 762
Cdd:cd02667  268 VLKSEAYLLFYE 279
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
62-132 5.57e-15

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 69.98  E-value: 5.57e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594150411   62 CSECLKERRfcdgqpvlpadVWLCLKCGLQGCGKNSESqHSLRHFKSSGtesHCVVISLSTWVIWCYECNE 132
Cdd:pfam02148   1 CSLCGNTSN-----------LWLCLTCGHVGCGRYQNS-HALEHYEETG---HPLAVNLSTLTVYCYPCDD 56
 
Name Accession Description Interval E-value
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-762 2.77e-91

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: 287.36  E-value: 2.77e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 192 GITNLGNTCFFNAVIQNLAQTYILFELMNEikedgtkfkislssapqleplvvelsspgpltsalflflhsmkeaekgpl 271
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTeetkriqasilkafnnpttktaddetrkkvkaygkegvkmnFI 351
Cdd:cd02667   31 TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLRT-----------------------------------------FI 69
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 352 DRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEERNqlshdrkhlrkwpseeektvvthpkndnleasppastlste 431
Cdd:cd02667   70 DSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK----------------------------------------- 108
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 432 aslnesltdgserdaslessvdadseasepeiaskqpvllrsrgdscghaeqhphlplaselpqakethggeeemaeaia 511
Cdd:cd02667      --------------------------------------------------------------------------------
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 512 elhlsgtvtgnrdfhrekqplnvpnnlcfsegkhtrlhsaqnafqtlsqsyvttsKECSVQSCLYQFTSMELLMGNNKLL 591
Cdd:cd02667  109 -------------------------------------------------------SECSIESCLKQFTEVEILEGNNKFA 133
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 592 CEDCTEkrrkchketssaekkaggvytnARKQLLISAVPAILILHLKRFHQAGL-SLRKVNRHVDFPLTLDLAPFCAATC 670
Cdd:cd02667  134 CENCTK----------------------AKKQYLISKLPPVLVIHLKRFQQPRSaNLRKVSRHVSFPEILDLAPFCDPKC 191
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 671 KNISVGEKVLYGLYGIVEHSGSMRGGHYTAYVKVRVPSRKLSECITGRKTAAGLKEPDGElgghWVHVSDTYVQVVPESR 750
Cdd:cd02667  192 NSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQRLSDLTKSKPAADEAGPGSGQ----WYYISDSDVREVSLEE 267
                        570
                 ....*....|..
gi 594150411 751 ALSAQAYLLFYE 762
Cdd:cd02667  268 VLKSEAYLLFYE 279
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
192-761 1.22e-33

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 131.41  E-value: 1.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  192 GITNLGNTCFFNAVIQNLAQTYILFELMNEIKEDGTKFKISLSSApqleplvvelsspgpLTSALFLFLHSMKEAEKG-P 270
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------------LLCALRDLFKALQKNSKSsS 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  271 LSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTEEtkriqasilkafnNPTTKTADDetrkkvkaygkegvkmNF 350
Cdd:pfam00443  67 VSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDL-------------NGNHSTENE----------------SL 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  351 IDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEernqlshdrkhlrkwpseeektvvthpkndnleasppastlst 430
Cdd:pfam00443 118 ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG------------------------------------------- 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  431 easlnesltdgserdaslessvdadseasepeiaskqpvllrsrgdscghaeqhphlplaselpqakethggeeemaeai 510
Cdd:pfam00443     --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  511 aelhlsgtvtgnrdfhrekqplnvpnnlcfsegkhtrlhsaqnafqtlsqsYVTTSKECSVQSCLYQFTSMELLMGNNKL 590
Cdd:pfam00443 155 ---------------------------------------------------DSAELKTASLQICFLQFSKLEELDDEEKY 183
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  591 LCEDCtekrrKCHKETSsaekkaggvytnarKQLLISAVPAILILHLKRFHQAGLSLRKVNRHVDFPLTLDLAPFCAATc 670
Cdd:pfam00443 184 YCDKC-----GCKQDAI--------------KQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRYLAEE- 243
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  671 KNISVGEKVLYGLYGIVEHSGSMRGGHYTAYVKvrvpsrklsecitgrktaaglKEPDGElgghWVHVSDTYVQVVPESR 750
Cdd:pfam00443 244 LKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIK---------------------AYENNR----WYKFDDEKVTEVDEET 298
                         570
                  ....*....|..
gi 594150411  751 A-LSAQAYLLFY 761
Cdd:pfam00443 299 AvLSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
192-763 4.46e-27

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 117.68  E-value: 4.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 192 GITNLGNTCFFNAVIQNLAQTYilfELMNEIKEDGTKFKISLSSapqlePLVVElsspGPLTSALFLFLHSMKEAEKGPL 271
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTW---ELRDYFLSDEYEESINEEN-----PLGMH----GSVASAYADLIKQLYDGNLHAF 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRtEETKRIQasILKAFNNPTTKTADDETRKKV-KAYGKEGVKMN- 349
Cdd:COG5560  335 TPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLH-EDLNRII--KKPYTSKPDLSPGDDVVVKKKaKECWWEHLKRNd 411
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 350 -FIDRIFIGELTSTVMCEECANISTMKDPFIDISLPIieERNQlshdrkhlrKWpseeEKTVVTHPKNDNLeaSPPASTL 428
Cdd:COG5560  412 sIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL--PVSM---------VW----KHTIVVFPESGRR--QPLKIEL 474
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 429 STEAS---LNESLTDGSERDASLESSVDA---DSEASEPEIASKQPVLLRSRGDSC----------------GHAEQ--- 483
Cdd:COG5560  475 DASSTirgLKKLVDAEYGKLGCFEIKVMCiyyGGNYNMLEPADKVLLQDIPQTDFVylyetndngievpvvhLRIEKgyk 554
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 484 ------HPHLPLASELPQA------KE-------THGGEEEMAEAIAELHLSGTVTG---------NRDFHREKQ----- 530
Cdd:COG5560  555 skrlfgDPFLQLNVLIKASiydklvKEfeellvlVEMKKTDVDLVSEQVRLLREESSpsswlkletEIDTKREEQveeeg 634
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 531 ----PLNVpNNLCFSEGKhtrlhSAQNAFQT----LSQSYVTTSKECSVQSCLYQFTSMELLMGNNKLLCEDCTEKRRkc 602
Cdd:COG5560  635 qmnfNDAV-VISCEWEEK-----RYLSLFSYdplwTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQ-- 706
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 603 hketssaekkaggvytnARKQLLISAVPAILILHLKRFHQAGLSLRKVNRHVDFPLT-LDLAPFCAATcknisVGEKVLY 681
Cdd:COG5560  707 -----------------ASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDdLDLSGVEYMV-----DDPRLIY 764
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 682 GLYGIVEHSGSMRGGHYTAYVkvrvpsrklsecitgrktaaglKEPDgelGGHWVHVSDTYVQVVPESRALSAQAYLLFY 761
Cdd:COG5560  765 DLYAVDNHYGGLSGGHYTAYA----------------------RNFA---NNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819

                 ..
gi 594150411 762 ER 763
Cdd:COG5560  820 RR 821
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
62-132 5.57e-15

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 69.98  E-value: 5.57e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594150411   62 CSECLKERRfcdgqpvlpadVWLCLKCGLQGCGKNSESqHSLRHFKSSGtesHCVVISLSTWVIWCYECNE 132
Cdd:pfam02148   1 CSLCGNTSN-----------LWLCLTCGHVGCGRYQNS-HALEHYEETG---HPLAVNLSTLTVYCYPCDD 56
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
62-122 1.93e-06

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 45.43  E-value: 1.93e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594150411    62 CSECLkerrfcdgqpvLPADVWLCLKCGLQGCGkNSESQHSLRHFKSSGtesHCVVISLST 122
Cdd:smart00290   2 CSVCG-----------TIENLWLCLTCGQVGCG-RYQNGHALEHFEETG---HPLVVKLGT 47
 
Name Accession Description Interval E-value
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-762 2.77e-91

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: 287.36  E-value: 2.77e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 192 GITNLGNTCFFNAVIQNLAQTYILFELMNEikedgtkfkislssapqleplvvelsspgpltsalflflhsmkeaekgpl 271
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTeetkriqasilkafnnpttktaddetrkkvkaygkegvkmnFI 351
Cdd:cd02667   31 TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLRT-----------------------------------------FI 69
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 352 DRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEERNqlshdrkhlrkwpseeektvvthpkndnleasppastlste 431
Cdd:cd02667   70 DSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK----------------------------------------- 108
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 432 aslnesltdgserdaslessvdadseasepeiaskqpvllrsrgdscghaeqhphlplaselpqakethggeeemaeaia 511
Cdd:cd02667      --------------------------------------------------------------------------------
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 512 elhlsgtvtgnrdfhrekqplnvpnnlcfsegkhtrlhsaqnafqtlsqsyvttsKECSVQSCLYQFTSMELLMGNNKLL 591
Cdd:cd02667  109 -------------------------------------------------------SECSIESCLKQFTEVEILEGNNKFA 133
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 592 CEDCTEkrrkchketssaekkaggvytnARKQLLISAVPAILILHLKRFHQAGL-SLRKVNRHVDFPLTLDLAPFCAATC 670
Cdd:cd02667  134 CENCTK----------------------AKKQYLISKLPPVLVIHLKRFQQPRSaNLRKVSRHVSFPEILDLAPFCDPKC 191
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 671 KNISVGEKVLYGLYGIVEHSGSMRGGHYTAYVKVRVPSRKLSECITGRKTAAGLKEPDGElgghWVHVSDTYVQVVPESR 750
Cdd:cd02667  192 NSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQRLSDLTKSKPAADEAGPGSGQ----WYYISDSDVREVSLEE 267
                        570
                 ....*....|..
gi 594150411 751 ALSAQAYLLFYE 762
Cdd:cd02667  268 VLKSEAYLLFYE 279
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
192-761 1.22e-33

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 131.41  E-value: 1.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  192 GITNLGNTCFFNAVIQNLAQTYILFELMNEIKEDGTKFKISLSSApqleplvvelsspgpLTSALFLFLHSMKEAEKG-P 270
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------------LLCALRDLFKALQKNSKSsS 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  271 LSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTEEtkriqasilkafnNPTTKTADDetrkkvkaygkegvkmNF 350
Cdd:pfam00443  67 VSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDL-------------NGNHSTENE----------------SL 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  351 IDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEernqlshdrkhlrkwpseeektvvthpkndnleasppastlst 430
Cdd:pfam00443 118 ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG------------------------------------------- 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  431 easlnesltdgserdaslessvdadseasepeiaskqpvllrsrgdscghaeqhphlplaselpqakethggeeemaeai 510
Cdd:pfam00443     --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  511 aelhlsgtvtgnrdfhrekqplnvpnnlcfsegkhtrlhsaqnafqtlsqsYVTTSKECSVQSCLYQFTSMELLMGNNKL 590
Cdd:pfam00443 155 ---------------------------------------------------DSAELKTASLQICFLQFSKLEELDDEEKY 183
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  591 LCEDCtekrrKCHKETSsaekkaggvytnarKQLLISAVPAILILHLKRFHQAGLSLRKVNRHVDFPLTLDLAPFCAATc 670
Cdd:pfam00443 184 YCDKC-----GCKQDAI--------------KQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRYLAEE- 243
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  671 KNISVGEKVLYGLYGIVEHSGSMRGGHYTAYVKvrvpsrklsecitgrktaaglKEPDGElgghWVHVSDTYVQVVPESR 750
Cdd:pfam00443 244 LKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIK---------------------AYENNR----WYKFDDEKVTEVDEET 298
                         570
                  ....*....|..
gi 594150411  751 A-LSAQAYLLFY 761
Cdd:pfam00443 299 AvLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
563-762 7.54e-33

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: 127.60  E-value: 7.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 563 VTTSKECSVQSCLYQFTSMELLMGNNKLLCEdctekrrkchketssaekkaGGVYTNARKQLLISAVPAILILHLKRFHQ 642
Cdd:cd02257   93 VKGLPQVSLEDCLEKFFKEEILEGDNCYKCE--------------------KKKKQEATKRLKIKKLPPVLIIHLKRFSF 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 643 AG-LSLRKVNRHVDFPLTLDLAPFCAATCKNISVGEK-VLYGLYGIVEHSG-SMRGGHYTAYVKVRVPsrklsecitgrk 719
Cdd:cd02257  153 NEdGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNGsYKYELVAVVVHSGtSADSGHYVAYVKDPSD------------ 220
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 594150411 720 taaglkepdgelgGHWVHVSDTYVQVVPESRAL-----SAQAYLLFYE 762
Cdd:cd02257  221 -------------GKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
567-762 4.05e-30

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: 118.93  E-value: 4.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 567 KECSVQSCLYQFTSMELLMGNNKLLCEDCTEKRrkchketssaekkaggvytNARKQLLISAVPAILILHLKRFHQAGLS 646
Cdd:cd02674   82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKR-------------------KATKKLTISRLPKVLIIHLKRFSFSRGS 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 647 LRKVNRHVDFPLT-LDLAPFCAATCKNISvgekVLYGLYGIVEHSGSMRGGHYTAYVKVRVPSRklsecitgrktaaglk 725
Cdd:cd02674  143 TRKLTTPVTFPLNdLDLTPYVDTRSFTGP----FKYDLYAVVNHYGSLNGGHYTAYCKNNETND---------------- 202
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 594150411 726 epdgelgghWVHVSDTYVQVVPESRALSAQAYLLFYE 762
Cdd:cd02674  203 ---------WYKFDDSRVTKVSESSVVSSSAYILFYE 230
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
570-761 1.14e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 119.69  E-value: 1.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 570 SVQSCLYQFTSMELLMGNNKLLCEDCTEKrrkchketssaekkaggvyTNARKQLLISAVPAILILHLKRFhqAGLSLRK 649
Cdd:cd02661  163 SLEDALEQFTKPEQLDGENKYKCERCKKK-------------------VKASKQLTIHRAPNVLTIHLKRF--SNFRGGK 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 650 VNRHVDFPLTLDLAPFCAAtckniSVGEKVLYGLYGIVEHSG-SMRGGHYTAYVKvrvpsrklsecitgrkTAAGLkepd 728
Cdd:cd02661  222 INKQISFPETLDLSPYMSQ-----PNDGPLKYKLYAVLVHSGfSPHSGHYYCYVK----------------SSNGK---- 276
                        170       180       190
                 ....*....|....*....|....*....|...
gi 594150411 729 gelgghWVHVSDTYVQVVPESRALSAQAYLLFY 761
Cdd:cd02661  277 ------WYNMDDSKVSPVSIETVLSQKAYILFY 303
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
192-763 4.46e-27

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 117.68  E-value: 4.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 192 GITNLGNTCFFNAVIQNLAQTYilfELMNEIKEDGTKFKISLSSapqlePLVVElsspGPLTSALFLFLHSMKEAEKGPL 271
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTW---ELRDYFLSDEYEESINEEN-----PLGMH----GSVASAYADLIKQLYDGNLHAF 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRtEETKRIQasILKAFNNPTTKTADDETRKKV-KAYGKEGVKMN- 349
Cdd:COG5560  335 TPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLH-EDLNRII--KKPYTSKPDLSPGDDVVVKKKaKECWWEHLKRNd 411
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 350 -FIDRIFIGELTSTVMCEECANISTMKDPFIDISLPIieERNQlshdrkhlrKWpseeEKTVVTHPKNDNLeaSPPASTL 428
Cdd:COG5560  412 sIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL--PVSM---------VW----KHTIVVFPESGRR--QPLKIEL 474
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 429 STEAS---LNESLTDGSERDASLESSVDA---DSEASEPEIASKQPVLLRSRGDSC----------------GHAEQ--- 483
Cdd:COG5560  475 DASSTirgLKKLVDAEYGKLGCFEIKVMCiyyGGNYNMLEPADKVLLQDIPQTDFVylyetndngievpvvhLRIEKgyk 554
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 484 ------HPHLPLASELPQA------KE-------THGGEEEMAEAIAELHLSGTVTG---------NRDFHREKQ----- 530
Cdd:COG5560  555 skrlfgDPFLQLNVLIKASiydklvKEfeellvlVEMKKTDVDLVSEQVRLLREESSpsswlkletEIDTKREEQveeeg 634
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 531 ----PLNVpNNLCFSEGKhtrlhSAQNAFQT----LSQSYVTTSKECSVQSCLYQFTSMELLMGNNKLLCEDCTEKRRkc 602
Cdd:COG5560  635 qmnfNDAV-VISCEWEEK-----RYLSLFSYdplwTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQ-- 706
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 603 hketssaekkaggvytnARKQLLISAVPAILILHLKRFHQAGLSLRKVNRHVDFPLT-LDLAPFCAATcknisVGEKVLY 681
Cdd:COG5560  707 -----------------ASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDdLDLSGVEYMV-----DDPRLIY 764
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 682 GLYGIVEHSGSMRGGHYTAYVkvrvpsrklsecitgrktaaglKEPDgelGGHWVHVSDTYVQVVPESRALSAQAYLLFY 761
Cdd:COG5560  765 DLYAVDNHYGGLSGGHYTAYA----------------------RNFA---NNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819

                 ..
gi 594150411 762 ER 763
Cdd:COG5560  820 RR 821
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
191-761 1.06e-26

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: 111.70  E-value: 1.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 191 KGITNLGNTCFFNAVIQNLAQTYILFE-LMNEIKEDGTKFKISLSSAP-QLEPLVVELSSPGpltsalflflhsmkeaEK 268
Cdd:cd02660    1 RGLINLGATCFMNVILQALLHNPLLRNyFLSDRHSCTCLSCSPNSCLScAMDEIFQEFYYSG----------------DR 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 269 GPLSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTEETKRiqasilkafnnpttktaddetrkkVKAYGKEGVKM 348
Cdd:cd02660   65 SPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGD------------------------KNEANDESHCN 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 349 NFIDRIFIGELTSTVMCEECANISTMKDPFIDISLPIieernqlshdrkhlrkwpseeektvvthpkndnleasppastl 428
Cdd:cd02660  121 CIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDI------------------------------------------- 157
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 429 steaslnesltdgserdaslessvdadseasepeiaskqpvllrsrgdscghaeqhphlplaselpQAKETHGGEEEMAE 508
Cdd:cd02660  158 ------------------------------------------------------------------PNKSTPSWALGESG 171
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 509 AIAELHLSGtvtgnrdfhrekqplnvpnnlcfsegkhtrlhsaqnafqtlsqsyvttskecsvqsCLYQFTSMELLmGNN 588
Cdd:cd02660  172 VSGTPTLSD--------------------------------------------------------CLDRFTRPEKL-GDF 194
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 589 KLLCEDCtekrrkchketssaekkagGVYTNARKQLLISAVPAILILHLKRF-HQAGLSLRKVNRHVDFPLTLDLAPFCA 667
Cdd:cd02660  195 AYKCSGC-------------------GSTQEATKQLSIKKLPPVLCFQLKRFeHSLNKTSRKIDTYVQFPLELNMTPYTS 255
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 668 ATCKNISVGE----KVLYGLYGIVEHSGSMRGGHYTAYVKVRvpsrklsecitgrktaaglkepdgelGGHWVHVSDTYV 743
Cdd:cd02660  256 SSIGDTQDSNsldpDYTYDLFAVVVHKGTLDTGHYTAYCRQG--------------------------DGQWFKFDDAMI 309
                        570
                 ....*....|....*...
gi 594150411 744 QVVPESRALSAQAYLLFY 761
Cdd:cd02660  310 TRVSEEEVLKSQAYLLFY 327
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
570-764 2.32e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 98.87  E-value: 2.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 570 SVQSCLYQFTSMELLMGNNKLLCEDCTEKRRkchketssaekkaggvytnARKQLLISAVPAILILHLKRFHQAGLSLR- 648
Cdd:cd02659  152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVD-------------------AEKGVCFKKLPPVLTLQLKRFEFDFETMMr 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 649 -KVNRHVDFPLTLDLAPFCAATCKNISVGEKV------LYGLYGIVEHSGSMRGGHYTAYVKVRVPSR--KLSECITGRK 719
Cdd:cd02659  213 iKINDRFEFPLELDMEPYTEKGLAKKEGDSEKkdsesyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKwyKFNDDVVTPF 292
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 594150411 720 TAAGLKEPDGelGGHwvhVSDTYVQVVPESRALSAQAYLLFYERI 764
Cdd:cd02659  293 DPNDAEEECF--GGE---ETQKTYDSGPRAFKRTTNAYMLFYERK 332
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
549-762 5.88e-20

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: 89.73  E-value: 5.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 549 HSAQNAFQ----TLSQSY-----VTTSKECSVQSC------LYQFTSMELLMGNNKLLCEDCTEKRrkCHKETSSAEKKA 613
Cdd:cd02662   35 QDAHELFQvlleTLEQLLkfpfdGLLASRIVCLQCgesskvRYESFTMLSLPVPNQSSGSGTTLEH--CLDDFLSTEIID 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 614 GgvYTNARKQLLISAVPAILILHLKR--FHQAGLSLRKvNRHVDFPLTLDlapfcaatcknisvgeKVLYGLYGIVEHSG 691
Cdd:cd02662  113 D--YKCDRCQTVIVRLPQILCIHLSRsvFDGRGTSTKN-SCKVSFPERLP----------------KVLYRLRAVVVHYG 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 594150411 692 SMRGGHYTAYVKVRVPSRKLSECITGRktaagLKEPDGELGGHWVHVSDTYVQVVPESRAL-SAQAYLLFYE 762
Cdd:cd02662  174 SHSSGHYVCYRRKPLFSKDKEPGSFVR-----MREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
567-762 2.75e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 77.35  E-value: 2.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 567 KECSVQSCLYQFTSMELLMGNNKLLCEDCtekrrKCHKEtssaekkaggvytnARKQLLISAVPAILILHLKRFHQAGls 646
Cdd:cd02663  145 QNTSITSCLRQFSATETLCGRNKFYCDEC-----CSLQE--------------AEKRMKIKKLPKILALHLKRFKYDE-- 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 647 lrKVNRH------VDFPLTLDLapfcaatCKNISVGEKV--LYGLYGIVEHSGS--MRGgHYTAYVKVrvpsrklsecit 716
Cdd:cd02663  204 --QLNRYiklfyrVVFPLELRL-------FNTTDDAENPdrLYELVAVVVHIGGgpNHG-HYVSIVKS------------ 261
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 594150411 717 grktaaglkepdgelGGHWVHVSDTYVQVVPES--------RALSAQAYLLFYE 762
Cdd:cd02663  262 ---------------HGGWLLFDDETVEKIDENaveeffgdSPNQATAYVLFYQ 300
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
62-132 5.57e-15

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 69.98  E-value: 5.57e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594150411   62 CSECLKERRfcdgqpvlpadVWLCLKCGLQGCGKNSESqHSLRHFKSSGtesHCVVISLSTWVIWCYECNE 132
Cdd:pfam02148   1 CSLCGNTSN-----------LWLCLTCGHVGCGRYQNS-HALEHYEETG---HPLAVNLSTLTVYCYPCDD 56
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
626-764 1.30e-14

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 74.84  E-value: 1.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 626 ISAVPAILILHLKRFHQAGlSLRKVNRHVDFPLTLDLAPfcaatCKNISVGEKVLYGLYGIVEHSGSMRGGHYTAYVKVr 705
Cdd:COG5533  176 FVKLPKILTIQLKRFANLG-GNQKIDTEVDEKFELPVKH-----DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK- 248
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 594150411 706 vpsrklsecitgrktaaglkepdgelGGHWVHVSDTYVQVVPESRAL---SAQAYLLFYERI 764
Cdd:COG5533  249 --------------------------GGKWEKANDSDVTPVSEEEAInekAKNAYLYFYERI 284
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
188-703 1.35e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 72.62  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 188 PSVKGITNLGNTCFFNAVIQNLaqtyilfELMNEIKEdGTKFKISL-SSAPQLEplvvelsspgpltsALFLFLHSMKEA 266
Cdd:cd02671   22 LPFVGLNNLGNTCYLNSVLQVL-------YFCPGFKH-GLKHLVSLiSSVEQLQ--------------SSFLLNPEKYND 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 267 EKGPLSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRteetkriqasilkafnnpttktaddetrkkvkaygkegv 346
Cdd:cd02671   80 ELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQ--------------------------------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 347 kmNFIDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEERNQLSHDRKHLRKWPSEEEKTVVTHPKndnleasppas 426
Cdd:cd02671  121 --ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESSEISPDPKTEMKTLKWAIS----------- 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 427 tlsteaslnesltdgserdaslessvdadseasepeiaskqpvllrsrgdscghaeqhphlplaselpqakethggeeem 506
Cdd:cd02671      --------------------------------------------------------------------------------
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 507 aeaiaelhlsgtvtgnrdfhrekqplnvpnnlcfsegkhtrlhsaqnafqtlsqsyvttskecsvqsclyQFTSMELLMG 586
Cdd:cd02671  188 ----------------------------------------------------------------------QFASVERIVG 197
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 587 NNKLLCEDCTEkrrkchketssaekkaggvYTNARKQLLISAVPAILILHLKRFHQAGLS------LRKVNRHVDFPLTL 660
Cdd:cd02671  198 EDKYFCENCHH-------------------YTEAERSLLFDKLPEVITIHLKCFAANGSEfdcyggLSKVNTPLLTPLKL 258
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 594150411 661 dlapfcaaTCKNISVGEKV-LYGLYGIVEHSG-SMRGGHYTAYVK 703
Cdd:cd02671  259 --------SLEEWSTKPKNdVYRLFAVVMHSGaTISSGHYTAYVR 295
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
569-762 4.34e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 70.98  E-value: 4.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 569 CSVQSCLYQFTSMELLMGNNKLLCEDCtekRRKChketssaekkaggvytNARKQLLISAVPAILILHLKRFH--QAGLS 646
Cdd:cd02664  134 PSVQDLLNYFLSPEKLTGDNQYYCEKC---ASLQ----------------DAEKEMKVTGAPEYLILTLLRFSydQKTHV 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 647 LRKVNRHVDFPLTLDLaPFCAATCKNISVGEK---------------VLYGLYGIVEHSG-SMRGGHYTAYvkvrvpsrk 710
Cdd:cd02664  195 REKIMDNVSINEVLSL-PVRVESKSSESPLEKkeeesgddgelvtrqVHYRLYAVVVHSGySSESGHYFTY--------- 264
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 594150411 711 LSECITGRKTAAGLKEP----DGELGGHWVHVSDTYV-QVVPE------SRALSAQAYLLFYE 762
Cdd:cd02664  265 ARDQTDADSTGQECPEPkdaeENDESKNWYLFNDSRVtFSSFEsvqnvtSRFPKDTPYILFYE 327
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
570-703 5.93e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 70.53  E-value: 5.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 570 SVQSCLYQFTSMELLMGNNKLLCEDCTEKRrkchketssaekkaggvytNARKQLLISAVPAILILHLKR--FHQAGLSL 647
Cdd:cd02668  157 TLEECIDEFLKEEQLTGDNQYFCESCNSKT-------------------DATRRIRLTTLPPTLNFQLLRfvFDRKTGAK 217
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 594150411 648 RKVNRHVDFPLTLDLAPFCAATCKNISVgekvlYGLYGIVEHSG-SMRGGHYTAYVK 703
Cdd:cd02668  218 KKLNASISFPEILDMGEYLAESDEGSYV-----YELSGVLIHQGvSAYSGHYIAHIK 269
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
570-726 3.72e-12

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 70.28  E-value: 3.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411  570 SVQSCLYQFTSMELLMGNNKLLCEDctekrrkcHKetssaekkaggvYTNARKQLLISAVPAILILHLKRFHQAGLS--L 647
Cdd:COG5077   339 NLQESFRRYIQVETLDGDNRYNAEK--------HG------------LQDAKKGVIFESLPPVLHLQLKRFEYDFERdmM 398
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594150411  648 RKVNRHVDFPLTLDLAPFCAATCKNiSVGEKVLYGLYGIVEHSGSMRGGHYTAYVKVRVPSRKLSECITgRKTAAGLKE 726
Cdd:COG5077   399 VKINDRYEFPLEIDLLPFLDRDADK-SENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDT-RVTRATEKE 475
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
605-762 9.08e-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 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: 63.89  E-value: 9.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 605 ETSSAEKKAGGVYTnarKQLLISAVPAILILHLKRFHQAGLSLR--KVNRHVDFPLTLDLAPFCAATCknisvgekvLYG 682
Cdd:cd02657  175 EKHSPTLGRDAIYT---KTSRISRLPKYLTVQFVRFFWKRDIQKkaKILRKVKFPFELDLYELCTPSG---------YYE 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 683 LYGIVEHSG-SMRGGHYTAYVKVrvpsrklsecitgrktaaglkepdgELGGHWVHVSDTYVQVVPESRALSAQ------ 755
Cdd:cd02657  243 LVAVITHQGrSADSGHYVAWVRR-------------------------KNDGKWIKFDDDKVSEVTEEDILKLSgggdwh 297

                 ....*...
gi 594150411 756 -AYLLFYE 762
Cdd:cd02657  298 iAYILLYK 305
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-376 9.81e-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: 60.42  E-value: 9.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 192 GITNLGNTCFFNAVIQNLaqtyilfELMNEIKEDGTKFKISLSSAPQleplvvelsSPGPLTSALFLFLHSMKEAEKgPL 271
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCL-------RSVPELRDALKNYNPARRGANQ---------SSDNLTNALRDLFDTMDKKQE-PV 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 272 SPKVLFNQLCQKAPRFK------GFQQQDSQELLhhlldavrteetkriqASILKAFNNpttktaddetrkkvkAYGKEG 345
Cdd:cd02657   64 PPIEFLQLLRMAFPQFAekqnqgGYAQQDAEECW----------------SQLLSVLSQ---------------KLPGAG 112
                        170       180       190
                 ....*....|....*....|....*....|.
gi 594150411 346 VKMNFIDRIFIGELTSTVMCEECANISTMKD 376
Cdd:cd02657  113 SKGSFIDQLFGIELETKMKCTESPDEEEVST 143
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-387 1.76e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 56.73  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 192 GITNLGNTCFFNAVIQNLAQT-YILFELMNEIKEDGtkfkislssAPQLEPLVVELSspgpltsaLFLFLHSMKEAEKGP 270
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAkDFRRQVLSLNLPRL---------GDSQSVMKKLQL--------LQAHLMHTQRRAEAP 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 271 lsPKVLFNQlcQKAPRFKGFQQQDSQELLHHLLDAVRTeetkriqasilkafnnpttktaddetrkkvkaygkegvkmnF 350
Cdd:cd02664   64 --PDYFLEA--SRPPWFTPGSQQDCSEYLRYLLDRLHT-----------------------------------------L 98
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 594150411 351 IDRIFIGELTSTVMCEECANISTMKD--PFIDISLPIIE 387
Cdd:cd02664   99 IEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSFPSVQ 137
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
62-122 1.93e-06

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 45.43  E-value: 1.93e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594150411    62 CSECLkerrfcdgqpvLPADVWLCLKCGLQGCGkNSESQHSLRHFKSSGtesHCVVISLST 122
Cdd:smart00290   2 CSVCG-----------TIENLWLCLTCGQVGCG-RYQNGHALEHFEETG---HPLVVKLGT 47
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
626-762 2.90e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 46.37  E-value: 2.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 626 ISAVPAILILHLKRFHQAGLSLRKVNRHVDFPLTLDLAPFCAAT---CKNISVGEKVLYG--------------LYGIVE 688
Cdd:cd02670   95 FAKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVADDpraCSKCQLECRVCYDdkdfsptcgkfklsLCSAVC 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 689 HSG-SMRGGHYTAYVkvrvpsrklsecitgRKTAAGLKEPDGELG-GHWVHVSD-------TYVQVVPESRALSaQAYLL 759
Cdd:cd02670  175 HRGtSLETGHYVAFV---------------RYGSYSLTETDNEAYnAQWVFFDDmadrdgvSNGFNIPAARLLE-DPYML 238

                 ...
gi 594150411 760 FYE 762
Cdd:cd02670  239 FYQ 241
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
611-762 3.28e-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: 46.55  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 611 KKAGGVYTNARKQLLISAVPAILILHLKRFH-QAGLSLRKVNRHVDFPLTLDLAPfcaatcknisvgekvlYGLYGIVEH 689
Cdd:cd02658  197 CSTCKEKTTATKTTGFKTFPDYLVINMKRFQlLENWVPKKLDVPIDVPEELGPGK----------------YELIAFISH 260
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594150411 690 SG-SMRGGHYTAYVKvrvpsrklsecitgrktaaglKEPDGElgGHWVHVSDTYVQVVPESRALSAQAYLLFYE 762
Cdd:cd02658  261 KGtSVHSGHYVAHIK---------------------KEIDGE--GKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-385 1.25e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 44.72  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 192 GITNLGNTCFFNAVIQnlaqtyILFelMN-EIKEDGTKFKISLSSAPQLEPLVVELSSPGPLTSALFLFLHsMKEAEKGP 270
Cdd:cd02668    1 GLKNLGATCYVNSFLQ------LWF--MNlEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQ-LQFGNRSV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 271 LSPKVLFNQLcqkapRFKGFQQQDSQELLHHLLDAvrteetkrIQASILKAFNNpttktaddetrkKVKaygkegvkmNF 350
Cdd:cd02668   72 VDPSGFVKAL-----GLDTGQQQDAQEFSKLFLSL--------LEAKLSKSKNP------------DLK---------NI 117
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 594150411 351 IDRIFIGELTSTVMCEECANISTMKDPFIDISLPI 385
Cdd:cd02668  118 VQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL 152
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-309 2.84e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 39.85  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150411 192 GITNLGNTCFFNAVIQnlaqtyILFELMNEIKEDGTKFKISLSSAPQLEplvVELSSPGPLTsalflfLHSMKEAEKGP- 270
Cdd:cd02665    1 GLKNVGNTCWFSAVIQ------SLFSQQQDVSEFTHLLLDWLEDAFQAA---AEAISPGEKS------KNPMVQLFYGTf 65
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 594150411 271 LSPKVLFNQLCQKAPRFKGFQ-QQDSQELLHHLLDAVRTE 309
Cdd:cd02665   66 LTEGVLEGKPFCNCETFGQYPlQVNGYGNLHECLEAAMFE 105
 
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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