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Conserved domains on  [gi|564350490|ref|XP_006238003|]
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ubiquitin carboxyl-terminal hydrolase 45 isoform X3 [Rattus norvegicus]

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 3.90e-90

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: 284.28  E-value: 3.90e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 192 GITNLGNTCFFNAVIQNLAQTYILFELMNEikedgtkfkislssapqleplvvelsspgpltsalflflhsmkeaekgpl 271
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTeetkriqasilkafnnpttktadeetrkkvkaygkegvkmnFI 351
Cdd:cd02667   31 TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLRT-----------------------------------------FI 69
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 352 DRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEErtllshdrkhlrkwpseeertvgthpnsenseasplagilsne 431
Cdd:cd02667   70 DSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDE------------------------------------------- 106
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 432 aslnesptegserdtslessvdadseasepevaykpsvllrssgdpgahgeqhphlplaselphtkethdcdeemaeama 511
Cdd:cd02667      --------------------------------------------------------------------------------
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 512 elhlsgtvtgnrdfhrekqplnvpnnvcfsegkhtklhsaqnafqtlsqsyvtTSKECSVQSCLYQFTSMELLMGNNKLL 591
Cdd:cd02667  107 -----------------------------------------------------IKSECSIESCLKQFTEVEILEGNNKFA 133
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 592 CEDCTEkkrkcqketssaerkaggvytnARKQLLISAVPAILILHLKRFHQAGL-SLRKVNRHVDFPLTLDLAPFCAATC 670
Cdd:cd02667  134 CENCTK----------------------AKKQYLISKLPPVLVIHLKRFQQPRSaNLRKVSRHVSFPEILDLAPFCDPKC 191
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 671 KNISVGEKVLYGLYGIVEHSGSMRGGHYTAYVKVRVPSRKLSECITGRKTAPGlKEADSelgGHWVHVSDTYVQVVPESR 750
Cdd:cd02667  192 NSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQRLSDLTKSKPAADE-AGPGS---GQWYYISDSDVREVSLEE 267
                        570
                 ....*....|..
gi 564350490 751 ALSAQAYLLFYE 762
Cdd:cd02667  268 VLKSEAYLLFYE 279
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
62-132 1.57e-16

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 74.22  E-value: 1.57e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564350490   62 CSECLKErrlcdgqpvlpSDVWLCLKCGFQGCGKNSESqHSLRHFKSSGaesHCVVISLSTWVIWCYECNE 132
Cdd:pfam02148   1 CSLCGNT-----------SNLWLCLTCGHVGCGRYQNS-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 3.90e-90

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: 284.28  E-value: 3.90e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 192 GITNLGNTCFFNAVIQNLAQTYILFELMNEikedgtkfkislssapqleplvvelsspgpltsalflflhsmkeaekgpl 271
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTeetkriqasilkafnnpttktadeetrkkvkaygkegvkmnFI 351
Cdd:cd02667   31 TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLRT-----------------------------------------FI 69
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 352 DRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEErtllshdrkhlrkwpseeertvgthpnsenseasplagilsne 431
Cdd:cd02667   70 DSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDE------------------------------------------- 106
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 432 aslnesptegserdtslessvdadseasepevaykpsvllrssgdpgahgeqhphlplaselphtkethdcdeemaeama 511
Cdd:cd02667      --------------------------------------------------------------------------------
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 512 elhlsgtvtgnrdfhrekqplnvpnnvcfsegkhtklhsaqnafqtlsqsyvtTSKECSVQSCLYQFTSMELLMGNNKLL 591
Cdd:cd02667  107 -----------------------------------------------------IKSECSIESCLKQFTEVEILEGNNKFA 133
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 592 CEDCTEkkrkcqketssaerkaggvytnARKQLLISAVPAILILHLKRFHQAGL-SLRKVNRHVDFPLTLDLAPFCAATC 670
Cdd:cd02667  134 CENCTK----------------------AKKQYLISKLPPVLVIHLKRFQQPRSaNLRKVSRHVSFPEILDLAPFCDPKC 191
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 671 KNISVGEKVLYGLYGIVEHSGSMRGGHYTAYVKVRVPSRKLSECITGRKTAPGlKEADSelgGHWVHVSDTYVQVVPESR 750
Cdd:cd02667  192 NSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQRLSDLTKSKPAADE-AGPGS---GQWYYISDSDVREVSLEE 267
                        570
                 ....*....|..
gi 564350490 751 ALSAQAYLLFYE 762
Cdd:cd02667  268 VLKSEAYLLFYE 279
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
192-761 3.44e-34

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 132.95  E-value: 3.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  192 GITNLGNTCFFNAVIQNLAQTYILFELMNEIKEDGTKFKISLSSApqleplvvelsspgpLTSALFLFLHSMKEAEKG-P 270
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------------LLCALRDLFKALQKNSKSsS 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  271 LSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTEEtkriqasilkafnNPTTKTADEetrkkvkaygkegvkmNF 350
Cdd:pfam00443  67 VSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDL-------------NGNHSTENE----------------SL 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  351 IDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEertllshdrkhlrkwpseeertvgthpnsenseasplagilsn 430
Cdd:pfam00443 118 ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG------------------------------------------- 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  431 easlnesptegserdtslessvdadseasepevaykpsvllrssgdpgahgeqhphlplaselphtkethdcdeemaeam 510
Cdd:pfam00443     --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  511 aelhlsgtvtgnrdfhrekqplnvpnnvcfsegkhtklhsaqnafqtlsqsYVTTSKECSVQSCLYQFTSMELLMGNNKL 590
Cdd:pfam00443 155 ---------------------------------------------------DSAELKTASLQICFLQFSKLEELDDEEKY 183
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  591 LCEDCTEKKrkcqketssaerkaggvytNARKQLLISAVPAILILHLKRFHQAGLSLRKVNRHVDFPLTLDLAPFCAATc 670
Cdd:pfam00443 184 YCDKCGCKQ-------------------DAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRYLAEE- 243
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  671 KNISVGEKVLYGLYGIVEHSGSMRGGHYTAYVKvrvpsrklsecitgrktapglkeadSELGGHWVHVSDTYVQVVPESR 750
Cdd:pfam00443 244 LKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIK-------------------------AYENNRWYKFDDEKVTEVDEET 298
                         570
                  ....*....|..
gi 564350490  751 A-LSAQAYLLFY 761
Cdd:pfam00443 299 AvLSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
192-763 1.98e-27

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 118.83  E-value: 1.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 192 GITNLGNTCFFNAVIQNLAQTYilfELMNEIKEDGTKFKISLSSapqlePLVVElsspGPLTSALFLFLHSMKEAEKGPL 271
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTW---ELRDYFLSDEYEESINEEN-----PLGMH----GSVASAYADLIKQLYDGNLHAF 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRtEETKRIQasILKAFNNPTTKTADEETRKKV-KAYGKEGVKMN- 349
Cdd:COG5560  335 TPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLH-EDLNRII--KKPYTSKPDLSPGDDVVVKKKaKECWWEHLKRNd 411
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 350 -FIDRIFIGELTSTVMCEECANISTMKDPFIDISLPiIEERTLLSHD--------RKHLRKWPSEEERTVGTHPN--SEN 418
Cdd:COG5560  412 sIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLP-LPVSMVWKHTivvfpesgRRQPLKIELDASSTIRGLKKlvDAE 490
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 419 SEASPLAGILSNEASLNESPTEGSERDTSLESSV-DADS----EASEPEVAYkPSVLLRS-SGDPGAHGEQHPHLPLASE 492
Cdd:COG5560  491 YGKLGCFEIKVMCIYYGGNYNMLEPADKVLLQDIpQTDFvylyETNDNGIEV-PVVHLRIeKGYKSKRLFGDPFLQLNVL 569
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 493 LPHT------KETHDCDEEMAEAMAELHLSGTVTG----------------NRDFHREKQP-----LNVPNNV---CFSE 542
Cdd:COG5560  570 IKASiydklvKEFEELLVLVEMKKTDVDLVSEQVRllreesspsswlkletEIDTKREEQVeeegqMNFNDAVvisCEWE 649
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 543 GKHTKLHSAQNAFQTLSQSyVTTSKECSVQSCLYQFTSMELLMGNNKLLCEDCTEKKRkcqketssaerkaggvytnARK 622
Cdd:COG5560  650 EKRYLSLFSYDPLWTIREI-GAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQ-------------------ASK 709
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 623 QLLISAVPAILILHLKRFHQAGLSLRKVNRHVDFPLT-LDLAPFCAATcknisVGEKVLYGLYGIVEHSGSMRGGHYTAY 701
Cdd:COG5560  710 QMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDdLDLSGVEYMV-----DDPRLIYDLYAVDNHYGGLSGGHYTAY 784
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564350490 702 VKvrvpsrklsecitgrktapglKEADselgGHWVHVSDTYVQVVPESRALSAQAYLLFYER 763
Cdd:COG5560  785 AR---------------------NFAN----NGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
62-132 1.57e-16

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 74.22  E-value: 1.57e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564350490   62 CSECLKErrlcdgqpvlpSDVWLCLKCGFQGCGKNSESqHSLRHFKSSGaesHCVVISLSTWVIWCYECNE 132
Cdd:pfam02148   1 CSLCGNT-----------SNLWLCLTCGHVGCGRYQNS-HALEHYEETG---HPLAVNLSTLTVYCYPCDD 56
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
62-122 3.57e-07

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 47.36  E-value: 3.57e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564350490    62 CSECLkerrlcdgqpvLPSDVWLCLKCGFQGCGkNSESQHSLRHFKSSGaesHCVVISLST 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 3.90e-90

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: 284.28  E-value: 3.90e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 192 GITNLGNTCFFNAVIQNLAQTYILFELMNEikedgtkfkislssapqleplvvelsspgpltsalflflhsmkeaekgpl 271
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTeetkriqasilkafnnpttktadeetrkkvkaygkegvkmnFI 351
Cdd:cd02667   31 TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLRT-----------------------------------------FI 69
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 352 DRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEErtllshdrkhlrkwpseeertvgthpnsenseasplagilsne 431
Cdd:cd02667   70 DSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDE------------------------------------------- 106
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 432 aslnesptegserdtslessvdadseasepevaykpsvllrssgdpgahgeqhphlplaselphtkethdcdeemaeama 511
Cdd:cd02667      --------------------------------------------------------------------------------
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 512 elhlsgtvtgnrdfhrekqplnvpnnvcfsegkhtklhsaqnafqtlsqsyvtTSKECSVQSCLYQFTSMELLMGNNKLL 591
Cdd:cd02667  107 -----------------------------------------------------IKSECSIESCLKQFTEVEILEGNNKFA 133
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 592 CEDCTEkkrkcqketssaerkaggvytnARKQLLISAVPAILILHLKRFHQAGL-SLRKVNRHVDFPLTLDLAPFCAATC 670
Cdd:cd02667  134 CENCTK----------------------AKKQYLISKLPPVLVIHLKRFQQPRSaNLRKVSRHVSFPEILDLAPFCDPKC 191
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 671 KNISVGEKVLYGLYGIVEHSGSMRGGHYTAYVKVRVPSRKLSECITGRKTAPGlKEADSelgGHWVHVSDTYVQVVPESR 750
Cdd:cd02667  192 NSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQRLSDLTKSKPAADE-AGPGS---GQWYYISDSDVREVSLEE 267
                        570
                 ....*....|..
gi 564350490 751 ALSAQAYLLFYE 762
Cdd:cd02667  268 VLKSEAYLLFYE 279
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
192-761 3.44e-34

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 132.95  E-value: 3.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  192 GITNLGNTCFFNAVIQNLAQTYILFELMNEIKEDGTKFKISLSSApqleplvvelsspgpLTSALFLFLHSMKEAEKG-P 270
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------------LLCALRDLFKALQKNSKSsS 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  271 LSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTEEtkriqasilkafnNPTTKTADEetrkkvkaygkegvkmNF 350
Cdd:pfam00443  67 VSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDL-------------NGNHSTENE----------------SL 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  351 IDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEertllshdrkhlrkwpseeertvgthpnsenseasplagilsn 430
Cdd:pfam00443 118 ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG------------------------------------------- 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  431 easlnesptegserdtslessvdadseasepevaykpsvllrssgdpgahgeqhphlplaselphtkethdcdeemaeam 510
Cdd:pfam00443     --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  511 aelhlsgtvtgnrdfhrekqplnvpnnvcfsegkhtklhsaqnafqtlsqsYVTTSKECSVQSCLYQFTSMELLMGNNKL 590
Cdd:pfam00443 155 ---------------------------------------------------DSAELKTASLQICFLQFSKLEELDDEEKY 183
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  591 LCEDCTEKKrkcqketssaerkaggvytNARKQLLISAVPAILILHLKRFHQAGLSLRKVNRHVDFPLTLDLAPFCAATc 670
Cdd:pfam00443 184 YCDKCGCKQ-------------------DAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRYLAEE- 243
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  671 KNISVGEKVLYGLYGIVEHSGSMRGGHYTAYVKvrvpsrklsecitgrktapglkeadSELGGHWVHVSDTYVQVVPESR 750
Cdd:pfam00443 244 LKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIK-------------------------AYENNRWYKFDDEKVTEVDEET 298
                         570
                  ....*....|..
gi 564350490  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 7.47e-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: 7.47e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 563 VTTSKECSVQSCLYQFTSMELLMGNNKLLCEdctekkrkcqketssaerkaGGVYTNARKQLLISAVPAILILHLKRFHQ 642
Cdd:cd02257   93 VKGLPQVSLEDCLEKFFKEEILEGDNCYKCE--------------------KKKKQEATKRLKIKKLPPVLIIHLKRFSF 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 643 AG-LSLRKVNRHVDFPLTLDLAPFCAATCKNISVGEK-VLYGLYGIVEHSG-SMRGGHYTAYVKVRVPsrklsecitgrk 719
Cdd:cd02257  153 NEdGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNGsYKYELVAVVVHSGtSADSGHYVAYVKDPSD------------ 220
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564350490 720 tapglkeadselgGHWVHVSDTYVQVVPESRAL-----SAQAYLLFYE 762
Cdd:cd02257  221 -------------GKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
570-761 1.98e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 122.00  E-value: 1.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 570 SVQSCLYQFTSMELLMGNNKLLCEDCTEKkrkcqketssaerkaggvyTNARKQLLISAVPAILILHLKRFhqAGLSLRK 649
Cdd:cd02661  163 SLEDALEQFTKPEQLDGENKYKCERCKKK-------------------VKASKQLTIHRAPNVLTIHLKRF--SNFRGGK 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 650 VNRHVDFPLTLDLAPFCAAtckniSVGEKVLYGLYGIVEHSG-SMRGGHYTAYVkvrvpsrklsecitgrKTAPGLkead 728
Cdd:cd02661  222 INKQISFPETLDLSPYMSQ-----PNDGPLKYKLYAVLVHSGfSPHSGHYYCYV----------------KSSNGK---- 276
                        170       180       190
                 ....*....|....*....|....*....|...
gi 564350490 729 selgghWVHVSDTYVQVVPESRALSAQAYLLFY 761
Cdd:cd02661  277 ------WYNMDDSKVSPVSIETVLSQKAYILFY 303
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
567-762 5.62e-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: 118.54  E-value: 5.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 567 KECSVQSCLYQFTSMELLMGNNKLLCEDCtEKKRKcqketssaerkaggvytnARKQLLISAVPAILILHLKRFHQAGLS 646
Cdd:cd02674   82 PKVTLEDCLRLFTKEETLDGDNAWKCPKC-KKKRK------------------ATKKLTISRLPKVLIIHLKRFSFSRGS 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 647 LRKVNRHVDFPLT-LDLAPFCAATCKNISvgekVLYGLYGIVEHSGSMRGGHYTAYVKVRVPSRklsecitgrktapglk 725
Cdd:cd02674  143 TRKLTTPVTFPLNdLDLTPYVDTRSFTGP----FKYDLYAVVNHYGSLNGGHYTAYCKNNETND---------------- 202
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 564350490 726 eadselgghWVHVSDTYVQVVPESRALSAQAYLLFYE 762
Cdd:cd02674  203 ---------WYKFDDSRVTKVSESSVVSSSAYILFYE 230
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
192-763 1.98e-27

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 118.83  E-value: 1.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 192 GITNLGNTCFFNAVIQNLAQTYilfELMNEIKEDGTKFKISLSSapqlePLVVElsspGPLTSALFLFLHSMKEAEKGPL 271
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTW---ELRDYFLSDEYEESINEEN-----PLGMH----GSVASAYADLIKQLYDGNLHAF 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRtEETKRIQasILKAFNNPTTKTADEETRKKV-KAYGKEGVKMN- 349
Cdd:COG5560  335 TPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLH-EDLNRII--KKPYTSKPDLSPGDDVVVKKKaKECWWEHLKRNd 411
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 350 -FIDRIFIGELTSTVMCEECANISTMKDPFIDISLPiIEERTLLSHD--------RKHLRKWPSEEERTVGTHPN--SEN 418
Cdd:COG5560  412 sIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLP-LPVSMVWKHTivvfpesgRRQPLKIELDASSTIRGLKKlvDAE 490
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 419 SEASPLAGILSNEASLNESPTEGSERDTSLESSV-DADS----EASEPEVAYkPSVLLRS-SGDPGAHGEQHPHLPLASE 492
Cdd:COG5560  491 YGKLGCFEIKVMCIYYGGNYNMLEPADKVLLQDIpQTDFvylyETNDNGIEV-PVVHLRIeKGYKSKRLFGDPFLQLNVL 569
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 493 LPHT------KETHDCDEEMAEAMAELHLSGTVTG----------------NRDFHREKQP-----LNVPNNV---CFSE 542
Cdd:COG5560  570 IKASiydklvKEFEELLVLVEMKKTDVDLVSEQVRllreesspsswlkletEIDTKREEQVeeegqMNFNDAVvisCEWE 649
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 543 GKHTKLHSAQNAFQTLSQSyVTTSKECSVQSCLYQFTSMELLMGNNKLLCEDCTEKKRkcqketssaerkaggvytnARK 622
Cdd:COG5560  650 EKRYLSLFSYDPLWTIREI-GAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQ-------------------ASK 709
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 623 QLLISAVPAILILHLKRFHQAGLSLRKVNRHVDFPLT-LDLAPFCAATcknisVGEKVLYGLYGIVEHSGSMRGGHYTAY 701
Cdd:COG5560  710 QMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDdLDLSGVEYMV-----DDPRLIYDLYAVDNHYGGLSGGHYTAY 784
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564350490 702 VKvrvpsrklsecitgrktapglKEADselgGHWVHVSDTYVQVVPESRALSAQAYLLFYER 763
Cdd:COG5560  785 AR---------------------NFAN----NGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
191-761 2.54e-27

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: 113.62  E-value: 2.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 191 KGITNLGNTCFFNAVIQNLAQTYILFE-LMNEIKEDGTKFKISLSSAP-QLEPLVVELSSPGpltsalflflhsmkeaEK 268
Cdd:cd02660    1 RGLINLGATCFMNVILQALLHNPLLRNyFLSDRHSCTCLSCSPNSCLScAMDEIFQEFYYSG----------------DR 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 269 GPLSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTEETKRiqasilkafnnpttktadeetrkkVKAYGKEGVKM 348
Cdd:cd02660   65 SPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGD------------------------KNEANDESHCN 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 349 NFIDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEERTllshdrkhlrkwpseeertvgthpnsenseasplagil 428
Cdd:cd02660  121 CIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKST-------------------------------------- 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 429 sneaslnesptegserdtslessvdadseasepevaykpsvllRSSGDPGAHGEQHPHLplaselphtkethdcdeemae 508
Cdd:cd02660  163 -------------------------------------------PSWALGESGVSGTPTL--------------------- 178
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 509 amaelhlsgtvtgnrdfhrekqplnvpnnvcfsegkhtklhsaqnafqtlsqsyvttskecsvQSCLYQFTSMELLmGNN 588
Cdd:cd02660  179 ---------------------------------------------------------------SDCLDRFTRPEKL-GDF 194
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 589 KLLCEDCtekkrkcqketssaerkagGVYTNARKQLLISAVPAILILHLKRF-HQAGLSLRKVNRHVDFPLTLDLAPFCA 667
Cdd:cd02660  195 AYKCSGC-------------------GSTQEATKQLSIKKLPPVLCFQLKRFeHSLNKTSRKIDTYVQFPLELNMTPYTS 255
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 668 ATCKNISVGE----KVLYGLYGIVEHSGSMRGGHYTAYVKVRvpsrklsecitgrktapglkeadselGGHWVHVSDTYV 743
Cdd:cd02660  256 SSIGDTQDSNsldpDYTYDLFAVVVHKGTLDTGHYTAYCRQG--------------------------DGQWFKFDDAMI 309
                        570
                 ....*....|....*...
gi 564350490 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 5.65e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 100.79  E-value: 5.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 570 SVQSCLYQFTSMELLMGNNKLLCEDCTEKKRkcqketssaerkaggvytnARKQLLISAVPAILILHLKRFHQAGLSLR- 648
Cdd:cd02659  152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVD-------------------AEKGVCFKKLPPVLTLQLKRFEFDFETMMr 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 649 -KVNRHVDFPLTLDLAPFCAATCKNISVGEKV------LYGLYGIVEHSGSMRGGHYTAYVKVRVPSR-------KLSEC 714
Cdd:cd02659  213 iKINDRFEFPLELDMEPYTEKGLAKKEGDSEKkdsesyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKwykfnddVVTPF 292
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564350490 715 itgrktapGLKEADSE-LGGhwvHVSDTYVQVVPESRALSAQAYLLFYERI 764
Cdd:cd02659  293 --------DPNDAEEEcFGG---EETQKTYDSGPRAFKRTTNAYMLFYERK 332
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
549-762 1.46e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 88.58  E-value: 1.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 549 HSAQNAFQ----TLSQSY-----VTTSKECSVQSC------LYQFTSMELLMGNNKLLCEDCTEKKrkCQKETSSAERKA 613
Cdd:cd02662   35 QDAHELFQvlleTLEQLLkfpfdGLLASRIVCLQCgesskvRYESFTMLSLPVPNQSSGSGTTLEH--CLDDFLSTEIID 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 614 GgvYTNARKQLLISAVPAILILHLKR--FHQAGLSLRKvNRHVDFPLTLDlapfcaatcknisvgeKVLYGLYGIVEHSG 691
Cdd:cd02662  113 D--YKCDRCQTVIVRLPQILCIHLSRsvFDGRGTSTKN-SCKVSFPERLP----------------KVLYRLRAVVVHYG 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564350490 692 SMRGGHYTAYVKVRVPSRKLSECITGRktapgLKEADSELGGHWVHVSDTYVQVVPESRAL-SAQAYLLFYE 762
Cdd:cd02662  174 SHSSGHYVCYRRKPLFSKDKEPGSFVR-----MREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
62-132 1.57e-16

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 74.22  E-value: 1.57e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564350490   62 CSECLKErrlcdgqpvlpSDVWLCLKCGFQGCGKNSESqHSLRHFKSSGaesHCVVISLSTWVIWCYECNE 132
Cdd:pfam02148   1 CSLCGNT-----------SNLWLCLTCGHVGCGRYQNS-HALEHYEETG---HPLAVNLSTLTVYCYPCDD 56
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
567-762 9.41e-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: 75.81  E-value: 9.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 567 KECSVQSCLYQFTSMELLMGNNKLLCEDCTEKKrkcqketssaerkaggvytNARKQLLISAVPAILILHLKRFHQAGls 646
Cdd:cd02663  145 QNTSITSCLRQFSATETLCGRNKFYCDECCSLQ-------------------EAEKRMKIKKLPKILALHLKRFKYDE-- 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 647 lrKVNRH------VDFPLTLDLapfcaatCKNISVGEKV--LYGLYGIVEHSGS--MRGgHYTAYVKVrvpsrklsecit 716
Cdd:cd02663  204 --QLNRYiklfyrVVFPLELRL-------FNTTDDAENPdrLYELVAVVVHIGGgpNHG-HYVSIVKS------------ 261
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564350490 717 grktapglkeadselGGHWVHVSDTYVQVVPES--------RALSAQAYLLFYE 762
Cdd:cd02663  262 ---------------HGGWLLFDDETVEKIDENaveeffgdSPNQATAYVLFYQ 300
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 564350490 626 ISAVPAILILHLKRFHQAGlSLRKVNRHVDFPLTLDLAPfcaatCKNISVGEKVLYGLYGIVEHSGSMRGGHYTAYVKVr 705
Cdd:COG5533  176 FVKLPKILTIQLKRFANLG-GNQKIDTEVDEKFELPVKH-----DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK- 248
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564350490 706 vpsrklsecitgrktapglkeadselGGHWVHVSDTYVQVVPESRAL---SAQAYLLFYERI 764
Cdd:COG5533  249 --------------------------GGKWEKANDSDVTPVSEEEAInekAKNAYLYFYERI 284
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
188-703 5.05e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 74.16  E-value: 5.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 188 PSVKGITNLGNTCFFNAVIQNLaqtyilfELMNEIKEdGTKFKISL-SSAPQLEplvvelsspgpltsALFLFLHSMKEA 266
Cdd:cd02671   22 LPFVGLNNLGNTCYLNSVLQVL-------YFCPGFKH-GLKHLVSLiSSVEQLQ--------------SSFLLNPEKYND 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 267 EKGPLSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRteetkriqasilkafnnpttktadeetrkkvkaygkegv 346
Cdd:cd02671   80 ELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQ--------------------------------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 347 kmNFIDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEERTLlshdrkhlrkwPSEEERTVGTHPNSENSEASplag 426
Cdd:cd02671  121 --ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELS-----------KSEESSEISPDPKTEMKTLK---- 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 427 ilsneaslnesptegserdtslessvdadseasepevaYKPSvllrssgdpgahgeqhphlplaselphtkethdcdeem 506
Cdd:cd02671  184 --------------------------------------WAIS-------------------------------------- 187
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 507 aeamaelhlsgtvtgnrdfhrekqplnvpnnvcfsegkhtklhsaqnafqtlsqsyvttskecsvqsclyQFTSMELLMG 586
Cdd:cd02671  188 ----------------------------------------------------------------------QFASVERIVG 197
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 587 NNKLLCEDCTEkkrkcqketssaerkaggvYTNARKQLLISAVPAILILHLKRFHQAGLS------LRKVNRHVDFPLTL 660
Cdd:cd02671  198 EDKYFCENCHH-------------------YTEAERSLLFDKLPEVITIHLKCFAANGSEfdcyggLSKVNTPLLTPLKL 258
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 564350490 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 3.65e-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: 71.37  E-value: 3.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 569 CSVQSCLYQFTSMELLMGNNKLLCEDCtekKRKCQKETSSAerkaggvytnarkqllISAVPAILILHLKRFH--QAGLS 646
Cdd:cd02664  134 PSVQDLLNYFLSPEKLTGDNQYYCEKC---ASLQDAEKEMK----------------VTGAPEYLILTLLRFSydQKTHV 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 647 LRKVNRHVDFPLTLDLaPFCAATCKNISVGEK---------------VLYGLYGIVEHSG-SMRGGHYTAYVKVRVPSRK 710
Cdd:cd02664  195 REKIMDNVSINEVLSL-PVRVESKSSESPLEKkeeesgddgelvtrqVHYRLYAVVVHSGySSESGHYFTYARDQTDADS 273
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564350490 711 lseciTGRKTAPGLKEADSELGGHWVHVSDTYV-QVVPE------SRALSAQAYLLFYE 762
Cdd:cd02664  274 -----TGQECPEPKDAEENDESKNWYLFNDSRVtFSSFEsvqnvtSRFPKDTPYILFYE 327
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
570-703 6.32e-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: 6.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 570 SVQSCLYQFTSMELLMGNNKLLCEDCTEKkrkcqketssaerkaggvyTNARKQLLISAVPAILILHLKR--FHQAGLSL 647
Cdd:cd02668  157 TLEECIDEFLKEEQLTGDNQYFCESCNSK-------------------TDATRRIRLTTLPPTLNFQLLRfvFDRKTGAK 217
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564350490 648 RKVNRHVDFPLTLDLAPFCAATCKNISVgekvlYGLYGIVEHSG-SMRGGHYTAYVK 703
Cdd:cd02668  218 KKLNASISFPEILDMGEYLAESDEGSYV-----YELSGVLIHQGvSAYSGHYIAHIK 269
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
570-763 5.11e-12

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 69.51  E-value: 5.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  570 SVQSCLYQFTSMELLMGNNKLLCEDCTekkrkcqketssaerkaggvYTNARKQLLISAVPAILILHLKRFHQAGLS--L 647
Cdd:COG5077   339 NLQESFRRYIQVETLDGDNRYNAEKHG--------------------LQDAKKGVIFESLPPVLHLQLKRFEYDFERdmM 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490  648 RKVNRHVDFPLTLDLAPFCAATCKNiSVGEKVLYGLYGIVEHSGSMRGGHYTAYVKVRVPSRKLSECITgRKTAPGLKEA 727
Cdd:COG5077   399 VKINDRYEFPLEIDLLPFLDRDADK-SENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDT-RVTRATEKEV 476
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 564350490  728 DSE-LGGHWVHvSDTYVQVVPESRALSaqAYLLFYER 763
Cdd:COG5077   477 LEEnFGGDHPY-KDKIRDHSGIKRFMS--AYMLVYLR 510
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
597-762 3.24e-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 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: 65.04  E-value: 3.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 597 EKKRKCQKETSSAERKAGGVYTnarKQLLISAVPAILILHLKRFHQAGLSLR--KVNRHVDFPLTLDLAPFCAATCknis 674
Cdd:cd02657  167 KKGLEEEIEKHSPTLGRDAIYT---KTSRISRLPKYLTVQFVRFFWKRDIQKkaKILRKVKFPFELDLYELCTPSG---- 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 675 vgekvLYGLYGIVEHSG-SMRGGHYTAYVKvrvpsrklsecitgrktapglkeadSELGGHWVHVSDTYVQVVPESRALS 753
Cdd:cd02657  240 -----YYELVAVITHQGrSADSGHYVAWVR-------------------------RKNDGKWIKFDDDKVSEVTEEDILK 289
                        170
                 ....*....|....*.
gi 564350490 754 AQ-------AYLLFYE 762
Cdd:cd02657  290 LSgggdwhiAYILLYK 305
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-376 9.89e-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: 9.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 192 GITNLGNTCFFNAVIQNLaqtyilfELMNEIKEDGTKFKISLSSAPQleplvvelsSPGPLTSALFLFLHSMKEAEKgPL 271
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCL-------RSVPELRDALKNYNPARRGANQ---------SSDNLTNALRDLFDTMDKKQE-PV 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 272 SPKVLFNQLCQKAPRFK------GFQQQDSQELLhhlldavrteetkriqASILKAFNNpttktadeetrkkvkAYGKEG 345
Cdd:cd02657   64 PPIEFLQLLRMAFPQFAekqnqgGYAQQDAEECW----------------SQLLSVLSQ---------------KLPGAG 112
                        170       180       190
                 ....*....|....*....|....*....|.
gi 564350490 346 VKMNFIDRIFIGELTSTVMCEECANISTMKD 376
Cdd:cd02657  113 SKGSFIDQLFGIELETKMKCTESPDEEEVST 143
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-406 3.05e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 58.86  E-value: 3.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 192 GITNLGNTCFFNAVIQNLAQTYILfelmneikedgtkfkislssapqleplvvelsspgpltSALFLFLHSMKEAEK--G 269
Cdd:cd02663    1 GLENFGNTCYCNSVLQALYFENLL--------------------------------------TCLKDLFESISEQKKrtG 42
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 270 PLSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLdavrteetkriqasilkafnNPTTKTADEEtRKKVKAYGKEGVKM- 348
Cdd:cd02663   43 VISPKKFITRLKRENELFDNYMHQDAHEFLNFLL--------------------NEIAEILDAE-RKAEKANRKLNNNNn 101
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564350490 349 -----NFIDRIFIGELTSTVMCEECANISTMKDPFIDISLPiIEERTLLSHdrkHLRKWPSEE 406
Cdd:cd02663  102 aepqpTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSID-VEQNTSITS---CLRQFSATE 160
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-387 1.82e-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: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 192 GITNLGNTCFFNAVIQNLAQT-YILFELMNEIKEDGtkfkislssAPQLEPLVVELSspgpltsaLFLFLHSMKEAEKGP 270
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAkDFRRQVLSLNLPRL---------GDSQSVMKKLQL--------LQAHLMHTQRRAEAP 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 271 lsPKVLFNQlcQKAPRFKGFQQQDSQELLHHLLDAVRTeetkriqasilkafnnpttktadeetrkkvkaygkegvkmnF 350
Cdd:cd02664   64 --PDYFLEA--SRPPWFTPGSQQDCSEYLRYLLDRLHT-----------------------------------------L 98
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564350490 351 IDRIFIGELTSTVMCEECANISTMKD--PFIDISLPIIE 387
Cdd:cd02664   99 IEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSFPSVQ 137
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
62-122 3.57e-07

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 47.36  E-value: 3.57e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564350490    62 CSECLkerrlcdgqpvLPSDVWLCLKCGFQGCGkNSESQHSLRHFKSSGaesHCVVISLST 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 3.06e-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: 45.98  E-value: 3.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 626 ISAVPAILILHLKRFHQAGLSLRKVNRHVDFPLTLDLAPFCAAT---CKNISVGEKVLYG--------------LYGIVE 688
Cdd:cd02670   95 FAKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVADDpraCSKCQLECRVCYDdkdfsptcgkfklsLCSAVC 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 689 HSG-SMRGGHYTAYVKvrvpsrklseciTGRKTAPGLKEADSElgGHWVHVSD-------TYVQVVPESRALSaQAYLLF 760
Cdd:cd02670  175 HRGtSLETGHYVAFVR------------YGSYSLTETDNEAYN--AQWVFFDDmadrdgvSNGFNIPAARLLE-DPYMLF 239

                 ..
gi 564350490 761 YE 762
Cdd:cd02670  240 YQ 241
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-391 4.75e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 46.26  E-value: 4.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 192 GITNLGNTCFFNAVIQnlaqtyILFelMN-EIKEDGTKFKISLSSAPQLEPLVVELSSPGPLTSALFLFLHsMKEAEKGP 270
Cdd:cd02668    1 GLKNLGATCYVNSFLQ------LWF--MNlEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQ-LQFGNRSV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 271 LSPKVLFNQLcqkapRFKGFQQQDSQELLHHLLDAvrteetkrIQASILKAFNNpttktadeetrkKVKaygkegvkmNF 350
Cdd:cd02668   72 VDPSGFVKAL-----GLDTGQQQDAQEFSKLFLSL--------LEAKLSKSKNP------------DLK---------NI 117
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564350490 351 IDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEERTL 391
Cdd:cd02668  118 VQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
615-762 9.39e-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: 45.01  E-value: 9.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 615 GVYTNARKQLLISAVPAILILHLKRFH-QAGLSLRKVNRHVDFPLTLDLAPfcaatcknisvgekvlYGLYGIVEHSG-S 692
Cdd:cd02658  201 KEKTTATKTTGFKTFPDYLVINMKRFQlLENWVPKKLDVPIDVPEELGPGK----------------YELIAFISHKGtS 264
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 693 MRGGHYTAYVKvrvpsrklsecitgrktapglKEADSElgGHWVHVSDTYVQVVPESRALSAQAYLLFYE 762
Cdd:cd02658  265 VHSGHYVAHIK---------------------KEIDGE--GKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-309 3.31e-03

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 39.85  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350490 192 GITNLGNTCFFNAVIQnlaqtyILFELMNEIKEDGTKFKISLSSAPQLEplvVELSSPGPLTsalflfLHSMKEAEKGP- 270
Cdd:cd02665    1 GLKNVGNTCWFSAVIQ------SLFSQQQDVSEFTHLLLDWLEDAFQAA---AEAISPGEKS------KNPMVQLFYGTf 65
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 564350490 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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