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Conserved domains on  [gi|86563443|ref|NP_497422|]
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Ubiquitin carboxyl-terminal hydrolase [Caenorhabditis elegans]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 10119220)

ubiquitin carboxyl-terminal hydrolase family protein is a C19 family peptidase that may deubiquitinate polyubiquitinated target proteins

CATH:  3.90.70.10
EC:  3.4.19.12
Gene Ontology:  GO:0016579|GO:0004843
MEROPS:  C19
PubMed:  7845226|11517925
SCOP:  4003158

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
46-463 1.26e-62

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: 203.37  E-value: 1.26e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443  46 GLANQGNTCYMNALLQGLASCPSFVGWLKSLKPQdigiqggfvdhlsnllhllneptgstltaqsiveslkahgwsitvg 125
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 126 veHDLYELFNVFVTTWEDELKSSRRILMNQSIENCHSSSSEDdedvvvestslrgspsiirklmsfqrcasmaridaslr 205
Cdd:cd02662  35 --QDAHELFQVLLETLEQLLKFPFDGLLASRIVCLQCGESSK-------------------------------------- 74
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 206 spcvgltateyrccntncgyrtVKYESFTVLTLAIPNSQMGTSTNTESLLRRFFCSEIIRDAICDKCrasdrkqqgflkK 285
Cdd:cd02662  75 ----------------------VRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC------------Q 120
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 286 HGIVKLPQTLMIRIERVGMLPNG-SMKLSEHVHFGECLslqdvcfrknpkinqksyeesslhwqlpdgtsrvvggaeetr 364
Cdd:cd02662 121 TVIVRLPQILCIHLSRSVFDGRGtSTKNSCKVSFPERL------------------------------------------ 158
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 365 srrspihpsqaaifgdlasnyalidggsfvaerreaQKYAYQLRAVSEHRGGPYSGHFVTYRRASAP------------- 431
Cdd:cd02662 159 ------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepgsfvrmr 202
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 86563443 432 -----NHHTWYYTSDAQVTRVPYSHV-AACQSYMLFYE 463
Cdd:cd02662 203 egpssTSHPWWRISDTTVKEVSESEVlEQKSAYMLFYE 240
 
Name Accession Description Interval E-value
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
46-463 1.26e-62

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: 203.37  E-value: 1.26e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443  46 GLANQGNTCYMNALLQGLASCPSFVGWLKSLKPQdigiqggfvdhlsnllhllneptgstltaqsiveslkahgwsitvg 125
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 126 veHDLYELFNVFVTTWEDELKSSRRILMNQSIENCHSSSSEDdedvvvestslrgspsiirklmsfqrcasmaridaslr 205
Cdd:cd02662  35 --QDAHELFQVLLETLEQLLKFPFDGLLASRIVCLQCGESSK-------------------------------------- 74
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 206 spcvgltateyrccntncgyrtVKYESFTVLTLAIPNSQMGTSTNTESLLRRFFCSEIIRDAICDKCrasdrkqqgflkK 285
Cdd:cd02662  75 ----------------------VRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC------------Q 120
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 286 HGIVKLPQTLMIRIERVGMLPNG-SMKLSEHVHFGECLslqdvcfrknpkinqksyeesslhwqlpdgtsrvvggaeetr 364
Cdd:cd02662 121 TVIVRLPQILCIHLSRSVFDGRGtSTKNSCKVSFPERL------------------------------------------ 158
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 365 srrspihpsqaaifgdlasnyalidggsfvaerreaQKYAYQLRAVSEHRGGPYSGHFVTYRRASAP------------- 431
Cdd:cd02662 159 ------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepgsfvrmr 202
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 86563443 432 -----NHHTWYYTSDAQVTRVPYSHV-AACQSYMLFYE 463
Cdd:cd02662 203 egpssTSHPWWRISDTTVKEVSESEVlEQKSAYMLFYE 240
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
46-462 5.55e-25

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 104.83  E-value: 5.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443    46 GLANQGNTCYMNALLQGLASCPSFVGWLKSLKP--------QDIGI----QGGFVDHLSNLLHLLNEPTGSTLTAQSIVE 113
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPlsedsrynKDINLlcalRDLFKALQKNSKSSSVSPKMFKKSLGKLNP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443   114 SLKAHGwsitvgvEHDLYELFNVFVTTWEDELKSSrrilmnqsienchsssseddedvvvestSLRGSPSIIRKLmsFQr 193
Cdd:pfam00443  82 DFSGYK-------QQDAQEFLLFLLDGLHEDLNGN----------------------------HSTENESLITDL--FR- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443   194 casmaridaslrspcvGLTATEYRCCNtnCGYRTVKYESFTVLTLAIPNSQmgTSTNTESLLRRFFCSEIIR------DA 267
Cdd:pfam00443 124 ----------------GQLKSRLKCLS--CGEVSETFEPFSDLSLPIPGDS--AELKTASLQICFLQFSKLEelddeeKY 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443   268 ICDKCRasdRKQQGfLKKHGIVKLPQTLMIRIERVGMLPNGSMKLSEHVHFGECLSLQDVCFRKNPKinqksyeesslhw 347
Cdd:pfam00443 184 YCDKCG---CKQDA-IKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRYLAEELKP------------- 246
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443   348 qlpdgtsrvvggaeetrsrrspihpsqaaifgdlasnyalidggsfvaerREAQKYAYQLRAVSEHRGGPYSGHFVTYRR 427
Cdd:pfam00443 247 --------------------------------------------------KTNNLQDYRLVAVVVHSGSLSSGHYIAYIK 276
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 86563443   428 asAPNHHTWYYTSDAQVTRVPYSH-VAACQSYMLFY 462
Cdd:pfam00443 277 --AYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
399-464 5.75e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 52.19  E-value: 5.75e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86563443 399 EAQKYAYQLRAVSEHRGGPYSGHFVTYRRASAPNhhTWYYTSDAQVTRVPYSHVAACQSYMLFYER 464
Cdd:COG5560 758 DDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANN--GWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
 
Name Accession Description Interval E-value
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
46-463 1.26e-62

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: 203.37  E-value: 1.26e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443  46 GLANQGNTCYMNALLQGLASCPSFVGWLKSLKPQdigiqggfvdhlsnllhllneptgstltaqsiveslkahgwsitvg 125
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 126 veHDLYELFNVFVTTWEDELKSSRRILMNQSIENCHSSSSEDdedvvvestslrgspsiirklmsfqrcasmaridaslr 205
Cdd:cd02662  35 --QDAHELFQVLLETLEQLLKFPFDGLLASRIVCLQCGESSK-------------------------------------- 74
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 206 spcvgltateyrccntncgyrtVKYESFTVLTLAIPNSQMGTSTNTESLLRRFFCSEIIRDAICDKCrasdrkqqgflkK 285
Cdd:cd02662  75 ----------------------VRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC------------Q 120
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 286 HGIVKLPQTLMIRIERVGMLPNG-SMKLSEHVHFGECLslqdvcfrknpkinqksyeesslhwqlpdgtsrvvggaeetr 364
Cdd:cd02662 121 TVIVRLPQILCIHLSRSVFDGRGtSTKNSCKVSFPERL------------------------------------------ 158
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 365 srrspihpsqaaifgdlasnyalidggsfvaerreaQKYAYQLRAVSEHRGGPYSGHFVTYRRASAP------------- 431
Cdd:cd02662 159 ------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepgsfvrmr 202
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 86563443 432 -----NHHTWYYTSDAQVTRVPYSHV-AACQSYMLFYE 463
Cdd:cd02662 203 egpssTSHPWWRISDTTVKEVSESEVlEQKSAYMLFYE 240
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
46-463 6.42e-32

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: 122.59  E-value: 6.42e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443  46 GLANQGNTCYMNALLQGLAScpsfvgwlkslkpqdigiqggfvdhlsnllhllneptgstltaqsiveslkahgwsitvg 125
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 126 VEHDLYELFNVFVTTWEDELKSSRRILMNQSIEnchsssseddedvvvestslrgsPSIIRKLmsFQrcasmaridaslr 205
Cdd:cd02257  21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL-----------------------KSLIHDL--FG------------- 62
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 206 spcvGLTATEYRCCNtnCGYRTVKYESFTVLTLAIPNSQMGTSTNTEsLLRRFFCSEIIRDAICDKCraSDRKQQGFLKK 285
Cdd:cd02257  63 ----GKLESTIVCLE--CGHESVSTEPELFLSLPLPVKGLPQVSLED-CLEKFFKEEILEGDNCYKC--EKKKKQEATKR 133
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 286 HGIVKLPQTLMIRIERVGMLPNGSM-KLSEHVHFGECLSLQDVCFRKNPKINQksyeesslhwqlpdgtsrvvggaeetr 364
Cdd:cd02257 134 LKIKKLPPVLIIHLKRFSFNEDGTKeKLNTKVSFPLELDLSPYLSEGEKDSDS--------------------------- 186
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 365 srrspihpsqaaifgdlasnyalidggsfvaerrEAQKYAYQLRAVSEHRGG-PYSGHFVTYRRAsaPNHHTWYYTSDAQ 443
Cdd:cd02257 187 ----------------------------------DNGSYKYELVAVVVHSGTsADSGHYVAYVKD--PSDGKWYKFNDDK 230
                       410       420
                ....*....|....*....|....*
gi 86563443 444 VTRVPYSHVAA-----CQSYMLFYE 463
Cdd:cd02257 231 VTEVSEEEVLEfgslsSSAYILFYE 255
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
46-462 5.55e-25

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 104.83  E-value: 5.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443    46 GLANQGNTCYMNALLQGLASCPSFVGWLKSLKP--------QDIGI----QGGFVDHLSNLLHLLNEPTGSTLTAQSIVE 113
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPlsedsrynKDINLlcalRDLFKALQKNSKSSSVSPKMFKKSLGKLNP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443   114 SLKAHGwsitvgvEHDLYELFNVFVTTWEDELKSSrrilmnqsienchsssseddedvvvestSLRGSPSIIRKLmsFQr 193
Cdd:pfam00443  82 DFSGYK-------QQDAQEFLLFLLDGLHEDLNGN----------------------------HSTENESLITDL--FR- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443   194 casmaridaslrspcvGLTATEYRCCNtnCGYRTVKYESFTVLTLAIPNSQmgTSTNTESLLRRFFCSEIIR------DA 267
Cdd:pfam00443 124 ----------------GQLKSRLKCLS--CGEVSETFEPFSDLSLPIPGDS--AELKTASLQICFLQFSKLEelddeeKY 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443   268 ICDKCRasdRKQQGfLKKHGIVKLPQTLMIRIERVGMLPNGSMKLSEHVHFGECLSLQDVCFRKNPKinqksyeesslhw 347
Cdd:pfam00443 184 YCDKCG---CKQDA-IKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRYLAEELKP------------- 246
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443   348 qlpdgtsrvvggaeetrsrrspihpsqaaifgdlasnyalidggsfvaerREAQKYAYQLRAVSEHRGGPYSGHFVTYRR 427
Cdd:pfam00443 247 --------------------------------------------------KTNNLQDYRLVAVVVHSGSLSSGHYIAYIK 276
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 86563443   428 asAPNHHTWYYTSDAQVTRVPYSH-VAACQSYMLFY 462
Cdd:pfam00443 277 --AYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
218-463 2.61e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 89.65  E-value: 2.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 218 CCnTNCGYRTVKYESFTVLTLAIPNSQMGTSTNT-ESLLRRFFCSEIIRDAICDKCRASDRKQQGFlKKHGIVKLPQTLM 296
Cdd:cd02674  53 TC-LTCGKTSTTFEPFTYLSLPIPSGSGDAPKVTlEDCLRLFTKEETLDGDNAWKCPKCKKKRKAT-KKLTISRLPKVLI 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 297 IRIERVGMLPNGSMKLSEHVHFgeclSLQDVCFRKNPKinqksyeesslhwqlpdgtsrvvggaeeTRSRRSPIHpsqaa 376
Cdd:cd02674 131 IHLKRFSFSRGSTRKLTTPVTF----PLNDLDLTPYVD----------------------------TRSFTGPFK----- 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 377 ifgdlasnyalidggsfvaerreaqkyaYQLRAVSEHRGGPYSGHFVTYRRASAPNhhTWYYTSDAQVTRVPYSHVAACQ 456
Cdd:cd02674 174 ----------------------------YDLYAVVNHYGSLNGGHYTAYCKNNETN--DWYKFDDSRVTKVSESSVVSSS 223

                ....*..
gi 86563443 457 SYMLFYE 463
Cdd:cd02674 224 AYILFYE 230
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
218-463 9.29e-16

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: 77.43  E-value: 9.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 218 CCNtnCGYRTVKYESFtvLTLAIPNSQMGTSTNT-ESLLRRFFCSEIIRDA---ICDKC-RASdrkqqgflKKHGIVKLP 292
Cdd:cd02667  83 CES--CGTVSLVYEPF--LDLSLPRSDEIKSECSiESCLKQFTEVEILEGNnkfACENCtKAK--------KQYLISKLP 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 293 QTLMIRIERVGMLPNGSM-KLSEHVHFGECLSLQDVCfrkNPKINQKSYEESSLhwqlpdgtsrvvggaeetrsrrspih 371
Cdd:cd02667 151 PVLVIHLKRFQQPRSANLrKVSRHVSFPEILDLAPFC---DPKCNSSEDKSSVL-------------------------- 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 372 psqaaifgdlasnyalidggsfvaerreaqkyaYQLRAVSEHRGGPYSGHFVTYRRASAPNHHT---------------- 435
Cdd:cd02667 202 ---------------------------------YRLYGVVEHSGTMRSGHYVAYVKVRPPQQRLsdltkskpaadeagpg 248
                       250       260       270
                ....*....|....*....|....*....|.
gi 86563443 436 ---WYYTSDAQVTRVPYSHVAACQSYMLFYE 463
Cdd:cd02667 249 sgqWYYISDSDVREVSLEEVLKSEAYLLFYE 279
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
45-462 4.77e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 69.61  E-value: 4.77e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443  45 PGLANQGNTCYMNALLQGLASCPSFVGWLKSLK-PQDIGIQG-GFVDHLSNLLHLLNEPTGSTLTAQSIVESLKAHGWSI 122
Cdd:cd02661   2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREhSKDCCNEGfCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 123 TVGVEHDLYELFNVFvttwedelkssrrilmnqsIENCHSSSS-----EDDEDVVVESTSLrgspsiirklmsfqrcasM 197
Cdd:cd02661  82 RIGRQEDAHEFLRYL-------------------LDAMQKACLdrfkkLKAVDPSSQETTL------------------V 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 198 ARI-DASLRSpcvgltatEYRCCNtnCGYRTVKYESFTVLTLAIPNSQmgtstNTESLLRRFFCSEIIRD---AICDKCR 273
Cdd:cd02661 125 QQIfGGYLRS--------QVKCLN--CKHVSNTYDPFLDLSLDIKGAD-----SLEDALEQFTKPEQLDGenkYKCERCK 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 274 --ASDRKQqgFLkkhgIVKLPQTLMIRIERVGMLPNGsmKLSEHVHFGECLSLQDVCFRKNpkinqksyeesslhwqlpd 351
Cdd:cd02661 190 kkVKASKQ--LT----IHRAPNVLTIHLKRFSNFRGG--KINKQISFPETLDLSPYMSQPN------------------- 242
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 352 gtsrvvggaeetrsrrspihpsqaaifgdlasnyalidGGSFVaerreaqkyaYQLRAVSEHRGG-PYSGHFVTYRRASa 430
Cdd:cd02661 243 --------------------------------------DGPLK----------YKLYAVLVHSGFsPHSGHYYCYVKSS- 273
                       410       420       430
                ....*....|....*....|....*....|..
gi 86563443 431 pnHHTWYYTSDAQVTRVPYSHVAACQSYMLFY 462
Cdd:cd02661 274 --NGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
46-467 7.56e-12

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: 66.51  E-value: 7.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443  46 GLANQGNTCYMNALLQGLASCPSF----VGWL-KSLKPQDIGI----QGGFVDH-LSNLLHLLNEPTGSTltaqsivesl 115
Cdd:cd02659   4 GLKNQGATCYMNSLLQQLYMTPEFrnavYSIPpTEDDDDNKSVplalQRLFLFLqLSESPVKTTELTDKT---------- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 116 KAHGW-SITVGVEHDLYELFNVFVTTWEDELKSSRRilmNQSIENChsssseddedvvvestsLRGspsiirKLMSFQRC 194
Cdd:cd02659  74 RSFGWdSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQ---EGLIKNL-----------------FGG------KLVNYIIC 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 195 asmaridaslrspcvgltateyrccnTNCGYRTVKYESFTVLTLAIpnsqMGTSTNTESlLRRFFCSEIIRDA---ICDK 271
Cdd:cd02659 128 --------------------------KECPHESEREEYFLDLQVAV----KGKKNLEES-LDAYVQGETLEGDnkyFCEK 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 272 CrasdRKQQGFLKKHGIVKLPQTLMIRIERVG--MLPNGSMKLSEHVHFGEclslqdvcfrknpKINQKSYEESSLHwql 349
Cdd:cd02659 177 C----GKKVDAEKGVCFKKLPPVLTLQLKRFEfdFETMMRIKINDRFEFPL-------------ELDMEPYTEKGLA--- 236
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 350 pdgtsrvvggaeetrsrrspihpsqaaifgdlasnyalidGGSFVAERREAQKYAYQLRAVSEHRGGPYSGHFVTYRRAS 429
Cdd:cd02659 237 ----------------------------------------KKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDR 276
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 430 APNHhtWYYTSDAQVTR----------------------VPYSHVAACQSYMLFYERVKP 467
Cdd:cd02659 277 DDGK--WYKFNDDVVTPfdpndaeeecfggeetqktydsGPRAFKRTTNAYMLFYERKSP 334
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
399-464 5.75e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 52.19  E-value: 5.75e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86563443 399 EAQKYAYQLRAVSEHRGGPYSGHFVTYRRASAPNhhTWYYTSDAQVTRVPYSHVAACQSYMLFYER 464
Cdd:COG5560 758 DDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANN--GWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
403-462 8.93e-07

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 50.83  E-value: 8.93e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 403 YAYQLRAVSEHRGGPYSGHFVTYRRASAPnhhTWYYTSDAQVTRVPYSHVAACQSYMLFY 462
Cdd:cd02660 271 YTYDLFAVVVHKGTLDTGHYTAYCRQGDG---QWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
46-78 1.08e-05

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 47.33  E-value: 1.08e-05
                        10        20        30
                ....*....|....*....|....*....|...
gi 86563443  46 GLANQGNTCYMNALLQGLASCPSFVGWLKSLKP 78
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNP 33
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
46-76 4.52e-04

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 42.19  E-value: 4.52e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 86563443  46 GLANQGNTCYMNALLQGLASCPSFVGWLKSL 76
Cdd:cd02671  26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKHL 56
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
405-463 4.68e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 41.75  E-value: 4.68e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86563443 405 YQLRAVSEHRG-GPYSGHFVTYRRASApNHHTWYYTSDAQVTRVPYSHV---AACQSYMLFYE 463
Cdd:cd02673 184 YSLVAVICHLGeSPYDGHYIAYTKELY-NGSSWLYCSDDEIRPVSKNDVstnARSSGYLIFYD 245
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
46-64 6.07e-04

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 41.71  E-value: 6.07e-04
                        10
                ....*....|....*....
gi 86563443  46 GLANQGNTCYMNALLQGLA 64
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILA 19
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
46-463 1.12e-03

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 40.94  E-value: 1.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443  46 GLANQGNTCYMNALLQGLASCPSFVGWLKSLKPQDIGiqggfvdhlsnllhllnePTGSTLTAQsivESLKAHgWSITvg 125
Cdd:cd02664   1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLG------------------DSQSVMKKL---QLLQAH-LMHT-- 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 126 veHDLYELfnvfvtTWEDELKSSRRILMNQSIENchsSSSEddedvvvestslrgspsIIRKLMSfqrcasmaRIDASLR 205
Cdd:cd02664  57 --QRRAEA------PPDYFLEASRPPWFTPGSQQ---DCSE-----------------YLRYLLD--------RLHTLIE 100
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 206 SPCVGLTATEYRCcnTNCGYRTVKYESFTVLTLAIPNSQmgtstnteSLLrRFFCSEIIRDA----ICDKCrasdRKQQG 281
Cdd:cd02664 101 KMFGGKLSTTIRC--LNCNSTSARTERFRDLDLSFPSVQ--------DLL-NYFLSPEKLTGdnqyYCEKC----ASLQD 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 282 FLKKHGIVKLPQTLMIRIERVGMLP--NGSMKLSEHVHFGECLSLqdvcfrknP-KINQKSYEESSLHWQLPDGTSrvvg 358
Cdd:cd02664 166 AEKEMKVTGAPEYLILTLLRFSYDQktHVREKIMDNVSINEVLSL--------PvRVESKSSESPLEKKEEESGDD---- 233
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 359 GAEETRsrrsPIHpsqaaifgdlasnyalidggsfvaerreaqkyaYQLRAVSEHRG-GPYSGHFVTYRR---------A 428
Cdd:cd02664 234 GELVTR----QVH---------------------------------YRLYAVVVHSGySSESGHYFTYARdqtdadstgQ 276
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 86563443 429 SAPNHH---------TWYYTSDAQVTRVPYSHVAACQS-------YMLFYE 463
Cdd:cd02664 277 ECPEPKdaeendeskNWYLFNDSRVTFSSFESVQNVTSrfpkdtpYILFYE 327
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
46-78 1.37e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 40.77  E-value: 1.37e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 86563443  46 GLANQGNTCYMNALLQGLASCPSFVGWLKSLKP 78
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLEN 33
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
46-67 1.98e-03

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 40.64  E-value: 1.98e-03
                        10        20
                ....*....|....*....|..
gi 86563443  46 GLANQGNTCYMNALLQGLASCP 67
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTW 288
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
46-448 3.03e-03

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 39.71  E-value: 3.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443  46 GLANQGNTCYMNALLQ----------GLASCPS-------FVGWLKSLKPQDIGIQ------------GGFVDhlsnllh 96
Cdd:cd02668   1 GLKNLGATCYVNSFLQlwfmnlefrkAVYECNStedaelkNMPPDKPHEPQTIIDQlqlifaqlqfgnRSVVD------- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443  97 llnePTGstltaqsIVESLkahgwSITVGVEHDLYELFNVFVTTWEDELKSSRrilmNQSIENchsssseddedvvvest 176
Cdd:cd02668  74 ----PSG-------FVKAL-----GLDTGQQQDAQEFSKLFLSLLEAKLSKSK----NPDLKN----------------- 116
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 177 slrgspsIIRKLMsfqrCASMARIDaslrspcvgltateyrCCNtNCGYRTVKYESFTVLTLaipnsQMGTSTNTESLLR 256
Cdd:cd02668 117 -------IVQDLF----RGEYSYVT----------------QCS-KCGRESSLPSKFYELEL-----QLKGHKTLEECID 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 257 RFFCSEIIRDA---ICDKCrasDRKQQGfLKKHGIVKLPQTLmiriervgmlpngsmklsehvhfgeCLSLQDVCFrkNP 333
Cdd:cd02668 164 EFLKEEQLTGDnqyFCESC---NSKTDA-TRRIRLTTLPPTL-------------------------NFQLLRFVF--DR 212
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563443 334 KINQKSYEESSLHwqLPDgtsrvvggaeetrsrrspihpsqaaifgdlasnyaLIDGGSFVAERREaQKYAYQLRAVSEH 413
Cdd:cd02668 213 KTGAKKKLNASIS--FPE-----------------------------------ILDMGEYLAESDE-GSYVYELSGVLIH 254
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 86563443 414 RG-GPYSGHFVTYRRasAPNHHTWYYTSDAQVTRVP 448
Cdd:cd02668 255 QGvSAYSGHYIAHIK--DEQTGEWYKFNDEDVEEMP 288
 
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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