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Conserved domains on  [gi|767995422|ref|XP_011523370|]
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ubiquitin carboxyl-terminal hydrolase 36 isoform X6 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 10119183)

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_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-256 9.49e-147

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: 437.48  E-value: 9.49e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422   1 MLCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKACLNGCAKL---DRQTQATTLVH 77
Cdd:cd02661   46 MMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQ 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  78 QIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSN 157
Cdd:cd02661  126 QIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPN 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 158 VLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLV 237
Cdd:cd02661  206 VLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKV 285
                        250
                 ....*....|....*....
gi 767995422 238 HSSNVKVVLNQQAYVLFYL 256
Cdd:cd02661  286 SPVSIETVLSQKAYILFYI 304
PHA03247 super family cl33720
large tegument protein UL36; Provisional
341-675 1.14e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  341 PPKLPSGSPSPKLSQTPTHMPTILDDPGKKVKKPAPPQHFSPRTAQGL-------------------------------- 388
Cdd:PHA03247 2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqassppqrprrraarptvgsltsladpp 2702
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  389 -----PGTSNSNSSRSGSQRQGSWDSRDVVLSTSPKLLATATANGHGLKGNDESAGLDRRGSSSSSPEHSASSDSTKAPQ 463
Cdd:PHA03247 2703 pppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  464 TPRSGAAHLCDSQETncstaghSKTPPSGADSKTVKLKSPVLSNTTTEPASTMSPPPAKKLALSAKKASTL--------W 535
Cdd:PHA03247 2783 LTRPAVASLSESRES-------LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplggS 2855
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  536 RATGNDLRPPPPSPSSdLTHPMKTSHPvvastwPVHRARAVSPAPQSSSRLQPPFSPHPtllssTPKPPGTSEPRscssi 615
Cdd:PHA03247 2856 VAPGGDVRRRPPSRSP-AAKPAAPARP------PVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQ----- 2918
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767995422  616 stalPQVNEDLVSLPHQLPEASEPPQSPSEKRKKTF-VGEPQRLGSETRLPQHIREATAAP 675
Cdd:PHA03247 2919 ----PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGALVPGRVAVP 2975
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-256 9.49e-147

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: 437.48  E-value: 9.49e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422   1 MLCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKACLNGCAKL---DRQTQATTLVH 77
Cdd:cd02661   46 MMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQ 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  78 QIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSN 157
Cdd:cd02661  126 QIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPN 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 158 VLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLV 237
Cdd:cd02661  206 VLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKV 285
                        250
                 ....*....|....*....
gi 767995422 238 HSSNVKVVLNQQAYVLFYL 256
Cdd:cd02661  286 SPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1-255 1.72e-59

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 206.14  E-value: 1.72e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422    1 MLCVMQNHIVQAFANS-GNAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAClngcaKLDRQTQATTLVHQI 79
Cdd:pfam00443  47 LLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422   80 FGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVR------ALELFVKADVLSGENAYMCAKCKKKVPASKRFTIH 153
Cdd:pfam00443 122 FRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKIS 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  154 RTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLNIRPYMSQNN----GDPVMYGLYAVLVHSGySCHAGHYYCYVKA-SN 226
Cdd:pfam00443 202 RLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELDLSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyEN 280
                         250       260       270
                  ....*....|....*....|....*....|
gi 767995422  227 GQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 255
Cdd:pfam00443 281 NRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; ...
19-258 2.25e-25

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


Pssm-ID: 227820 [Multi-domain]  Cd Length: 415  Bit Score: 110.11  E-value: 2.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  19 AIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAcLNGCAKLDRQTQAT------------------------- 73
Cdd:COG5533  140 SISPRNFIDILSGRNKLFSGDMQQDSQEFLIFFLDLLHED-LNGNKSRSPILELKdefeevreelplshfshhewnlhlr 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  74 ---TLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAA--NIVRALELFVKADVLSGENAYMCAKCKKKVPASK 148
Cdd:COG5533  219 snkSLVAKTFFGQDKSRLQCEACNYTSTTIAMFSTLLVPPYEVVqlGLQECIDRFYEEEKLEGKDAWRCPKCGRKESSRK 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 149 RFTIHRTSNVLTLSLKRFANFsggkitkdVGYPEFLNIRPYMS-------------QNNGD--PVMYGLYAVLVHSGySC 213
Cdd:COG5533  299 RMEILVLPDVLIIHISRFHIS--------VMGRKKIDTPQGWKntasvevnvtllfNNGIGyiPRKYSLLGVVCHNG-TL 369
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 767995422 214 HAGHYYCYVKASNGqWYQMNDSLVHS-SNVKVVLNQQAYVLFYLRI 258
Cdd:COG5533  370 NGGHYFSEVKRSGT-WNVYDDSQVRKgSRTTSGSHPSSYILFYTRS 414
PHA03247 PHA03247
large tegument protein UL36; Provisional
341-675 1.14e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  341 PPKLPSGSPSPKLSQTPTHMPTILDDPGKKVKKPAPPQHFSPRTAQGL-------------------------------- 388
Cdd:PHA03247 2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqassppqrprrraarptvgsltsladpp 2702
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  389 -----PGTSNSNSSRSGSQRQGSWDSRDVVLSTSPKLLATATANGHGLKGNDESAGLDRRGSSSSSPEHSASSDSTKAPQ 463
Cdd:PHA03247 2703 pppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  464 TPRSGAAHLCDSQETncstaghSKTPPSGADSKTVKLKSPVLSNTTTEPASTMSPPPAKKLALSAKKASTL--------W 535
Cdd:PHA03247 2783 LTRPAVASLSESRES-------LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplggS 2855
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  536 RATGNDLRPPPPSPSSdLTHPMKTSHPvvastwPVHRARAVSPAPQSSSRLQPPFSPHPtllssTPKPPGTSEPRscssi 615
Cdd:PHA03247 2856 VAPGGDVRRRPPSRSP-AAKPAAPARP------PVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQ----- 2918
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767995422  616 stalPQVNEDLVSLPHQLPEASEPPQSPSEKRKKTF-VGEPQRLGSETRLPQHIREATAAP 675
Cdd:PHA03247 2919 ----PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGALVPGRVAVP 2975
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-256 9.49e-147

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: 437.48  E-value: 9.49e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422   1 MLCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKACLNGCAKL---DRQTQATTLVH 77
Cdd:cd02661   46 MMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQ 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  78 QIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSN 157
Cdd:cd02661  126 QIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPN 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 158 VLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLV 237
Cdd:cd02661  206 VLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKV 285
                        250
                 ....*....|....*....
gi 767995422 238 HSSNVKVVLNQQAYVLFYL 256
Cdd:cd02661  286 SPVSIETVLSQKAYILFYI 304
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
38-255 5.37e-61

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: 208.11  E-value: 5.37e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  38 FGNQEDAHEFLRYTIDAMQKACLNGCAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDP--YLDVALEIRQAA- 114
Cdd:cd02257   19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPelFLSLPLPVKGLPq 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 115 -NIVRALELFVKADVLSGENAYMCaKCKKKVPASKRFTIHRTSNVLTLSLKRFA---NFSGGKITKDVGYPEFLNIRPYM 190
Cdd:cd02257   99 vSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767995422 191 SQNNGD------PVMYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVL-----NQQAYVLFY 255
Cdd:cd02257  178 SEGEKDsdsdngSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFY 254
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1-255 1.72e-59

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 206.14  E-value: 1.72e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422    1 MLCVMQNHIVQAFANS-GNAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAClngcaKLDRQTQATTLVHQI 79
Cdd:pfam00443  47 LLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422   80 FGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVR------ALELFVKADVLSGENAYMCAKCKKKVPASKRFTIH 153
Cdd:pfam00443 122 FRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKIS 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  154 RTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLNIRPYMSQNN----GDPVMYGLYAVLVHSGySCHAGHYYCYVKA-SN 226
Cdd:pfam00443 202 RLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELDLSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyEN 280
                         250       260       270
                  ....*....|....*....|....*....|
gi 767995422  227 GQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 255
Cdd:pfam00443 281 NRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
3-255 1.28e-54

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: 192.97  E-value: 1.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422   3 CVMQNhIVQAFANSGNAiKPVSFIRDLK---KIARHFRFGNQEDAHEFLRYTIDAMQKACLNGCAKLDRQTQATTLVHQI 79
Cdd:cd02660   49 CAMDE-IFQEFYYSGDR-SPYGPINLLYlswKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQT 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  80 FGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRA---------------LELFVKADVLsGENAYMCAKCKKKV 144
Cdd:cd02660  127 FSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWAlgesgvsgtptlsdcLDRFTRPEKL-GDFAYKCSGCGSTQ 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 145 PASKRFTIHRTSNVLTLSLKRFANFSGG---KITKDVGYPEFLNIRPYMSQNNGDPVM---------YGLYAVLVHSGyS 212
Cdd:cd02660  206 EATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKIDTYVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKG-T 284
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 767995422 213 CHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 255
Cdd:cd02660  285 LDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
22-255 2.38e-46

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: 167.56  E-value: 2.38e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  22 PVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQkaclngcakldrqtqatTLVHQIFGGYLRSRVKCSVCKSVSDTYD 101
Cdd:cd02667   32 PKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 102 PYLDVAL----EIRQAANIVRALELFVKADVLSGENAYMCAKCKKkvpASKRFTIHRTSNVLTLSLKRF-----ANFSgg 172
Cdd:cd02667   95 PFLDLSLprsdEIKSECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqprsANLR-- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 173 KITKDVGYPEFLNIRPYMSQNN-----GDPVMYGLYAVLVHSGySCHAGHYYCYVKASN--------------------- 226
Cdd:cd02667  170 KVSRHVSFPEILDLAPFCDPKCnssedKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpg 248
                        250       260       270
                 ....*....|....*....|....*....|
gi 767995422 227 -GQWYQMNDSLVHSSNVKVVLNQQAYVLFY 255
Cdd:cd02667  249 sGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-255 1.13e-45

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: 164.00  E-value: 1.13e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  38 FGNQEDAHEFLRYTIDamqkaclngcaKLDRqtqattLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIV 117
Cdd:cd02674   19 SADQQDAQEFLLFLLD-----------GLHS------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 118 RA------LELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNFSGG---KITKDVGYP-EFLNIR 187
Cdd:cd02674   82 PKvtledcLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 188 PY-MSQNNGDPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 255
Cdd:cd02674  161 PYvDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
39-258 5.26e-42

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: 157.03  E-value: 5.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  39 GNQEDAHEFLRYTIDAMQKaclngcaKLdRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVR 118
Cdd:cd02659   84 FEQHDVQEFFRVLFDKLEE-------KL-KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEE 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 119 ALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNF-----SGGKITKDVGYPEFLNIRPYMSQN 193
Cdd:cd02659  156 SLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRF-EFdfetmMRIKINDRFEFPLELDMEPYTEKG 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 194 NG-----------DPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQ------------ 249
Cdd:cd02659  235 LAkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECfggeetqktyds 313
                        250
                 ....*....|....*....
gi 767995422 250 ----------AYVLFYLRI 258
Cdd:cd02659  314 gprafkrttnAYMLFYERK 332
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
20-255 7.96e-36

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: 137.83  E-value: 7.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  20 IKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTI----DAMQKACLNGCAKLDRQ-----TQATTLVHQIFGGYLRSRVKC 90
Cdd:cd02663   44 ISPKKFITRLKRENELFDNYMHQDAHEFLNFLLneiaEILDAERKAEKANRKLNnnnnaEPQPTWVHEIFQGILTNETRC 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  91 SVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA-NF 169
Cdd:cd02663  124 LTCETVSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKyDE 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 170 SGGKITK---DVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKaSNGQWYQMND---SLVHSSNVK 243
Cdd:cd02663  204 QLNRYIKlfyRVVFPLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDetvEKIDENAVE 282
                        250
                 ....*....|....*..
gi 767995422 244 VVLNQ-----QAYVLFY 255
Cdd:cd02663  283 EFFGDspnqaTAYVLFY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-237 4.24e-31

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: 124.84  E-value: 4.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422   2 LCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARHFRFGN-------------------QEDAHEFLRYTIDAMQkaclng 62
Cdd:cd02668   30 ECNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE------ 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  63 cAKLDRQT--QATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKC 140
Cdd:cd02668  104 -AKLSKSKnpDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESC 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 141 KKKVPASKRFTIHRTSNVLTLSLKRFA----NFSGGKITKDVGYPEFLNIRPY-MSQNNGDPVmYGLYAVLVHSGYSCHA 215
Cdd:cd02668  183 NSKTDATRRIRLTTLPPTLNFQLLRFVfdrkTGAKKKLNASISFPEILDMGEYlAESDEGSYV-YELSGVLIHQGVSAYS 261
                        250       260
                 ....*....|....*....|...
gi 767995422 216 GHYYCYVK-ASNGQWYQMNDSLV 237
Cdd:cd02668  262 GHYIAHIKdEQTGEWYKFNDEDV 284
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
36-255 1.26e-28

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: 117.59  E-value: 1.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  36 FRFGNQEDAHEFLRYTIDamqkaclngcaKLDrqtqatTLVHQIFGGYLRSRVKCSVCKSVSDTYD--PYLDVALeirqa 113
Cdd:cd02664   76 FTPGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSF----- 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 114 ANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA-NFSGG---KITKDVGYPEFLNI--- 186
Cdd:cd02664  134 PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSLpvr 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 187 -----------RPYMSQNNGD-----PVMYGLYAVLVHSGYSCHAGHYYCYV---------------------KASNGQW 229
Cdd:cd02664  214 veskssespleKKEEESGDDGelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNW 293
                        250       260       270
                 ....*....|....*....|....*....|...
gi 767995422 230 YQMNDSLVHSSNVKVVLN-------QQAYVLFY 255
Cdd:cd02664  294 YLFNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; ...
19-258 2.25e-25

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


Pssm-ID: 227820 [Multi-domain]  Cd Length: 415  Bit Score: 110.11  E-value: 2.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  19 AIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAcLNGCAKLDRQTQAT------------------------- 73
Cdd:COG5533  140 SISPRNFIDILSGRNKLFSGDMQQDSQEFLIFFLDLLHED-LNGNKSRSPILELKdefeevreelplshfshhewnlhlr 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  74 ---TLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAA--NIVRALELFVKADVLSGENAYMCAKCKKKVPASK 148
Cdd:COG5533  219 snkSLVAKTFFGQDKSRLQCEACNYTSTTIAMFSTLLVPPYEVVqlGLQECIDRFYEEEKLEGKDAWRCPKCGRKESSRK 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 149 RFTIHRTSNVLTLSLKRFANFsggkitkdVGYPEFLNIRPYMS-------------QNNGD--PVMYGLYAVLVHSGySC 213
Cdd:COG5533  299 RMEILVLPDVLIIHISRFHIS--------VMGRKKIDTPQGWKntasvevnvtllfNNGIGyiPRKYSLLGVVCHNG-TL 369
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 767995422 214 HAGHYYCYVKASNGqWYQMNDSLVHS-SNVKVVLNQQAYVLFYLRI 258
Cdd:COG5533  370 NGGHYFSEVKRSGT-WNVYDDSQVRKgSRTTSGSHPSSYILFYTRS 414
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
41-289 3.87e-20

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 96.48  E-value: 3.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422   41 QEDAHEFLRYTIDAMQKAClngcakldRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRAL 120
Cdd:COG5077   273 QHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESF 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  121 ELFVKADVLSGENAYMCAKcKKKVPASKRFTIHRTSNVLTLSLKRF-ANFSGG---KITKDVGYPEFLNIRPYMSQN--- 193
Cdd:COG5077   345 RRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEIDLLPFLDRDadk 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  194 --NGDPVmYGLYAVLVHSGySCHAGHYYCYVKAS-NGQWYQMNDSLVHSSNVKVVLNQ---------------------- 248
Cdd:COG5077   424 seNSDAV-YVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdhsgikrfm 501
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767995422  249 QAYVLFYLRipgsKKSPEGLISrtgssslPGRPSVIPDHSK 289
Cdd:COG5077   502 SAYMLVYLR----KSMLDDLLN-------PVAAVDIPPHVE 531
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
20-255 7.42e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 88.53  E-value: 7.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  20 IKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAClngcaKLDRQTQATTLvhqiFGGYLRSRVKCSVCKSVSDT 99
Cdd:cd02658   79 IKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRES-----FKNLGLNPNDL----FKFMIEDRLECLSCKKVKYT 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 100 YDP--YLDVALEIRQAANIVRALELFVKADV-------LSGE-NAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANF 169
Cdd:cd02658  150 SELseILSLPVPKDEATEKEEGELVYEPVPLedclkayFAPEtIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLL 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 170 SGG---KITKDVGYPEFLnirpymsqnngDPVMYGLYAVLVHSGYSCHAGHYYCYVK---ASNGQWYQMNDSLVHSSNVK 243
Cdd:cd02658  230 ENWvpkKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVASQDP 298
                        250
                 ....*....|..
gi 767995422 244 VVLNQQAYVLFY 255
Cdd:cd02658  299 PEMKKLGYIYFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
120-257 8.45e-17

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 85.32  E-value: 8.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 120 LELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEF-LNIRPYMSQNNGD 196
Cdd:COG5560  681 LNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPIDdLDLSGVEYMVDDP 760
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767995422 197 PVMYGLYAVLVHSGYScHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYLR 257
Cdd:COG5560  761 RLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
41-255 2.80e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 78.01  E-value: 2.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  41 QEDAHEFLRYTIDAMQKaclngcakldrqtqattLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQA------- 113
Cdd:cd02671  105 QHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESelsksee 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 114 ------------ANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFS------GG--K 173
Cdd:cd02671  168 sseispdpktemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefdcyGGlsK 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 174 ITKDVGYPEFLNIRPYMSQNNGDpvMYGLYAVLVHSGYSCHAGHYYCYVKasngqWYQMNDSLVHSSNVKVVLN------ 247
Cdd:cd02671  248 VNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFLEalspnt 320
                        250
                 ....*....|.
gi 767995422 248 ---QQAYVLFY 255
Cdd:cd02671  321 sstSTPYLLFY 331
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
3-255 2.33e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 73.55  E-value: 2.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422   3 CVMqNHIVQAFANSGnaikpvSFIRDLKkiarhfRFGNQEDAHEFLRYTIDAMQKACLNgcakldrqtqattlvhqIFGG 82
Cdd:cd02662    9 CFM-NSVLQALASLP------SLIEYLE------EFLEQQDAHELFQVLLETLEQLLKF-----------------PFDG 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  83 YLRSRVKCSVCKSVS-DTYDPYLDVALEIRQA-----ANIVRALELFVKADVLSGenaYMCAKCKKKVPASKRftihrts 156
Cdd:cd02662   59 LLASRIVCLQCGESSkVRYESFTMLSLPVPNQssgsgTTLEHCLDDFLSTEIIDD---YKCDRCQTVIVRLPQ------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 157 nVLTLSLKRFAnFSG-GKITKD---VGYPEFLNirpymsqnngdPVMYGLYAVLVHSGySCHAGHYYCYVKAS------- 225
Cdd:cd02662  129 -ILCIHLSRSV-FDGrGTSTKNsckVSFPERLP-----------KVLYRLRAVVVHYG-SHSSGHYVCYRRKPlfskdke 194
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 767995422 226 --------------NGQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 255
Cdd:cd02662  195 pgsfvrmregpsstSHPWWRISDTTVkEVSESEVLEQKSAYMLFY 239
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
70-237 1.81e-12

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 433195 [Multi-domain]  Cd Length: 305  Bit Score: 69.22  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422   70 TQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEI-RQAANIVRALELFVKADVL----SGENAY--MCAKCKK 142
Cdd:pfam13423 122 SPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYpRKPSSNNKKPPNQTFSSILksslERETTTkaWCEKCKR 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  143 KVPASKRFTIHRTSNVLTLSLKRFaNFSGGKITKDVGY-PEFLNIRPYM-SQNNGDPVMYGLYAVLVHSGYSCHAGHYYC 220
Cdd:pfam13423 202 YQPLESRRTVRNLPPVLSLNAALT-NEEWRQLWKTPGWlPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVS 280
                         170       180
                  ....*....|....*....|....*
gi 767995422  221 YVKASN--------GQWYQMNDSLV 237
Cdd:pfam13423 281 FVKVADseledpteSQWYLFNDFLV 305
UBP14 COG5207
Uncharacterized Zn-finger protein, UBP-type [General function prediction only];
18-192 2.71e-10

Uncharacterized Zn-finger protein, UBP-type [General function prediction only];


Pssm-ID: 227532 [Multi-domain]  Cd Length: 749  Bit Score: 64.32  E-value: 2.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  18 NAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAclngcakldRQTQATTLVHQIFGGYLRSRVKCSVCKSVS 97
Cdd:COG5207  371 NGISPLDFKMLIGQDHPEFGKFAQQDAHEFLLFLLEKIRKG---------ERSYLIPPITSLFEFEVERRLSCSGCMDVS 441
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  98 DTYDPYLDVALEIRQ---AANIVRALELFVKADVLSgenaYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGG 172
Cdd:COG5207  442 YSYESMLMICIFLEGndePQDIRKSVEAFFLPDTIE----WSCENCKGKKKASRKPFIKSLPKYLILQVGRYSlqNYKVE 517
                        170       180
                 ....*....|....*....|..
gi 767995422 173 KITK--DVGYPEFLNIRPYMSQ 192
Cdd:COG5207  518 KLSDpiEMRSDDMIKLGSFMSK 539
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
15-237 5.12e-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 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: 52.33  E-value: 5.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  15 NSGNAIKPVSFIRDLKKIARHF----RFGN--QEDAHEFLRYTIDAMQkaclngcAKLDRQTQATTLVHQIFGGYLRSRV 88
Cdd:cd02657   58 KKQEPVPPIEFLQLLRMAFPQFaekqNQGGyaQQDAEECWSQLLSVLS-------QKLPGAGSKGSFIDQLFGIELETKM 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  89 KC---SVCKSVSDTYDPYLDVALEIRQaanIVRALELFVKADvLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKR 165
Cdd:cd02657  131 KCtesPDEEEVSTESEYKLQCHISITT---EVNYLQDGLKKG-LEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVR 206
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767995422 166 F-----ANfSGGKITKDVGYPEFLNIRPYMSqNNGdpvMYGLYAVLVHSGYSCHAGHYYCYVKASN-GQWYQMNDSLV 237
Cdd:cd02657  207 FfwkrdIQ-KKAKILRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKV 279
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
29-255 5.90e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 51.76  E-value: 5.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  29 LKKIARHFRFGNQEDAHEFLRYTI----DAMQKACLNGCAKLDRQTQATTLvhQIFGGYLRSRVKCSVCKSVSDTYDPYL 104
Cdd:cd02673   21 IGKINTEFDNDDQQDAHEFLLTLLeaidDIMQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENVSDVGN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 105 DVALEIRQaaNIVRALELFVKADVLSGENAYMCAKCKKKVpASKRFTIHRTSNVLTLSLKRF-ANFSGGKITKDvgypEF 183
Cdd:cd02673   99 FLDVSMID--NKLDIDELLISNFKTWSPIEKDCSSCKCES-AISSERIMTFPECLSINLKRYkLRIATSDYLKK----NE 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767995422 184 LNIRPYMSQnngdPVMYGLYAVLVHSGYSCHAGHYYCYVKAS--NGQWYQMNDSLVH---SSNVKVVLNQQAYVLFY 255
Cdd:cd02673  172 EIMKKYCGT----DAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEIRpvsKNDVSTNARSSGYLIFY 244
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
36-248 7.22e-06

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 49.62  E-value: 7.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  36 FRFGNQEDAHEFLRYTIDAMqKACLNGCAKldrqtQATTLVHQIFGGYLR-----------------SRVKCSVCKSVSD 98
Cdd:cd02669  202 FSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeeegskdKFFKDSRVKKTSV 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  99 TYDPYLDVALEIR------QAANIVRALELFvkaDVLSGENAYMCAKCKKKVpasKRFTIHRTSNVLTLSLKRF--ANFS 170
Cdd:cd02669  276 SPFLLLTLDLPPPplfkdgNEENIIPQVPLK---QLLKKYDGKTETELKDSL---KRYLISRLPKYLIFHIKRFskNNFF 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 171 GGKITKDVGYP-EFLNIRPYMSQNNGD---PVMYGLYAVLVHSGYSCHAGHYYCYV-KASNGQWYQMNDslvhsSNVKVV 245
Cdd:cd02669  350 KEKNPTIVNFPiKNLDLSDYVHFDKPSlnlSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQD-----LNVKEV 424

                 ...
gi 767995422 246 LNQ 248
Cdd:cd02669  425 LPQ 427
PHA03247 PHA03247
large tegument protein UL36; Provisional
341-675 1.14e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  341 PPKLPSGSPSPKLSQTPTHMPTILDDPGKKVKKPAPPQHFSPRTAQGL-------------------------------- 388
Cdd:PHA03247 2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqassppqrprrraarptvgsltsladpp 2702
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  389 -----PGTSNSNSSRSGSQRQGSWDSRDVVLSTSPKLLATATANGHGLKGNDESAGLDRRGSSSSSPEHSASSDSTKAPQ 463
Cdd:PHA03247 2703 pppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  464 TPRSGAAHLCDSQETncstaghSKTPPSGADSKTVKLKSPVLSNTTTEPASTMSPPPAKKLALSAKKASTL--------W 535
Cdd:PHA03247 2783 LTRPAVASLSESRES-------LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplggS 2855
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  536 RATGNDLRPPPPSPSSdLTHPMKTSHPvvastwPVHRARAVSPAPQSSSRLQPPFSPHPtllssTPKPPGTSEPRscssi 615
Cdd:PHA03247 2856 VAPGGDVRRRPPSRSP-AAKPAAPARP------PVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQ----- 2918
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767995422  616 stalPQVNEDLVSLPHQLPEASEPPQSPSEKRKKTF-VGEPQRLGSETRLPQHIREATAAP 675
Cdd:PHA03247 2919 ----PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGALVPGRVAVP 2975
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-256 2.52e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 46.40  E-value: 2.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422  38 FGNQEDAHEFLRYTIDAMQKA-------------CLNGCAKLDRQTQATTLVHqiFGGYLRsrvKCSVCKSVSDTYDPY- 103
Cdd:cd02665   19 FSQQQDVSEFTHLLLDWLEDAfqaaaeaispgekSKNPMVQLFYGTFLTEGVL--EGKPFC---NCETFGQYPLQVNGYg 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 104 -LDVALEirqAANI-VRALELFVKADVLSG-ENAYMcakckkKVPAskrftihrtsnVLTLSLKRFA--NFSGGKITKDV 178
Cdd:cd02665   94 nLHECLE---AAMFeGEVELLPSDHSVKSGqERWFT------ELPP-----------VLTFELSRFEfnQGRPEKIHDKL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 179 GYPEFLNIRPYMsqnngdpvmygLYAVLVHSGySCHAGHYYCYV-KASNGQWYQMND-SLVHSSNVKVV-------LNQQ 249
Cdd:cd02665  154 EFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYNDiSVTESSWEEVErdsfgggRNPS 221

                 ....*..
gi 767995422 250 AYVLFYL 256
Cdd:cd02665  222 AYCLMYI 228
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
9-110 4.72e-05

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 47.19  E-value: 4.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422   9 IVQAFANSGNAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAcLNGCA-------------------KLDRQ 69
Cdd:COG5560  323 IKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHED-LNRIIkkpytskpdlspgddvvvkKKAKE 401
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767995422  70 T------QATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEI 110
Cdd:COG5560  402 CwwehlkRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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