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Conserved domains on  [gi|1050361400|gb|OCT63605|]
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Protein Classification

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List of domain hits

Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
280-617 1.07e-38

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 334078 [Multi-domain]  Cd Length: 305  Bit Score: 144.45  E-value: 1.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLLSVQPFvSDLLQQKIPYKTF----QEFVFIRNLYNLIRRKDRYSlKKRRKLLLKLKDSVSIS 355
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQCLFSIPPF-RDYLLRISPLSEDsrynKDINLLCALADLFKALQSEK-KSSSVSPKEFKKTLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 356 AERFADNEQHDAHDFLTECFSLMKEDiaqLSNEMKNPISCPVKSNFEFDLEYIYICNKCGETRISVNQNNCLFVDIlqed 435
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHED---LNGKHSTENESLITDLFRGQLKSRLKCLNCGKESYTFEPFLDLSLPI---- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 436 snSDSASETLQDAVDYYFLDETVEFS----CEKCGGNESTLKQ-KFRSLPRVLIVKLKRYgrtADDTFRIGKLKDKIGVT 510
Cdd:pfam00443 153 --PSLKNYDLQDCLKAFTKEEILKGEnmyyCPKCKGKCGAIKKlKISRLPPVLIIHLKRF---SYNRSTWEKLNTEVEFP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 511 LSLAVASHCTARTTLPPTSPemdgnveeketkksekkkpskknkfQPYELKSIVNHSGeSAEYGHYFSDVYDRRTKTWLA 590
Cdd:pfam00443 228 EELDLSEYLAEGLDEKEVEP-------------------------TKYRLVAVVVHSG-SLSSGHYIAYIKKYENGRWYK 281
                         330       340
                  ....*....|....*....|....*..
gi 1050361400 591 YDDADINEIDEDVLLPSRAytgYLFFY 617
Cdd:pfam00443 282 FDDEKVTEVDEEEVLNKSA---YILFY 305
Ig super family cl11960
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
47-124 1.93e-03

Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


The actual alignment was detected with superfamily member cd16091:

Pssm-ID: 353325  Cd Length: 91  Bit Score: 37.69  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400  47 IISCYFTPrssirNDKVSLEWEKEKggEYIPLIQFVDNKvKKVSLQDNRF----QVFKNLVHRGNCSLIISSTKLIDSGN 122
Cdd:cd16091     2 ILPCSFTP-----GGEEVIHWYKLN--SDIPVHSYYYNK-DQLEHQDQRYrgrtSLFKDQISKGNASLLLKNVKVQDEGR 73

                  ..
gi 1050361400 123 YQ 124
Cdd:cd16091    74 YK 75
TMEM132D_C super family cl24320
Mature oligodendrocyte transmembrane protein, TMEM132D, C-term; TMEM132D_C is the C-terminal ...
211-237 5.34e-03

Mature oligodendrocyte transmembrane protein, TMEM132D, C-term; TMEM132D_C is the C-terminal family of chordate proteins implicated in panic disorder. TMEM132D is a single-pass transmembrane protein that is highly expressed in the cortical regions of the human and mouse brain. The function is still unknown. It may act as a cell-surface marker for oligodendrocyte differentiation. Additionally, as it may be most strongly expressed in neurons and it colocalizes with actin filaments TMEM132D may be implicated in neuronal sprouting and connectivity in brain regions important for anxiety-related behaviour.


The actual alignment was detected with superfamily member pfam15706:

Pssm-ID: 318007  Cd Length: 84  Bit Score: 36.15  E-value: 5.34e-03
                          10        20
                  ....*....|....*....|....*..
gi 1050361400 211 ICSVAVLTFVIACVVYCYRTRSKQKAP 237
Cdd:pfam15706  40 VFCLAILVFLINCVVFALKYRRKKSPV 66
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
280-617 1.07e-38

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 334078 [Multi-domain]  Cd Length: 305  Bit Score: 144.45  E-value: 1.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLLSVQPFvSDLLQQKIPYKTF----QEFVFIRNLYNLIRRKDRYSlKKRRKLLLKLKDSVSIS 355
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQCLFSIPPF-RDYLLRISPLSEDsrynKDINLLCALADLFKALQSEK-KSSSVSPKEFKKTLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 356 AERFADNEQHDAHDFLTECFSLMKEDiaqLSNEMKNPISCPVKSNFEFDLEYIYICNKCGETRISVNQNNCLFVDIlqed 435
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHED---LNGKHSTENESLITDLFRGQLKSRLKCLNCGKESYTFEPFLDLSLPI---- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 436 snSDSASETLQDAVDYYFLDETVEFS----CEKCGGNESTLKQ-KFRSLPRVLIVKLKRYgrtADDTFRIGKLKDKIGVT 510
Cdd:pfam00443 153 --PSLKNYDLQDCLKAFTKEEILKGEnmyyCPKCKGKCGAIKKlKISRLPPVLIIHLKRF---SYNRSTWEKLNTEVEFP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 511 LSLAVASHCTARTTLPPTSPemdgnveeketkksekkkpskknkfQPYELKSIVNHSGeSAEYGHYFSDVYDRRTKTWLA 590
Cdd:pfam00443 228 EELDLSEYLAEGLDEKEVEP-------------------------TKYRLVAVVVHSG-SLSSGHYIAYIKKYENGRWYK 281
                         330       340
                  ....*....|....*....|....*..
gi 1050361400 591 YDDADINEIDEDVLLPSRAytgYLFFY 617
Cdd:pfam00443 282 FDDEKVTEVDEEEVLNKSA---YILFY 305
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
280-618 5.47e-35

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: 132.61  E-value: 5.47e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLLSvqpfvsdllqqkipyktfqefvfirnlynlirrkdryslkkrrklllklkdsvsisaerf 359
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 360 adnEQHDAHDFLTECFSLMKEDIAQLSNEMK--NPISCPVKSNFEFDLEYIYICNKCGETRISVNQNNCLFVDIlqedSN 437
Cdd:cd02257    21 ---EQQDAHEFLLFLLDKLHEELKKSSKRTSdsSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPL----PV 93
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 438 SDSASETLQDAVDYYFLDETVE----FSCEKCGGNESTLKQKFRSLPRVLIVKLKRYgrTADDTFRIGKLKDKIGVTLSL 513
Cdd:cd02257    94 KGLPQVSLEDCLEKFFKEEILEgdncYKCEKKKKQEATKRLKIKKLPPVLIIHLKRF--SFNEDGTKEKLNTKVSFPLEL 171
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 514 AVASHCTARTTLPPTSPEMDgnveeketkksekkkpskknkfqPYELKSIVNHSGESAEYGHYFSDVYDRRTKTWLAYDD 593
Cdd:cd02257   172 DLSPYLSEGEKDSDSDNGSY-----------------------KYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFND 228
                         330       340
                  ....*....|....*....|....*..
gi 1050361400 594 ADINEIDED--VLLPSRAYTGYLFFYI 618
Cdd:cd02257   229 DKVTEVSEEevLEFGSLSSSAYILFYE 255
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; ...
274-617 5.99e-18

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


Pssm-ID: 227820 [Multi-domain]  Cd Length: 415  Bit Score: 86.23  E-value: 5.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 274 ENPKPQGFPNLGNTCYMNATLQSLLSVQPFVSDLLQQKipYKTFQEFVFIRN------------LYNLIRRKDRYSlkkr 341
Cdd:COG5533    67 DNLPPNGLRNKGNTCYMNCALQCLLSIGDLNTMLQGRF--YLQNINTDFPRGkpgsnafkqfiaLYETPGCHGPKS---- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 342 rKLLLKLKDSVSISAERFADNEQHDAHDFLTECFSLMKED---------IAQLSNE---MKNPISCPVKSNFEFDLEYIY 409
Cdd:COG5533   141 -ISPRNFIDILSGRNKLFSGDMQQDSQEFLIFFLDLLHEDlngnksrspILELKDEfeeVREELPLSHFSHHEWNLHLRS 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 410 I-----------------CNKCGETRISVNQNNCLFVDIlqedsnSDSASETLQDAVDYYFLDETVE----FSCEKCGGN 468
Cdd:COG5533   220 NkslvaktffgqdksrlqCEACNYTSTTIAMFSTLLVPP------YEVVQLGLQECIDRFYEEEKLEgkdaWRCPKCGRK 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 469 ESTLKQ-KFRSLPRVLIVKLKRYgrtadDTFRIGKLKdkigVTLSLAVASHCTARTTLPPTSPEMDGNVEEKetkksekk 547
Cdd:COG5533   294 ESSRKRmEILVLPDVLIIHISRF-----HISVMGRKK----IDTPQGWKNTASVEVNVTLLFNNGIGYIPRK-------- 356
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1050361400 548 kpskknkfqpYELKSIVNHSGeSAEYGHYFSDVYdrRTKTWLAYDDADINEIdedvllpSRAYTG-----YLFFY 617
Cdd:COG5533   357 ----------YSLLGVVCHNG-TLNGGHYFSEVK--RSGTWNVYDDSQVRKG-------SRTTSGshpssYILFY 411
Ig_HHLA2 cd16091
Immunoglobulin (Ig) domain in HERV-H LTR-associating 2; HERV-H LTR-associating 2 (HHLA2) is a ...
47-124 1.93e-03

Immunoglobulin (Ig) domain in HERV-H LTR-associating 2; HERV-H LTR-associating 2 (HHLA2) is a protein ligand found on the surface of monocytes which is believed to regulate cell-mediated immunity by binding to a receptor on T lymphocytes and inhibiting the proliferation of these cells. Alternate splicing results in multiple transcript variants. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 319340  Cd Length: 91  Bit Score: 37.69  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400  47 IISCYFTPrssirNDKVSLEWEKEKggEYIPLIQFVDNKvKKVSLQDNRF----QVFKNLVHRGNCSLIISSTKLIDSGN 122
Cdd:cd16091     2 ILPCSFTP-----GGEEVIHWYKLN--SDIPVHSYYYNK-DQLEHQDQRYrgrtSLFKDQISKGNASLLLKNVKVQDEGR 73

                  ..
gi 1050361400 123 YQ 124
Cdd:cd16091    74 YK 75
TMEM132D_C pfam15706
Mature oligodendrocyte transmembrane protein, TMEM132D, C-term; TMEM132D_C is the C-terminal ...
211-237 5.34e-03

Mature oligodendrocyte transmembrane protein, TMEM132D, C-term; TMEM132D_C is the C-terminal family of chordate proteins implicated in panic disorder. TMEM132D is a single-pass transmembrane protein that is highly expressed in the cortical regions of the human and mouse brain. The function is still unknown. It may act as a cell-surface marker for oligodendrocyte differentiation. Additionally, as it may be most strongly expressed in neurons and it colocalizes with actin filaments TMEM132D may be implicated in neuronal sprouting and connectivity in brain regions important for anxiety-related behaviour.


Pssm-ID: 318007  Cd Length: 84  Bit Score: 36.15  E-value: 5.34e-03
                          10        20
                  ....*....|....*....|....*..
gi 1050361400 211 ICSVAVLTFVIACVVYCYRTRSKQKAP 237
Cdd:pfam15706  40 VFCLAILVFLINCVVFALKYRRKKSPV 66
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
280-617 1.07e-38

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 334078 [Multi-domain]  Cd Length: 305  Bit Score: 144.45  E-value: 1.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLLSVQPFvSDLLQQKIPYKTF----QEFVFIRNLYNLIRRKDRYSlKKRRKLLLKLKDSVSIS 355
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQCLFSIPPF-RDYLLRISPLSEDsrynKDINLLCALADLFKALQSEK-KSSSVSPKEFKKTLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 356 AERFADNEQHDAHDFLTECFSLMKEDiaqLSNEMKNPISCPVKSNFEFDLEYIYICNKCGETRISVNQNNCLFVDIlqed 435
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHED---LNGKHSTENESLITDLFRGQLKSRLKCLNCGKESYTFEPFLDLSLPI---- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 436 snSDSASETLQDAVDYYFLDETVEFS----CEKCGGNESTLKQ-KFRSLPRVLIVKLKRYgrtADDTFRIGKLKDKIGVT 510
Cdd:pfam00443 153 --PSLKNYDLQDCLKAFTKEEILKGEnmyyCPKCKGKCGAIKKlKISRLPPVLIIHLKRF---SYNRSTWEKLNTEVEFP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 511 LSLAVASHCTARTTLPPTSPemdgnveeketkksekkkpskknkfQPYELKSIVNHSGeSAEYGHYFSDVYDRRTKTWLA 590
Cdd:pfam00443 228 EELDLSEYLAEGLDEKEVEP-------------------------TKYRLVAVVVHSG-SLSSGHYIAYIKKYENGRWYK 281
                         330       340
                  ....*....|....*....|....*..
gi 1050361400 591 YDDADINEIDEDVLLPSRAytgYLFFY 617
Cdd:pfam00443 282 FDDEKVTEVDEEEVLNKSA---YILFY 305
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
280-618 5.47e-35

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: 132.61  E-value: 5.47e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLLSvqpfvsdllqqkipyktfqefvfirnlynlirrkdryslkkrrklllklkdsvsisaerf 359
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 360 adnEQHDAHDFLTECFSLMKEDIAQLSNEMK--NPISCPVKSNFEFDLEYIYICNKCGETRISVNQNNCLFVDIlqedSN 437
Cdd:cd02257    21 ---EQQDAHEFLLFLLDKLHEELKKSSKRTSdsSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPL----PV 93
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 438 SDSASETLQDAVDYYFLDETVE----FSCEKCGGNESTLKQKFRSLPRVLIVKLKRYgrTADDTFRIGKLKDKIGVTLSL 513
Cdd:cd02257    94 KGLPQVSLEDCLEKFFKEEILEgdncYKCEKKKKQEATKRLKIKKLPPVLIIHLKRF--SFNEDGTKEKLNTKVSFPLEL 171
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 514 AVASHCTARTTLPPTSPEMDgnveeketkksekkkpskknkfqPYELKSIVNHSGESAEYGHYFSDVYDRRTKTWLAYDD 593
Cdd:cd02257   172 DLSPYLSEGEKDSDSDNGSY-----------------------KYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFND 228
                         330       340
                  ....*....|....*....|....*..
gi 1050361400 594 ADINEIDED--VLLPSRAYTGYLFFYI 618
Cdd:cd02257   229 DKVTEVSEEevLEFGSLSSSAYILFYE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
279-618 2.19e-25

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: 107.07  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 279 QGFPNLGNTCYMNATLQSLLSVQPFVSDLLQQKIPY----------------KTFQEFVFI--RNLYNLIRrkdryslkk 340
Cdd:cd02660     1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCtclscspnsclscamdEIFQEFYYSgdRSPYGPIN--------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 341 rrklllkLKDSVSISAERFADNEQHDAHDFLTECFSLMKEDIAQLSNEM--KNPISCPVKSNFEFDLEYIYICNKCGETR 418
Cdd:cd02660    72 -------LLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEAndESHCNCIIHQTFSGSLQSSVTCQRCGGVS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 419 ISVNQnnclFVDI---LQEDSNSDSASE--------TLQDAVDYYFLDETVE---FSCEKCGGNESTLKQ-KFRSLPRVL 483
Cdd:cd02660   145 TTVDP----FLDLsldIPNKSTPSWALGesgvsgtpTLSDCLDRFTRPEKLGdfaYKCSGCGSTQEATKQlSIKKLPPVL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 484 IVKLKRYGRTADDTFRigKLKDKIGVTLSLAVASHCTARTTLPPTSPEMDGNVEeketkksekkkpskknkfqpYELKSI 563
Cdd:cd02660   221 CFQLKRFEHSLNKTSR--KIDTYVQFPLELNMTPYTSSSIGDTQDSNSLDPDYT--------------------YDLFAV 278
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1050361400 564 VNHSGeSAEYGHYFSDVYDRRtKTWLAYDDADINEIDEDVLLPSRAytgYLFFYI 618
Cdd:cd02660   279 VVHKG-TLDTGHYTAYCRQGD-GQWFKFDDAMITRVSEEEVLKSQA---YLLFYH 328
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-617 1.74e-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: 89.30  E-value: 1.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLLSVQPFVSDLLQQKIPYktFQEFVFIRNLYNLIRRK-------DRYSLKKRRKLLLKLK-DS 351
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKF--PSDVVDPANDLNCQLIKladgllsGRYSKPASLKSENDPYqVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 352 VSISA---------ERFADNEQHDAHDFLTECFSLMKEDIAQlsNEMKNPIScpvksNFEFDLEYIYICNKCGETRISVN 422
Cdd:cd02658    79 IKPSMfkaligkghPEFSTMRQQDALEFLLHLIDKLDRESFK--NLGLNPND-----LFKFMIEDRLECLSCKKVKYTSE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 423 QNNCLFVDILQEDSNSDSASE------TLQDAVDYYFLDETVEFSCEKCGG-NESTLKQKFRSLPRVLIVKLKRYgrtad 495
Cdd:cd02658   152 LSEILSLPVPKDEATEKEEGElvyepvPLEDCLKAYFAPETIEDFCSTCKEkTTATKTTGFKTFPDYLVINMKRF----- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 496 dTFRIGKLKDKIGVTLSLavashctarttlpptsPEMDGNVeeketkksekkkpskknkfqPYELKSIVNHSGESAEYGH 575
Cdd:cd02658   227 -QLLENWVPKKLDVPIDV----------------PEELGPG--------------------KYELIAFISHKGTSVHSGH 269
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1050361400 576 YFsdVYDRR----TKTWLAYDdadineiDEDVLL----PSRAYTGYLFFY 617
Cdd:cd02658   270 YV--AHIKKeidgEGKWVLFN-------DEKVVAsqdpPEMKKLGYIYFY 310
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
278-618 2.80e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 88.49  E-value: 2.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 278 PQGFPNLGNTCYMNATLQSLLSVQPFVSDLL-QQKIPYKTFQEFVFIRNLYNLIRRKdrYSLKKRRKLLLKLKDSVSISA 356
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLsREHSKDCCNEGFCMMCALEAHVERA--LASSGPGSAPRIFSSNLKQIS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 357 ERFADNEQHDAHDFLTecFSLMKEDIAQLSNEMKNPISCPVksnfefDLEYIYICNKCGETRISvnQNNCL--------- 427
Cdd:cd02661    79 KHFRIGRQEDAHEFLR--YLLDAMQKACLDRFKKLKAVDPS------SQETTLVQQIFGGYLRS--QVKCLnckhvsnty 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 428 --FVDILQEDSNSDSASETLQDAVDYYFLDETVEFSCEKCGGNESTLKQ-KFRSLPRVLIVKLKRYGrtaddTFRIGKLK 504
Cdd:cd02661   149 dpFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQlTIHRAPNVLTIHLKRFS-----NFRGGKIN 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 505 DKIGVTLSLAVASHCTARTTLPPtspemdgnveeketkksekkkpskknkfqPYELKSIVNHSGESAEYGHYFSDVYDRR 584
Cdd:cd02661   224 KQISFPETLDLSPYMSQPNDGPL-----------------------------KYKLYAVLVHSGFSPHSGHYYCYVKSSN 274
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1050361400 585 tKTWLAYDDADINEIDEDVLLPSRAytgYLFFYI 618
Cdd:cd02661   275 -GKWYNMDDSKVSPVSIETVLSQKA---YILFYI 304
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; ...
274-617 5.99e-18

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


Pssm-ID: 227820 [Multi-domain]  Cd Length: 415  Bit Score: 86.23  E-value: 5.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 274 ENPKPQGFPNLGNTCYMNATLQSLLSVQPFVSDLLQQKipYKTFQEFVFIRN------------LYNLIRRKDRYSlkkr 341
Cdd:COG5533    67 DNLPPNGLRNKGNTCYMNCALQCLLSIGDLNTMLQGRF--YLQNINTDFPRGkpgsnafkqfiaLYETPGCHGPKS---- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 342 rKLLLKLKDSVSISAERFADNEQHDAHDFLTECFSLMKED---------IAQLSNE---MKNPISCPVKSNFEFDLEYIY 409
Cdd:COG5533   141 -ISPRNFIDILSGRNKLFSGDMQQDSQEFLIFFLDLLHEDlngnksrspILELKDEfeeVREELPLSHFSHHEWNLHLRS 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 410 I-----------------CNKCGETRISVNQNNCLFVDIlqedsnSDSASETLQDAVDYYFLDETVE----FSCEKCGGN 468
Cdd:COG5533   220 NkslvaktffgqdksrlqCEACNYTSTTIAMFSTLLVPP------YEVVQLGLQECIDRFYEEEKLEgkdaWRCPKCGRK 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 469 ESTLKQ-KFRSLPRVLIVKLKRYgrtadDTFRIGKLKdkigVTLSLAVASHCTARTTLPPTSPEMDGNVEEKetkksekk 547
Cdd:COG5533   294 ESSRKRmEILVLPDVLIIHISRF-----HISVMGRKK----IDTPQGWKNTASVEVNVTLLFNNGIGYIPRK-------- 356
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1050361400 548 kpskknkfqpYELKSIVNHSGeSAEYGHYFSDVYdrRTKTWLAYDDADINEIdedvllpSRAYTG-----YLFFY 617
Cdd:COG5533   357 ----------YSLLGVVCHNG-TLNGGHYFSEVK--RSGTWNVYDDSQVRKG-------SRTTSGshpssYILFY 411
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-600 1.28e-17

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: 84.01  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLLSVQPF---------VSDLLQQKIPYKTFQEFVFIRNLYNLIRRKDRYSlkkrrklLLKLKD 350
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFrkavyecnsTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFG-------NRSVVD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 351 SVS-ISAERFADNEQHDAHDFLTECFSLMKEDIAQLSNEMKNPIscpVKSNFEFDLEYIYICNKCGETRISVNQnnclFV 429
Cdd:cd02668    74 PSGfVKALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNI---VQDLFRGEYSYVTQCSKCGRESSLPSK----FY 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 430 DI-LQEdsnsdSASETLQDAVDYYFLDETVE----FSCEKCGGNES-TLKQKFRSLPRVLIVKLKRYGRTADDTFRiGKL 503
Cdd:cd02668   147 ELeLQL-----KGHKTLEECIDEFLKEEQLTgdnqYFCESCNSKTDaTRRIRLTTLPPTLNFQLLRFVFDRKTGAK-KKL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 504 KDKIGVTLSLAVASHCtarttlpptSPEMDGNVEeketkksekkkpskknkfqpYELKSIVNHSGESAEYGHYFSDVYDR 583
Cdd:cd02668   221 NASISFPEILDMGEYL---------AESDEGSYV--------------------YELSGVLIHQGVSAYSGHYIAHIKDE 271
                         330
                  ....*....|....*..
gi 1050361400 584 RTKTWLAYDDADINEID 600
Cdd:cd02668   272 QTGEWYKFNDEDVEEMP 288
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-602 2.62e-17

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: 83.46  E-value: 2.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLLSVQPFVSDLLQQKIPYK--------TFQEFVFIrNLYNLIRRKDRYSLKKRRKLLLKLKDS 351
Cdd:cd02659     4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDdddnksvpLALQRLFL-FLQLSESPVKTTELTDKTRSFGWDSLN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 352 VsisaerfadNEQHDAHDFLTECFSlmkediaQLSNEMKN-PISCPVKSNFEFDLEYIYICNKCGetRISVNQNNclFVD 430
Cdd:cd02659    83 T---------FEQHDVQEFFRVLFD-------KLEEKLKGtGQEGLIKNLFGGKLVNYIICKECP--HESEREEY--FLD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 431 ILQEDSNSDSASETLQDAVDYYFLDETVEFSCEKCGGNESTLKQ-KFRSLPRVLIVKLKRYgrTAD-DTFRIGKLKDKIG 508
Cdd:cd02659   143 LQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGvCFKKLPPVLTLQLKRF--EFDfETMMRIKINDRFE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 509 VTLSLAVASHCTARTTLPPTSPEMDGNVEEKetkksekkkpskknkfqpYELKSIVNHSGeSAEYGHYFSDVYDRRTKTW 588
Cdd:cd02659   221 FPLELDMEPYTEKGLAKKEGDSEKKDSESYI------------------YELHGVLVHSG-DAHGGHYYSYIKDRDDGKW 281
                         330
                  ....*....|....
gi 1050361400 589 LAYDDADINEIDED 602
Cdd:cd02659   282 YKFNDDVVTPFDPN 295
UBP14 COG5207
Uncharacterized Zn-finger protein, UBP-type [General function prediction only];
280-507 1.64e-16

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


Pssm-ID: 227532 [Multi-domain]  Cd Length: 749  Bit Score: 83.19  E-value: 1.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLLSVQPFVS--DLLQQKIP--YKTFQEFVFIRNLYNLIRRKDRYSLKKRRKLLLKL-KDSVSI 354
Cdd:COG5207   305 GLINLGNSCYLSSVIQSLVGYAVSKEefDLLQHFEIcyMKNPLECLFCQLMKLLSKMKETPDNEYVNGISPLDfKMLIGQ 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 355 SAERFADNEQHDAHDFLTECFSLMKEDIAQLSnemknpiSCPVKSNFEFDLEYIYICNKCGETRISVNQnnclfVDILQE 434
Cdd:COG5207   385 DHPEFGKFAQQDAHEFLLFLLEKIRKGERSYL-------IPPITSLFEFEVERRLSCSGCMDVSYSYES-----MLMICI 452
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1050361400 435 DSNSDSASETLQDAVDYYFLDETVEFSCEKCGGN-ESTLKQKFRSLPRVLIVKLKRYGRtadDTFRIGKLKDKI 507
Cdd:COG5207   453 FLEGNDEPQDIRKSVEAFFLPDTIEWSCENCKGKkKASRKPFIKSLPKYLILQVGRYSL---QNYKVEKLSDPI 523
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
283-618 3.04e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 78.10  E-value: 3.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 283 NLGNTCYMNATLQSLLsvqpfvsdllqqkipyktfqefvfirnlynlirrkdryslkkrrklllklkdsvsisaerfadN 362
Cdd:cd02674     4 NLGNTCYMNSILQCLS---------------------------------------------------------------A 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 363 EQHDAHDFLTECFSLMKEDIAQLsnemknpiscpvksnFEFDLEYIYICNKCGETRISVNQNNCLFVDIlqeDSNSDSAS 442
Cdd:cd02674    21 DQQDAQEFLLFLLDGLHSIIVDL---------------FQGQLKSRLTCLTCGKTSTTFEPFTYLSLPI---PSGSGDAP 82
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 443 E-TLQDAVDYYF----LDETVEFSCEKCGGNESTLKQ-KFRSLPRVLIVKLKRYGRTADDTfriGKLKDKIGVTLSLAVa 516
Cdd:cd02674    83 KvTLEDCLRLFTkeetLDGDNAWKCPKCKKKRKATKKlTISRLPKVLIIHLKRFSFSRGST---RKLTTPVTFPLNDLD- 158
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 517 shctARTTLPPTSPEMDGNveeketkksekkkpskknkfqpYELKSIVNHSGeSAEYGHYFSDVYDRRTKTWLAYDDADI 596
Cdd:cd02674   159 ----LTPYVDTRSFTGPFK----------------------YDLYAVVNHYG-SLNGGHYTAYCKNNETNDWYKFDDSRV 211
                         330       340
                  ....*....|....*....|..
gi 1050361400 597 NEIDEDVLLPSRAytgYLFFYI 618
Cdd:cd02674   212 TKVSESSVVSSSA---YILFYE 230
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-617 9.00e-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: 77.81  E-value: 9.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQsLLSVQPFVSDLLQQKiPyktfqefvfiRNLYNLIRRKdryslkkrrklllklkdsvsisAERF 359
Cdd:cd02667     1 GLSNLGNTCFFNAVMQ-NLSQTPALRELLSET-P----------KELFSQVCRK----------------------APQF 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 360 ADNEQHDAHDFLTecfslmkediaQLSNEMKNPIscpvKSNFEFDLEYIYICNKCGETRISVNQNNCLFVDILQEDSNSD 439
Cdd:cd02667    47 KGYQQQDSHELLR-----------YLLDGLRTFI----DSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIKSEC 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 440 SASETLQDAVDYYFLDETVEFSCEKCggNESTLKQKFRSLPRVLIVKLKRYGRTADDTFRigKLKDKIGVTLSLAVASHC 519
Cdd:cd02667   112 SIESCLKQFTEVEILEGNNKFACENC--TKAKKQYLISKLPPVLVIHLKRFQQPRSANLR--KVSRHVSFPEILDLAPFC 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 520 TARTtlppTSPEMDGNVEeketkksekkkpskknkfqpYELKSIVNHSGeSAEYGHYFSDVYDR--------RTKT---- 587
Cdd:cd02667   188 DPKC----NSSEDKSSVL--------------------YRLYGVVEHSG-TMRSGHYVAYVKVRppqqrlsdLTKSkpaa 242
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1050361400 588 ---------WLAYDDADINEIDEDVLLPSRAytgYLFFY 617
Cdd:cd02667   243 deagpgsgqWYYISDSDVREVSLEEVLKSEA---YLLFY 278
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-578 2.73e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 77.15  E-value: 2.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLLSVQPFVSDLLQQKIPYKT-----------FQEFVFIRNLYNLIRRKDRYSlkkrrklllkl 348
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGdsqsvmkklqlLQAHLMHTQRRAEAPPDYFLE----------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 349 kdsvSISAERFADNEQHDAHDFLteCFSLmkEDIAQLSNEMknpiscpvksnFEFDLEYIYICNKCGetriSVNQNNCLF 428
Cdd:cd02664    70 ----ASRPPWFTPGSQQDCSEYL--RYLL--DRLHTLIEKM-----------FGGKLSTTIRCLNCN----STSARTERF 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 429 VDIlqedsnsDSASETLQDAVDYYF----LDETVEFSCEKCGGNESTLKQ-KFRSLPRVLIVKLKRYGRTADDTFRiGKL 503
Cdd:cd02664   127 RDL-------DLSFPSVQDLLNYFLspekLTGDNQYYCEKCASLQDAEKEmKVTGAPEYLILTLLRFSYDQKTHVR-EKI 198
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1050361400 504 KDK--IGVTLSLAVASHcTARTTLPPTSPEMDGNVEEKETKKSEkkkpskknkfqPYELKSIVNHSGESAEYGHYFS 578
Cdd:cd02664   199 MDNvsINEVLSLPVRVE-SKSSESPLEKKEEESGDDGELVTRQV-----------HYRLYAVVVHSGYSSESGHYFT 263
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
283-617 1.51e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 73.33  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 283 NLGNTCYMNATLQSLLSVQPFVSDllqqkipyktfqefvfirnlynlirrkdryslkkrrklllklkdsvsisaerFADN 362
Cdd:cd02673     4 NTGNSCYFNSTMQALSSIGKINTE----------------------------------------------------FDND 31
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 363 EQHDAHDFLTECFSLMkEDIAQLSNEMKNPISCPVKS-----NFEFDLEYIYICNKCGETRISVNQNNCLFVDIlqedsn 437
Cdd:cd02673    32 DQQDAHEFLLTLLEAI-DDIMQVNRTNVPPSNIEIKRlnpleAFKYTIESSYVCIGCSFEENVSDVGNFLDVSM------ 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 438 SDSASETLQDAVDYYFLDETVEFSCEKCGGNESTLKQKFRSLPRVLIVKLKRYgrtaddTFRIGKLKDKIGVTLSLAVAS 517
Cdd:cd02673   105 IDNKLDIDELLISNFKTWSPIEKDCSSCKCESAISSERIMTFPECLSINLKRY------KLRIATSDYLKKNEEIMKKYC 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 518 HCTARttlpptspemdgnveeketkksekkkpskknkfqpYELKSIVNHSGESAEYGHYFSdvYDR---RTKTWLAYDDA 594
Cdd:cd02673   179 GTDAK-----------------------------------YSLVAVICHLGESPYDGHYIA--YTKelyNGSSWLYCSDD 221
                         330       340
                  ....*....|....*....|...
gi 1050361400 595 DINEIDEDVLLPSRAYTGYLFFY 617
Cdd:cd02673   222 EIRPVSKNDVSTNARSSGYLIFY 244
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-617 7.36e-13

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 69.92  E-value: 7.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLLSVQPFVSDL--LQQKIPYKTFQEFVFIRNlynlirrKDRYSLKKRRKLLLKLKDSVSISAE 357
Cdd:cd02671    26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLkhLVSLISSVEQLQSSFLLN-------PEKYNDELANQAPRRLLNALREVNP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 358 RFADNEQHDAHDFLtECfslmkediaqlsneMKNPISCPVKSNFEFDLEYIYICNKCGetriSVNQNNCLFVDI---LQE 434
Cdd:cd02671    99 MYEGYLQHDAQEVL-QC--------------ILGNIQELVEKDFQGQLVLRTRCLECE----TFTERREDFQDIsvpVQE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 435 D--SNSDSASE----------TLQDAVDYYFLDETV----EFSCEKCGG-NESTLKQKFRSLPRVLIVKLKRYGRTADDT 497
Cdd:cd02671   160 SelSKSEESSEispdpktemkTLKWAISQFASVERIvgedKYFCENCHHyTEAERSLLFDKLPEVITIHLKCFAANGSEF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 498 FRIG---KLKDKIGVTLSLAVASHCTArttlpPTSPEmdgnveeketkksekkkpskknkfqpYELKSIVNHSGESAEYG 574
Cdd:cd02671   240 DCYGglsKVNTPLLTPLKLSLEEWSTK-----PKNDV--------------------------YRLFAVVMHSGATISSG 288
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1050361400 575 HYFSDVydrrtkTWLAYDDADI---NEID-EDVLLPSRAYTG--YLFFY 617
Cdd:cd02671   289 HYTAYV------RWLLFDDSEVkvtEEKDfLEALSPNTSSTStpYLLFY 331
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-617 7.64e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 69.26  E-value: 7.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLLSVQPFVS--DLLQQKIPYKTFQEFVFIRNLYNLIRRKdryslkkrrklllklkdsvsisAE 357
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYFENLLTClkDLFESISEQKKRTGVISPKKFITRLKRE----------------------NE 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 358 RFADNEQHDAHDFL-------TECF----SLMKEDIAQLSNEMKNPISCPVKSNFEFDLEYIYICNKCgETRISVNQNNC 426
Cdd:cd02663    59 LFDNYMHQDAHEFLnfllneiAEILdaerKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTC-ETVSSRDETFL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 427 -LFVDILQEDS-----NSDSASETLQdavdyyfldETVEFSCEKCGG-NESTLKQKFRSLPRVLIVKLKRYGRTaDDTFR 499
Cdd:cd02663   138 dLSIDVEQNTSitsclRQFSATETLC---------GRNKFYCDECCSlQEAEKRMKIKKLPKILALHLKRFKYD-EQLNR 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 500 IGKLKDKIGVTLSLAVAShctarTTLPPTSPEmdgnveeketkksekkkpskknkfQPYELKSIVNHSGESAEYGHYFSD 579
Cdd:cd02663   208 YIKLFYRVVFPLELRLFN-----TTDDAENPD------------------------RLYELVAVVVHIGGGPNHGHYVSI 258
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1050361400 580 VydRRTKTWLAYDDADINEIDE----DVLLPSRA-YTGYLFFY 617
Cdd:cd02663   259 V--KSHGGWLLFDDETVEKIDEnaveEFFGDSPNqATAYVLFY 299
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-617 1.24e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 67.78  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLLSVQPFVSDLlqqkipyktfQEFVfirnlynlirrkdryslkkrrklllklkdsvsisaerf 359
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEYL----------EEFL-------------------------------------- 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 360 adnEQHDAHDFltecFSLMkedIAQLSNEMKNPiscpvksnFEFDLEYIYICNKCGE-TRISVNQNNCLFVDILQEDSNS 438
Cdd:cd02662    33 ---EQQDAHEL----FQVL---LETLEQLLKFP--------FDGLLASRIVCLQCGEsSKVRYESFTMLSLPVPNQSSGS 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 439 dsaSETLQDAVDYYFLDETVE-FSCEKCggnestlKQKFRSLPRVLIVKLKRYGRTADDTFRigklKDKIGVTLslavas 517
Cdd:cd02662    95 ---GTTLEHCLDDFLSTEIIDdYKCDRC-------QTVIVRLPQILCIHLSRSVFDGRGTST----KNSCKVSF------ 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 518 hctarttlpptsPEMDGNVEeketkksekkkpskknkfqpYELKSIVNHSGeSAEYGHY--------------------F 577
Cdd:cd02662   155 ------------PERLPKVL--------------------YRLRAVVVHYG-SHSSGHYvcyrrkplfskdkepgsfvrM 201
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1050361400 578 SDVYDRRTKTWLAYDDADINEIDE-DVLLPSRAytgYLFFY 617
Cdd:cd02662   202 REGPSSTSHPWWRISDTTVKEVSEsEVLEQKSA---YMLFY 239
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-602 4.95e-10

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 60.81  E-value: 4.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLLSVqPFVSDLLQQKIPYKT------FQEFVFIRNLYNLIRRKdryslkKRRKLLLKLKDSVS 353
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSV-PELRDALKNYNPARRganqssDNLTNALRDLFDTMDKK------QEPVPPIEFLQLLR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 354 ISAERFADNE------QHDAHdfltECFSLMkedIAQLSNEMKNPISCP--VKSNFEFDLEYIYICNKCG-ETRISVNQN 424
Cdd:cd02657    74 MAFPQFAEKQnqggyaQQDAE----ECWSQL---LSVLSQKLPGAGSKGsfIDQLFGIELETKMKCTESPdEEEVSTESE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 425 NclfvdILQEDSNSDSASETLQDAVDYYfLDETVEFSCEKCGGNES-TLKQKFRSLPRVLIVKLKR--YGRtadDTFRIG 501
Cdd:cd02657   147 Y-----KLQCHISITTEVNYLQDGLKKG-LEEEIEKHSPTLGRDAIyTKTSRISRLPKYLTVQFVRffWKR---DIQKKA 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 502 KLKDKIGVTLSLAVASHCTarttlpptspeMDGNveeketkksekkkpskknkfqpYELKSIVNHSGESAEYGHYFSDVY 581
Cdd:cd02657   218 KILRKVKFPFELDLYELCT-----------PSGY----------------------YELVAVITHQGRSADSGHYVAWVR 264
                         330       340
                  ....*....|....*....|.
gi 1050361400 582 DRRTKTWLAYDDADINEIDED 602
Cdd:cd02657   265 RKNDGKWIKFDDDKVSEVTEE 285
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
280-593 3.36e-08

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 315986 [Multi-domain]  Cd Length: 295  Bit Score: 55.11  E-value: 3.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 280 GFPNLGNTCYMNATLQSLlsvqpFVSDLLQQKIPYKTFQ----------EFVFIRNLYNLIRRKDRYSLKKRRKLLLKLK 349
Cdd:pfam13423   2 GLENHLDNSYLNALLQLY-----FFIPDLFEAILGHSFDecppencllcELGFLFDMLDKSNGQNCQATNFLRTFSTIPE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 350 DSVSI------SAERFADNEQHdaHDFLTECFSLMKEDiaqLSNEMKNPIScpvkSNFEFDLEYIYICNKCGETRISVNQ 423
Cdd:pfam13423  77 AAALGlqqdiqEANRFILEQLS--LPLLTLKPSIENRR---DSSEAESQLS----ELFGTGLINSIRCISCNNESVKEES 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 424 NncLFVDILQEDSNSdsaSETLQDAVDYYFLDET-VEFSCEKCGGNESTL-KQKFRSLPRVLIVKLKRYGRTadDTFRIG 501
Cdd:pfam13423 148 T--LTVELPYPPSEK---GQNFSNILKSSIRREKiVTIWCSSCNKYQPVLiRKTFVSLPPILGICLKRYSEK--DNFWAV 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 502 KLKDKIGVTLSLAVASHCTAR-TTLPPTSPEMDgnveeketkksekkkpskknkfqpYELKSIVNHSGESAEYGHYFS-- 578
Cdd:pfam13423 221 RLNLFVDIPLEINMPHFIQDDeQNERPLSGLFK------------------------YELQGVVCHIGDSLTSGHLVSfi 276
                         330
                  ....*....|....*.
gi 1050361400 579 DVYDRRTKT-WLAYDD 593
Cdd:pfam13423 277 RVAPSSENSqWYLFND 292
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
280-601 9.35e-07

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 51.79  E-value: 9.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400  280 GFPNLGNTCYMNATLQSLLSVQPFVSDLLQqkIPYKTFQEfvfiRNLYNLIRRKDRYSLKKRRKLLLKLKDSVSISAERF 359
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYG--IPTDHPRG----RDSVALALQRLFYNLQTGEEPVDTTELTRSFGWDSD 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400  360 ADNEQHDAHDFLTECF-SL---MKEDIAQ--LSNE----MKNPISCpVKSNFEfdleyiyicnkcgETRISVnqnnclFV 429
Cdd:COG5077    269 DSFMQHDIQEFNRVLQdNLeksMRGTVVEnaLNGIfvgkMKSYIKC-VNVNYE-------------SARVED------FW 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400  430 DILQEDSNSDSASETLQDAVDYYFLDETVEFSCEKCGGNESTLKQKFRSLPRVLIVKLKRYgrtaDDTFRIG---KLKDK 506
Cdd:COG5077    329 DIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRF----EYDFERDmmvKINDR 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400  507 IGVTLSLAVashctarttLPPTSPEMDGNVEEKETkksekkkpskknkfqpYELKSIVNHSGESAEyGHYFSDVYDRRTK 586
Cdd:COG5077    405 YEFPLEIDL---------LPFLDRDADKSENSDAV----------------YVLYGVLVHSGDLHE-GHYYALLKPEKDG 458
                          330
                   ....*....|....*
gi 1050361400  587 TWLAYDDADINEIDE 601
Cdd:COG5077    459 RWYKFDDTRVTRATE 473
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
557-618 5.15e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 47.94  E-value: 5.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1050361400 557 PYELKSIVNHSGEsAEYGHYFSDVYDRRTKTWLAYDD-----ADINEIDEDVLLPSRAYTGYLFFYI 618
Cdd:cd02665   163 PYELHAVLVHEGQ-ANAGHYWAYIYKQSRQEWEKYNDisvteSSWEEVERDSFGGGRNPSAYCLMYI 228
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
444-621 5.39e-06

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 49.50  E-value: 5.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 444 TLQDAVDYYF----LDETVEFSCEKCGGNESTLKQ-KFRSLPRVLIVKLKRYgrTADDTFRigklkDKIGVTLSLAVASH 518
Cdd:COG5560   676 TLQDCLNEFSkpeqLGLSDSWYCPGCKEFRQASKQmELWRLPMILIIHLKRF--SSVRSFR-----DKIDDLVEYPIDDL 748
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 519 CTARTTLPPTSPEMDgnveeketkksekkkpskknkfqpYELKSIVNHSGESAEyGHYFSDVYDRRTKTWLAYDDADINE 598
Cdd:COG5560   749 DLSGVEYMVDDPRLI------------------------YDLYAVDNHYGGLSG-GHYTAYARNFANNGWYLFDDSRITE 803
                         170       180
                  ....*....|....*....|...
gi 1050361400 599 IDEDVLLPSRAytgYLFFYIHKS 621
Cdd:COG5560   804 VDPEDSVTSSA---YVLFYRRKS 823
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
425-617 1.05e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 40.97  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 425 NCLFVDILqEDSNSDSASETLQDAVDYYFldetvefscekcggNESTLKQkfrsLPRVLIVKLKRYGRTADDTFrigKLK 504
Cdd:cd02670    63 NERLLQIP-VPDDDDGGGITLEQCLEQYF--------------NNSVFAK----APSCLIICLKRYGKTEGKAQ---KMF 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400 505 DKIGVTLSLAVASHctarttLPPTSPEMDGNVEEKETKKSEKKKPSKKNKFQpYELKSIVNHSGESAEYGHYFSDV---- 580
Cdd:cd02670   121 KKILIPDEIDIPDF------VADDPRACSKCQLECRVCYDDKDFSPTCGKFK-LSLCSAVCHRGTSLETGHYVAFVrygs 193
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1050361400 581 -------YDRRTKTWLAYDD-ADINEIDEDVLLPSRAYT--GYLFFY 617
Cdd:cd02670   194 ysltetdNEAYNAQWVFFDDmADRDGVSNGFNIPAARLLedPYMLFY 240
Ig_HHLA2 cd16091
Immunoglobulin (Ig) domain in HERV-H LTR-associating 2; HERV-H LTR-associating 2 (HHLA2) is a ...
47-124 1.93e-03

Immunoglobulin (Ig) domain in HERV-H LTR-associating 2; HERV-H LTR-associating 2 (HHLA2) is a protein ligand found on the surface of monocytes which is believed to regulate cell-mediated immunity by binding to a receptor on T lymphocytes and inhibiting the proliferation of these cells. Alternate splicing results in multiple transcript variants. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 319340  Cd Length: 91  Bit Score: 37.69  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400  47 IISCYFTPrssirNDKVSLEWEKEKggEYIPLIQFVDNKvKKVSLQDNRF----QVFKNLVHRGNCSLIISSTKLIDSGN 122
Cdd:cd16091     2 ILPCSFTP-----GGEEVIHWYKLN--SDIPVHSYYYNK-DQLEHQDQRYrgrtSLFKDQISKGNASLLLKNVKVQDEGR 73

                  ..
gi 1050361400 123 YQ 124
Cdd:cd16091    74 YK 75
Ig_Siglec_N cd05712
Immunoglobulin (Ig) domain at the N terminus of Siglec (sialic acid-binding Ig-like lectins); ...
47-133 4.26e-03

Immunoglobulin (Ig) domain at the N terminus of Siglec (sialic acid-binding Ig-like lectins); Ig_Siglec_N: immunoglobulin (Ig) domain at the N terminus of Siglec (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, organized as an extracellular module composed of Ig-like domains (an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains), followed by transmembrane and short cytoplasmic domains. Human siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11.


Pssm-ID: 143189  Cd Length: 119  Bit Score: 37.40  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050361400  47 IISCYFT-PRSSIRNDKVSLEWEKekGGEYIPLIQFV----DNKVKKVSLQDnRFQVFKNLVHrGNCSLIISSTKLIDSG 121
Cdd:cd05712    18 LIPCSFSyPADWPVSNGVHGIWYK--GHPYPKNRPPVatnnRSRLVHESTRG-RFRLLGDLGK-KNCSLLISDAQPEDSG 93
                          90
                  ....*....|..
gi 1050361400 122 NYQLRLTVGGKL 133
Cdd:cd05712    94 KYFFRVELGDSN 105
TMEM132D_C pfam15706
Mature oligodendrocyte transmembrane protein, TMEM132D, C-term; TMEM132D_C is the C-terminal ...
211-237 5.34e-03

Mature oligodendrocyte transmembrane protein, TMEM132D, C-term; TMEM132D_C is the C-terminal family of chordate proteins implicated in panic disorder. TMEM132D is a single-pass transmembrane protein that is highly expressed in the cortical regions of the human and mouse brain. The function is still unknown. It may act as a cell-surface marker for oligodendrocyte differentiation. Additionally, as it may be most strongly expressed in neurons and it colocalizes with actin filaments TMEM132D may be implicated in neuronal sprouting and connectivity in brain regions important for anxiety-related behaviour.


Pssm-ID: 318007  Cd Length: 84  Bit Score: 36.15  E-value: 5.34e-03
                          10        20
                  ....*....|....*....|....*..
gi 1050361400 211 ICSVAVLTFVIACVVYCYRTRSKQKAP 237
Cdd:pfam15706  40 VFCLAILVFLINCVVFALKYRRKKSPV 66
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
278-302 7.64e-03

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 38.63  E-value: 7.64e-03
                          10        20
                  ....*....|....*....|....*
gi 1050361400 278 PQGFPNLGNTCYMNATLQSLLSVQP 302
Cdd:cd02666     1 PAGLDNIGNTCYLNSLLQYFFTIKP 25
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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