|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
437-742 |
3.74e-162 |
|
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: 476.00 E-value: 3.74e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 437 PRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRIL-SHMRSINCQ 515
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 516 IGDGSQEDAHEFLRLLVASMPSICLERLGGETKVDPRLQETTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEIYG 595
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 596 WvEFFQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMT 675
Cdd:cd02661 161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11993475 676 RTGDVPPLYMLYAVIVHLDTLNasFSGHYISYVKDLRGNWYRIDDSEIHPVPMTQVMSEGAYMLFYM 742
Cdd:cd02661 240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
438-741 |
5.88e-72 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 240.04 E-value: 5.88e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 438 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWC--LMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 513
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDlfKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 514 CQIGDGSQEDAHEFLRLLvasmpsicLERLGGETKVDPRLQETTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEI 593
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFL--------LDGLHEDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 594 YG-----WVEFFQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYG--KINKCISFPE 666
Cdd:pfam00443 153 PGdsaelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTweKLNTEVEFPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 667 MLDMIPFMTRTGDVP----PLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHPVPM-TQVMSEGAYMLF 740
Cdd:pfam00443 233 ELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGSLS---SGHYIAYIKAYENNrWYKFDDEKVTEVDEeTAVLSSSAYILF 309
|
.
gi 11993475 741 Y 741
Cdd:pfam00443 310 Y 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
439-743 |
5.42e-28 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 121.90 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPL--VAYLLRRSHSRscsGKDWCLMCeLEQHVMMLRESGGPLSASRIlshMRSINCQI 516
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFrkDVYGIPTDHPR---GRDSVALA-LQRLFYNLQTGEEPVDTTEL---TRSFGWDS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 517 GDG-SQEDAHEFLRLLVASmpsicLERLGGETKVDPRLQEttlvqhMFGGRLHSKVKCLRCDHESERYENIMDLTLEIYG 595
Cdd:COG5077 268 DDSfMQHDIQEFNRVLQDN-----LEKSMRGTVVENALNG------IFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 596 wVEFFQDALIQFTRPEDLDGENMYRCSRcAGYVRARKELSIHEAPNILTIVLKRFQ----EGRYGKINKCISFPEMLDMI 671
Cdd:COG5077 337 -MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEydfeRDMMVKINDRYEFPLEIDLL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 672 PFMTRTGD----VPPLYMLYAVIVHLDTLNasfSGHYISYVK-DLRGNWYRIDDSEIHPVPMTQVMSE------------ 734
Cdd:COG5077 415 PFLDRDADksenSDAVYVLYGVLVHSGDLH---EGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdki 491
|
330
....*....|....*....
gi 11993475 735 ----------GAYMLFYMR 743
Cdd:COG5077 492 rdhsgikrfmSAYMLVYLR 510
|
|
| zf-MYND |
pfam01753 |
MYND finger; |
130-167 |
8.17e-11 |
|
MYND finger;
Pssm-ID: 460312 Cd Length: 39 Bit Score: 57.43 E-value: 8.17e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 11993475 130 CARCFGPAKT--RCSRCKSVRYCSGKCQIIHWRVaHKDEC 167
Cdd:pfam01753 1 CAVCGKEALKllRCSRCKSVYYCSKECQKADWPY-HKKEC 39
|
|
| zf-HIT_ZNHIT1_like |
cd21437 |
HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar ... |
128-158 |
1.55e-03 |
|
HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar proteins; The family includes ZNHIT1 and its yeast counterpart, the vacuolar protein sorting-associated protein 71 (Vps71p). ZNHIT1, also known as cyclin-G1-binding protein 1 (CGBP1), zinc finger protein subfamily 4A member 1 (ZNFN4A1), or p18 Hamlet, may have a role in inducing apoptosis through p53 signaling. It binds to Rev-erb beta and releases its inhibitory effect on the transcription of apolipoprotein C3 (APOC3) without affecting its DNA-binding activity. The yeast counterpart Vps71p, also referred to as SWR complex protein 6 (Swc6p), plays a role in the exchange of histone H2A for the H2A variant HZT1, a euchromatin-specific factor, leading to chromatin remodeling and transcriptional changes of targeted genes. It is indirectly involved in vacuolar protein sorting. Members of this family contain a zf-HIT domain characterized by a "treble-clef" fold through interleaved CCCC and CCHC zinc finger motifs, both of which bind a zinc ion.
Pssm-ID: 467791 Cd Length: 43 Bit Score: 37.21 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|.
gi 11993475 128 HVCARCFGPAKTRCSRCkSVRYCSGKCQIIH 158
Cdd:cd21437 8 KFCSVCGYWGKYTCVRC-GARYCSLKCLETH 37
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
437-742 |
3.74e-162 |
|
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: 476.00 E-value: 3.74e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 437 PRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRIL-SHMRSINCQ 515
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 516 IGDGSQEDAHEFLRLLVASMPSICLERLGGETKVDPRLQETTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEIYG 595
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 596 WvEFFQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMT 675
Cdd:cd02661 161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11993475 676 RTGDVPPLYMLYAVIVHLDTLNasFSGHYISYVKDLRGNWYRIDDSEIHPVPMTQVMSEGAYMLFYM 742
Cdd:cd02661 240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
438-741 |
5.88e-72 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 240.04 E-value: 5.88e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 438 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWC--LMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 513
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDlfKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 514 CQIGDGSQEDAHEFLRLLvasmpsicLERLGGETKVDPRLQETTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEI 593
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFL--------LDGLHEDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 594 YG-----WVEFFQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYG--KINKCISFPE 666
Cdd:pfam00443 153 PGdsaelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTweKLNTEVEFPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 667 MLDMIPFMTRTGDVP----PLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHPVPM-TQVMSEGAYMLF 740
Cdd:pfam00443 233 ELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGSLS---SGHYIAYIKAYENNrWYKFDDEKVTEVDEeTAVLSSSAYILF 309
|
.
gi 11993475 741 Y 741
Cdd:pfam00443 310 Y 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
439-742 |
4.86e-63 |
|
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: 213.50 E-value: 4.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCtkplvayllrrshsrscsgkdwclmceleqhvmmlresggplsasrilshmrsincqigd 518
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 519 gSQEDAHEFLRLLVASMpsiCLERLGGETKVDPRLQETTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEI---YG 595
Cdd:cd02257 21 -EQQDAHEFLLFLLDKL---HEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkGL 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 596 WVEFFQDALIQFTRPEDLDGENMYRCSRCaGYVRARKELSIHEAPNILTIVLKRFQ---EGRYGKINKCISFPEMLDMIP 672
Cdd:cd02257 97 PQVSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 673 FMT------RTGDVPPLYMLYAVIVHLDTlnASFSGHYISYVKD-LRGNWYRIDDSEIHPVPMTQVMSEG-----AYMLF 740
Cdd:cd02257 176 YLSegekdsDSDNGSYKYELVAVVVHSGT--SADSGHYVAYVKDpSDGKWYKFNDDKVTEVSEEEVLEFGslsssAYILF 253
|
..
gi 11993475 741 YM 742
Cdd:cd02257 254 YE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
438-741 |
6.28e-61 |
|
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: 210.31 E-value: 6.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 438 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDW--CLMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 513
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPnsCLSCAMDEifQEFYYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 514 CQIGDGSQEDAHEFLRLLVASMPSICLERLGGETKVDPrlqeTTLVQHM-FGGRLHSKVKCLRCDHESERYENIMDLTLE 592
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESH----CNCIIHQtFSGSLQSSVTCQRCGGVSTTVDPFLDLSLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 593 IYGWVEFF--------------QDALIQFTRPEDLdGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQ---EGRY 655
Cdd:cd02660 157 IPNKSTPSwalgesgvsgtptlSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhslNKTS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 656 GKINKCISFPEMLDMIPFMT----RTGDVPPL-----YMLYAVIVHLDTLNasfSGHYISYVKDLRGNWYRIDDSEIHPV 726
Cdd:cd02660 236 RKIDTYVQFPLELNMTPYTSssigDTQDSNSLdpdytYDLFAVVVHKGTLD---TGHYTAYCRQGDGQWFKFDDAMITRV 312
|
330
....*....|....*
gi 11993475 727 PMTQVMSEGAYMLFY 741
Cdd:cd02660 313 SEEEVLKSQAYLLFY 327
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-746 |
3.64e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 191.70 E-value: 3.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLR---RSHSRSCSGKdwclMCELEQHVMMLRESGGPLSASRILSHMRSINCQ 515
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSV----PLALQRLFLFLQLSESPVKTTELTDKTRSFGWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 516 IGD-GSQEDAHEFLRLLVASMpsiclerlggETKVDPRLQETtLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEIY 594
Cdd:cd02659 80 SLNtFEQHDVQEFFRVLFDKL----------EEKLKGTGQEG-LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 595 GWVEFfQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGRYGKINKCISFPEMLDM 670
Cdd:cd02659 149 GKKNL-EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFefdfETMMRIKINDRFEFPLELDM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 671 IPFMTRTGDVPP-----------LYMLYAVIVHLDTLNasfSGHYISYVKDLR-GNWYRIDDSEIHPVPMTQVMSE---- 734
Cdd:cd02659 228 EPYTEKGLAKKEgdsekkdsesyIYELHGVLVHSGDAH---GGHYYSYIKDRDdGKWYKFNDDVVTPFDPNDAEEEcfgg 304
|
330 340 350
....*....|....*....|....*....|
gi 11993475 735 ------------------GAYMLFYMRSYP 746
Cdd:cd02659 305 eetqktydsgprafkrttNAYMLFYERKSP 334
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-741 |
2.80e-52 |
|
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: 182.49 E-value: 2.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLtctkplvayllrrshsrscsgkdwclmceleqhvmmlresggplsasrilSHMrsincqigd 518
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL--------------------------------------------------SAD--------- 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 519 gsQEDAHEFLRLLVASMPSIclerlggetkvdprlqettlVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEIYGWVE 598
Cdd:cd02674 22 --QQDAQEFLLFLLDGLHSI--------------------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSG 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 599 FF-----QDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF--QEGRYGKINKCISFP-EMLDM 670
Cdd:cd02674 80 DApkvtlEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFsfSRGSTRKLTTPVTFPlNDLDL 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11993475 671 IPFMTRTGDVPP-LYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHPVPMTQVMSEGAYMLFY 741
Cdd:cd02674 160 TPYVDTRSFTGPfKYDLYAVVNHYGSLN---GGHYTAYCKNNETNdWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-741 |
1.98e-51 |
|
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: 181.82 E-value: 1.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRShsrscsgkdwclmceleqhVMMLREsggplsasrilshMRSINCQIGD 518
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETP-------------------KELFSQ-------------VCRKAPQFKG 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 519 GSQEDAHEFLRLLVASMpsiclerlggetkvdprlqeTTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEIYGWVE 598
Cdd:cd02667 49 YQQQDSHELLRYLLDGL--------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 599 ---FFQDALIQFTRPEDLDGENMYRCSRCagyVRARKELSIHEAPNILTIVLKRFQEGRYG---KINKCISFPEMLDMIP 672
Cdd:cd02667 109 secSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSAnlrKVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 673 FMTRTGDVP-----PLYMLYAVIVHLDTLNasfSGHYISYVKD----------------------LRGNWYRIDDSEIHP 725
Cdd:cd02667 186 FCDPKCNSSedkssVLYRLYGVVEHSGTMR---SGHYVAYVKVrppqqrlsdltkskpaadeagpGSGQWYYISDSDVRE 262
|
330
....*....|....*.
gi 11993475 726 VPMTQVMSEGAYMLFY 741
Cdd:cd02667 263 VSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-741 |
4.94e-37 |
|
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: 141.29 E-value: 4.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSL------TCTKPLVayllrrsHSRSCSGKDWclmceleqhvmmlresgGPLSASRILSHMRSI 512
Cdd:cd02663 1 GLENFGNTCYCNSVLQALyfenllTCLKDLF-------ESISEQKKRT-----------------GVISPKKFITRLKRE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 513 NcQIGDGS-QEDAHEFLRLLVASmpsiCLERLGGETKVDPRLQ----------ETTLVQHMFGGRLHSKVKCLRCDHESE 581
Cdd:cd02663 57 N-ELFDNYmHQDAHEFLNFLLNE----IAEILDAERKAEKANRklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 582 RYENIMDLTLEIYGWVEFfQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGRYGK 657
Cdd:cd02663 132 RDETFLDLSIDVEQNTSI-TSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkydeQLNRYIK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 658 INKCISFPemLDMIPFMTRTGDVPP--LYMLYAVIVHLDtlNASFSGHYISYVKdLRGNWYRIDDSEIHPVPMTQVM--- 732
Cdd:cd02663 211 LFYRVVFP--LELRLFNTTDDAENPdrLYELVAVVVHIG--GGPNHGHYVSIVK-SHGGWLLFDDETVEKIDENAVEeff 285
|
330
....*....|....
gi 11993475 733 -----SEGAYMLFY 741
Cdd:cd02663 286 gdspnQATAYVLFY 299
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-741 |
1.08e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 141.09 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRScsGKDWCLMCELEQHVMML----RESGGP----LSASRILShmr 510
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL--GDSQSVMKKLQLLQAHLmhtqRRAEAPpdyfLEASRPPW--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 511 sincqIGDGSQEDAHEFLRLLvasmpsicLERLggetkvdprlqeTTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLT 590
Cdd:cd02664 76 -----FTPGSQQDCSEYLRYL--------LDRL------------HTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 591 LEiygwVEFFQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGR-YGK---------INK 660
Cdd:cd02664 131 LS----FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQkTHVrekimdnvsINE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 661 CISFP-----------EMLDMIPFMTRTG--DVPPLYMLYAVIVHLDTlnASFSGHYISYV------------------- 708
Cdd:cd02664 207 VLSLPvrveskssespLEKKEEESGDDGElvTRQVHYRLYAVVVHSGY--SSESGHYFTYArdqtdadstgqecpepkda 284
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 11993475 709 --KDLRGNWYRIDDSEIHPVPMTQVM-------SEGAYMLFY 741
Cdd:cd02664 285 eeNDESKNWYLFNDSRVTFSSFESVQnvtsrfpKDTPYILFY 326
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-741 |
6.19e-33 |
|
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: 130.23 E-value: 6.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLvayllRRShsrscsgkdwCLMCELEQHVMMLR-ESGGPLSASRILSHMRSINCQ-- 515
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEF-----RKA----------VYECNSTEDAELKNmPPDKPHEPQTIIDQLQLIFAQlq 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 516 -----------------IGDGSQEDAHEFLRLLVASMPSiCLERLGgetkvDPRLQetTLVQHMFGGRLHSKVKCLRCDH 578
Cdd:cd02668 66 fgnrsvvdpsgfvkalgLDTGQQQDAQEFSKLFLSLLEA-KLSKSK-----NPDLK--NIVQDLFRGEYSYVTQCSKCGR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 579 ESERYENIMDLTLEIYGwVEFFQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGR 654
Cdd:cd02668 138 ESSLPSKFYELELQLKG-HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFvfdrKTGA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 655 YGKINKCISFPEMLDMIPFMTRTGDVPPLYMLYAVIVHLDtlNASFSGHYISYVKD-LRGNWYRIDDSEIHPVPMTQVM- 732
Cdd:cd02668 217 KKKLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQG--VSAYSGHYIAHIKDeQTGEWYKFNDEDVEEMPGKPLKl 294
|
330 340
....*....|....*....|....*....
gi 11993475 733 --------------------SEGAYMLFY 741
Cdd:cd02668 295 gnsedpakprkseikkgthsSRTAYMLVY 323
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
439-743 |
5.42e-28 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 121.90 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPL--VAYLLRRSHSRscsGKDWCLMCeLEQHVMMLRESGGPLSASRIlshMRSINCQI 516
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFrkDVYGIPTDHPR---GRDSVALA-LQRLFYNLQTGEEPVDTTEL---TRSFGWDS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 517 GDG-SQEDAHEFLRLLVASmpsicLERLGGETKVDPRLQEttlvqhMFGGRLHSKVKCLRCDHESERYENIMDLTLEIYG 595
Cdd:COG5077 268 DDSfMQHDIQEFNRVLQDN-----LEKSMRGTVVENALNG------IFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 596 wVEFFQDALIQFTRPEDLDGENMYRCSRcAGYVRARKELSIHEAPNILTIVLKRFQ----EGRYGKINKCISFPEMLDMI 671
Cdd:COG5077 337 -MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEydfeRDMMVKINDRYEFPLEIDLL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 672 PFMTRTGD----VPPLYMLYAVIVHLDTLNasfSGHYISYVK-DLRGNWYRIDDSEIHPVPMTQVMSE------------ 734
Cdd:COG5077 415 PFLDRDADksenSDAVYVLYGVLVHSGDLH---EGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdki 491
|
330
....*....|....*....
gi 11993475 735 ----------GAYMLFYMR 743
Cdd:COG5077 492 rdhsgikrfmSAYMLVYLR 510
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-741 |
1.19e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 111.91 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLtCTKPLVAYLLRRSHSRSCSGKDWCLMCEL--EQHVMMLRESggplSASRILSHMRSINCQI 516
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVL-YFCPGFKHGLKHLVSLISSVEQLQSSFLLnpEKYNDELANQ----APRRLLNALREVNPMY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 517 GDGSQEDAHEFLRLLVASmpsiclerlggetkvdprLQEttLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTL----- 591
Cdd:cd02671 101 EGYLQHDAQEVLQCILGN------------------IQE--LVEKDFQGQLVLRTRCLECETFTERREDFQDISVpvqes 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 592 ---------EIYGWVEF----FQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQE------ 652
Cdd:cd02671 161 elskseessEISPDPKTemktLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAAngsefd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 653 --GRYGKINKCISFPemLDMIPFMTRTGDVPPLYMLYAVIVHLD-TLNasfSGHYISYVKdlrgnWYRIDDSEIHpvPMT 729
Cdd:cd02671 241 cyGGLSKVNTPLLTP--LKLSLEEWSTKPKNDVYRLFAVVMHSGaTIS---SGHYTAYVR-----WLLFDDSEVK--VTE 308
|
330 340
....*....|....*....|...
gi 11993475 730 QVMSEGA-----------YMLFY 741
Cdd:cd02671 309 EKDFLEAlspntsststpYLLFY 331
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-741 |
2.38e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 105.53 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRrshsrscsgkdwclmcELEQHvmmlresggplsasrilshmrsincqigd 518
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEE----------------FLEQQ----------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 519 gsqeDAHEFLRLLVAsmpsiCLERlggetkvdprlqettLVQHMFGGRLHSKVKCLRCDHESE-RYENIMDLTL----EI 593
Cdd:cd02662 36 ----DAHELFQVLLE-----TLEQ---------------LLKFPFDGLLASRIVCLQCGESSKvRYESFTMLSLpvpnQS 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 594 YGWVEFFQDALIQFTRPEDLDGenmYRCSRCAgyvrarkeLSIHEAPNILTIVLKRFQEGRYGKI--NKC-ISFPEMLDm 670
Cdd:cd02662 92 SGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVFDGRGTStkNSCkVSFPERLP- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 671 ipfmtrtgdvPPLYMLYAVIVHLDTLNasfSGHYISY---------------------VKDLRGNWYRIDDSEIHPVPMT 729
Cdd:cd02662 160 ----------KVLYRLRAVVVHYGSHS---SGHYVCYrrkplfskdkepgsfvrmregPSSTSHPWWRISDTTVKEVSES 226
|
330
....*....|...
gi 11993475 730 QVMSEG-AYMLFY 741
Cdd:cd02662 227 EVLEQKsAYMLFY 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
601-743 |
8.89e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 94.95 E-value: 8.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 601 QDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYG--KINKCISFP-EMLDMIPFMTRT 677
Cdd:COG5560 678 QDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFrdKIDDLVEYPiDDLDLSGVEYMV 757
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11993475 678 GDVPPLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHPVPMTQVMSEGAYMLFYMR 743
Cdd:COG5560 758 DDPRLIYDLYAVDNHYGGLS---GGHYTAYARNFANNgWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-741 |
2.90e-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: 89.69 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKD--WCLMCELEQ--HVMM----LRESGGPLSASRILSHMR 510
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQLIKlaDGLLsgrySKPASLKSENDPYQVGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 511 SI---NCqIGDGSQE-------DAHEFLRLLvasmpsicLERLGGETKVDPRLQETTLVQHMFGGRLhskvKCLRCDH-- 578
Cdd:cd02658 81 PSmfkAL-IGKGHPEfstmrqqDALEFLLHL--------IDKLDRESFKNLGLNPNDLFKFMIEDRL----ECLSCKKvk 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 579 ESERYENIMDLTLE------------IYGWVEfFQDALIQFTRPEDLDgenmYRCSRCAGYVRARKELSIHEAPNILTIV 646
Cdd:cd02658 148 YTSELSEILSLPVPkdeatekeegelVYEPVP-LEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVIN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 647 LKRFQEGRYG---KINKCISFPEMLDmipfmtrtgdvPPLYMLYAVIVHLDTlnASFSGHYISYVK---DLRGNWYRIDD 720
Cdd:cd02658 223 MKRFQLLENWvpkKLDVPIDVPEELG-----------PGKYELIAFISHKGT--SVHSGHYVAHIKkeiDGEGKWVLFND 289
|
330 340
....*....|....*....|.
gi 11993475 721 SEIHPVPMTQVMSEGAYMLFY 741
Cdd:cd02658 290 EKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-741 |
1.06e-18 |
|
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: 87.77 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLR--RSHSRSCSGKDWcLMCELEQHVMMLRESGGPLSASRILSHMRSINCQI 516
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNynPARRGANQSSDN-LTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 517 ------GDGSQEDAHEFLRLLVaSMPSICLERLGGETKVdprlqettlVQHMFGGRLHSKVKCLRCDHESE---RYENIM 587
Cdd:cd02657 80 aekqnqGGYAQQDAEECWSQLL-SVLSQKLPGAGSKGSF---------IDQLFGIELETKMKCTESPDEEEvstESEYKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 588 DLTLEIYGWVEFFQDALIQftRPEDLDGENMYRCSRCAGYVRARKelsIHEAPNILTIVLKRF----QEGRYGKINKCIS 663
Cdd:cd02657 150 QCHISITTEVNYLQDGLKK--GLEEEIEKHSPTLGRDAIYTKTSR---ISRLPKYLTVQFVRFfwkrDIQKKAKILRKVK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 664 FPEMLDMIPFMTRTGdvppLYMLYAVIVHlDTLNASfSGHYISYVK-DLRGNWYRIDDSEIHPVPMTQV--MSEG----- 735
Cdd:cd02657 225 FPFELDLYELCTPSG----YYELVAVITH-QGRSAD-SGHYVAWVRrKNDGKWIKFDDDKVSEVTEEDIlkLSGGgdwhi 298
|
....*.
gi 11993475 736 AYMLFY 741
Cdd:cd02657 299 AYILLY 304
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
439-743 |
6.03e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 82.16 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDwclMCELEQHVMMLRESGGPLSASRILSH--MRSINCQi 516
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVLKN---VIRKPEPDLNQEEALKLFTALWSSKEhkVGWIPPM- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 517 gdGSQEDAHEFLRLLvasmpsiclerlggetkvdprLQETTLVQHMFGGRLHSKVKClrcDHESERYENIMDLTLE--IY 594
Cdd:COG5533 77 --GSQEDAHELLGKL---------------------LDELKLDLVNSFTIRIFKTTK---DKKKTSTGDWFDIIIElpDQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 595 GWVEF---FQDALIQFTRPEDLD-----GENMYRCSRCagyvRARKELSIHEAPNILTIVLKRF-QEGRYGKINKCISfp 665
Cdd:COG5533 131 TWVNNlktLQEFIDNMEELVDDEtgvkaKENEELEVQA----KQEYEVSFVKLPKILTIQLKRFaNLGGNQKIDTEVD-- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 666 EMLDMIPFMTRTGDVPP--LYMLYAVIVHLDTLNasfSGHYISYVKdLRGNWYRIDDSEIHPVPMTQ---VMSEGAYMLF 740
Cdd:COG5533 205 EKFELPVKHDQILNIVKetYYDLVGFVLHQGSLE---GGHYIAYVK-KGGKWEKANDSDVTPVSEEEainEKAKNAYLYF 280
|
...
gi 11993475 741 YMR 743
Cdd:COG5533 281 YER 283
|
|
| zf-MYND |
pfam01753 |
MYND finger; |
130-167 |
8.17e-11 |
|
MYND finger;
Pssm-ID: 460312 Cd Length: 39 Bit Score: 57.43 E-value: 8.17e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 11993475 130 CARCFGPAKT--RCSRCKSVRYCSGKCQIIHWRVaHKDEC 167
Cdd:pfam01753 1 CAVCGKEALKllRCSRCKSVYYCSKECQKADWPY-HKKEC 39
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
440-741 |
1.96e-08 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 56.00 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 440 LVNCGNSCYANAVLQSLtctkplvayllrrshsrSCSGKdwclmceleqhvmmlresggplsasrilshmrsINCQIGDG 519
Cdd:cd02673 2 LVNTGNSCYFNSTMQAL-----------------SSIGK---------------------------------INTEFDND 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 520 SQEDAHEFLRLLVASMPSIcLERLGGETKVDPRLQETTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEI----YG 595
Cdd:cd02673 32 DQQDAHEFLLTLLEAIDDI-MQVNRTNVPPSNIEIKRLNPLEAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMidnkLD 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 596 WVEFFQDALIQFTRPEDldgenmyRCSRCAGYVRARKElSIHEAPNILTIVLKRFQE----GRYGKINKCIsfpemldMI 671
Cdd:cd02673 111 IDELLISNFKTWSPIEK-------DCSSCKCESAISSE-RIMTFPECLSINLKRYKLriatSDYLKKNEEI-------MK 175
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11993475 672 PFMTRtgdvPPLYMLYAVIVHL-DTLNAsfsGHYISYVKDLRGN--WYRIDDSEIHPVPMTQVMSE---GAYMLFY 741
Cdd:cd02673 176 KYCGT----DAKYSLVAVICHLgESPYD---GHYIAYTKELYNGssWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
439-593 |
2.58e-04 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 44.87 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCS--------GKDWCLMCELEQHVMMLRESGgpLSASRILSHMR 510
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINeenplgmhGSVASAYADLIKQLYDGNLHA--FTPSGFKKTIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 511 SINCQIGDGSQEDAHEFLRLLVASM---------------PSIC------LERLGGETKVDPRLQETTLVQHMFGGRLHS 569
Cdd:COG5560 345 SFNEEFSGYDQQDSQEFIAFLLDGLhedlnriikkpytskPDLSpgddvvVKKKAKECWWEHLKRNDSIITDLFQGMYKS 424
|
170 180
....*....|....*....|....
gi 11993475 570 KVKCLRCDHESERYENIMDLTLEI 593
Cdd:COG5560 425 TLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| zf-HIT_ZNHIT1_like |
cd21437 |
HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar ... |
128-158 |
1.55e-03 |
|
HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar proteins; The family includes ZNHIT1 and its yeast counterpart, the vacuolar protein sorting-associated protein 71 (Vps71p). ZNHIT1, also known as cyclin-G1-binding protein 1 (CGBP1), zinc finger protein subfamily 4A member 1 (ZNFN4A1), or p18 Hamlet, may have a role in inducing apoptosis through p53 signaling. It binds to Rev-erb beta and releases its inhibitory effect on the transcription of apolipoprotein C3 (APOC3) without affecting its DNA-binding activity. The yeast counterpart Vps71p, also referred to as SWR complex protein 6 (Swc6p), plays a role in the exchange of histone H2A for the H2A variant HZT1, a euchromatin-specific factor, leading to chromatin remodeling and transcriptional changes of targeted genes. It is indirectly involved in vacuolar protein sorting. Members of this family contain a zf-HIT domain characterized by a "treble-clef" fold through interleaved CCCC and CCHC zinc finger motifs, both of which bind a zinc ion.
Pssm-ID: 467791 Cd Length: 43 Bit Score: 37.21 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|.
gi 11993475 128 HVCARCFGPAKTRCSRCkSVRYCSGKCQIIH 158
Cdd:cd21437 8 KFCSVCGYWGKYTCVRC-GARYCSLKCLETH 37
|
|
|