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Conserved domains on  [gi|1215375879|gb|OXB47777|]
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hypothetical protein B1J92_I06600g [Nakaseomyces glabratus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
374-811 1.19e-45

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 166.08  E-value: 1.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 374 RGIINNANICFMSSVLQVLLYCAPFVDILNVVSTRNMNAKSGSSSAkLLDACLTIYKKFDKAnyekekekesekekpgsk 453
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKN------------------ 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 454 kssppayaSITEAVNPDEFYRSLSTIpkFKDLRWGHQEDAEEFLTHLLDQLHEELISaiDSLSENEilnllqsihdedlk 533
Cdd:pfam00443  62 --------SKSSSVSPKMFKKSLGKL--NPDFSGYKQQDAQEFLLFLLDGLHEDLNG--NHSTENE-------------- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 534 iyiirnlsrykdaefiknmspqlkdqinkygtisddseegngwhevsgsskkgkktktaakrtvefipSPISNLFGGQFR 613
Cdd:pfam00443 116 --------------------------------------------------------------------SLITDLFRGQLK 127
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 614 SVLDIPQNKEsQSITLDPFQTIQLDISDPGVDSLEAAL---------KKFSEYELLPFKSSSGNDVEAKKQTFIDKLPQI 684
Cdd:pfam00443 128 SRLKCLSCGE-VSETFEPFSDLSLPIPGDSAELKTASLqicflqfskLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPV 206
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 685 LLIQLKRFSFisnadkdNGMTNynaysgriEKIRKKISYGHTLEIpDETLASSALRN-NSSKTYELSGVIYHHGmSPDGG 763
Cdd:pfam00443 207 LIIHLKRFSY-------NRSTW--------EKLNTEVEFPLELDL-SRYLAEELKPKtNNLQDYRLVAVVVHSG-SLSSG 269
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1215375879 764 HYTADVFHKQTKTWYRIDDVNITKLEDDDVLKggednmdSRTAYILMY 811
Cdd:pfam00443 270 HYIAYIKAYENNRWYKFDDEKVTEVDEETAVL-------SSSAYILFY 310
PspC_subgroup_1 super family cl41462
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
149-334 7.13e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


The actual alignment was detected with superfamily member NF033838:

Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 43.08  E-value: 7.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 149 SKIKEETTSFPMFfnTNEKDFAEAKAKRYHLSLKALDHEEQPIQKEPQVQSE-----------QVKQEEQIQKKQDFQQl 217
Cdd:NF033838  288 SSVGEETLPSPSL--KPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKtleleiaesdvKVKEAELELVKEEAKE- 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 218 SIEEEDIKDLKSgdKTDIVLPETTtNKENIQqgTEIKVSSPEMGNKQASGSPVEETATPYITPAPTP---KPAAKSWSAI 294
Cdd:NF033838  365 PRNEEKIKQAKA--KVESKKAEAT-RLEKIK--TDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPqpeKPAPKPEKPA 439
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1215375879 295 ASSAISKGKPSNVSSPISRPGS------THQQPQKKSKKYVPATPK 334
Cdd:NF033838  440 EQPKAEKPADQQAEEDYARRSEeeynrlTQQQPPKTEKPAQPSTPK 485
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
374-811 1.19e-45

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 166.08  E-value: 1.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 374 RGIINNANICFMSSVLQVLLYCAPFVDILNVVSTRNMNAKSGSSSAkLLDACLTIYKKFDKAnyekekekesekekpgsk 453
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKN------------------ 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 454 kssppayaSITEAVNPDEFYRSLSTIpkFKDLRWGHQEDAEEFLTHLLDQLHEELISaiDSLSENEilnllqsihdedlk 533
Cdd:pfam00443  62 --------SKSSSVSPKMFKKSLGKL--NPDFSGYKQQDAQEFLLFLLDGLHEDLNG--NHSTENE-------------- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 534 iyiirnlsrykdaefiknmspqlkdqinkygtisddseegngwhevsgsskkgkktktaakrtvefipSPISNLFGGQFR 613
Cdd:pfam00443 116 --------------------------------------------------------------------SLITDLFRGQLK 127
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 614 SVLDIPQNKEsQSITLDPFQTIQLDISDPGVDSLEAAL---------KKFSEYELLPFKSSSGNDVEAKKQTFIDKLPQI 684
Cdd:pfam00443 128 SRLKCLSCGE-VSETFEPFSDLSLPIPGDSAELKTASLqicflqfskLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPV 206
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 685 LLIQLKRFSFisnadkdNGMTNynaysgriEKIRKKISYGHTLEIpDETLASSALRN-NSSKTYELSGVIYHHGmSPDGG 763
Cdd:pfam00443 207 LIIHLKRFSY-------NRSTW--------EKLNTEVEFPLELDL-SRYLAEELKPKtNNLQDYRLVAVVVHSG-SLSSG 269
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1215375879 764 HYTADVFHKQTKTWYRIDDVNITKLEDDDVLKggednmdSRTAYILMY 811
Cdd:pfam00443 270 HYIAYIKAYENNRWYKFDDEKVTEVDEETAVL-------SSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
489-812 1.64e-40

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: 149.56  E-value: 1.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 489 HQEDAEEFLTHLLDQLHEELISAIDSLSENEILnllqsihdedlkiyiirnlsrykdaefiknmspqlkdqinkygtisd 568
Cdd:cd02257    21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL----------------------------------------------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 569 dseegngwhevsgsskkgkktktaakrtvefiPSPISNLFGGQFRSVL-DIPQNKESQSITLDPFQTIQLDISDPGVDSL 647
Cdd:cd02257    54 --------------------------------KSLIHDLFGGKLESTIvCLECGHESVSTEPELFLSLPLPVKGLPQVSL 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 648 EAALKKFSEYELL----PFKSSSGNDVEAKKQTFIDKLPQILLIQLKRFSFisnadkdngmtnynAYSGRIEKIRKKISY 723
Cdd:cd02257   102 EDCLEKFFKEEILegdnCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSF--------------NEDGTKEKLNTKVSF 167
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 724 GHTLEIPDETLASSALR--NNSSKTYELSGVIYHHGMSPDGGHYTADVFHKQTKTWYRIDDVNITKLEDDDVLKGGEdnm 801
Cdd:cd02257   168 PLELDLSPYLSEGEKDSdsDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGS--- 244
                         330
                  ....*....|.
gi 1215375879 802 DSRTAYILMYQ 812
Cdd:cd02257   245 LSSSAYILFYE 255
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
678-811 1.84e-12

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 68.68  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 678 IDKLPQILLIQLKRFsfisnadkdngmtnynAYSGRIEKIRKKIsyGHTLEIPDETLASSALRNNSskTYELSGVIYHHG 757
Cdd:COG5533   176 FVKLPKILTIQLKRF----------------ANLGGNQKIDTEV--DEKFELPVKHDQILNIVKET--YYDLVGFVLHQG 235
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1215375879 758 mSPDGGHYTADVfhKQTKTWYRIDDVNITKLEDDDvlkggEDNMDSRTAYILMY 811
Cdd:COG5533   236 -SLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEE-----AINEKAKNAYLYFY 281
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
149-334 7.13e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 43.08  E-value: 7.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 149 SKIKEETTSFPMFfnTNEKDFAEAKAKRYHLSLKALDHEEQPIQKEPQVQSE-----------QVKQEEQIQKKQDFQQl 217
Cdd:NF033838  288 SSVGEETLPSPSL--KPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKtleleiaesdvKVKEAELELVKEEAKE- 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 218 SIEEEDIKDLKSgdKTDIVLPETTtNKENIQqgTEIKVSSPEMGNKQASGSPVEETATPYITPAPTP---KPAAKSWSAI 294
Cdd:NF033838  365 PRNEEKIKQAKA--KVESKKAEAT-RLEKIK--TDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPqpeKPAPKPEKPA 439
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1215375879 295 ASSAISKGKPSNVSSPISRPGS------THQQPQKKSKKYVPATPK 334
Cdd:NF033838  440 EQPKAEKPADQQAEEDYARRSEeeynrlTQQQPPKTEKPAQPSTPK 485
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
374-811 1.19e-45

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 166.08  E-value: 1.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 374 RGIINNANICFMSSVLQVLLYCAPFVDILNVVSTRNMNAKSGSSSAkLLDACLTIYKKFDKAnyekekekesekekpgsk 453
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKN------------------ 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 454 kssppayaSITEAVNPDEFYRSLSTIpkFKDLRWGHQEDAEEFLTHLLDQLHEELISaiDSLSENEilnllqsihdedlk 533
Cdd:pfam00443  62 --------SKSSSVSPKMFKKSLGKL--NPDFSGYKQQDAQEFLLFLLDGLHEDLNG--NHSTENE-------------- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 534 iyiirnlsrykdaefiknmspqlkdqinkygtisddseegngwhevsgsskkgkktktaakrtvefipSPISNLFGGQFR 613
Cdd:pfam00443 116 --------------------------------------------------------------------SLITDLFRGQLK 127
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 614 SVLDIPQNKEsQSITLDPFQTIQLDISDPGVDSLEAAL---------KKFSEYELLPFKSSSGNDVEAKKQTFIDKLPQI 684
Cdd:pfam00443 128 SRLKCLSCGE-VSETFEPFSDLSLPIPGDSAELKTASLqicflqfskLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPV 206
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 685 LLIQLKRFSFisnadkdNGMTNynaysgriEKIRKKISYGHTLEIpDETLASSALRN-NSSKTYELSGVIYHHGmSPDGG 763
Cdd:pfam00443 207 LIIHLKRFSY-------NRSTW--------EKLNTEVEFPLELDL-SRYLAEELKPKtNNLQDYRLVAVVVHSG-SLSSG 269
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1215375879 764 HYTADVFHKQTKTWYRIDDVNITKLEDDDVLKggednmdSRTAYILMY 811
Cdd:pfam00443 270 HYIAYIKAYENNRWYKFDDEKVTEVDEETAVL-------SSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
489-812 1.64e-40

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: 149.56  E-value: 1.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 489 HQEDAEEFLTHLLDQLHEELISAIDSLSENEILnllqsihdedlkiyiirnlsrykdaefiknmspqlkdqinkygtisd 568
Cdd:cd02257    21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL----------------------------------------------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 569 dseegngwhevsgsskkgkktktaakrtvefiPSPISNLFGGQFRSVL-DIPQNKESQSITLDPFQTIQLDISDPGVDSL 647
Cdd:cd02257    54 --------------------------------KSLIHDLFGGKLESTIvCLECGHESVSTEPELFLSLPLPVKGLPQVSL 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 648 EAALKKFSEYELL----PFKSSSGNDVEAKKQTFIDKLPQILLIQLKRFSFisnadkdngmtnynAYSGRIEKIRKKISY 723
Cdd:cd02257   102 EDCLEKFFKEEILegdnCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSF--------------NEDGTKEKLNTKVSF 167
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 724 GHTLEIPDETLASSALR--NNSSKTYELSGVIYHHGMSPDGGHYTADVFHKQTKTWYRIDDVNITKLEDDDVLKGGEdnm 801
Cdd:cd02257   168 PLELDLSPYLSEGEKDSdsDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGS--- 244
                         330
                  ....*....|.
gi 1215375879 802 DSRTAYILMYQ 812
Cdd:cd02257   245 LSSSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
373-811 4.04e-34

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: 132.78  E-value: 4.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 373 PRGIINNANICFMSSVLQVLLYCAPFVDIlnvvstrnMNAKSGSSSAKLLDAC-LTIYKKFDKAnyekekekesekekpg 451
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANY--------LLSREHSKDCCNEGFCmMCALEAHVER---------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 452 skkssppAYASITEAVNPDEFYRSLSTIPKfkDLRWGHQEDAEEFLTHLLDQLHeelisaidslseneilnllqsihded 531
Cdd:cd02661    57 -------ALASSGPGSAPRIFSSNLKQISK--HFRIGRQEDAHEFLRYLLDAMQ-------------------------- 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 532 lKIYiirnLSRYKdaefiknmspqlkdqinKYGTISDDSEEgngwhevsgsskkgkktktaakrtvefiPSPISNLFGGQ 611
Cdd:cd02661   102 -KAC----LDRFK-----------------KLKAVDPSSQE----------------------------TTLVQQIFGGY 131
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 612 FRSvldipQNKESQ----SITLDPFQTIQLDIsdPGVDSLEAALKKFSEYELLP----FKSSSGND-VEAKKQTFIDKLP 682
Cdd:cd02661   132 LRS-----QVKCLNckhvSNTYDPFLDLSLDI--KGADSLEDALEQFTKPEQLDgenkYKCERCKKkVKASKQLTIHRAP 204
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 683 QILLIQLKRFSFIsnadkdngmtnynaysgRIEKIRKKISYGHTLEIPDetLASSAlrNNSSKTYELSGVIYHHGMSPDG 762
Cdd:cd02661   205 NVLTIHLKRFSNF-----------------RGGKINKQISFPETLDLSP--YMSQP--NDGPLKYKLYAVLVHSGFSPHS 263
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1215375879 763 GHYTADVfHKQTKTWYRIDDVNITKLEDDDVLkggednmdSRTAYILMY 811
Cdd:cd02661   264 GHYYCYV-KSSNGKWYNMDDSKVSPVSIETVL--------SQKAYILFY 303
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
598-812 2.28e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 128.17  E-value: 2.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 598 EFIPSPISNLFGGQFRSVLdIPQNKESQSITLDPFQTIQLDI----SDPGVDSLEAALKKFSEYELL-----PFKSSSGN 668
Cdd:cd02674    34 DGLHSIIVDLFQGQLKSRL-TCLTCGKTSTTFEPFTYLSLPIpsgsGDAPKVTLEDCLRLFTKEETLdgdnaWKCPKCKK 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 669 DVEAKKQTFIDKLPQILLIQLKRFSFisnadkDNGMTNynaysgrieKIRKKISYghTLEIPDETLASSALRNNSSKTYE 748
Cdd:cd02674   113 KRKATKKLTISRLPKVLIIHLKRFSF------SRGSTR---------KLTTPVTF--PLNDLDLTPYVDTRSFTGPFKYD 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215375879 749 LSGVIYHHGmSPDGGHYTADVFHKQTKTWYRIDDVNITKLEDDDVlkggednmDSRTAYILMYQ 812
Cdd:cd02674   176 LYAVVNHYG-SLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSV--------VSSSAYILFYE 230
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
375-811 7.14e-24

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: 102.79  E-value: 7.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 375 GIINNANICFMSSVLQVLLYCAPFVDILnvvstRNMNAKSGS---SSAKLLDACLTIYKKFDKAnyekekekesekekpg 451
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDAL-----KNYNPARRGanqSSDNLTNALRDLFDTMDKK---------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 452 skkssppayasiTEAVNPDEFYRSLSTI-PKF--KDLRWGH-QEDAEEFLTHLLDQLHEELISAIDSlseneilnllqsi 527
Cdd:cd02657    60 ------------QEPVPPIEFLQLLRMAfPQFaeKQNQGGYaQQDAEECWSQLLSVLSQKLPGAGSK------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 528 hdedlkiyiirnlsrykdaefiknmspqlkdqinkygtisddseegngwhevsgsskkgkktktaakrtvefiPSPISNL 607
Cdd:cd02657   115 -------------------------------------------------------------------------GSFIDQL 121
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 608 FGGQFRSVLDIPQNKESQSITLDPFQTIQLDIS-DPGVDSLEAALKKFSEYELLPFKSSSGNDVEAKKQTFIDKLPQILL 686
Cdd:cd02657   122 FGIELETKMKCTESPDEEEVSTESEYKLQCHISiTTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLT 201
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 687 IQLKRFSFisnadKDNgmTNYNAysgrieKIRKKISYGHTLEIPDeTLASSALrnnssktYELSGVIYHHGMSPDGGHYT 766
Cdd:cd02657   202 VQFVRFFW-----KRD--IQKKA------KILRKVKFPFELDLYE-LCTPSGY-------YELVAVITHQGRSADSGHYV 260
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1215375879 767 ADVFHKQTKTWYRIDDVNITKLEDDDVLK---GGEDNMdsrtAYILMY 811
Cdd:cd02657   261 AWVRRKNDGKWIKFDDDKVSEVTEEDILKlsgGGDWHI----AYILLY 304
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
374-811 8.57e-22

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: 97.44  E-value: 8.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 374 RGIINNANICFMSSVLQVLLYcAPFvdILNVVSTRNMNAKSGSSSAKLLDACLT--IYKKFdkanyekekekesekekpg 451
Cdd:cd02660     1 RGLINLGATCFMNVILQALLH-NPL--LRNYFLSDRHSCTCLSCSPNSCLSCAMdeIFQEF------------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 452 skkssppayaSITEAVNPDEFYRSLSTIpkfkdlrWGH--------QEDAEEFLTHLLDQLHEELisaidslseneilnl 523
Cdd:cd02660    59 ----------YYSGDRSPYGPINLLYLS-------WKHsrnlagysQQDAHEFFQFLLDQLHTHY--------------- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 524 lqsihdedlkiyiirnlsrykdaefiknmspqlKDQINKYGTISDdseegngwhevsgsskkgkktktaakrtvefIPSP 603
Cdd:cd02660   107 ---------------------------------GGDKNEANDESH-------------------------------CNCI 122
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 604 ISNLFGGQFRSVLdIPQNKESQSITLDPFQTIQLDISDPGVDS-------------LEAALKKF-SEYELLPFK---SSS 666
Cdd:cd02660   123 IHQTFSGSLQSSV-TCQRCGGVSTTVDPFLDLSLDIPNKSTPSwalgesgvsgtptLSDCLDRFtRPEKLGDFAykcSGC 201
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 667 GNDVEAKKQTFIDKLPQILLIQLKRFSFISNadkdngmtnynaysGRIEKIRKKISYGHTLEIPDETLASSALR-----N 741
Cdd:cd02660   202 GSTQEATKQLSIKKLPPVLCFQLKRFEHSLN--------------KTSRKIDTYVQFPLELNMTPYTSSSIGDTqdsnsL 267
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 742 NSSKTYELSGVIYHHGMSpDGGHYTADVFHkQTKTWYRIDDVNITKLEDDDVLKggednmdSRtAYILMY 811
Cdd:cd02660   268 DPDYTYDLFAVVVHKGTL-DTGHYTAYCRQ-GDGQWFKFDDAMITRVSEEEVLK-------SQ-AYLLFY 327
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
604-814 3.92e-20

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 92.32  E-value: 3.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 604 ISNLFGGQFRSVLdIPQNKESQSITLDPFQTIQLDISdpGVDSLEAALKKFSEYELLP-----FKSSSGNDVEAKKQTFI 678
Cdd:cd02659   113 IKNLFGGKLVNYI-ICKECPHESEREEYFLDLQVAVK--GKKNLEESLDAYVQGETLEgdnkyFCEKCGKKVDAEKGVCF 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 679 DKLPQILLIQLKRFsfisnadkdngmtNYNAYSGRIEKIRKKISYGHTLEI-P--DETLA----SSALRNNSSKTYELSG 751
Cdd:cd02659   190 KKLPPVLTLQLKRF-------------EFDFETMMRIKINDRFEFPLELDMePytEKGLAkkegDSEKKDSESYIYELHG 256
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215375879 752 VIYHHGmSPDGGHYTAdvFHKQTKT--WYRIDDVNITKLEDDDVLK---GGEDNMDSRT-----------AYILMYQNV 814
Cdd:cd02659   257 VLVHSG-DAHGGHYYS--YIKDRDDgkWYKFNDDVVTPFDPNDAEEecfGGEETQKTYDsgprafkrttnAYMLFYERK 332
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
604-811 4.24e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 89.40  E-value: 4.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 604 ISNLFGGQFRSVLDIPQNKESqSITLDPFQTIQLDISdpGVDSLEAALKKFSEYELLP-----FKSSSGNDVEAKKQTFI 678
Cdd:cd02668   118 VQDLFRGEYSYVTQCSKCGRE-SSLPSKFYELELQLK--GHKTLEECIDEFLKEEQLTgdnqyFCESCNSKTDATRRIRL 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 679 DKLPQILLIQLKRFSFISNadkdngmtnynaySGRIEKIRKKISYGHTLEIpDETLASSalrNNSSKTYELSGVIYHHGM 758
Cdd:cd02668   195 TTLPPTLNFQLLRFVFDRK-------------TGAKKKLNASISFPEILDM-GEYLAES---DEGSYVYELSGVLIHQGV 257
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215375879 759 SPDGGHYTADVFHKQTKTWYRIDDVNITKLEDDDVLKGGEDN-------------MDSRTAYILMY 811
Cdd:cd02668   258 SAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDpakprkseikkgtHSSRTAYMLVY 323
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
646-812 1.29e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 84.28  E-value: 1.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 646 SLEAALKKFSEYELLP-----FKSSSGNDVEAKKQTFIDKLPQILLIQLKRFSFisnadkdngMTNYNAYSgrieKIRKK 720
Cdd:cd02663   148 SITSCLRQFSATETLCgrnkfYCDECCSLQEAEKRMKIKKLPKILALHLKRFKY---------DEQLNRYI----KLFYR 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 721 ISYGHTLEIPDETLASsalrNNSSKTYELSGVIYHHGMSPDGGHYTADVfhKQTKTWYRIDDVNITKLEDDDVLKGGEDN 800
Cdd:cd02663   215 VVFPLELRLFNTTDDA----ENPDRLYELVAVVVHIGGGPNHGHYVSIV--KSHGGWLLFDDETVEKIDENAVEEFFGDS 288
                         170
                  ....*....|..
gi 1215375879 801 MDSRTAYILMYQ 812
Cdd:cd02663   289 PNQATAYVLFYQ 300
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
604-812 1.68e-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: 80.51  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 604 ISNLFGGQFRSVLdIPQNKESQSITLDPFQTIQLDISDP--GVDSLEAALKKFSEYELLPFKSSSGNDV--EAKKQTFID 679
Cdd:cd02667    69 IDSIFGGELTSTI-MCESCGTVSLVYEPFLDLSLPRSDEikSECSIESCLKQFTEVEILEGNNKFACENctKAKKQYLIS 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 680 KLPQILLIQLKRFSfisnadkdngmtnyNAYSGRIEKIRKKISYGHTLEI-PDETLASSALRNNSSKTYELSGVIYHHGM 758
Cdd:cd02667   148 KLPPVLVIHLKRFQ--------------QPRSANLRKVSRHVSFPEILDLaPFCDPKCNSSEDKSSVLYRLYGVVEHSGT 213
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215375879 759 SpDGGHYTADV-----------FHKQTKT----------WYRIDDVNITKLEDDDVLKGgednmdsrTAYILMYQ 812
Cdd:cd02667   214 M-RSGHYVAYVkvrppqqrlsdLTKSKPAadeagpgsgqWYYISDSDVREVSLEEVLKS--------EAYLLFYE 279
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
678-811 1.84e-12

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 68.68  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 678 IDKLPQILLIQLKRFsfisnadkdngmtnynAYSGRIEKIRKKIsyGHTLEIPDETLASSALRNNSskTYELSGVIYHHG 757
Cdd:COG5533   176 FVKLPKILTIQLKRF----------------ANLGGNQKIDTEV--DEKFELPVKHDQILNIVKET--YYDLVGFVLHQG 235
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1215375879 758 mSPDGGHYTADVfhKQTKTWYRIDDVNITKLEDDDvlkggEDNMDSRTAYILMY 811
Cdd:COG5533   236 -SLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEE-----AINEKAKNAYLYFY 281
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
604-811 1.02e-10

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 65.66  E-value: 1.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879  604 ISNLFGGQFRSVLD-IPQNKESQSItlDPFQTIQLDISdpGVDSLEAALKKFSEYELLpfkssSGND---------VEAK 673
Cdd:COG5077    300 LNGIFVGKMKSYIKcVNVNYESARV--EDFWDIQLNVK--GMKNLQESFRRYIQVETL-----DGDNrynaekhglQDAK 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879  674 KQTFIDKLPQILLIQLKRFsfisnadkdngmtNYNAYSGRIEKIRKKisyghtLEIPDET-----LASSALRN-NSSKTY 747
Cdd:COG5077    371 KGVIFESLPPVLHLQLKRF-------------EYDFERDMMVKINDR------YEFPLEIdllpfLDRDADKSeNSDAVY 431
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215375879  748 ELSGVIYHHGmSPDGGHYTADVFHKQTKTWYRIDDVNITKLEDDDVLK---GGEDNMDSR-----------TAYILMY 811
Cdd:COG5077    432 VLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEenfGGDHPYKDKirdhsgikrfmSAYMLVY 508
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
375-812 4.48e-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 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: 61.96  E-value: 4.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 375 GIINNANICFMSSVLQVLL----YCAPFVDILNVVS------TRNMNaksgSSSAKLLDACLTiykkfdkanyekekeke 444
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFsipsFQWRYDDLENKFPsdvvdpANDLN----CQLIKLADGLLS----------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 445 SEKEKPGSKKSSPPAYasiTEAVNPDEFYRSLS-TIPKFKDlrwGHQEDAEEFLTHLLDQLHEELISaidslseNEILNl 523
Cdd:cd02658    60 GRYSKPASLKSENDPY---QVGIKPSMFKALIGkGHPEFST---MRQQDALEFLLHLIDKLDRESFK-------NLGLN- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 524 lqsihdedlkiyiirnlsrykdaeFIKNMSPQLKDQInkygtisddseEGNGWHEVSGSSkkgkktktaakRTVEFIPSP 603
Cdd:cd02658   126 ------------------------PNDLFKFMIEDRL-----------ECLSCKKVKYTS-----------ELSEILSLP 159
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 604 ISnlfggqfrsvLDIPQNKESQSITLDPFqtiqldisdpgvdSLEAALKKFSEYELLP-FKSSSGNDVEAKKQTFIDKLP 682
Cdd:cd02658   160 VP----------KDEATEKEEGELVYEPV-------------PLEDCLKAYFAPETIEdFCSTCKEKTTATKTTGFKTFP 216
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 683 QILLIQLKRFSFISNadkdngmtnynaysgrieKIRKKISYghTLEIPDETLassalrnnsSKTYELSGVIYHHGMSPDG 762
Cdd:cd02658   217 DYLVINMKRFQLLEN------------------WVPKKLDV--PIDVPEELG---------PGKYELIAFISHKGTSVHS 267
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1215375879 763 GHYTADVFHKQTK--TWYRIDDVNITKLEDDDVLKGgednmdsrTAYILMYQ 812
Cdd:cd02658   268 GHYVAHIKKEIDGegKWVLFNDEKVVASQDPPEMKK--------LGYIYFYQ 311
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
604-812 4.14e-09

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 59.04  E-value: 4.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 604 ISNLFGGQFRSVLDIPQ-NKESQSITLDPFqtiqLDISDPGVDSLeaaLKKFSEYELLPF-------KSSSGNDVEAKKQ 675
Cdd:cd02664    99 IEKMFGGKLSTTIRCLNcNSTSARTERFRD----LDLSFPSVQDL---LNYFLSPEKLTGdnqyyceKCASLQDAEKEMK 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 676 tfIDKLPQILLIQLKRFSfisnadkdngmtnYNAYSGRIEKIRKKISYGHTLEIP--DETLASSALRNNSSKT------- 746
Cdd:cd02664   172 --VTGAPEYLILTLLRFS-------------YDQKTHVREKIMDNVSINEVLSLPvrVESKSSESPLEKKEEEsgddgel 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 747 ------YELSGVIYHHGMSPDGGHY--------------TADVFHKQ------TKTWYRIDDVNITKLEDDDVlkggeDN 800
Cdd:cd02664   237 vtrqvhYRLYAVVVHSGYSSESGHYftyardqtdadstgQECPEPKDaeendeSKNWYLFNDSRVTFSSFESV-----QN 311
                         250
                  ....*....|....*.
gi 1215375879 801 MDSR----TAYILMYQ 812
Cdd:cd02664   312 VTSRfpkdTPYILFYE 327
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
671-811 1.42e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 57.21  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 671 EAKKQTFIDKLPQILLIQLKRFSFISNADKdngmtnynaYSGRIEKIRKKISYghTLEIPDETLASsalrNNSSKTYELS 750
Cdd:cd02671   211 EAERSLLFDKLPEVITIHLKCFAANGSEFD---------CYGGLSKVNTPLLT--PLKLSLEEWST----KPKNDVYRLF 275
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215375879 751 GVIYHHGMSPDGGHYTADVfhkqtkTWYRIDDVNITKLEDDDVLKGGEDNMDS-RTAYILMY 811
Cdd:cd02671   276 AVVMHSGATISSGHYTAYV------RWLLFDDSEVKVTEEKDFLEALSPNTSStSTPYLLFY 331
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
646-812 7.81e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 53.91  E-value: 7.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 646 SLEAALKKFSEYELLpfksssgNDVEA-KKQTFIDKLPQILLIQLKRFSFisnaDKDNGMTNYNAysgriekirkKISYG 724
Cdd:cd02662    97 TLEHCLDDFLSTEII-------DDYKCdRCQTVIVRLPQILCIHLSRSVF----DGRGTSTKNSC----------KVSFP 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 725 HTLeipdetlassalrnnSSKTYELSGVIYHHGmSPDGGHYTA------DVFHKQTK--------------TWYRIDDVN 784
Cdd:cd02662   156 ERL---------------PKVLYRLRAVVVHYG-SHSSGHYVCyrrkplFSKDKEPGsfvrmregpsstshPWWRISDTT 219
                         170       180
                  ....*....|....*....|....*...
gi 1215375879 785 ITKLEDDDVLKGGEdnmdsrtAYILMYQ 812
Cdd:cd02662   220 VKEVSESEVLEQKS-------AYMLFYE 240
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
631-815 9.81e-08

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 55.66  E-value: 9.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 631 PFQTIQLDISDPgvdSLEAALKKFSEYELLPFKSS-----SGNDVEAKKQTFIDKLPQILLIQLKRFSFISnadkdngmt 705
Cdd:COG5560   664 TIREIGAAERTI---TLQDCLNEFSKPEQLGLSDSwycpgCKEFRQASKQMELWRLPMILIIHLKRFSSVR--------- 731
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 706 nynaysgrieKIRKKISygHTLEIPDETLASS---ALRNNSSKTYELSGVIYHHGMSpDGGHYTADVFHKQTKTWYRIDD 782
Cdd:COG5560   732 ----------SFRDKID--DLVEYPIDDLDLSgveYMVDDPRLIYDLYAVDNHYGGL-SGGHYTAYARNFANNGWYLFDD 798
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1215375879 783 VNITKLEDDDVLKGgednmdsrTAYILMYQNVH 815
Cdd:COG5560   799 SRITEVDPEDSVTS--------SAYVLFYRRKS 823
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
645-811 2.05e-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: 49.48  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 645 DSLEAALKKfSEYELLPfkssSGNDVEAKKQTFIDKLPQILLIQLKRFSFisnadkdngmtnynaYSGRIEKIRKKisyg 724
Cdd:cd02665    97 ECLEAAMFE-GEVELLP----SDHSVKSGQERWFTELPPVLTFELSRFEF---------------NQGRPEKIHDK---- 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 725 htLEIPDETlassalrnnSSKTYELSGVIYHHGMSpDGGHYTADVFHKQTKTWYRIDDVNITKLEDDDVLKGGEDNMDSR 804
Cdd:cd02665   153 --LEFPQII---------QQVPYELHAVLVHEGQA-NAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNP 220

                  ....*..
gi 1215375879 805 TAYILMY 811
Cdd:cd02665   221 SAYCLMY 227
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
467-789 7.00e-06

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 49.24  E-value: 7.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 467 VNPDEFYRSLSTIPKfKDLRWGHQEDAEEFLTHLLDQLHEELISAIDSLSeneilNLLQSIHDEDLKIYIIRNlsrykda 546
Cdd:cd02669   185 VSPHELLQAVSKVSK-KKFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNS-----SIIHDCFQGKVQIETQKI------- 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 547 efiknmSPQLKDQINKYGTISDDseegngwhevsgsskkgkktktaakRTVEFIPSPISNLfggqfrsVLDIPQNKesqs 626
Cdd:cd02669   252 ------KPHAEEEGSKDKFFKDS-------------------------RVKKTSVSPFLLL-------TLDLPPPP---- 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 627 itldPFQTIQLDISDPGVdSLEAALKKF---SEYELlpfksssgndVEAKKQTFIDKLPQILLIQLKRFSfisnadKDNG 703
Cdd:cd02669   290 ----LFKDGNEENIIPQV-PLKQLLKKYdgkTETEL----------KDSLKRYLISRLPKYLIFHIKRFS------KNNF 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 704 MTNYNaysGRIekirkkISYGHTLEIPDETLASSALRNNSSKTYELSGVIYHHGMSPDGGHYTADVFHKQTKTWYRIDDV 783
Cdd:cd02669   349 FKEKN---PTI------VNFPIKNLDLSDYVHFDKPSLNLSTKYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDL 419

                  ....*.
gi 1215375879 784 NITKLE 789
Cdd:cd02669   420 NVKEVL 425
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
622-811 6.33e-04

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


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 42.13  E-value: 6.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 622 KESQSITLDPFQTIQLDISDPGVD-SLEAALKKFSEYELlpfKSSSGNDVEAKKQTFIDKLPQILLIQLKRFSF---ISN 697
Cdd:cd02673    89 FEENVSDVGNFLDVSMIDNKLDIDeLLISNFKTWSPIEK---DCSSCKCESAISSERIMTFPECLSINLKRYKLriaTSD 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 698 ADKDNgmtnynaysgriEKIRKKisygHTLEIPdetlassalrnnsskTYELSGVIYHHGMSPDGGHYTAdvFHKQT--- 774
Cdd:cd02673   166 YLKKN------------EEIMKK----YCGTDA---------------KYSLVAVICHLGESPYDGHYIA--YTKELyng 212
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1215375879 775 KTWYRIDDVNITKLEDDDVLKGGednmdSRTAYILMY 811
Cdd:cd02673   213 SSWLYCSDDEIRPVSKNDVSTNA-----RSSGYLIFY 244
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
149-334 7.13e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 43.08  E-value: 7.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 149 SKIKEETTSFPMFfnTNEKDFAEAKAKRYHLSLKALDHEEQPIQKEPQVQSE-----------QVKQEEQIQKKQDFQQl 217
Cdd:NF033838  288 SSVGEETLPSPSL--KPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKtleleiaesdvKVKEAELELVKEEAKE- 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 218 SIEEEDIKDLKSgdKTDIVLPETTtNKENIQqgTEIKVSSPEMGNKQASGSPVEETATPYITPAPTP---KPAAKSWSAI 294
Cdd:NF033838  365 PRNEEKIKQAKA--KVESKKAEAT-RLEKIK--TDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPqpeKPAPKPEKPA 439
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1215375879 295 ASSAISKGKPSNVSSPISRPGS------THQQPQKKSKKYVPATPK 334
Cdd:NF033838  440 EQPKAEKPADQQAEEDYARRSEeeynrlTQQQPPKTEKPAQPSTPK 485
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
680-812 1.37e-03

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


Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 41.36  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 680 KLPQILLIQLKRFsfisnadkdnGMTNYNAYsgrieKIRKKISYGHTLEIPD-------ETLASSALRNNSSKTYE---- 748
Cdd:cd02670    97 KAPSCLIICLKRY----------GKTEGKAQ-----KMFKKILIPDEIDIPDfvaddprACSKCQLECRVCYDDKDfspt 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375879 749 -------LSGVIYHHGMSPDGGHYTADVfHKQTKT------------WYRIDDvnitkLEDDDVLKGGEDNMDSRT---A 806
Cdd:cd02670   162 cgkfklsLCSAVCHRGTSLETGHYVAFV-RYGSYSltetdneaynaqWVFFDD-----MADRDGVSNGFNIPAARLledP 235

                  ....*.
gi 1215375879 807 YILMYQ 812
Cdd:cd02670   236 YMLFYQ 241
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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