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Conserved domains on  [gi|1720405306|ref|XP_030108701|]
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ubiquitin carboxyl-terminal hydrolase 13 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
86-605 1.73e-122

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: 364.34  E-value: 1.73e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  86 GLKNLGNSCYLSSVMQAIFSIPEFQRAYvGNLPRIFDYSPLDPTQDFNTQMTKLGHGLLSGQYSKPPVKselieqvmKEE 165
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRY-DDLENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKPASL--------KSE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 166 HKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERN--RIGSENPSDVFRFLVEERIQCCQTRKVRYTER 243
Cdd:cd02658    72 NDPYQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDREsfKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 244 VDYLMQLPVAMEAATNKDElityelmrreaeanrrplPELVRAKIPFSACLQAFAEPDNVDDFWSSaLQAKSAGVKTSRF 323
Cdd:cd02658   152 LSEILSLPVPKDEATEKEE------------------GELVYEPVPLEDCLKAYFAPETIEDFCST-CKEKTTATKTTGF 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 324 ASFPEYLVVQIKKFTFGLDWVPRKFDVSIDMPDLLdishlrarglqpgeeelpdisppivipddskdrlmnqlidpsdid 403
Cdd:cd02658   213 KTFPDYLVINMKRFQLLENWVPKKLDVPIDVPEEL--------------------------------------------- 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 404 essvmqlaemgfpleacrkavyftgntgaevafnwiivhmeepdfaeplaipgyggagasvfgatgldnqppeeivaiit 483
Cdd:cd02658       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 484 smgfqrnqavqalqatnhnleraldwifshpefeedsdfviemennananivseakpegprvkdGSGMYELFAFISHMGT 563
Cdd:cd02658   248 ----------------------------------------------------------------GPGKYELIAFISHKGT 263
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1720405306 564 STMSGHYVCHIKK----EGRWVIYNDHKVCASERPP--KDLGYMYFYR 605
Cdd:cd02658   264 SVHSGHYVAHIKKeidgEGKWVLFNDEKVVASQDPPemKKLGYIYFYQ 311
UBA1_UBP13 cd14384
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
401-449 7.43e-26

UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13, is an ortholog of UBP5 implicated in catalyzing hydrolysis of various ubiquitin (Ub)-chains. It contains a zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. Due to the non-activating catalysis for K63-polyubiquitin chains, UBP13 may function differently from USP5 in cellular deubiquitination processes. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA1 domain.


:

Pssm-ID: 270567  Cd Length: 49  Bit Score: 100.10  E-value: 7.43e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720405306 401 DIDESSVMQLAEMGFPLEACRKAVYFTGNTGAEVAFNWIIVHMEEPDFA 449
Cdd:cd14384     1 DIDESSVMQLAEMGFPLEACRKAVYYTGNMGAEVAFNWIIAHMEEPDFA 49
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
474-515 4.14e-19

UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA2 domain.


:

Pssm-ID: 270569 [Multi-domain]  Cd Length: 43  Bit Score: 80.84  E-value: 4.14e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720405306 474 PPEEIVAIITSMGFQRNQAVQALQATNHNLERALDWIFSHPE 515
Cdd:cd14386     1 VPEEAVAMLVSMGFTRDQAIKALKATDNNVERAADWIFSHPD 42
 
Name Accession Description Interval E-value
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
86-605 1.73e-122

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: 364.34  E-value: 1.73e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  86 GLKNLGNSCYLSSVMQAIFSIPEFQRAYvGNLPRIFDYSPLDPTQDFNTQMTKLGHGLLSGQYSKPPVKselieqvmKEE 165
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRY-DDLENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKPASL--------KSE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 166 HKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERN--RIGSENPSDVFRFLVEERIQCCQTRKVRYTER 243
Cdd:cd02658    72 NDPYQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDREsfKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 244 VDYLMQLPVAMEAATNKDElityelmrreaeanrrplPELVRAKIPFSACLQAFAEPDNVDDFWSSaLQAKSAGVKTSRF 323
Cdd:cd02658   152 LSEILSLPVPKDEATEKEE------------------GELVYEPVPLEDCLKAYFAPETIEDFCST-CKEKTTATKTTGF 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 324 ASFPEYLVVQIKKFTFGLDWVPRKFDVSIDMPDLLdishlrarglqpgeeelpdisppivipddskdrlmnqlidpsdid 403
Cdd:cd02658   213 KTFPDYLVINMKRFQLLENWVPKKLDVPIDVPEEL--------------------------------------------- 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 404 essvmqlaemgfpleacrkavyftgntgaevafnwiivhmeepdfaeplaipgyggagasvfgatgldnqppeeivaiit 483
Cdd:cd02658       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 484 smgfqrnqavqalqatnhnleraldwifshpefeedsdfviemennananivseakpegprvkdGSGMYELFAFISHMGT 563
Cdd:cd02658   248 ----------------------------------------------------------------GPGKYELIAFISHKGT 263
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1720405306 564 STMSGHYVCHIKK----EGRWVIYNDHKVCASERPP--KDLGYMYFYR 605
Cdd:cd02658   264 SVHSGHYVAHIKKeidgEGKWVLFNDEKVVASQDPPemKKLGYIYFYQ 311
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
85-377 1.27e-58

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 198.82  E-value: 1.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  85 TGLKNLGNSCYLSSVMQAIFSIPEFqRAYVGNLPRIFDYSPLDPTQDFNTQMTKLGHGLLsgqyskppvkselieqvmke 164
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPF-RDYLLRISPLSEDSRYNKDINLLCALRDLFKALQ-------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 165 eHKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERN------RIGSENPSDVFRFLVEERIQCCQTRKV 238
Cdd:pfam00443  60 -KNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDlngnhsTENESLITDLFRGQLKSRLKCLSCGEV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 239 RYTERVDYLMQLPVAMEAATNKDELItyelmrreaeanrrplpelvrakIPFSACLQAFAEPDNVDDFWSSALQAKSAGV 318
Cdd:pfam00443 139 SETFEPFSDLSLPIPGDSAELKTASL-----------------------QICFLQFSKLEELDDEEKYYCDKCGCKQDAI 195
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720405306 319 KTSRFASFPEYLVVQIKKFTFGLdWVPRKFDVSIDMPDLLDISHLRARGLQPGEEELPD 377
Cdd:pfam00443 196 KQLKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD 253
UBA1_UBP13 cd14384
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
401-449 7.43e-26

UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13, is an ortholog of UBP5 implicated in catalyzing hydrolysis of various ubiquitin (Ub)-chains. It contains a zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. Due to the non-activating catalysis for K63-polyubiquitin chains, UBP13 may function differently from USP5 in cellular deubiquitination processes. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270567  Cd Length: 49  Bit Score: 100.10  E-value: 7.43e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720405306 401 DIDESSVMQLAEMGFPLEACRKAVYFTGNTGAEVAFNWIIVHMEEPDFA 449
Cdd:cd14384     1 DIDESSVMQLAEMGFPLEACRKAVYYTGNMGAEVAFNWIIAHMEEPDFA 49
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
474-515 4.14e-19

UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA2 domain.


Pssm-ID: 270569 [Multi-domain]  Cd Length: 43  Bit Score: 80.84  E-value: 4.14e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720405306 474 PPEEIVAIITSMGFQRNQAVQALQATNHNLERALDWIFSHPE 515
Cdd:cd14386     1 VPEEAVAMLVSMGFTRDQAIKALKATDNNVERAADWIFSHPD 42
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
83-254 6.53e-12

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 68.76  E-value: 6.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  83 GYTGLKNLGNSCYLSSVMQAIFSIPEFQrayvgnlprifDYSPLDPTQDFNTQMTKLG-HGLLSGQYSkppvksELIEQV 161
Cdd:COG5560   264 GTCGLRNLGNTCYMNSALQCLMHTWELR-----------DYFLSDEYEESINEENPLGmHGSVASAYA------DLIKQL 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 162 mkeeHKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVER--NRIG----SENPS---------------- 219
Cdd:COG5560   327 ----YDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEdlNRIIkkpyTSKPDlspgddvvvkkkakec 402
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720405306 220 -------------DVFRFLVEERIQC--CQTRKVRYTERVDYLMQLPVAM 254
Cdd:COG5560   403 wwehlkrndsiitDLFQGMYKSTLTCpgCGSVSITFDPFMDLTLPLPVSM 452
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
474-510 6.03e-10

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 54.37  E-value: 6.03e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1720405306 474 PPEEIVAIITSMGFQRNQAVQALQATNHNLERALDWI 510
Cdd:pfam00627   1 EDEEAIQRLVEMGFDREQVREALRATGNNVERAAEYL 37
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
475-511 1.83e-09

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 53.26  E-value: 1.83e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1720405306  475 PEEIVAIITSMGFQRNQAVQALQATNHNLERALDWIF 511
Cdd:smart00165   1 DEEKIDQLLEMGFSREEALKALRAANGNVERAAEYLL 37
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
402-439 4.83e-07

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 46.28  E-value: 4.83e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720405306 402 IDESSVMQLAEMGFPLEACRKAVYFTGNtGAEVAFNWI 439
Cdd:pfam00627   1 EDEEAIQRLVEMGFDREQVREALRATGN-NVERAAEYL 37
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
403-440 5.27e-06

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 43.24  E-value: 5.27e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1720405306  403 DESSVMQLAEMGFPLEACRKAVYFTGNTgAEVAFNWII 440
Cdd:smart00165   1 DEEKIDQLLEMGFSREEALKALRAANGN-VERAAEYLL 37
 
Name Accession Description Interval E-value
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
86-605 1.73e-122

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: 364.34  E-value: 1.73e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  86 GLKNLGNSCYLSSVMQAIFSIPEFQRAYvGNLPRIFDYSPLDPTQDFNTQMTKLGHGLLSGQYSKPPVKselieqvmKEE 165
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRY-DDLENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKPASL--------KSE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 166 HKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERN--RIGSENPSDVFRFLVEERIQCCQTRKVRYTER 243
Cdd:cd02658    72 NDPYQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDREsfKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 244 VDYLMQLPVAMEAATNKDElityelmrreaeanrrplPELVRAKIPFSACLQAFAEPDNVDDFWSSaLQAKSAGVKTSRF 323
Cdd:cd02658   152 LSEILSLPVPKDEATEKEE------------------GELVYEPVPLEDCLKAYFAPETIEDFCST-CKEKTTATKTTGF 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 324 ASFPEYLVVQIKKFTFGLDWVPRKFDVSIDMPDLLdishlrarglqpgeeelpdisppivipddskdrlmnqlidpsdid 403
Cdd:cd02658   213 KTFPDYLVINMKRFQLLENWVPKKLDVPIDVPEEL--------------------------------------------- 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 404 essvmqlaemgfpleacrkavyftgntgaevafnwiivhmeepdfaeplaipgyggagasvfgatgldnqppeeivaiit 483
Cdd:cd02658       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 484 smgfqrnqavqalqatnhnleraldwifshpefeedsdfviemennananivseakpegprvkdGSGMYELFAFISHMGT 563
Cdd:cd02658   248 ----------------------------------------------------------------GPGKYELIAFISHKGT 263
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1720405306 564 STMSGHYVCHIKK----EGRWVIYNDHKVCASERPP--KDLGYMYFYR 605
Cdd:cd02658   264 SVHSGHYVAHIKKeidgEGKWVLFNDEKVVASQDPPemKKLGYIYFYQ 311
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
85-377 1.27e-58

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 198.82  E-value: 1.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  85 TGLKNLGNSCYLSSVMQAIFSIPEFqRAYVGNLPRIFDYSPLDPTQDFNTQMTKLGHGLLsgqyskppvkselieqvmke 164
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPF-RDYLLRISPLSEDSRYNKDINLLCALRDLFKALQ-------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 165 eHKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERN------RIGSENPSDVFRFLVEERIQCCQTRKV 238
Cdd:pfam00443  60 -KNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDlngnhsTENESLITDLFRGQLKSRLKCLSCGEV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 239 RYTERVDYLMQLPVAMEAATNKDELItyelmrreaeanrrplpelvrakIPFSACLQAFAEPDNVDDFWSSALQAKSAGV 318
Cdd:pfam00443 139 SETFEPFSDLSLPIPGDSAELKTASL-----------------------QICFLQFSKLEELDDEEKYYCDKCGCKQDAI 195
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720405306 319 KTSRFASFPEYLVVQIKKFTFGLdWVPRKFDVSIDMPDLLDISHLRARGLQPGEEELPD 377
Cdd:pfam00443 196 KQLKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD 253
UBA1_UBP13 cd14384
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
401-449 7.43e-26

UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13, is an ortholog of UBP5 implicated in catalyzing hydrolysis of various ubiquitin (Ub)-chains. It contains a zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. Due to the non-activating catalysis for K63-polyubiquitin chains, UBP13 may function differently from USP5 in cellular deubiquitination processes. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270567  Cd Length: 49  Bit Score: 100.10  E-value: 7.43e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720405306 401 DIDESSVMQLAEMGFPLEACRKAVYFTGNTGAEVAFNWIIVHMEEPDFA 449
Cdd:cd14384     1 DIDESSVMQLAEMGFPLEACRKAVYYTGNMGAEVAFNWIIAHMEEPDFA 49
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
86-605 1.14e-23

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: 100.64  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  86 GLKNLGNSCYLSSVMQAIFSipefqrayvgnlprifdyspldptqdfntqmtklghgllsgqyskppvkselieqvmkee 165
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 166 hkpqqngisprmfkafvskshpefssnRQQDAQEFFLHLVNLVER-----------NRIGSENPSDVFRFLVEERIQCCQ 234
Cdd:cd02257    21 ---------------------------EQQDAHEFLLFLLDKLHEelkksskrtsdSSSLKSLIHDLFGGKLESTIVCLE 73
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 235 TRKVRYTERVDYLMQLPvameaatnkdelityelmrreaeanrrpLPELVRAKIPFSACLQAFAEPDNVDDFWSSA--LQ 312
Cdd:cd02257    74 CGHESVSTEPELFLSLP----------------------------LPVKGLPQVSLEDCLEKFFKEEILEGDNCYKceKK 125
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 313 AKSAGVKTSRFASFPEYLVVQIKKFTFGLDWVPRKFDVSIDMPDLLDISHLRARGLQPGEEElpdisppivipddskdrl 392
Cdd:cd02257   126 KKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSD------------------ 187
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 393 mnqlidpsdidessvmqlaemgfpleacrkavyftgntgaevafnwiivhmeepdfaeplaipgyggagasvfgatgldn 472
Cdd:cd02257       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 473 qppeeivaiitsmgfqrnqavqalqatnhnleraldwifshpefeedsdfviemennananivseakpegprvkDGSGMY 552
Cdd:cd02257   188 --------------------------------------------------------------------------NGSYKY 193
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720405306 553 ELFAFISHMGTSTMSGHYVCHIKK--EGRWVIYNDHKVCASE-------RPPKDLGYMYFYR 605
Cdd:cd02257   194 ELVAVVVHSGTSADSGHYVAYVKDpsDGKWYKFNDDKVTEVSeeevlefGSLSSSAYILFYE 255
UBA1_UBP5_like cd14294
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; ...
404-447 2.02e-22

UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13, is an ortholog of UBP5. It has similar domain architecture, but functions differently from USP5 in cellular deubiquitination processes. It exhibits a weak deubiquitinating activity preferring to Lys63-linked polyubiquitin in a non-activation manner. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270480 [Multi-domain]  Cd Length: 44  Bit Score: 90.06  E-value: 2.02e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1720405306 404 ESSVMQLAEMGFPLEACRKAVYFTGNTGAEVAFNWIIVHMEEPD 447
Cdd:cd14294     1 EAVVSQLAEMGFPLEACRKAVYHTNNSGLEAAMNWIMEHMDDPD 44
UBA1_UBP5 cd14383
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
402-449 8.92e-20

UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA1 domain.


Pssm-ID: 270566 [Multi-domain]  Cd Length: 49  Bit Score: 82.80  E-value: 8.92e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720405306 402 IDESSVMQLAEMGFPLEACRKAVYFTGNTGAEVAFNWIIVHMEEPDFA 449
Cdd:cd14383     2 LDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFA 49
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
474-515 4.14e-19

UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA2 domain.


Pssm-ID: 270569 [Multi-domain]  Cd Length: 43  Bit Score: 80.84  E-value: 4.14e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720405306 474 PPEEIVAIITSMGFQRNQAVQALQATNHNLERALDWIFSHPE 515
Cdd:cd14386     1 VPEEAVAMLVSMGFTRDQAIKALKATDNNVERAADWIFSHPD 42
UBA2_UBP13 cd14387
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
476-510 1.19e-15

UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13 is an ortholog of UBP5 implicated in catalyzing hydrolysis of various ubiquitin (Ub)-chains. It contains a zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. Due to the non-activating catalysis for K63-polyubiquitin chains, UBP13 may function differently from USP5 in cellular deubiquitination processes. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270570  Cd Length: 35  Bit Score: 70.87  E-value: 1.19e-15
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1720405306 476 EEIVAIITSMGFQRNQAVQALQATNHNLERALDWI 510
Cdd:cd14387     1 EESIAILMSMGFPRNRAIEALKRTNNNLDRALDWL 35
UBA1_spUBP14_like cd14385
UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
403-447 1.32e-14

UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270568 [Multi-domain]  Cd Length: 47  Bit Score: 68.21  E-value: 1.32e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1720405306 403 DESSVMQLAEMGFPLEACRKAVYFTGNTGAEVAFNWIIVHMEEPD 447
Cdd:cd14385     1 NAEALAQLLGMGFPEVRCKKALLATGNSDAEAAMNWLFEHMDDPD 45
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
83-378 8.43e-14

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 72.68  E-value: 8.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  83 GYTGLKNLGNSCYLSSVMQAIFSIPEFQRAyvgnLPRIFDYSPLDPTQDFNTQMTKLghgLLSGQYSKPPVKselieqvm 162
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNA----VYSIPPTEDDDDNKSVPLALQRL---FLFLQLSESPVK-------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 163 keehkpqqngiSPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERNRIGSENP---SDVFRFLVEERIQC--Cqtrk 237
Cdd:cd02659    66 -----------TTELTDKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEgliKNLFGGKLVNYIICkeC---- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 238 VRYTERVDYLMQLPVAMeaaTNKDELityelmrreAEAnrrplpelvrakipfsacLQAFAEPDNVDDfwSSALQAKSAG 317
Cdd:cd02659   131 PHESEREEYFLDLQVAV---KGKKNL---------EES------------------LDAYVQGETLEG--DNKYFCEKCG 178
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720405306 318 -----VKTSRFASFPEYLVVQIKKFTFglDWVP---RKFDVSIDMPDLLDISHLRARGLQPGEEELPDI 378
Cdd:cd02659   179 kkvdaEKGVCFKKLPPVLTLQLKRFEF--DFETmmrIKINDRFEFPLELDMEPYTEKGLAKKEGDSEKK 245
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
86-361 1.36e-12

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 68.57  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  86 GLKNLGNSCYLSSVMQAIFSipefqrayvgnlprifdyspldptqdfntqmTKLGHGLLSGqyskppvkselieqvmkee 165
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQ-------------------------------TPALRELLSE------------------- 30
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 166 hkpqqngiSPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVeRNRIGSenpsdVFRFLVEERIQCCQTRKVryTERVD 245
Cdd:cd02667    31 --------TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGL-RTFIDS-----IFGGELTSTIMCESCGTV--SLVYE 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 246 YLMQLpvameaatnkdelityelmrreaeanrrPLPELVRAKIPFS--ACLQAFAEP----DNVDDFWSSALQAKsagvK 319
Cdd:cd02667    95 PFLDL----------------------------SLPRSDEIKSECSieSCLKQFTEVeileGNNKFACENCTKAK----K 142
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1720405306 320 TSRFASFPEYLVVQIKKFTFGLDWVPRKFDVSIDMPDLLDIS 361
Cdd:cd02667   143 QYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLA 184
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
191-371 2.32e-12

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 66.93  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 191 SNRQQDAQEFFLHLVNLVeRNRIgsenpSDVFRFLVEERIQCCQTRKVRYTERVDYLMQLPVAMeaatnkdelityelmr 270
Cdd:cd02674    19 SADQQDAQEFLLFLLDGL-HSII-----VDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPS---------------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 271 reaeaNRRPLPelvraKIPFSACLQAFAEPDNVDDF--WS-SALQAKSAGVKTSRFASFPEYLVVQIKKFTFGLDWvPRK 347
Cdd:cd02674    77 -----GSGDAP-----KVTLEDCLRLFTKEETLDGDnaWKcPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGS-TRK 145
                         170       180
                  ....*....|....*....|....*.
gi 1720405306 348 FDVSIDMP--DLLDISHLRARGLQPG 371
Cdd:cd02674   146 LTTPVTFPlnDLDLTPYVDTRSFTGP 171
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
403-447 6.09e-12

UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270481 [Multi-domain]  Cd Length: 45  Bit Score: 60.46  E-value: 6.09e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1720405306 403 DESSVMQLAEMGFPLEACRKAVYFTGNTGAEVAFNWIIVHMEEPD 447
Cdd:cd14295     1 DQELVAQLMEMGFPKVRAEKALFFTQNKGLEEAMEWLEEHSEDAD 45
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
83-254 6.53e-12

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 68.76  E-value: 6.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  83 GYTGLKNLGNSCYLSSVMQAIFSIPEFQrayvgnlprifDYSPLDPTQDFNTQMTKLG-HGLLSGQYSkppvksELIEQV 161
Cdd:COG5560   264 GTCGLRNLGNTCYMNSALQCLMHTWELR-----------DYFLSDEYEESINEENPLGmHGSVASAYA------DLIKQL 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 162 mkeeHKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVER--NRIG----SENPS---------------- 219
Cdd:COG5560   327 ----YDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEdlNRIIkkpyTSKPDlspgddvvvkkkakec 402
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720405306 220 -------------DVFRFLVEERIQC--CQTRKVRYTERVDYLMQLPVAM 254
Cdd:COG5560   403 wwehlkrndsiitDLFQGMYKSTLTCpgCGSVSITFDPFMDLTLPLPVSM 452
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
86-337 1.83e-11

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: 65.43  E-value: 1.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  86 GLKNLGNSCYLSSVMQAIFSIPEFQRAyvgnlprIFDYSPldptqdfNTQMTKLGHGLLSGQYSKppvkseLIEQVMKee 165
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDA-------LKNYNP-------ARRGANQSSDNLTNALRD------LFDTMDK-- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 166 hkpQQNGISPRMFKAFVSKSHPEFSSN------RQQDAQEFFLHLVNLVERN-RIGSENPS---DVFRFLVEERIQCCQ- 234
Cdd:cd02657    59 ---KQEPVPPIEFLQLLRMAFPQFAEKqnqggyAQQDAEECWSQLLSVLSQKlPGAGSKGSfidQLFGIELETKMKCTEs 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 235 -TRKVRYTERvDYLMQLPVAmeaatnkDELITYELmrreaeanrrplpelvrakipFSACLQAFAEPDNVDdfwSSALQA 313
Cdd:cd02657   136 pDEEEVSTES-EYKLQCHIS-------ITTEVNYL---------------------QDGLKKGLEEEIEKH---SPTLGR 183
                         250       260
                  ....*....|....*....|....
gi 1720405306 314 KSAGVKTSRFASFPEYLVVQIKKF 337
Cdd:cd02657   184 DAIYTKTSRISRLPKYLTVQFVRF 207
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
476-514 5.56e-11

UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270483 [Multi-domain]  Cd Length: 39  Bit Score: 57.49  E-value: 5.56e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720405306 476 EEIVAIITSMGFQRNQAVQALQATNHNLERALDWIFSHP 514
Cdd:cd14297     1 EDLVKQLVDMGFTEAQARKALRKTNNNVERAVDWLFEGP 39
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
539-599 1.34e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 62.82  E-value: 1.34e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720405306 539 KPEGPRVKDGSGMYELFAFISHMGTSTMSGHYVCHIKKE--GRWVIYNDHKVcaSERPPKDLG 599
Cdd:cd02668   233 GEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEqtGEWYKFNDEDV--EEMPGKPLK 293
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
476-513 1.80e-10

UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270482 [Multi-domain]  Cd Length: 39  Bit Score: 56.10  E-value: 1.80e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720405306 476 EEIVAIITSMGFQRNQAVQALQAT-NHNLERALDWIFSH 513
Cdd:cd14296     1 EEAVSQLMSMGFSENAAKRALYYTgNSSVEAAMNWLFEH 39
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
404-442 5.39e-10

UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270482 [Multi-domain]  Cd Length: 39  Bit Score: 54.56  E-value: 5.39e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720405306 404 ESSVMQLAEMGFPLEACRKAVYFTGNTGAEVAFNWIIVH 442
Cdd:cd14296     1 EEAVSQLMSMGFSENAAKRALYYTGNSSVEAAMNWLFEH 39
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
474-510 6.03e-10

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 54.37  E-value: 6.03e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1720405306 474 PPEEIVAIITSMGFQRNQAVQALQATNHNLERALDWI 510
Cdd:pfam00627   1 EDEEAIQRLVEMGFDREQVREALRATGNNVERAAEYL 37
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
475-511 1.83e-09

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 53.26  E-value: 1.83e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1720405306  475 PEEIVAIITSMGFQRNQAVQALQATNHNLERALDWIF 511
Cdd:smart00165   1 DEEKIDQLLEMGFSREEALKALRAANGNVERAAEYLL 37
UBA_RUP1p cd14307
UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ...
476-513 8.22e-09

UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ubiquitin-associated (UBA) domain-containing protein encoded by a nonessential yeast gene RUP1. It can mediate the association of Rsp5 and Ubp2. The N-terminal UBA domain is responsible for antagonizing Rsp5 function, as well as bridging the Rsp5-Ubp2 interaction. No other characterized functional domains or motifs are found in RUP1p.


Pssm-ID: 270492  Cd Length: 38  Bit Score: 51.53  E-value: 8.22e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720405306 476 EEIVAIITSMGFQRNQAVQALQATNHNLERALDWIFSH 513
Cdd:cd14307     1 EEAVASLLEMGIPREVAIEALRETNGDVEAAANYIFSN 38
UBA2_scUBP14_like cd14298
UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
476-513 1.11e-08

UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270484 [Multi-domain]  Cd Length: 38  Bit Score: 50.92  E-value: 1.11e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720405306 476 EEIVAIITSMGFQRNQAVQALQATNHNLERALDWIFSH 513
Cdd:cd14298     1 DEALAQLVSMGFDPEVARKALILTNGNVERAIEWLFSN 38
UBA_PUB_plant cd14290
UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family ...
401-448 4.64e-08

UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family includes some uncharacterized hypothetical proteins found in plants. Although their biological function remain unclear, all family members contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal PUB domain. UBA domain, along with UBL (ubiquitin-like) domain, has been implicated in proteasomal degradation by associating with substrates destined for degradation as well as with subunits of the proteasome, thus regulating protein turnover. PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins.


Pssm-ID: 270476 [Multi-domain]  Cd Length: 49  Bit Score: 49.75  E-value: 4.64e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720405306 401 DIDESSVMQLAEMGFPLEACRKAVYFTGNTGAEVAFNWIIVHMEEPDF 448
Cdd:cd14290     1 EVNADLLKELEAMGFPRARAVRALHHTGNTSVEAAVNWIVEHENDPDI 48
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
547-604 4.91e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 54.97  E-value: 4.91e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720405306 547 DGSGMYELFAFISHMGTSTMSGHYVCHIKK-EGRWVIYNDHKV--CASERPPKDLGYMYFY 604
Cdd:cd02661   243 DGPLKYKLYAVLVHSGFSPHSGHYYCYVKSsNGKWYNMDDSKVspVSIETVLSQKAYILFY 303
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
547-597 7.72e-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 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: 54.26  E-value: 7.72e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720405306 547 DGSGMYELFAFISHMGTSTMSGHYVCHIKKE--GRWVIYNDHKVcaSERPPKD 597
Cdd:cd02657   236 TPSGYYELVAVITHQGRSADSGHYVAWVRRKndGKWIKFDDDKV--SEVTEED 286
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
551-604 9.69e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 53.85  E-value: 9.69e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720405306 551 MYELFAFISHMGTSTMSGHYVCHIKKEGRWVIYNDHKVCA----------SERPPKDLGYMYFY 604
Cdd:cd02663   236 LYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVEKidenaveeffGDSPNQATAYVLFY 299
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
405-445 1.58e-07

UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also called SAPK substrate protein 1 (SAKS1) or UBA/UBX 33.3 kDa protein, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (UBX) domain. It binds polyubiquitin and valosin-containing protein (VCP), and has been identified as a substrate for stress-activated protein kinases (SAPKs). Moreover, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and may be involved in the Ub-proteasome proteolytic pathways. In addition, UBXN1 can associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domain.


Pssm-ID: 270487 [Multi-domain]  Cd Length: 41  Bit Score: 47.67  E-value: 1.58e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720405306 405 SSVMQLAEMGFPLEACRKAVYFTGNTGAEVAFNWIIVHMEE 445
Cdd:cd14302     1 SELQTLIEMGFSRNRAEKALAKTGNQGVEAAMEWLLAHEDD 41
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
538-607 2.22e-07

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 52.88  E-value: 2.22e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720405306 538 AKPEGPRVKDGSGMYELFAFISHMGTSTmSGHYVCHIKKEGRWVIYNDHKVCA-----SERPPKDLGYMYFYRRI 607
Cdd:COG5533   211 VKHDQILNIVKETYYDLVGFVLHQGSLE-GGHYIAYVKKGGKWEKANDSDVTPvseeeAINEKAKNAYLYFYERI 284
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
477-513 3.29e-07

UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins.


Pssm-ID: 270512 [Multi-domain]  Cd Length: 38  Bit Score: 46.91  E-value: 3.29e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720405306 477 EIVAIITSMGFQRNQAVQALQATNHN-LERALDWIFSH 513
Cdd:cd14327     1 EAVAQLVEMGFSRERAEEALRAVGTNsVELAMEWLFTN 38
UBA cd14270
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ...
479-508 3.41e-07

UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ubiquitin-associated (UBA) domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only the bind UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains.


Pssm-ID: 270456 [Multi-domain]  Cd Length: 30  Bit Score: 46.58  E-value: 3.41e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 1720405306 479 VAIITSMGFQRNQAVQALQATNHNLERALD 508
Cdd:cd14270     1 LAQLVEMGFSREQARRALRATNGDVEAAVE 30
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
402-439 4.83e-07

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 46.28  E-value: 4.83e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720405306 402 IDESSVMQLAEMGFPLEACRKAVYFTGNtGAEVAFNWI 439
Cdd:pfam00627   1 EDEEAIQRLVEMGFDREQVREALRATGN-NVERAAEYL 37
UBA1_NUB1_like cd14291
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ...
476-510 8.90e-07

UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called negative regulator of ubiquitin-like proteins 1, renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) which may function in the regulation of cell cycle progression. NUB1 contains three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif. This model corresponds to UBA1 domain.


Pssm-ID: 270477 [Multi-domain]  Cd Length: 36  Bit Score: 45.52  E-value: 8.90e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1720405306 476 EEIVAIITSMGFQRNQAVQALQATNHNLERALDWI 510
Cdd:cd14291     2 EDKLQQLMEMGFSEAEARLALRACNGNVERAVDYI 36
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
86-361 1.35e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 50.45  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  86 GLKNLGNSCYLSSVMQAIFSIPEFQRAYVGNLPRIFDYSPLDPT----------QDFNTQMTKLGHGLLSGQYSkppvks 155
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSclscamdeifQEFYYSGDRSPYGPINLLYL------ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 156 elieqvmkeehkpqqngisprmfkafVSKSHPEFSSNRQQDAQEFFLHLVNLVERNRIGSENPSD-----------VFRF 224
Cdd:cd02660    76 --------------------------SWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANdeshcnciihqTFSG 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 225 LVEERIQCCQTRKVRYTerVDYLMQLPVAMEAATNKdelityelmrreaeanRRPLPELVRAKIP-FSACLQAFAEPDNV 303
Cdd:cd02660   130 SLQSSVTCQRCGGVSTT--VDPFLDLSLDIPNKSTP----------------SWALGESGVSGTPtLSDCLDRFTRPEKL 191
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 304 DDFWS--SALQAKSAGVKTSRFASFPEYLVVQIKKFTFGLDWVPRKFDVSIDMPDLLDIS 361
Cdd:cd02660   192 GDFAYkcSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLELNMT 251
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
86-347 1.54e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 49.67  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  86 GLKNLGNSCYLSSVMQAIFSIPEFqrayvgnlprifdyspldptqdfntqmtklghgllsgqyskppvkSELIEQVMKee 165
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSL---------------------------------------------IEYLEEFLE-- 33
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 166 hkpqqngisprmfkafvskshpefssnrQQDAQEFFLHLVNLVERNrigSENPsdvFRFLVEERIQCCQ---TRKVRYTE 242
Cdd:cd02662    34 ----------------------------QQDAHELFQVLLETLEQL---LKFP---FDGLLASRIVCLQcgeSSKVRYES 79
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 243 RVDYLMQLPVAMEAATNKDElityelmrreaeanrrplpelvrakipfsACLQAFAEPDNVDDFWSSALQAKsagvktsr 322
Cdd:cd02662    80 FTMLSLPVPNQSSGSGTTLE-----------------------------HCLDDFLSTEIIDDYKCDRCQTV-------- 122
                         250       260
                  ....*....|....*....|....*
gi 1720405306 323 FASFPEYLVVQIKKFTFGLDWVPRK 347
Cdd:cd02662   123 IVRLPQILCIHLSRSVFDGRGTSTK 147
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
86-210 2.03e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 50.18  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  86 GLKNLGNSCYLSSVMQAIFSIPEFQRAYV-GNLPRifdyspldpTQDFNTQMTKlghgllsgqyskppvkseLIEQVMKE 164
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLsLNLPR---------LGDSQSVMKK------------------LQLLQAHL 53
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720405306 165 EHKPQQNGISPRMFkaFVSKSHPEFSSNRQQDAQEFFLHLVN----LVER 210
Cdd:cd02664    54 MHTQRRAEAPPDYF--LEASRPPWFTPGSQQDCSEYLRYLLDrlhtLIEK 101
UBA1_spUBP14_like cd14385
UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
476-515 3.84e-06

UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270568 [Multi-domain]  Cd Length: 47  Bit Score: 43.94  E-value: 3.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720405306 476 EEIVAIITSMGFQRNQAVQALQATNH-NLERALDWIFSHPE 515
Cdd:cd14385     2 AEALAQLLGMGFPEVRCKKALLATGNsDAEAAMNWLFEHMD 42
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
403-440 5.27e-06

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 43.24  E-value: 5.27e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1720405306  403 DESSVMQLAEMGFPLEACRKAVYFTGNTgAEVAFNWII 440
Cdd:smart00165   1 DEEKIDQLLEMGFSREEALKALRAANGN-VERAAEYLL 37
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
552-605 5.51e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 48.05  E-value: 5.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 552 YELFAFISHMGtSTMSGHYVCHIKKE--GRWVIYNDHKVcaSERPPKDLG----YMYFYR 605
Cdd:cd02674   174 YDLYAVVNHYG-SLNGGHYTAYCKNNetNDWYKFDDSRV--TKVSESSVVsssaYILFYE 230
UBA_PUB_plant cd14290
UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family ...
475-522 9.93e-06

UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family includes some uncharacterized hypothetical proteins found in plants. Although their biological function remain unclear, all family members contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal PUB domain. UBA domain, along with UBL (ubiquitin-like) domain, has been implicated in proteasomal degradation by associating with substrates destined for degradation as well as with subunits of the proteasome, thus regulating protein turnover. PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins.


Pssm-ID: 270476 [Multi-domain]  Cd Length: 49  Bit Score: 42.81  E-value: 9.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720405306 475 PEEIVAIITSMGFQRNQAVQALQAT-NHNLERALDWIFSHpefEEDSDF 522
Cdd:cd14290     3 NADLLKELEAMGFPRARAVRALHHTgNTSVEAAVNWIVEH---ENDPDI 48
UBA1_Rad23 cd14377
UBA1 domain of Rad23 proteins found in metazoa; The family includes mammalian orthologs of ...
476-512 1.14e-05

UBA1 domain of Rad23 proteins found in metazoa; The family includes mammalian orthologs of yeast nucleotide excision repair (NER) proteins, Rad23p (in Saccharomyces cerevisiae) and Rhp23p (in Schizosaccharomyces pombe). Rad23 proteins play dual roles in DNA repair as well as in proteosomal degradation. They have affinity for both the proteasome and ubiquitinylated proteins and participate in translocating polyubiquitinated proteins to the proteasome. Rad23 proteins carry a ubiquitin-like (UBL) and two ubiquitin-associated (UBA) domains, as well as a xeroderma pigmentosum group C (XPC) protein-binding domain. UBL domain is responsible for the binding to proteasome. UBA domains are important for binding of ubiquitin (Ub) or multi-ubiquitinated substrates which suggests Rad23 proteins might be involved in certain pathways of ubiquitin metabolism. Both UBL domain and XPC-binding domain are necessary for efficient NER function of Rad23 proteins. This model corresponds to the UBA1 domain.


Pssm-ID: 270560  Cd Length: 40  Bit Score: 42.39  E-value: 1.14e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1720405306 476 EEIVAIITSMGFQRNQAVQALQATNHNLERALDWIFS 512
Cdd:cd14377     3 ENMVTEIMSMGFERDQVVRALRASFNNPDRAVEYLLS 39
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
485-513 1.25e-05

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.


Pssm-ID: 270491  Cd Length: 36  Bit Score: 42.43  E-value: 1.25e-05
                          10        20
                  ....*....|....*....|....*....
gi 1720405306 485 MGFQRNQAVQALQATNHNLERALDWIFSH 513
Cdd:cd14306     7 LGFPEEDCIRALRACGGNVEEAANWLLEN 35
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
479-515 1.82e-05

UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also called SAPK substrate protein 1 (SAKS1) or UBA/UBX 33.3 kDa protein, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (UBX) domain. It binds polyubiquitin and valosin-containing protein (VCP), and has been identified as a substrate for stress-activated protein kinases (SAPKs). Moreover, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and may be involved in the Ub-proteasome proteolytic pathways. In addition, UBXN1 can associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domain.


Pssm-ID: 270487 [Multi-domain]  Cd Length: 41  Bit Score: 41.89  E-value: 1.82e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720405306 479 VAIITSMGFQRNQAVQALQATNHN-LERALDWIFSHPE 515
Cdd:cd14302     3 LQTLIEMGFSRNRAEKALAKTGNQgVEAAMEWLLAHED 40
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
85-257 2.03e-05

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 46.89  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306  85 TGLKNLGNSCYLSSVMQAIFSIPefqrayvgnlPRIFDyspldptqdfntqmtklghgLLSGQYSKPPVKSEL-----IE 159
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTP----------PLANY--------------------LLSREHSKDCCNEGFcmmcaLE 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 160 QVMKEEHKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVN------LVERNRIGSENPS--------DVFRFL 225
Cdd:cd02661    52 AHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDamqkacLDRFKKLKAVDPSsqettlvqQIFGGY 131
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1720405306 226 VEERIQCCQTRKVryTERVDYLMQLPVAMEAA 257
Cdd:cd02661   132 LRSQVKCLNCKHV--SNTYDPFLDLSLDIKGA 161
UBA2_atUBP14 cd14388
UBA2 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
479-514 2.97e-05

UBA2 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain which show a high level of sequence similarity with mammalian ubiquitin-associated and SH3 domain-containing protein A (UBS3A).


Pssm-ID: 270571  Cd Length: 38  Bit Score: 41.40  E-value: 2.97e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1720405306 479 VAIITSMGFQRNQAVQALQATNHNLERALDWIFSHP 514
Cdd:cd14388     3 VDTLVSFGFAADVARKALKATGGDIERAAEWIFNNS 38
UBA1_Rad23_like cd14280
UBA1 domain of Rad23 proteins found in eukaryotes; The Rad23 family includes the yeast ...
476-512 3.06e-05

UBA1 domain of Rad23 proteins found in eukaryotes; The Rad23 family includes the yeast nucleotide excision repair (NER) proteins, Rad23p (in Saccharomyces cerevisiae) and Rhp23p (in Schizosaccharomyces pombe), their mammalian orthologs HR23A and HR23B, and putative DNA repair proteins from plants. Rad23 proteins play dual roles in DNA repair as well as in proteosomal degradation. They have affinity for both the proteasome and ubiquitinylated proteins and participate in translocating polyubiquitinated proteins to the proteasome. Rad23 proteins carry a ubiquitin-like (UBL) and two ubiquitin-associated (UBA) domains, as well as a xeroderma pigmentosum group C (XPC) protein-binding domain. UBL domain is responsible for the binding to proteasome. UBA domains are important for binding of ubiquitin (Ub) or multi-ubiquitinated substrates which suggests Rad23 proteins might be involved in certain pathways of ubiquitin metabolism. Both UBL domain and XPC-binding domain are necessary for efficient NER function of Rad23 proteins. This model corresponds to the UBA1 domain.


Pssm-ID: 270466  Cd Length: 39  Bit Score: 41.45  E-value: 3.06e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1720405306 476 EEIVAIITSMGFQRNQAVQALQATNHNLERALDWIFS 512
Cdd:cd14280     3 EATINNIMSMGFEREQVVRALRAAFNNPDRAVEYLLS 39
UBA_scDdi1_like cd14309
UBA domain found in Saccharomyces cerevisiae DNA-damage response protein Ddi1 and similar ...
476-506 3.46e-05

UBA domain found in Saccharomyces cerevisiae DNA-damage response protein Ddi1 and similar proteins; Ddi1, also called v-SNARE-master 1 (Vsm1), is a ubiquitin receptor involved in regulation of the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as a ubiquitin association domain (UBA)- ubiquitin-like-domain (UBL) shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. Ddi1 contains an N-terminal UBL domain and a C-terminal UBA domain. It also harbors a central retroviral aspartyl-protease-like domain (RVP) which may be important in cell-cycle control. At this point, Ddi1 may function proteolytically during regulated protein turnover in the cell. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also called transporter regulator RS1 (RS1) which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1.


Pssm-ID: 270494  Cd Length: 36  Bit Score: 40.98  E-value: 3.46e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1720405306 476 EEIVAIITSMGFQRNQAVQALQATNHNLERA 506
Cdd:cd14309     1 EEKIAQLMDLGFSREEAIQALEATNGNVELA 31
UBA_TDRD3 cd14282
UBA domain of Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a ...
476-512 4.60e-05

UBA domain of Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a modular protein containing Tudor domain, a DUF/OB-fold motif and a ubiquitin-associated (UBA) domain. It shows both nucleic acid- and methyl-binding properties and can interact with methylated RNA-binding proteins, such as fragile X mental retardation protein (FMRP) and DEAD/H box-3 (also known as DDX3X/Y, DBX/Y, HLP2 and DDX14) which is implicated in human genetic diseases. At this point, TDRD3 may play a central role in RNA processing regulatory pathways involving arginine methylation. TDRD3 localizes predominantly to the cytoplasm stress granules (SGs). The Tudor domain is essential and sufficient for its recruitment to SGs.


Pssm-ID: 270468  Cd Length: 39  Bit Score: 41.00  E-value: 4.60e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1720405306 476 EEIVAIITSMGFQRNQAVQALQATNHNLERALDWIFS 512
Cdd:cd14282     3 EKALRHITEMGFSKEAARQALMDNNNNLEAALNFLLT 39
UBA2_KPC2 cd14304
UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
474-512 4.67e-05

UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins; KPC2, also called ubiquitin-associated domain-containing protein 1 (UBAC1), or glialblastoma cell differentiation-related protein 1, is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains a ubiquitin-like (UBL) domain and two ubiquitin-associated (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270489  Cd Length: 39  Bit Score: 40.70  E-value: 4.67e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720405306 474 PPEEIVAIITSMGFQRNQAVQALQATNHNLERALDWIFS 512
Cdd:cd14304     1 PNPRAVQSLMEMGFEEEDVLEALRVTRNNQNAACEWLLG 39
UBA_UBS3B cd14301
UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and ...
481-513 6.32e-05

UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and similar proteins; UBS3B, or Cbl-interacting protein p70, suppressor of T-cell receptor signaling 1 (Sts-1), T-cell ubiquitin ligand 2 (TULA-2), or tyrosine-protein phosphatase STS1/TULA2, is ubiquitously expressed in mammalian tissues in a variety of cell types. It exhibits high phosphatase activity, but demonstrates no proapoptotic activity. It negatively regulates the tyrosine kinase Zap-70 activation and T cell receptor (TCR) signaling pathways that modulate T cell activation. Moreover, UBS3B acts as a Cbl- and ubiquitin-interacting protein that inhibits endocytosis of epidermal growth factor receptor (EGFR) and platelet-derived growth factor receptor.


Pssm-ID: 270486 [Multi-domain]  Cd Length: 38  Bit Score: 40.50  E-value: 6.32e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1720405306 481 IITSMGFQRNQAVQALQAT-NHNLERALDWIFSH 513
Cdd:cd14301     5 VLLSMGFPKHRAEKALAATgGRSVQLASDWLLSH 38
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
83-111 9.56e-05

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 45.63  E-value: 9.56e-05
                           10        20
                   ....*....|....*....|....*....
gi 1720405306   83 GYTGLKNLGNSCYLSSVMQAIFSIPEFQR 111
Cdd:COG5077    192 GYVGLRNQGATCYMNSLLQSLFFIAKFRK 220
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
476-515 1.12e-04

UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270481 [Multi-domain]  Cd Length: 45  Bit Score: 40.05  E-value: 1.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720405306 476 EEIVAIITSMGFQRNQAVQALQAT-NHNLERALDWIFSHPE 515
Cdd:cd14295     2 QELVAQLMEMGFPKVRAEKALFFTqNKGLEEAMEWLEEHSE 42
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
485-514 1.17e-04

UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, also called ARF-binding protein 1 (ARF-BP1), HECT, UBA and WWE domain-containing protein 1, homologous to E6AP carboxyl terminus homologs protein 9 (HectH9), large structure of UREB1 (LASU1), Mcl-1 ubiquitin ligase E3 (Mule), upstream regulatory element-binding protein 1 (URE-B1), or URE-binding protein 1, may function as a ubiquitin-protein ligase that involves in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase and modulates base excision repair (BER). HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involving in DNA damage-induced apoptosis. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation. HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N-terminus and a HECT domain at the C-terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain involves in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway. It also controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein.


Pssm-ID: 270474  Cd Length: 40  Bit Score: 39.69  E-value: 1.17e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1720405306 485 MGFQRNQAVQALQATNhNLERALDWIFSHP 514
Cdd:cd14288    12 MGFTREHALEALLHTS-TLEQATEYLLTHP 40
UBA_UBAC2 cd14305
UBA domain found in ubiquitin-associated domain-containing protein 2 (UBAC2) and similar ...
474-506 2.50e-04

UBA domain found in ubiquitin-associated domain-containing protein 2 (UBAC2) and similar proteins; UBAC2, also called phosphoglycerate dehydrogenase-like protein 1, is a ubiquitin-associated domain (UBA)-domain containing protein encoded by gene UBAC2 (or PHGDHL1), a risk gene for Behcet's disease (BD). It may play an important role in the development of BD through its transcriptional modulation. Members in this family contain an N-terminal rhomboid-like domain and a C-terminal UBA domain.


Pssm-ID: 270490  Cd Length: 38  Bit Score: 38.87  E-value: 2.50e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720405306 474 PPEEIVAIITSMGFQRNQAVQALQATNHNLERA 506
Cdd:cd14305     1 PSEEQVQQLVDMGFSREDVLEALRQSNNDVNAA 33
UBA_UBS3A_like cd14300
UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and ...
484-513 4.21e-04

UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and similar proteins; UBS3A, also called Cbl-interacting protein 4 (CLIP4), suppressor of T-cell receptor signaling 2 (Sts-2), or T-cell ubiquitin ligand 1 (TULA-1), is a lymphoid protein only detected in thymus, spleen, and bone marrow. UBS3A exhibits extremely low phosphatase activity, but is capable of promoting T-cell apoptosis independent of either T cell receptor (TCR)/CD3-mediated signaling or caspase activity. It functions as a negative regulator of TCR signaling. UBS3A can also inhibit HIV-1 biogenesis through the binding of ATP-binding cassette protein family E member 1 (ABCE-1), a host factor of HIV-1 assembly. Moreover, UBS3A acts as the Cbl- and ubiquitin-interacting protein that can inhibit endocytosis and downregulation of ligand-activated epidermal growth factor receptor (EGFR) by impairing Cbl-induced ubiquitination, as well as inhibit clathrin-dependent endocytosis in general. This family also includes Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and some uncharacterized AAA-type ATPase-like proteins found in plants.


Pssm-ID: 270485  Cd Length: 37  Bit Score: 37.91  E-value: 4.21e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1720405306 484 SMGFQRNQAVQALQAT-NHNLERALDWIFSH 513
Cdd:cd14300     6 AMGFPEDVARKALKATgGKSIEKATDWLLSH 36
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
552-604 6.98e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 41.97  E-value: 6.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720405306 552 YELFAFISHMGTSTmSGHYVCHIK-KEGRWVIYNDHKVCAS--ERPPKDLGYMYFY 604
Cdd:cd02660   273 YDLFAVVVHKGTLD-TGHYTAYCRqGDGQWFKFDDAMITRVseEEVLKSQAYLLFY 327
UBA1_KPC2 cd14303
UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
402-442 7.33e-04

UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins; KPC2, also called ubiquitin-associated domain-containing protein 1 (UBAC1), or glialblastoma cell differentiation-related protein 1, is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains a ubiquitin-like (UBL) domain and two ubiquitin-associated (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270488 [Multi-domain]  Cd Length: 41  Bit Score: 37.37  E-value: 7.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720405306 402 IDESSVMQLAEMGFPLEACRKAVYFTGNTgAEVAFNWIIVH 442
Cdd:cd14303     1 VDPEALKQLTEMGFPEARATKALLLNRMS-PTQAMEWLLEH 40
UBA_At3g58460_like cd14287
UBA domain found in uncharacterized protein At3g58460 from Arabidopsis thaliana and its ...
476-510 8.11e-04

UBA domain found in uncharacterized protein At3g58460 from Arabidopsis thaliana and its homologs from other plants; The uncharacterized protein At3g58460 from Arabidopsis thaliana is also known as rhomboid-like protein 15 which is encoded by RBL15 gene. Although the biological function of the family members remains unclear, they all contain an N-terminal rhomboid-like domain and a C-terminal ubiquitin-associated (UBA) domain.


Pssm-ID: 270473 [Multi-domain]  Cd Length: 36  Bit Score: 37.37  E-value: 8.11e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1720405306 476 EEIVAIITSMGFQRNQAVQALQATNHNLERALDWI 510
Cdd:cd14287     1 EALVQSLVAMGFEKHRARRALDAAGGDINTAVEIL 35
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
541-585 1.17e-03

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 41.49  E-value: 1.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720405306 541 EGPRVKDGSGMYELFAFISHMGTSTMSGHYVCHIK---------KEGRWVIYND 585
Cdd:pfam13423 249 DDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseledpTESQWYLFND 302
UBA_II_E2_UBE2K_like cd14313
UBA domain found in vertebrate ubiquitin-conjugating enzyme E2 K (UBE2K), Drosophila ...
482-511 1.50e-03

UBA domain found in vertebrate ubiquitin-conjugating enzyme E2 K (UBE2K), Drosophila melanogaster ubiquitin-conjugating enzyme E2-22 kDa (UbcD4) and similar proteins; UBE2K, also called Huntingtin-interacting protein 2 (HIP-2), ubiquitin carrier protein, ubiquitin-conjugating enzyme E2-25 kDa (E2-25K), or ubiquitin-protein ligase, is a multi-ubiquitinating enzyme with the ability to synthesize Lys48-linked polyubiquitin chains which is involved in the ubiquitin (Ub)-dependent proteolytic pathway. It interacts with the frameshift mutant of ubiquitin B and functions as a crucial factor regulating amyloid-beta neurotoxicity. It has also been characterized as Huntingtin-interacting protein that modulates the neurotoxicity of Amyloid-beta (Abeta), the principal protein involved in Alzheimer's disease pathogenesis. Moreover, E2-25K increases aggregate the formation of expanded polyglutamine proteins and polyglutamine-induced cell death in the pathology of polyglutamine diseases. UbcD4, also called ubiquitin carrier protein, or ubiquitin-protein ligase, is encoded by Drosophila E2 gene which is only expressed in pole cells in embryos. It is a putative E2 enzyme homologous to the Huntingtin interacting protein-2 (HIP2) of human. UbcD4 specifically interacts with the polyubiquitin-binding subunit of the proteasome. This family also includes a putative ubiquitin conjugating enzyme from plasmodium Yoelii (pyUCE). It shows a high level of sequence similarity with UBE2K and may also plays a role in the ubiquitin-mediated protein degradation pathway. All family members are class II E2 conjugating enzymes which contain a C-terminal ubiquitin-associated (UBA) domain in addition to an N-terminal catalytic ubiquitin-conjugating enzyme E2 (UBCc) domain.


Pssm-ID: 270498  Cd Length: 36  Bit Score: 36.53  E-value: 1.50e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1720405306 482 ITSMGFQRNQAVQALQATNHNLERALDWIF 511
Cdd:cd14313     7 LVDMGFDRDEAIVALSSNNWNLERATEYLF 36
UBA_UBS3B cd14301
UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and ...
405-442 1.53e-03

UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and similar proteins; UBS3B, or Cbl-interacting protein p70, suppressor of T-cell receptor signaling 1 (Sts-1), T-cell ubiquitin ligand 2 (TULA-2), or tyrosine-protein phosphatase STS1/TULA2, is ubiquitously expressed in mammalian tissues in a variety of cell types. It exhibits high phosphatase activity, but demonstrates no proapoptotic activity. It negatively regulates the tyrosine kinase Zap-70 activation and T cell receptor (TCR) signaling pathways that modulate T cell activation. Moreover, UBS3B acts as a Cbl- and ubiquitin-interacting protein that inhibits endocytosis of epidermal growth factor receptor (EGFR) and platelet-derived growth factor receptor.


Pssm-ID: 270486 [Multi-domain]  Cd Length: 38  Bit Score: 36.65  E-value: 1.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720405306 405 SSVMQLAEMGFPLEACRKAVYFTGNTGAEVAFNWIIVH 442
Cdd:cd14301     1 SALEVLLSMGFPKHRAEKALAATGGRSVQLASDWLLSH 38
UBA1_HR23B cd14426
UBA1 domain of UV excision repair protein RAD23 homolog B (HR23B) found in vertebrates; HR23B, ...
473-512 1.95e-03

UBA1 domain of UV excision repair protein RAD23 homolog B (HR23B) found in vertebrates; HR23B, also called xeroderma pigmentosum group C (XPC) repair-complementing complex 58 kDa protein (p58), is tightly complexed with XPC protein to form the XPC-HR23B complex. Although it displays a high affinity for both single- and double-stranded DNA, the XPC-HR23B complex functions as a global genome repair (GGR)-specific repair factor that is specifically involved in global genome but not transcription-coupled nucleotide excision repair (NER). HR23B also interacts specifically with S5a subunit of the human 26 S proteasome, and plays an important role in shuttling ubiquitinated cargo proteins to the proteasome. HR23B contains an N-terminal ubiquitin-like (UBL) domain that binds proteasomes and two C-terminal ubiquitin-associated (UBA) domains that bind ubiquitin or multi-ubiquitinated substrates. In addition, it has a XPC protein-binding domain that might be necessary for its efficient NER function. This model corresponds to the UBA1 domain.


Pssm-ID: 270609  Cd Length: 46  Bit Score: 36.65  E-value: 1.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720405306 473 QPPEEIVAIITSMGFQRNQAVQALQATNHNLERALDWIFS 512
Cdd:cd14426     4 QSYENMVTEIMSMGYEREQVIAALRASFNNPDRAVEYLLM 43
UBA1_KPC2 cd14303
UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
474-513 2.72e-03

UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins; KPC2, also called ubiquitin-associated domain-containing protein 1 (UBAC1), or glialblastoma cell differentiation-related protein 1, is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains a ubiquitin-like (UBL) domain and two ubiquitin-associated (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270488 [Multi-domain]  Cd Length: 41  Bit Score: 35.83  E-value: 2.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720405306 474 PPEEIVAIITSMGFQRNQAVQALQATNHNLERALDWIFSH 513
Cdd:cd14303     1 VDPEALKQLTEMGFPEARATKALLLNRMSPTQAMEWLLEH 40
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
552-605 3.43e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 39.88  E-value: 3.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720405306 552 YELFAFISHMGTSTMSGHYVCHIkkegRWVIYNDHKV-----------CASERPPKDLGYMYFYR 605
Cdd:cd02671   272 YRLFAVVMHSGATISSGHYTAYV----RWLLFDDSEVkvteekdfleaLSPNTSSTSTPYLLFYK 332
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
85-106 5.00e-03

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 39.40  E-value: 5.00e-03
                          10        20
                  ....*....|....*....|..
gi 1720405306  85 TGLKNLGNSCYLSSVMQAIFSI 106
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFFTI 23
UBA_PLCs_like cd14323
UBA domain of eukaryotic protein linking integrin-associated protein with cytoskeleton (PLIC) ...
476-511 6.53e-03

UBA domain of eukaryotic protein linking integrin-associated protein with cytoskeleton (PLIC) proteins, Saccharomyces cerevisiae proteins Dsk2p and Gts1p, and similar proteins; The PLIC proteins (or ubiquilins) family contains human homologs of the yeast ubiquitin-like Dsk2 protein, PLIC-1 (also called ubiquilin-1), PLIC-2 (also called ubiquilin-2 or Chap1), PLIC-3 (also called ubiquilin-3) and PLIC-4 (also called ubiquilin-4, Ataxin-1 interacting ubiquitin-like protein, A1Up, Connexin43-interacting protein of 75 kDa, or CIP75), and mouse PLIC proteins. They are ubiquitin-binding adaptor proteins involved in all protein degradation pathways through delivering ubiquitinated substrates to proteasomes. They also promote autophagy-dependent cell survival during nutrient starvation. Saccharomyces cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Gts1p, also called protein LSR1, is encoded by a pleiotropic gene GTS1 in budding yeast. The formation of Gts1p-mediated protein aggregates may induce reactive oxygen species (ROS) production and apoptosis. Gts1p also plays an important role in the regulation of heat and other stress responses under glucose-limited or -depleted conditions in either batch or continuous culture.


Pssm-ID: 270508  Cd Length: 39  Bit Score: 34.68  E-value: 6.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1720405306 476 EEIVAIITSMGFQRNQA-VQALQATNHNLERALDWIF 511
Cdd:cd14323     3 QQQLATLKEMGFNDTEKnLQALSATGGNINLAIERLF 39
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
536-605 7.04e-03

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 39.01  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405306 536 SEAKPEGPRVKDGSGM-----YELFAFISHMGTSTMSGHYVCHIK----------------------KEGRWVIYNDHKV 588
Cdd:cd02664   222 PLEKKEEESGDDGELVtrqvhYRLYAVVVHSGYSSESGHYFTYARdqtdadstgqecpepkdaeendESKNWYLFNDSRV 301
                          90       100
                  ....*....|....*....|....*.
gi 1720405306 589 CASE---------RPPKDLGYMYFYR 605
Cdd:cd02664   302 TFSSfesvqnvtsRFPKDTPYILFYE 327
UBA_UBL7 cd14326
UBA domain found in ubiquitin-like protein 7 (UBL7) and similar proteins; UBL7, also called ...
485-511 7.11e-03

UBA domain found in ubiquitin-like protein 7 (UBL7) and similar proteins; UBL7, also called bone marrow stromal cell ubiquitin-like protein (BMSC-UbP), or ubiquitin-like protein SB132, is a novel ubiquitin-like protein that may play roles in regulation of bone marrow stromal cell (BMSC) function or cell differentiation via an evocator-associated and cell-specific pattern. UBL7 contains an N-terminal ubiquitin domain (UBQ) and a C-terminal ubiquitin-associated (UBA) domain. UBQ domain interacts with 26S proteasome-dependent degradation, and UBA domain links cellular processes and the ubiquitin system.


Pssm-ID: 270511  Cd Length: 38  Bit Score: 34.61  E-value: 7.11e-03
                          10        20
                  ....*....|....*....|....*...
gi 1720405306 485 MGFQRNQ-AVQALQATNHNLERALDWIF 511
Cdd:cd14326    11 MGITDDSlSLRALQATGGDVQAALNLLF 38
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
407-439 8.47e-03

UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270483 [Multi-domain]  Cd Length: 39  Bit Score: 34.38  E-value: 8.47e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720405306 407 VMQLAEMGFPLEACRKAVYFTGNTgAEVAFNWI 439
Cdd:cd14297     4 VKQLVDMGFTEAQARKALRKTNNN-VERAVDWL 35
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
409-443 8.82e-03

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.


Pssm-ID: 270491  Cd Length: 36  Bit Score: 34.34  E-value: 8.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1720405306 409 QLAEMGFPLEACRKAVYFTGNTgAEVAFNWIIVHM 443
Cdd:cd14306     3 KLMELGFPEEDCIRALRACGGN-VEEAANWLLENA 36
 
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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