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Conserved domains on  [gi|383872294|ref|NP_001244771|]
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ubiquitin carboxyl-terminal hydrolase 5 [Macaca mulatta]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 13422570)

ubiquitin carboxyl-terminal hydrolase is a C19 family peptidase that deubiquitinates polyubiquitinated target proteins

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 ...
327-831 1.18e-141

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: 420.96  E-value: 1.18e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 327 GIQNLGNSCYLNSVVQVLFSIPDFQRKYvDKLEKIFQNAPTDPTQDFSTQVAKLGHGLLSGEYSKPVPESgdgervPEQK 406
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRY-DDLENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKPASLK------SEND 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 407 EVQDGIAPRMFKALIGKGHPEFSTNRQQDAQEFFLHLINMVERNCRSSE--NPNEVFRFLVEEKIKCLATEKVKYTQRVD 484
Cdd:cd02658   74 PYQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLglNPNDLFKFMIEDRLECLSCKKVKYTSELS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 485 YIMQLPVPMDAAlnkeelleyeekkrqAEEEKmplPELVRAQVPFSSCLEAYGAPEQVDDFWSTaLQAKSVAVKTTRFAS 564
Cdd:cd02658  154 EILSLPVPKDEA---------------TEKEE---GELVYEPVPLEDCLKAYFAPETIEDFCST-CKEKTTATKTTGFKT 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 565 FPDYLVIQIKKFTFGLDWVPKKLDVSIEMPEELdisqlrgtglqpgeeelpdiapplvtpdepkapmldesviiqlvemg 644
Cdd:cd02658  215 FPDYLVINMKRFQLLENWVPKKLDVPIDVPEEL----------------------------------------------- 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 645 fpmdacrkavyytgnsgaeaamnwvmshmddpdfanplilpgssgpgstsaaadpppedcvttivsmgfsrdqalkalra 724
Cdd:cd02658      --------------------------------------------------------------------------------
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 725 tnnsleravdwifshiddldaeaamdisegrsaadsisesvpvgpkvrdGPGKYQLFAFISHMGTSTMCGHYVCHIKK-- 802
Cdd:cd02658  248 -------------------------------------------------GPGKYELIAFISHKGTSVHSGHYVAHIKKei 278
                        490       500       510
                 ....*....|....*....|....*....|...
gi 383872294 803 --EGRWVIYNDQKVCASEKPP--KDLGYIYFYQ 831
Cdd:cd02658  279 dgEGKWVLFNDEKVVASQDPPemKKLGYIYFYQ 311
zf-UBP_var pfam17807
Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ...
16-79 7.36e-31

Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is related to the pfam02148 domain. However, it has an altered pattern of zinc binding residues.


:

Pssm-ID: 407678  Cd Length: 64  Bit Score: 115.39  E-value: 7.36e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383872294   16 IRVPKAGDRVHKDECAFSFDTPESEGGLYICMNTFLGFGKQYVERHFNKTGQRVYLHLRRTRRL 79
Cdd:pfam17807   1 VRVPSASDRVYKDECIFCFDTPESEGGLFVCLKCFLGFCKKHAQLHFERTGHPVYLNIKRTKKE 64
UBA1_UBP5 cd14383
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
632-679 1.14e-27

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: 105.91  E-value: 1.14e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 383872294 632 LDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFA 679
Cdd:cd14383    2 LDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFA 49
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
700-742 6.49e-23

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: 92.01  E-value: 6.49e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 383872294 700 PPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHIDD 742
Cdd:cd14386    1 VPEEAVAMLVSMGFTRDQAIKALKATDNNVERAADWIFSHPDE 43
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
199-272 1.23e-22

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 91.94  E-value: 1.23e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383872294  199 CSKCDMRENLWLNLTDGSILCGRRYfdgsggNNHAVEHYRETGYPLAVKLGTITpdgadVYSYDEDDMVLDPSL 272
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQ------NSHALEHYEETGHPLAVNLSTLT-----VYCYPCDDYVHDPSL 63
 
Name Accession Description Interval E-value
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
327-831 1.18e-141

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: 420.96  E-value: 1.18e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 327 GIQNLGNSCYLNSVVQVLFSIPDFQRKYvDKLEKIFQNAPTDPTQDFSTQVAKLGHGLLSGEYSKPVPESgdgervPEQK 406
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRY-DDLENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKPASLK------SEND 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 407 EVQDGIAPRMFKALIGKGHPEFSTNRQQDAQEFFLHLINMVERNCRSSE--NPNEVFRFLVEEKIKCLATEKVKYTQRVD 484
Cdd:cd02658   74 PYQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLglNPNDLFKFMIEDRLECLSCKKVKYTSELS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 485 YIMQLPVPMDAAlnkeelleyeekkrqAEEEKmplPELVRAQVPFSSCLEAYGAPEQVDDFWSTaLQAKSVAVKTTRFAS 564
Cdd:cd02658  154 EILSLPVPKDEA---------------TEKEE---GELVYEPVPLEDCLKAYFAPETIEDFCST-CKEKTTATKTTGFKT 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 565 FPDYLVIQIKKFTFGLDWVPKKLDVSIEMPEELdisqlrgtglqpgeeelpdiapplvtpdepkapmldesviiqlvemg 644
Cdd:cd02658  215 FPDYLVINMKRFQLLENWVPKKLDVPIDVPEEL----------------------------------------------- 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 645 fpmdacrkavyytgnsgaeaamnwvmshmddpdfanplilpgssgpgstsaaadpppedcvttivsmgfsrdqalkalra 724
Cdd:cd02658      --------------------------------------------------------------------------------
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 725 tnnsleravdwifshiddldaeaamdisegrsaadsisesvpvgpkvrdGPGKYQLFAFISHMGTSTMCGHYVCHIKK-- 802
Cdd:cd02658  248 -------------------------------------------------GPGKYELIAFISHKGTSVHSGHYVAHIKKei 278
                        490       500       510
                 ....*....|....*....|....*....|...
gi 383872294 803 --EGRWVIYNDQKVCASEKPP--KDLGYIYFYQ 831
Cdd:cd02658  279 dgEGKWVLFNDEKVVASQDPPemKKLGYIYFYQ 311
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
326-616 4.44e-51

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 181.49  E-value: 4.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294  326 TGIQNLGNSCYLNSVVQVLFSIPDFqRKYVDKLEKIFQNAPTDPTQDFSTQVAKLGHGLLSGEYSKPVPesgdgervpeq 405
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPF-RDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVS----------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294  406 kevqdgiaPRMFKALIGKGHPEFSTNRQQDAQEFFLHLINMVERNC------RSSENPNEVFRFLVEEKIKCLATEKVKY 479
Cdd:pfam00443  69 --------PKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLngnhstENESLITDLFRGQLKSRLKCLSCGEVSE 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294  480 TQRVDYIMQLPVPMDaalnkeelleyeekkrQAEEEKMPLPElvrAQVPFSSCLEaygaPEQVDDFWSTALQAKSVAVKT 559
Cdd:pfam00443 141 TFEPFSDLSLPIPGD----------------SAELKTASLQI---CFLQFSKLEE----LDDEEKYYCDKCGCKQDAIKQ 197
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 383872294  560 TRFASFPDYLVIQIKKFTFGLdWVPKKLDVSIEMPEELDISQLRGTGLQPGEEELPD 616
Cdd:pfam00443 198 LKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD 253
zf-UBP_var pfam17807
Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ...
16-79 7.36e-31

Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is related to the pfam02148 domain. However, it has an altered pattern of zinc binding residues.


Pssm-ID: 407678  Cd Length: 64  Bit Score: 115.39  E-value: 7.36e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383872294   16 IRVPKAGDRVHKDECAFSFDTPESEGGLYICMNTFLGFGKQYVERHFNKTGQRVYLHLRRTRRL 79
Cdd:pfam17807   1 VRVPSASDRVYKDECIFCFDTPESEGGLFVCLKCFLGFCKKHAQLHFERTGHPVYLNIKRTKKE 64
UBA1_UBP5 cd14383
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
632-679 1.14e-27

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: 105.91  E-value: 1.14e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 383872294 632 LDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFA 679
Cdd:cd14383    2 LDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFA 49
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
700-742 6.49e-23

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: 92.01  E-value: 6.49e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 383872294 700 PPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHIDD 742
Cdd:cd14386    1 VPEEAVAMLVSMGFTRDQAIKALKATDNNVERAADWIFSHPDE 43
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
199-272 1.23e-22

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 91.94  E-value: 1.23e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383872294  199 CSKCDMRENLWLNLTDGSILCGRRYfdgsggNNHAVEHYRETGYPLAVKLGTITpdgadVYSYDEDDMVLDPSL 272
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQ------NSHALEHYEETGHPLAVNLSTLT-----VYCYPCDDYVHDPSL 63
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
198-253 8.37e-18

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 77.79  E-value: 8.37e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 383872294   198 KCSKCDMRENLWLNLTDGSILCGRryfdgsGGNNHAVEHYRETGYPLAVKLGTITP 253
Cdd:smart00290   1 RCSVCGTIENLWLCLTCGQVGCGR------YQNGHALEHFEETGHPLVVKLGTQRV 50
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
700-736 1.59e-11

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: 59.38  E-value: 1.59e-11
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 383872294  700 PPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWI 736
Cdd:pfam00627   1 EDEEAIQRLVEMGFDREQVREALRATGNNVERAAEYL 37
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
290-445 1.57e-10

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 64.90  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 290 DKTMTELEIDMNQRIGEW---ELIQESGVPLKPLFGPGytGIQNLGNSCYLNSVVQVLFSIPDFqRKYV--DKLEK-IFQ 363
Cdd:COG5560  229 FEDRSVLLLSKITRNPDWlvdSIVDDHNRSINKEAGTC--GLRNLGNTCYMNSALQCLMHTWEL-RDYFlsDEYEEsINE 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 364 NAPtdptqdfstqvakLG-HGLLSGEYSKPVPESGDGErvpeqkevQDGIAPRMFKALIGKGHPEFSTNRQQDAQEFFLH 442
Cdd:COG5560  306 ENP-------------LGmHGSVASAYADLIKQLYDGN--------LHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAF 364

                 ...
gi 383872294 443 LIN 445
Cdd:COG5560  365 LLD 367
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
633-668 5.08e-09

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: 52.44  E-value: 5.08e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 383872294  633 DESVIIQLVEMGFPMDACRKAVYYTGNsGAEAAMNW 668
Cdd:pfam00627   2 DEEAIQRLVEMGFDREQVREALRATGN-NVERAAEY 36
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
705-737 9.03e-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: 51.72  E-value: 9.03e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 383872294   705 VTTIVSMGFSRDQALKALRATNNSLERAVDWIF 737
Cdd:smart00165   5 IDQLLEMGFSREEALKALRAANGNVERAAEYLL 37
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
633-670 3.29e-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: 44.40  E-value: 3.29e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 383872294   633 DESVIIQLVEMGFPMDACRKAVYYTGNSgAEAAMNWVM 670
Cdd:smart00165   1 DEEKIDQLLEMGFSREEALKALRAANGN-VERAAEYLL 37
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
676-762 2.31e-05

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 47.58  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294  676 PDFANPLILPGSSGPGSTSA-AADPPPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHI-DDLDAEAAMDISE 753
Cdd:TIGR00601 130 TAPESPSTSVPSSGSDAASTlVVGSERETTIEEIMEMGYEREEVERALRAAFNNPDRAVEYLLTGIpEDPEQPEPVQQTA 209

                  ....*....
gi 383872294  754 GRSAADSIS 762
Cdd:TIGR00601 210 ASTAAATTE 218
 
Name Accession Description Interval E-value
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
327-831 1.18e-141

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: 420.96  E-value: 1.18e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 327 GIQNLGNSCYLNSVVQVLFSIPDFQRKYvDKLEKIFQNAPTDPTQDFSTQVAKLGHGLLSGEYSKPVPESgdgervPEQK 406
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRY-DDLENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKPASLK------SEND 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 407 EVQDGIAPRMFKALIGKGHPEFSTNRQQDAQEFFLHLINMVERNCRSSE--NPNEVFRFLVEEKIKCLATEKVKYTQRVD 484
Cdd:cd02658   74 PYQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLglNPNDLFKFMIEDRLECLSCKKVKYTSELS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 485 YIMQLPVPMDAAlnkeelleyeekkrqAEEEKmplPELVRAQVPFSSCLEAYGAPEQVDDFWSTaLQAKSVAVKTTRFAS 564
Cdd:cd02658  154 EILSLPVPKDEA---------------TEKEE---GELVYEPVPLEDCLKAYFAPETIEDFCST-CKEKTTATKTTGFKT 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 565 FPDYLVIQIKKFTFGLDWVPKKLDVSIEMPEELdisqlrgtglqpgeeelpdiapplvtpdepkapmldesviiqlvemg 644
Cdd:cd02658  215 FPDYLVINMKRFQLLENWVPKKLDVPIDVPEEL----------------------------------------------- 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 645 fpmdacrkavyytgnsgaeaamnwvmshmddpdfanplilpgssgpgstsaaadpppedcvttivsmgfsrdqalkalra 724
Cdd:cd02658      --------------------------------------------------------------------------------
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 725 tnnsleravdwifshiddldaeaamdisegrsaadsisesvpvgpkvrdGPGKYQLFAFISHMGTSTMCGHYVCHIKK-- 802
Cdd:cd02658  248 -------------------------------------------------GPGKYELIAFISHKGTSVHSGHYVAHIKKei 278
                        490       500       510
                 ....*....|....*....|....*....|...
gi 383872294 803 --EGRWVIYNDQKVCASEKPP--KDLGYIYFYQ 831
Cdd:cd02658  279 dgEGKWVLFNDEKVVASQDPPemKKLGYIYFYQ 311
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
326-616 4.44e-51

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 181.49  E-value: 4.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294  326 TGIQNLGNSCYLNSVVQVLFSIPDFqRKYVDKLEKIFQNAPTDPTQDFSTQVAKLGHGLLSGEYSKPVPesgdgervpeq 405
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPF-RDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVS----------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294  406 kevqdgiaPRMFKALIGKGHPEFSTNRQQDAQEFFLHLINMVERNC------RSSENPNEVFRFLVEEKIKCLATEKVKY 479
Cdd:pfam00443  69 --------PKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLngnhstENESLITDLFRGQLKSRLKCLSCGEVSE 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294  480 TQRVDYIMQLPVPMDaalnkeelleyeekkrQAEEEKMPLPElvrAQVPFSSCLEaygaPEQVDDFWSTALQAKSVAVKT 559
Cdd:pfam00443 141 TFEPFSDLSLPIPGD----------------SAELKTASLQI---CFLQFSKLEE----LDDEEKYYCDKCGCKQDAIKQ 197
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 383872294  560 TRFASFPDYLVIQIKKFTFGLdWVPKKLDVSIEMPEELDISQLRGTGLQPGEEELPD 616
Cdd:pfam00443 198 LKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD 253
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
327-831 7.95e-32

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: 124.90  E-value: 7.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 327 GIQNLGNSCYLNSVVQVLFSipdfqrkyvdklekifqnaptdptqdfstqvaklghgllsgeyskpvpesgdgervpeqk 406
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 407 evqdgiaprmfkaligkghpefstnRQQDAQEFFLHLINMVERNC-----------RSSENPNEVFRFLVEEKIKCLATE 475
Cdd:cd02257   21 -------------------------EQQDAHEFLLFLLDKLHEELkksskrtsdssSLKSLIHDLFGGKLESTIVCLECG 75
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 476 KVKYTQRVDYIMQLPVPMDAALnkeelleyeekkrqaeeekmplpelvraQVPFSSCLEAYGAPEQVDDFWSTA--LQAK 553
Cdd:cd02257   76 HESVSTEPELFLSLPLPVKGLP----------------------------QVSLEDCLEKFFKEEILEGDNCYKceKKKK 127
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 554 SVAVKTTRFASFPDYLVIQIKKFTFGLDWVPKKLDVSIEMPEELDISQLrgtglqpgeeelpdiapplvtpdepkapmld 633
Cdd:cd02257  128 QEATKRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPY------------------------------- 176
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 634 esviiqlvemgfpmdacrkavyytgnsgaeaamnwvMSHMDDPDFANplilpgssgpgstsaaadpppedcvttivsmgf 713
Cdd:cd02257  177 ------------------------------------LSEGEKDSDSD--------------------------------- 187
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 714 srdqalkalratnnsleravdwifshiddldaeaamdisegrsaadsisesvpvgpkvrDGPGKYQLFAFISHMGTSTMC 793
Cdd:cd02257  188 -----------------------------------------------------------NGSYKYELVAVVVHSGTSADS 208
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 383872294 794 GHYVCHIKK--EGRWVIYNDQKVCASEK-------PPKDLGYIYFYQ 831
Cdd:cd02257  209 GHYVAYVKDpsDGKWYKFNDDKVTEVSEeevlefgSLSSSAYILFYE 255
zf-UBP_var pfam17807
Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ...
16-79 7.36e-31

Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is related to the pfam02148 domain. However, it has an altered pattern of zinc binding residues.


Pssm-ID: 407678  Cd Length: 64  Bit Score: 115.39  E-value: 7.36e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383872294   16 IRVPKAGDRVHKDECAFSFDTPESEGGLYICMNTFLGFGKQYVERHFNKTGQRVYLHLRRTRRL 79
Cdd:pfam17807   1 VRVPSASDRVYKDECIFCFDTPESEGGLFVCLKCFLGFCKKHAQLHFERTGHPVYLNIKRTKKE 64
UBA1_UBP5 cd14383
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
632-679 1.14e-27

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: 105.91  E-value: 1.14e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 383872294 632 LDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFA 679
Cdd:cd14383    2 LDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFA 49
UBA1_UBP5_like cd14294
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; ...
634-677 7.77e-26

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: 100.46  E-value: 7.77e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 383872294 634 ESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPD 677
Cdd:cd14294    1 EAVVSQLAEMGFPLEACRKAVYHTNNSGLEAAMNWIMEHMDDPD 44
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
700-742 6.49e-23

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: 92.01  E-value: 6.49e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 383872294 700 PPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHIDD 742
Cdd:cd14386    1 VPEEAVAMLVSMGFTRDQAIKALKATDNNVERAADWIFSHPDE 43
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
199-272 1.23e-22

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 91.94  E-value: 1.23e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383872294  199 CSKCDMRENLWLNLTDGSILCGRRYfdgsggNNHAVEHYRETGYPLAVKLGTITpdgadVYSYDEDDMVLDPSL 272
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQ------NSHALEHYEETGHPLAVNLSTLT-----VYCYPCDDYVHDPSL 63
UBA1_UBP13 cd14384
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
632-679 6.43e-19

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: 80.84  E-value: 6.43e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 383872294 632 LDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFA 679
Cdd:cd14384    2 IDESSVMQLAEMGFPLEACRKAVYYTGNMGAEVAFNWIIAHMEEPDFA 49
UBA1_spUBP14_like cd14385
UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
633-677 5.01e-18

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: 78.22  E-value: 5.01e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 383872294 633 DESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPD 677
Cdd:cd14385    1 NAEALAQLLGMGFPEVRCKKALLATGNSDAEAAMNWLFEHMDDPD 45
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
198-253 8.37e-18

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 77.79  E-value: 8.37e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 383872294   198 KCSKCDMRENLWLNLTDGSILCGRryfdgsGGNNHAVEHYRETGYPLAVKLGTITP 253
Cdd:smart00290   1 RCSVCGTIENLWLCLTCGQVGCGR------YQNGHALEHFEETGHPLVVKLGTQRV 50
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
634-672 1.53e-16

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: 73.82  E-value: 1.53e-16
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 383872294 634 ESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSH 672
Cdd:cd14296    1 EEAVSQLMSMGFSENAAKRALYYTGNSSVEAAMNWLFEH 39
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
324-617 1.99e-15

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 78.45  E-value: 1.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 324 GYTGIQNLGNSCYLNSVVQVLFSIPDFqRKYVdklEKIFQNAPTDPTQDFSTQVAKLGHGLLSGEYSKPVPEsgdgervP 403
Cdd:cd02659    1 GYVGLKNQGATCYMNSLLQQLYMTPEF-RNAV---YSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTE-------L 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 404 EQKEVQDGIAPrmfkaligkghpeFSTNRQQDAQEFFLHLINMVERNCRSSENPN---EVFRFLVEEKIKCLatEKVKYT 480
Cdd:cd02659   70 TDKTRSFGWDS-------------LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGlikNLFGGKLVNYIICK--ECPHES 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 481 QRVDYIMQLPVPMdaalnkeelleyeekkrqaeeekMPLPELVRAqvpfsscLEAYGAPEQVDDfwSTALQA-----KSV 555
Cdd:cd02659  135 EREEYFLDLQVAV-----------------------KGKKNLEES-------LDAYVQGETLEG--DNKYFCekcgkKVD 182
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383872294 556 AVKTTRFASFPDYLVIQIKKFTFglDWVPK---KLDVSIEMPEELDISQLRGTGLQPGEEELPDI 617
Cdd:cd02659  183 AEKGVCFKKLPPVLTLQLKRFEF--DFETMmriKINDRFEFPLELDMEPYTEKGLAKKEGDSEKK 245
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
633-677 4.36e-14

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: 67.01  E-value: 4.36e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 383872294 633 DESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPD 677
Cdd:cd14295    1 DQELVAQLMEMGFPKVRAEKALFFTQNKGLEEAMEWLEEHSEDAD 45
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
702-739 1.15e-13

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: 65.58  E-value: 1.15e-13
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSH 739
Cdd:cd14297    1 EDLVKQLVDMGFTEAQARKALRKTNNNVERAVDWLFEG 38
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
327-602 2.46e-13

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 71.59  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 327 GIQNLGNSCYLNSVVQVLFSIPDFQrkyvDKLeKIFQNAPTDPTQDFSTQVAKLGHglLSGEYSKpvpesgdgervpeqk 406
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELR----DAL-KNYNPARRGANQSSDNLTNALRD--LFDTMDK--------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 407 eVQDGIAPRMFKALIGKGHPEFSTN------RQQDAQEFFLHLINMVER----NCRSSENPNEVFRFLVEEKIKCLA--T 474
Cdd:cd02657   59 -KQEPVPPIEFLQLLRMAFPQFAEKqnqggyAQQDAEECWSQLLSVLSQklpgAGSKGSFIDQLFGIELETKMKCTEspD 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 475 EKVKYTQRvDYIMQLPVpmdaalnkeelleyeekkrQAEEEKMPLPELVRAQVpfsscleaygapEQVDDFWSTALQAKS 554
Cdd:cd02657  138 EEEVSTES-EYKLQCHI-------------------SITTEVNYLQDGLKKGL------------EEEIEKHSPTLGRDA 185
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 383872294 555 VAVKTTRFASFPDYLVIQIKKFtFGLDWVPKKLDV--SIEMPEELDISQL 602
Cdd:cd02657  186 IYTKTSRISRLPKYLTVQFVRF-FWKRDIQKKAKIlrKVKFPFELDLYEL 234
UBA1_NUB1_like cd14291
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ...
702-736 4.31e-12

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: 60.93  E-value: 4.31e-12
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNNSLERAVDWI 736
Cdd:cd14291    2 EDKLQQLMEMGFSEAEARLALRACNGNVERAVDYI 36
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
327-601 7.48e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 67.40  E-value: 7.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 327 GIQNLGNSCYLNSVVQVLFSIPDFQRKYvdkLEKIFQNAPTDPT-------------QDFSTQVAKLGHGLLSGEYSkpv 393
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYF---LSDRHSCTCLSCSpnsclscamdeifQEFYYSGDRSPYGPINLLYL--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 394 pesgdgervpeqkevqdgiaprMFKAligkgHPEFSTNRQQDAQEFFLHLINMVERNCRSSENPN-----------EVFR 462
Cdd:cd02660   76 ----------------------SWKH-----SRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEAndeshcnciihQTFS 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 463 FLVEEKIKCLATEKVKYTqrVDYIMQLPVPMDAalnkeelleyeekkrQAEEEKMPLPELVRAQVPFSSCLEAYGAPEQV 542
Cdd:cd02660  129 GSLQSSVTCQRCGGVSTT--VDPFLDLSLDIPN---------------KSTPSWALGESGVSGTPTLSDCLDRFTRPEKL 191
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383872294 543 DDFWS--TALQAKSVAVKTTRFASFPDYLVIQIKKFTFGLDWVPKKLDVSIEMPEELDISQ 601
Cdd:cd02660  192 GDFAYkcSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLELNMTP 252
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
327-600 1.24e-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 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: 66.26  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 327 GIQNLGNSCYLNSVVQVLFSIPdfqrkyvdKLEKIFQNAPTDptqdFSTQVAKLghgllsgeyskpvpesgdgervpeqk 406
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTP--------ALRELLSETPKE----LFSQVCRK-------------------------- 42
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 407 evqdgiaprmfkaligkgHPEFSTNRQQDAQEFFLHL----INMVERncrssenpneVFRFLVEEKIKClatEKVK-YTQ 481
Cdd:cd02667   43 ------------------APQFKGYQQQDSHELLRYLldglRTFIDS----------IFGGELTSTIMC---ESCGtVSL 91
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 482 RVDYIMQLpvpmdaalnkeelleyeekkrqaeeekmPLPELVRAQVPFS--SCLEAYGAPEQVddFWSTALQAKSV--AV 557
Cdd:cd02667   92 VYEPFLDL----------------------------SLPRSDEIKSECSieSCLKQFTEVEIL--EGNNKFACENCtkAK 141
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 383872294 558 KTTRFASFPDYLVIQIKKFTFGLDWVPKKLDVSIEMPEELDIS 600
Cdd:cd02667  142 KQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLA 184
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
700-736 1.59e-11

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: 59.38  E-value: 1.59e-11
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 383872294  700 PPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWI 736
Cdd:pfam00627   1 EDEEAIQRLVEMGFDREQVREALRATGNNVERAAEYL 37
UBA2_UBP13 cd14387
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
702-736 1.78e-11

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: 59.31  E-value: 1.78e-11
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNNSLERAVDWI 736
Cdd:cd14387    1 EESIAILMSMGFPRNRAIEALKRTNNNLDRALDWL 35
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
702-739 7.86e-11

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: 57.64  E-value: 7.86e-11
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNN-SLERAVDWIFSH 739
Cdd:cd14296    1 EEAVSQLMSMGFSENAAKRALYYTGNsSVEAAMNWLFEH 39
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
431-594 8.28e-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 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: 62.69  E-value: 8.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 431 NRQQDAQEFFLHLINMVERNCrssenpNEVFRFLVEEKIKCLATEKVKYTQRVDYIMQLPVPMdaalnkeelleyeekkr 510
Cdd:cd02674   20 ADQQDAQEFLLFLLDGLHSII------VDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPS----------------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 511 qaeeekmplpelVRAQVPFSS---CLEAYGAPEQVDDF--WS-TALQAKSVAVKTTRFASFPDYLVIQIKKFTFGLDWvP 584
Cdd:cd02674   77 ------------GSGDAPKVTledCLRLFTKEETLDGDnaWKcPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGS-T 143
                        170
                 ....*....|
gi 383872294 585 KKLDVSIEMP 594
Cdd:cd02674  144 RKLTTPVTFP 153
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
705-739 1.32e-10

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: 56.92  E-value: 1.32e-10
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 383872294 705 VTTIVSMGFSRDQALKALRATN-NSLERAVDWIFSH 739
Cdd:cd14327    3 VAQLVEMGFSRERAEEALRAVGtNSVELAMEWLFTN 38
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
290-445 1.57e-10

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 64.90  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 290 DKTMTELEIDMNQRIGEW---ELIQESGVPLKPLFGPGytGIQNLGNSCYLNSVVQVLFSIPDFqRKYV--DKLEK-IFQ 363
Cdd:COG5560  229 FEDRSVLLLSKITRNPDWlvdSIVDDHNRSINKEAGTC--GLRNLGNTCYMNSALQCLMHTWEL-RDYFlsDEYEEsINE 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 364 NAPtdptqdfstqvakLG-HGLLSGEYSKPVPESGDGErvpeqkevQDGIAPRMFKALIGKGHPEFSTNRQQDAQEFFLH 442
Cdd:COG5560  306 ENP-------------LGmHGSVASAYADLIKQLYDGN--------LHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAF 364

                 ...
gi 383872294 443 LIN 445
Cdd:COG5560  365 LLD 367
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
635-675 3.28e-10

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: 55.76  E-value: 3.28e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 383872294 635 SVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDD 675
Cdd:cd14302    1 SELQTLIEMGFSRNRAEKALAKTGNQGVEAAMEWLLAHEDD 41
UBA1_spUBP14_like cd14385
UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
702-744 7.42e-10

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: 55.11  E-value: 7.42e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNNS-LERAVDWIFSHIDDLD 744
Cdd:cd14385    2 AEALAQLLGMGFPEVRCKKALLATGNSdAEAAMNWLFEHMDDPD 45
UBA cd14270
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ...
705-734 1.28e-09

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: 53.89  E-value: 1.28e-09
                         10        20        30
                 ....*....|....*....|....*....|
gi 383872294 705 VTTIVSMGFSRDQALKALRATNNSLERAVD 734
Cdd:cd14270    1 LAQLVEMGFSREQARRALRATNGDVEAAVE 30
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
327-598 1.79e-09

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 58.92  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 327 GIQNLGNSCYLNSVVQVLFSIPDFqRKYVDKLekifqnaptdptqdfstqvaklghgllsgeyskpvpesgdgervpeqk 406
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSL-IEYLEEF------------------------------------------------ 31
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 407 evqdgiaprmfkaligkghpefstNRQQDAQEFFLHLINMVERNCRsseNPnevFRFLVEEKIKCLA---TEKVKYTQRv 483
Cdd:cd02662   32 ------------------------LEQQDAHELFQVLLETLEQLLK---FP---FDGLLASRIVCLQcgeSSKVRYESF- 80
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 484 dYIMQLPVPmdaalnkeelleyeekkrqaeEEKMPLPELVraqvpfSSCLEAYGAPEQVDDFWSTALQAKSVAvkttrfa 563
Cdd:cd02662   81 -TMLSLPVP---------------------NQSSGSGTTL------EHCLDDFLSTEIIDDYKCDRCQTVIVR------- 125
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 383872294 564 sFPDYLVIQIKKFTFGLDWVPKKLDVSIEMPEELD 598
Cdd:cd02662  126 -LPQILCIHLSRSVFDGRGTSTKNSCKVSFPERLP 159
UBA_RUP1p cd14307
UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ...
702-739 2.11e-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: 53.45  E-value: 2.11e-09
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSH 739
Cdd:cd14307    1 EEAVASLLEMGIPREVAIEALRETNGDVEAAANYIFSN 38
UBA_PUB_plant cd14290
UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family ...
633-678 3.83e-09

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: 52.83  E-value: 3.83e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 383872294 633 DESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDF 678
Cdd:cd14290    3 NADLLKELEAMGFPRARAVRALHHTGNTSVEAAVNWIVEHENDPDI 48
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
633-668 5.08e-09

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: 52.44  E-value: 5.08e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 383872294  633 DESVIIQLVEMGFPMDACRKAVYYTGNsGAEAAMNW 668
Cdd:pfam00627   2 DEEAIQRLVEMGFDREQVREALRATGN-NVERAAEY 36
UBA2_atUBP14 cd14388
UBA2 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
705-739 6.35e-09

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: 52.18  E-value: 6.35e-09
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 383872294 705 VTTIVSMGFSRDQALKALRATNNSLERAVDWIFSH 739
Cdd:cd14388    3 VDTLVSFGFAADVARKALKATGGDIERAAEWIFNN 37
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
705-737 9.03e-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: 51.72  E-value: 9.03e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 383872294   705 VTTIVSMGFSRDQALKALRATNNSLERAVDWIF 737
Cdd:smart00165   5 IDQLLEMGFSREEALKALRAANGNVERAAEYLL 37
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
327-600 9.50e-09

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 57.82  E-value: 9.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 327 GIQNLGNSCYLNSVVQVLFSIPDFqRKYV--------DKLEKIFQNAPTDPtQDFSTQVAKLgHGLLsgEYSkpvpesgd 398
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEF-RKAVyecnstedAELKNMPPDKPHEP-QTIIDQLQLI-FAQL--QFG-------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 399 gervpeQKEVQDGIAprMFKALigkghpEFSTNRQQDAQEFFLHLINMVERNCRSSENPNEV------FRFLVEEKIKCl 472
Cdd:cd02668   68 ------NRSVVDPSG--FVKAL------GLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKnivqdlFRGEYSYVTQC- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 473 atEKVKYTQRVdyimqlpvpmdaalnkeelleyeekkrqaEEEKMPLPELVRAQVPFSSCLEAYGAPEQVDD---FWSTA 549
Cdd:cd02668  133 --SKCGRESSL-----------------------------PSKFYELELQLKGHKTLEECIDEFLKEEQLTGdnqYFCES 181
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 383872294 550 LQAKSVAVKTTRFASFPDYLVIQIKKFTFGLDWVP-KKLDVSIEMPEELDIS 600
Cdd:cd02668  182 CNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAkKKLNASISFPEILDMG 233
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
774-831 1.59e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 56.14  E-value: 1.59e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383872294 774 GPGKYQLFAFISHMGtSTMCGHYVCHIKKE--GRWVIYNDQKVcaSEKPPKDLG----YIYFYQ 831
Cdd:cd02674  170 GPFKYDLYAVVNHYG-SLNGGHYTAYCKNNetNDWYKFDDSRV--TKVSESSVVsssaYILFYE 230
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-825 1.60e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 57.05  E-value: 1.60e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 383872294 778 YQLFAFISHMGTSTMCGHYVCHIKKE--GRWVIYNDQKVcaSEKPPKDLG 825
Cdd:cd02668  246 YELSGVLIHQGVSAYSGHYIAHIKDEqtGEWYKFNDEDV--EEMPGKPLK 293
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
326-600 3.32e-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: 56.13  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 326 TGIQNLGNSCYLNSVVQVLfsipdfqrkyvdklekifqnaptdptqdfsTQVAKLGHGLLSGEYSKPVPESGDGERVPEQ 405
Cdd:cd02661    2 AGLQNLGNTCFLNSVLQCL------------------------------THTPPLANYLLSREHSKDCCNEGFCMMCALE 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 406 KEVQ-------DGIAPRMFKALIGKGHPEFSTNRQQDAQEFFLHLINMVERNC----RSSENPNEVFR--FLVEE----- 467
Cdd:cd02661   52 AHVEralassgPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKACldrfKKLKAVDPSSQetTLVQQifggy 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 468 ---KIKCLATEKVkyTQRVDYIMQLPVPMDAAlnkeelleyeekkrqaeeekmplPELVRAqvpfsscLEAYGAPEQVDD 544
Cdd:cd02661  132 lrsQVKCLNCKHV--SNTYDPFLDLSLDIKGA-----------------------DSLEDA-------LEQFTKPEQLDG 179
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383872294 545 fwSTALQ-----AKSVAVKTTRFASFPDYLVIQIKKFTFGLDwvpKKLDVSIEMPEELDIS 600
Cdd:cd02661  180 --ENKYKcerckKKVKASKQLTIHRAPNVLTIHLKRFSNFRG---GKINKQISFPETLDLS 235
UBA2_scUBP14_like cd14298
UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
702-739 4.60e-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: 49.76  E-value: 4.60e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSH 739
Cdd:cd14298    1 DEALAQLVSMGFDPEVARKALILTNGNVERAIEWLFSN 38
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
773-830 1.06e-07

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 54.59  E-value: 1.06e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383872294 773 DGPGKYQLFAFISHMGTSTMCGHYVCHIKK-EGRWVIYNDQKV--CASEKPPKDLGYIYFY 830
Cdd:cd02661  243 DGPLKYKLYAVLVHSGFSPHSGHYYCYVKSsNGKWYNMDDSKVspVSIETVLSQKAYILFY 303
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
323-576 1.65e-07

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 54.13  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 323 PGYTGIQNLGNSCYLNSVVQVLFSIPDFQrkyvdklekifqnaptdptqdfsTQVAKLGHGLLSGEYSKPV----PESGD 398
Cdd:cd02671   22 LPFVGLNNLGNTCYLNSVLQVLYFCPGFK-----------------------HGLKHLVSLISSVEQLQSSfllnPEKYN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 399 GERVPEqkevqdgiAPRMFKALIGKGHPEFSTNRQQDAQEFFLHLINMVErncrssENPNEVFRFLVEEKIKCLATEKVK 478
Cdd:cd02671   79 DELANQ--------APRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQ------ELVEKDFQGQLVLRTRCLECETFT 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 479 yTQRVDYI-MQLPVPMDAALNKEELLEYeekkrqAEEEKMPLPELVRAQVPFSSCLEAYGApeqvDDFWSTALQAKSVAV 557
Cdd:cd02671  145 -ERREDFQdISVPVQESELSKSEESSEI------SPDPKTEMKTLKWAISQFASVERIVGE----DKYFCENCHHYTEAE 213
                        250
                 ....*....|....*....
gi 383872294 558 KTTRFASFPDYLVIQIKKF 576
Cdd:cd02671  214 RSLLFDKLPEVITIHLKCF 232
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
327-600 1.89e-07

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 53.65  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 327 GIQNLGNSCYLNSVVQVL-FSIPDFQrKYVDKLEKIFQNaptdptqdfstqvaklghglLSGEYSKPvpesgdgERVPEQ 405
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILaLYLPKLD-ELLDDLSKELKV--------------------LKNVIRKP-------EPDLNQ 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 406 KEvqdgiAPRMFKALIG----KGHPEFSTNRQQDAQEF---FLHLINMVERNCrssenpNEVFRFLVEEKikclatEKVK 478
Cdd:COG5533   53 EE-----ALKLFTALWSskehKVGWIPPMGSQEDAHELlgkLLDELKLDLVNS------FTIRIFKTTKD------KKKT 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 479 YTQRV-DYIMQLPvpmdaalnkeelleyeekKRQAEEEKMPLPELVRAQVPFSSclEAYGAPEQVDDFWStaLQAKSVAV 557
Cdd:COG5533  116 STGDWfDIIIELP------------------DQTWVNNLKTLQEFIDNMEELVD--DETGVKAKENEELE--VQAKQEYE 173
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 383872294 558 KTtrFASFPDYLVIQIKKFTFGLDwvPKKLDVSIEMPEELDIS 600
Cdd:COG5533  174 VS--FVKLPKILTIQLKRFANLGG--NQKIDTEVDEKFELPVK 212
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
705-742 1.96e-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: 48.06  E-value: 1.96e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 383872294 705 VTTIVSMGFSRDQALKALRAT-NNSLERAVDWIFSHIDD 742
Cdd:cd14302    3 LQTLIEMGFSRNRAEKALAKTgNQGVEAAMEWLLAHEDD 41
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
711-739 2.27e-07

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: 47.44  E-value: 2.27e-07
                         10        20
                 ....*....|....*....|....*....
gi 383872294 711 MGFSRDQALKALRATNNSLERAVDWIFSH 739
Cdd:cd14306    7 LGFPEEDCIRALRACGGNVEEAANWLLEN 35
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
777-831 3.38e-07

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 52.70  E-value: 3.38e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383872294 777 KYQLFAFISHMGTSTMCGHYVCHIKKEGRWVIYNDQKVCA----------SEKPPKDLGYIYFYQ 831
Cdd:cd02663  236 LYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVEKidenaveeffGDSPNQATAYVLFYQ 300
UBA_UBS3A_like cd14300
UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and ...
705-739 4.45e-07

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: 46.76  E-value: 4.45e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 383872294 705 VTTIVSMGFSRDQALKALRAT-NNSLERAVDWIFSH 739
Cdd:cd14300    1 LETLLAMGFPEDVARKALKATgGKSIEKATDWLLSH 36
UBA_UBS3B cd14301
UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and ...
703-739 4.72e-07

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: 46.67  E-value: 4.72e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 383872294 703 DCVTTIVSMGFSRDQALKALRAT-NNSLERAVDWIFSH 739
Cdd:cd14301    1 SALEVLLSMGFPKHRAEKALAATgGRSVQLASDWLLSH 38
UBA1_Rad23_like cd14280
UBA1 domain of Rad23 proteins found in eukaryotes; The Rad23 family includes the yeast ...
702-738 7.14e-07

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: 46.45  E-value: 7.14e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFS 738
Cdd:cd14280    3 EATINNIMSMGFEREQVVRALRAAFNNPDRAVEYLLS 39
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
778-832 8.77e-07

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 51.34  E-value: 8.77e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 778 YQLFAFISHMGTSTMcGHYVCHIKKEGRWVIYNDQKVCA-----SEKPPKDLGYIYFYQR 832
Cdd:COG5533  225 YDLVGFVLHQGSLEG-GHYIAYVKKGGKWEKANDSDVTPvseeeAINEKAKNAYLYFYER 283
UBA2_KPC2 cd14304
UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
700-738 8.86e-07

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: 46.10  E-value: 8.86e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 383872294 700 PPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFS 738
Cdd:cd14304    1 PNPRAVQSLMEMGFEEEDVLEALRVTRNNQNAACEWLLG 39
UBA1_Rad23 cd14377
UBA1 domain of Rad23 proteins found in metazoa; The family includes mammalian orthologs of ...
702-738 9.05e-07

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: 45.85  E-value: 9.05e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFS 738
Cdd:cd14377    3 ENMVTEIMSMGFERDQVVRALRASFNNPDRAVEYLLS 39
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
327-464 1.81e-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: 50.95  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294 327 GIQNLGNSCYLNSVVQVLFSIPDFQRKYVdkLEKIFQNAPTDPTQdFSTQVAKLgHGLLSGEYSKPVPEsgdgervpeqk 406
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRRQVL--SLNLPRLGDSQSVM-KKLQLLQA-HLMHTQRRAEAPPD----------- 65
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383872294 407 evqdgiapRMFKALIGkghPEFSTNRQQDAQEFFLHLIN----MVER-------------NCRSSENPNEVFRFL 464
Cdd:cd02664   66 --------YFLEASRP---PWFTPGSQQDCSEYLRYLLDrlhtLIEKmfggklsttirclNCNSTSARTERFRDL 129
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
633-670 3.29e-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: 44.40  E-value: 3.29e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 383872294   633 DESVIIQLVEMGFPMDACRKAVYYTGNSgAEAAMNWVM 670
Cdd:smart00165   1 DEEKIDQLLEMGFSREEALKALRAANGN-VERAAEYLL 37
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
637-673 4.87e-06

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: 43.97  E-value: 4.87e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 383872294 637 IIQLVEMGFPMDACRKAVYYTGNSgAEAAMNWVMSHM 673
Cdd:cd14306    1 VAKLMELGFPEEDCIRALRACGGN-VEEAANWLLENA 36
UBA_UBAC2 cd14305
UBA domain found in ubiquitin-associated domain-containing protein 2 (UBAC2) and similar ...
700-732 6.86e-06

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: 43.49  E-value: 6.86e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 383872294 700 PPEDCVTTIVSMGFSRDQALKALRATNNSLERA 732
Cdd:cd14305    1 PSEEQVQQLVDMGFSREDVLEALRQSNNDVNAA 33
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
705-744 8.95e-06

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: 43.51  E-value: 8.95e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 383872294 705 VTTIVSMGFSRDQALKALRAT-NNSLERAVDWIFSHIDDLD 744
Cdd:cd14295    5 VAQLMEMGFPKVRAEKALFFTqNKGLEEAMEWLEEHSEDAD 45
UBA1_HR23B cd14426
UBA1 domain of UV excision repair protein RAD23 homolog B (HR23B) found in vertebrates; HR23B, ...
702-740 1.48e-05

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: 42.81  E-value: 1.48e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHI 740
Cdd:cd14426    7 ENMVTEIMSMGYEREQVIAALRASFNNPDRAVEYLLMGI 45
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
700-739 1.62e-05

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: 42.39  E-value: 1.62e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 383872294 700 PPEDCVTTIVSMGFSRDQALKALRATnNSLERAVDWIFSH 739
Cdd:cd14288    1 VNEAHLQQLMDMGFTREHALEALLHT-STLEQATEYLLTH 39
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
676-762 2.31e-05

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 47.58  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872294  676 PDFANPLILPGSSGPGSTSA-AADPPPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHI-DDLDAEAAMDISE 753
Cdd:TIGR00601 130 TAPESPSTSVPSSGSDAASTlVVGSERETTIEEIMEMGYEREEVERALRAAFNNPDRAVEYLLTGIpEDPEQPEPVQQTA 209

                  ....*....
gi 383872294  754 GRSAADSIS 762
Cdd:TIGR00601 210 ASTAAATTE 218
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
639-673 2.99e-05

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: 41.70  E-value: 2.99e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 383872294 639 QLVEMGFPMDACRKAVYYTGNSgAEAAMNWVMSHM 673
Cdd:cd14297    6 QLVDMGFTEAQARKALRKTNNN-VERAVDWLFEGP 39
UBA_AAA_plant cd14389
UBA domain found in plant AAA-type ATPase-like proteins; This family includes some ...
708-739 3.87e-05

UBA domain found in plant AAA-type ATPase-like proteins; This family includes some uncharacterized AAA-type ATPase-like proteins found in plant. The AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. Members in this family contains an N-terminal ubiquitin-association (UBA) domain, a AAA-type ATPase domain and a C-terminal MgsA AAA+ ATPase domain. This model corresponds to the UBA domain which show a high level of sequence similarity with mammalian ubiquitin-associated and SH3 domain-containing protein A (UBS3A).


Pssm-ID: 270572  Cd Length: 37  Bit Score: 41.57  E-value: 3.87e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 383872294 708 IVSMGFSRDQALKALRAT-NNSLERAVDWIFSH 739
Cdd:cd14389    4 LVDMGFSSDLAAEALAATgGKSTQKATEWILSH 36
UBA_UBS3A_like cd14300
UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and ...
639-672 6.50e-05

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: 40.60  E-value: 6.50e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 383872294 639 QLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSH 672
Cdd:cd14300    3 TLLAMGFPEDVARKALKATGGKSIEKATDWLLSH 36
UBA1_UBAP1 cd14315
UBA1 domain found in vertebrate ubiquitin-associated protein 1 (UBAP-1); UBAP-1, also called ...
699-739 8.66e-05

UBA1 domain found in vertebrate ubiquitin-associated protein 1 (UBAP-1); UBAP-1, also called nasopharyngeal carcinoma-associated gene 20 protein, is a ubiquitously expressed protein that may play an important role in the ubiquitin pathway and cell progression. It co-localizes with TDP-43 proteins in neuronal cytoplasmic inclusions and acts as a genetic risk factor for frontotemporal lobar degeneration (FTLD). Moreover, UBAP-1, together with VPS37A, forms an endosome-specific endosomal sorting complexes I required for transport (ESCRT-I) complex that displays a restricted cellular function, ubiquitin-dependent endosomal sorting and multivesicular body (MVB) biogenesis. UBAP-1 contains an N-terminal UBAP-1-MVB12-associated (UMA) domain, and two tandem ubiquitin-associated (UBA) domains that may be responsible for the binding of ubiquitin-conjugating enzymes. This model corresponds to UBA1 domain.


Pssm-ID: 270500  Cd Length: 43  Bit Score: 40.61  E-value: 8.66e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 383872294 699 PPPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSH 739
Cdd:cd14315    3 PSERQCVETVVGMGYSYECVLKAMKKKGQNIEQILEYLFAH 43
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
326-347 9.09e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 45.56  E-value: 9.09e-05
                         10        20
                 ....*....|....*....|..
gi 383872294 326 TGIQNLGNSCYLNSVVQVLFSI 347
Cdd:cd02666    2 AGLDNIGNTCYLNSLLQYFFTI 23
UBA1_KPC2 cd14303
UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
700-739 1.20e-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: 40.07  E-value: 1.20e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 383872294 700 PPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSH 739
Cdd:cd14303    1 VDPEALKQLTEMGFPEARATKALLLNRMSPTQAMEWLLEH 40
UBA_PUB_plant cd14290
UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family ...
701-744 1.88e-04

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: 39.73  E-value: 1.88e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 383872294 701 PEDCVTTIVSMGFSRDQALKALRAT-NNSLERAVDWIFSHIDDLD 744
Cdd:cd14290    3 NADLLKELEAMGFPRARAVRALHHTgNTSVEAAVNWIVEHENDPD 47
UBA_atDRM2_like cd14330
UBA domain found in Arabidopsis thaliana DNA (cytosine-5)-methyltransferase DRM2 (atDRM2) and ...
705-738 2.09e-04

UBA domain found in Arabidopsis thaliana DNA (cytosine-5)-methyltransferase DRM2 (atDRM2) and similar proteins; atDRM2, also called protein domains rearranged methylase 2, is a homolog of the mammalian de novo methyltransferase DNMT3. It is the major de novo methyltransferase targeted to DNA by small interfering RNAs (siRNAs) in the RNA-directed DNA methylation (RdDM) pathway in Arabidopsis thaliana. atDRM2 is a part of the RdDM effector complex and plays a catalytic role in RdDM. It contains an N-terminal UBA domains and a C-terminal methyltransferase domain, both of which are required for normal RdDM.


Pssm-ID: 270515  Cd Length: 37  Bit Score: 39.35  E-value: 2.09e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 383872294 705 VTTIVSMGFSRDQALKALRATNNSLERAVDWIFS 738
Cdd:cd14330    4 IKTLVSMGFSESDARRALERCGYDVAAAADFLFS 37
UBA1_KPC2 cd14303
UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
633-672 2.10e-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: 39.30  E-value: 2.10e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 383872294 633 DESVIIQLVEMGFPMDACRKAVYYTGNSgAEAAMNWVMSH 672
Cdd:cd14303    2 DPEALKQLTEMGFPEARATKALLLNRMS-PTQAMEWLLEH 40
UBA_At3g58460_like cd14287
UBA domain found in uncharacterized protein At3g58460 from Arabidopsis thaliana and its ...
705-736 2.24e-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: 39.29  E-value: 2.24e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 383872294 705 VTTIVSMGFSRDQALKALRATNNSLERAVDWI 736
Cdd:cd14287    4 VQSLVAMGFEKHRARRALDAAGGDINTAVEIL 35
UBA_scDdi1_like cd14309
UBA domain found in Saccharomyces cerevisiae DNA-damage response protein Ddi1 and similar ...
702-732 3.25e-04

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: 38.67  E-value: 3.25e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNNSLERA 732
Cdd:cd14309    1 EEKIAQLMDLGFSREEAIQALEATNGNVELA 31
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
776-823 3.79e-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 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: 43.47  E-value: 3.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 383872294 776 GKYQLFAFISHMGTSTMCGHYVCHIKKE--GRWVIYNDQKVcaSEKPPKD 823
Cdd:cd02657  239 GYYELVAVITHQGRSADSGHYVAWVRRKndGKWIKFDDDKV--SEVTEED 286
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
324-359 4.13e-04

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 44.09  E-value: 4.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 383872294  324 GYTGIQNLGNSCYLNSVVQVLFSIPDFqRKYVDKLE 359
Cdd:COG5077   192 GYVGLRNQGATCYMNSLLQSLFFIAKF-RKDVYGIP 226
UBA_UBS3B cd14301
UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and ...
640-672 4.52e-04

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: 38.19  E-value: 4.52e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 383872294 640 LVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSH 672
Cdd:cd14301    6 LLSMGFPKHRAEKALAATGGRSVQLASDWLLSH 38
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
633-675 5.73e-04

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: 38.08  E-value: 5.73e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 383872294 633 DESVIIQLVEMGFPMDACRKAVYYTGNSgAEAAMNWVMSHMDD 675
Cdd:cd14386    2 PEEAVAMLVSMGFTRDQAIKALKATDNN-VERAADWIFSHPDE 43
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
635-672 6.01e-04

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: 38.05  E-value: 6.01e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 383872294 635 SVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSH 672
Cdd:cd14327    1 EAVAQLVEMGFSRERAEEALRAVGTNSVELAMEWLFTN 38
UBA_TDRD3 cd14282
UBA domain of Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a ...
702-738 6.05e-04

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: 37.91  E-value: 6.05e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFS 738
Cdd:cd14282    3 EKALRHITEMGFSKEAARQALMDNNNNLEAALNFLLT 39
UBA_Mud1_like cd14308
UBA domain found in Schizosaccharomyces pombe UBA domain-containing protein mud1 and similar ...
702-736 7.44e-04

UBA domain found in Schizosaccharomyces pombe UBA domain-containing protein mud1 and similar proteins; Schizosaccharomyces pombe mud1 is an ortholog of the Saccharomyces cerevisiae DNA-damage response protein Ddi1. S. cerevisiae Ddi1, also called v-SNARE-master 1 (Vsm1), belongs to a family of proteins known as the ubiquitin receptors which can bind ubiquitinated substrates and the proteasome. It is involved in the degradation of the F-box protein Ufo1, involved in the G1/S transition. It also participates in Mec1-mediated degradation of Ho endonuclease. Both S. pombe mud1 and S. cerevisiae Ddi1 contain an N-terminal ubiquitin-like (UBL) domain, an aspartyl protease-like domain, and a C-terminal ubiquitin-associated (UBA) domain. S. pombe mud1 binds to K48-linked polyubiquitin (polyUb) through UBA domain.


Pssm-ID: 270493  Cd Length: 36  Bit Score: 37.86  E-value: 7.44e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNNSLERAVDWI 736
Cdd:cd14308    1 PEKVRQLVDMGFTPTDAGRALKAANGDVTVAAEWL 35
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
632-672 8.35e-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: 37.76  E-value: 8.35e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 383872294 632 LDESVIIQLVEMGFPMDACRKAVYYTgnSGAEAAMNWVMSH 672
Cdd:cd14288    1 VNEAHLQQLMDMGFTREHALEALLHT--STLEQATEYLLTH 39
UBA_II_E2_UBE2K_like cd14313
UBA domain found in vertebrate ubiquitin-conjugating enzyme E2 K (UBE2K), Drosophila ...
702-737 9.09e-04

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: 37.30  E-value: 9.09e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIF 737
Cdd:cd14313    1 KKKVDKLVDMGFDRDEAIVALSSNNWNLERATEYLF 36
UBA1_Rhp23p_like cd14378
UBA1 domain of Schizosaccharomyces pombe UV excision repair protein Rhp23p and its homologs; ...
705-740 1.25e-03

UBA1 domain of Schizosaccharomyces pombe UV excision repair protein Rhp23p and its homologs; The subfamily contains several fungal multi-ubiquitin receptors, including Schizosaccharomyces pombe Rhp23p and Saccharomyces cerevisiae Rad23p, both of which are orthologs of human HR23A. They play roles in nucleotide excision repair (NER) and in cell cycle regulation. They also function as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. For instance, S. pombe Rhp23p forms a complex with Rhp41p to recognize photolesions and help initiate DNA repair, and it also protects ubiquitin chains against disassembly by deubiquitinating enzymes. Like human HR23A, members in this subfamily interact with the proteasome through their N-terminal ubiquitin-like domain (UBL), and with ubiquitin (Ub), or multi-ubiquitinated substrates, through their two ubiquitin-associated domains (UBA), termed internal UBA1 and C-terminal UBA2. In addition, they contain a xeroderma pigmentosum group C (XPC) protein-binding domain that might be necessary for its efficient NER function. This model corresponds to the UBA1 domain.


Pssm-ID: 270561  Cd Length: 47  Bit Score: 37.44  E-value: 1.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 383872294 705 VTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHI 740
Cdd:cd14378   11 VQNIMEMGYEREQVERALRASFNNPDRAVEYLLTGI 46
UBA_AAA_plant cd14389
UBA domain found in plant AAA-type ATPase-like proteins; This family includes some ...
639-672 1.46e-03

UBA domain found in plant AAA-type ATPase-like proteins; This family includes some uncharacterized AAA-type ATPase-like proteins found in plant. The AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. Members in this family contains an N-terminal ubiquitin-association (UBA) domain, a AAA-type ATPase domain and a C-terminal MgsA AAA+ ATPase domain. This model corresponds to the UBA domain which show a high level of sequence similarity with mammalian ubiquitin-associated and SH3 domain-containing protein A (UBS3A).


Pssm-ID: 270572  Cd Length: 37  Bit Score: 36.95  E-value: 1.46e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 383872294 639 QLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSH 672
Cdd:cd14389    3 QLVDMGFSSDLAAEALAATGGKSTQKATEWILSH 36
UBA1_Rad23_plant cd14379
UBA1 domain of putative DNA repair proteins Rad23 found in plant; The radiation sensitive 23 ...
702-740 1.63e-03

UBA1 domain of putative DNA repair proteins Rad23 found in plant; The radiation sensitive 23 (Rad23) subfamily consists of four isoforms of putative DNA repair proteins from Arabidopsis thaliana and similar proteins from other plants. The nuclear-enriched Rad23 proteins function in the cell cycle, morphology, and fertility of plants through their delivery of ubiquitin (Ub)/26S proteasome system (UPS) substrates to the 26S proteasome. Rad23 proteins contain an N-terminal ubiquitin-like (UBL) domain that associates with the 26S proteasome Ub receptor RPN10, and two C-terminal ubiquitin-associated (UBA) domains that bind Ub conjugates. This model corresponds to the UBA1 domain.


Pssm-ID: 270562  Cd Length: 50  Bit Score: 37.21  E-value: 1.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 383872294 702 EDCVTTIVSMG---FSRDQALKALRATNNSLERAVDWIFSHI 740
Cdd:cd14379    8 EQTVQQIMDMGggsWDRDTVVRALRAAYNNPERAVEYLYSGI 49
UBA cd14270
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ...
637-667 2.23e-03

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: 36.17  E-value: 2.23e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 383872294 637 IIQLVEMGFPMDACRKAVYYTGNSgAEAAMN 667
Cdd:cd14270    1 LAQLVEMGFSREQARRALRATNGD-VEAAVE 30
UBA1_HR23A cd14425
UBA1 domain of UV excision repair protein RAD23 homolog A (HR23A) found in vertebrates; HR23A, ...
705-738 4.20e-03

UBA1 domain of UV excision repair protein RAD23 homolog A (HR23A) found in vertebrates; HR23A, also called Rad23A, is a DNA repair protein that binds to 19S subunit of the 26S proteasome and shuttles ubiquitinated proteins to the proteasome for degradation which is required for efficient nucleotide excision repair (NER), a primary mechanism for removing UV-induced DNA lesions. HR23A also plays a critical role in the interaction of HIV-1 viral protein R (Vpr) with proteasome, especially facilitating Vpr to promote protein poly-ubiquitination. HR23A 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: 270608  Cd Length: 40  Bit Score: 35.87  E-value: 4.20e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 383872294 705 VTTIVSMGFSRDQALKALRATNNSLERAVDWIFS 738
Cdd:cd14425    6 LTEIMSMGYERERVVAALRASYNNPHRAVEYLLT 39
UBA_unchar_Eumetazoa cd14333
UBA domain found in some hypothetical proteins from Eumetazoa; The family includes some ...
702-736 4.25e-03

UBA domain found in some hypothetical proteins from Eumetazoa; The family includes some uncharacterized Eumetazoan proteins. Although their biological function remain unclear, they all contain a very conserved ubiquitin-associated (UBA) domain which is a commonly occurring sequence motif found in proteins involved in ubiquitin-mediated proteolysis.


Pssm-ID: 270518  Cd Length: 38  Bit Score: 35.60  E-value: 4.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 383872294 702 EDCVTTIVSMGFSRDQALKALRATNNSLERAVDWI 736
Cdd:cd14333    3 DSLLACLASMGFDLDDCQEAIQAGKLTVESAIEWL 37
UBA_cnDdi1_like cd14310
UBA domain found in Cryptococcus neoformans DNA-damage response protein Ddi1 and similar ...
707-733 6.53e-03

UBA domain found in Cryptococcus neoformans DNA-damage response protein Ddi1 and similar proteins; The family includes some uncharacterized Ddi and similar proteins which show a high level of sequence similarity with yeast Ddi1. Ddi1, also called v-SNARE-master 1 (Vsm1), is a ubiquitin receptor involved in regulation of the cell cycle and late secretory pathway in yeast. 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. 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.


Pssm-ID: 270495  Cd Length: 30  Bit Score: 34.82  E-value: 6.53e-03
                         10        20
                 ....*....|....*....|....*..
gi 383872294 707 TIVSMGFSRDQALKALRATNNSLERAV 733
Cdd:cd14310    3 TLVNLGATREQAINLLNAAGGNVDLAA 29
UBA2_KPC2 cd14304
UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
633-671 8.68e-03

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: 34.93  E-value: 8.68e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 383872294 633 DESVIIQLVEMGFPMDACRKAVYYTGNSgAEAAMNWVMS 671
Cdd:cd14304    2 NPRAVQSLMEMGFEEEDVLEALRVTRNN-QNAACEWLLG 39
 
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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