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Conserved domains on  [gi|521588939|gb|EPQ32473|]
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hypothetical protein PFL1_00668 [Pseudozyma flocculosa PF-1]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 1004990)

ubiquitin carboxyl-terminal hydrolase family protein may be 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 ...
309-875 1.81e-88

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: 283.44  E-value: 1.81e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 309 GLRNLGNSCYMASVLQSLFALPSFQSRYrDSYRPHTLACTAAPAACFD----------LGGQADVEMADPAAAAPadapi 378
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRY-DDLENKFPSDVVDPANDLNcqlikladglLSGRYSKPASLKSENDP----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 379 FQAGIRPSMFKALVGKGHEEFSTMRQQDADEFLKHLVDFIKRENRRLPAAaaaapanDPTAVFSFGLEQRLQCNSCKKVR 458
Cdd:cd02658   75 YQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGL-------NPNDLFKFMIEDRLECLSCKKVK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 459 YSVEaQDAGLGLPVPIRPRVKPSAGSsskqpaegvhapdaassakaasapVEYEAVSLVECLDLLTAPEEIEYHCPSCNA 538
Cdd:cd02658  148 YTSE-LSEILSLPVPKDEATEKEEGE------------------------LVYEPVPLEDCLKAYFAPETIEDFCSTCKE 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 539 KVSATKQTRFSSFPEVLAVQARRFQL-VNWVPTKVNVPVEVPlepfeldrylgkglqegEELLPeddaaaaaggsqggsa 617
Cdd:cd02658  203 KTTATKTTGFKTFPDYLVINMKRFQLlENWVPKKLDVPIDVP-----------------EELGP---------------- 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 618 agtvtfdagamsqlasmgfpevrcqkallatgnsdaeaamnwlfahmddadiddpidpsalfiggggggggafastsstt 697
Cdd:cd02658      --------------------------------------------------------------------------------
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 698 nkvdtamleemgftraqslkalrlnhnnaemavawlfehsddqgdvddaeepaagasaadaqpssaagagavvggtttlp 777
Cdd:cd02658      --------------------------------------------------------------------------------
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 778 ARYALKSFISHKGPSVHSGHYVAHIRRDVgagsgsgegegegeGAGEGWVFFNDEKVVKAplsakkpvADAEEHgdeveq 857
Cdd:cd02658  250 GKYELIAFISHKGTSVHSGHYVAHIKKEI--------------DGEGKWVLFNDEKVVAS--------QDPPEM------ 301
                        570
                 ....*....|....*...
gi 521588939 858 edvgvvglSKLAYEYFFE 875
Cdd:cd02658  302 --------KKLGYIYFYQ 311
zf-UBP_var pfam17807
Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ...
16-82 4.26e-24

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: 96.13  E-value: 4.26e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521588939   16 PRPSQQVHKEECTLCFDDHDTQNGIDVCLSCFNGACtgadndRNHSQLHFQKTQHPIVVNIRRVPKP 82
Cdd:pfam17807   4 PSASDRVYKDECIFCFDTPESEGGLFVCLKCFLGFC------KKHAQLHFERTGHPVYLNIKRTKKE 64
UBA1_spUBP14_like cd14385
UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
624-664 3.54e-23

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: 92.86  E-value: 3.54e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 521588939 624 DAGAMSQLASMGFPEVRCQKALLATGNSDAEAAMNWLFAHM 664
Cdd:cd14385    1 NAEALAQLLGMGFPEVRCKKALLATGNSDAEAAMNWLFEHM 41
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
181-255 8.12e-23

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 92.32  E-value: 8.12e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521588939  181 CGKCDLTSNLWLCLTCGHLGCGRAQfggvggNSHGLAHFEETGHPVSVKQGTITaegtadIYCYACNDARIDPLL 255
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQ------NSHALEHYEETGHPLAVNLSTLT------VYCYPCDDYVHDPSL 63
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
703-737 4.84e-12

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: 60.96  E-value: 4.84e-12
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 521588939 703 AMLEEMGFTRAQSLKALRLNHNNAEMAVAWLFEHS 737
Cdd:cd14297    5 KQLVDMGFTEAQARKALRKTNNNVERAVDWLFEGP 39
 
Name Accession Description Interval E-value
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
309-875 1.81e-88

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: 283.44  E-value: 1.81e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 309 GLRNLGNSCYMASVLQSLFALPSFQSRYrDSYRPHTLACTAAPAACFD----------LGGQADVEMADPAAAAPadapi 378
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRY-DDLENKFPSDVVDPANDLNcqlikladglLSGRYSKPASLKSENDP----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 379 FQAGIRPSMFKALVGKGHEEFSTMRQQDADEFLKHLVDFIKRENRRLPAAaaaapanDPTAVFSFGLEQRLQCNSCKKVR 458
Cdd:cd02658   75 YQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGL-------NPNDLFKFMIEDRLECLSCKKVK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 459 YSVEaQDAGLGLPVPIRPRVKPSAGSsskqpaegvhapdaassakaasapVEYEAVSLVECLDLLTAPEEIEYHCPSCNA 538
Cdd:cd02658  148 YTSE-LSEILSLPVPKDEATEKEEGE------------------------LVYEPVPLEDCLKAYFAPETIEDFCSTCKE 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 539 KVSATKQTRFSSFPEVLAVQARRFQL-VNWVPTKVNVPVEVPlepfeldrylgkglqegEELLPeddaaaaaggsqggsa 617
Cdd:cd02658  203 KTTATKTTGFKTFPDYLVINMKRFQLlENWVPKKLDVPIDVP-----------------EELGP---------------- 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 618 agtvtfdagamsqlasmgfpevrcqkallatgnsdaeaamnwlfahmddadiddpidpsalfiggggggggafastsstt 697
Cdd:cd02658      --------------------------------------------------------------------------------
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 698 nkvdtamleemgftraqslkalrlnhnnaemavawlfehsddqgdvddaeepaagasaadaqpssaagagavvggtttlp 777
Cdd:cd02658      --------------------------------------------------------------------------------
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 778 ARYALKSFISHKGPSVHSGHYVAHIRRDVgagsgsgegegegeGAGEGWVFFNDEKVVKAplsakkpvADAEEHgdeveq 857
Cdd:cd02658  250 GKYELIAFISHKGTSVHSGHYVAHIKKEI--------------DGEGKWVLFNDEKVVAS--------QDPPEM------ 301
                        570
                 ....*....|....*...
gi 521588939 858 edvgvvglSKLAYEYFFE 875
Cdd:cd02658  302 --------KKLGYIYFYQ 311
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
308-602 2.41e-43

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 159.92  E-value: 2.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939  308 TGLRNLGNSCYMASVLQSLFALPSFQsRYRDSYRPHTLACTaapaacfdLGGQADVEMADPAAAAPADAPIFQAGIRPSM 387
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFR-DYLLRISPLSEDSR--------YNKDINLLCALRDLFKALQKNSKSSSVSPKM 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939  388 FKALVGKGHEEFSTMRQQDADEFLKHLVDFIKREnrrLPAAAAAAPANDPTAVFSFGLEQRLQCNSCKKVRYSVEAQdag 467
Cdd:pfam00443  72 FKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHED---LNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPF--- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939  468 LGLPVPIRPRVKPSAGSSSKQpaegvhapdaassakaasapvEYEAVSLVECLDlltapEEIEYHCPSCNAKVSATKQTR 547
Cdd:pfam00443 146 SDLSLPIPGDSAELKTASLQI---------------------CFLQFSKLEELD-----DEEKYYCDKCGCKQDAIKQLK 199
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 521588939  548 FSSFPEVLAVQARRFQLVNWVPTKVNVPVEVPLEpFELDRYLGKGLQEGEELLPE 602
Cdd:pfam00443 200 ISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNNLQD 253
zf-UBP_var pfam17807
Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ...
16-82 4.26e-24

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: 96.13  E-value: 4.26e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521588939   16 PRPSQQVHKEECTLCFDDHDTQNGIDVCLSCFNGACtgadndRNHSQLHFQKTQHPIVVNIRRVPKP 82
Cdd:pfam17807   4 PSASDRVYKDECIFCFDTPESEGGLFVCLKCFLGFC------KKHAQLHFERTGHPVYLNIKRTKKE 64
UBA1_spUBP14_like cd14385
UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
624-664 3.54e-23

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: 92.86  E-value: 3.54e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 521588939 624 DAGAMSQLASMGFPEVRCQKALLATGNSDAEAAMNWLFAHM 664
Cdd:cd14385    1 NAEALAQLLGMGFPEVRCKKALLATGNSDAEAAMNWLFEHM 41
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
181-255 8.12e-23

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 92.32  E-value: 8.12e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521588939  181 CGKCDLTSNLWLCLTCGHLGCGRAQfggvggNSHGLAHFEETGHPVSVKQGTITaegtadIYCYACNDARIDPLL 255
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQ------NSHALEHYEETGHPLAVNLSTLT------VYCYPCDDYVHDPSL 63
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
180-234 9.96e-17

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 74.71  E-value: 9.96e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 521588939   180 SCGKCDLTSNLWLCLTCGHLGCGRAQfggvggNSHGLAHFEETGHPVSVKQGTIT 234
Cdd:smart00290   1 RCSVCGTIENLWLCLTCGQVGCGRYQ------NGHALEHFEETGHPLVVKLGTQR 49
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
703-737 4.84e-12

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: 60.96  E-value: 4.84e-12
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 521588939 703 AMLEEMGFTRAQSLKALRLNHNNAEMAVAWLFEHS 737
Cdd:cd14297    5 KQLVDMGFTEAQARKALRKTNNNVERAVDWLFEGP 39
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
269-416 1.23e-10

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 65.29  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 269 LSKTEKSMTELQLEQN---LKFDFTMTGEDGKRLEPLF--------GPGNTGLRNLGNSCYMASVLQSLFALPS----FQ 333
Cdd:COG5560  216 DGRVLHPLTRLELFEDrsvLLLSKITRNPDWLVDSIVDdhnrsinkEAGTCGLRNLGNTCYMNSALQCLMHTWElrdyFL 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 334 SR-YRDSY-RPHTLACTAAPAACF-DLGGQA-DVEMadpaaaapadapifqAGIRPSMFKALVGKGHEEFSTMRQQDADE 409
Cdd:COG5560  296 SDeYEESInEENPLGMHGSVASAYaDLIKQLyDGNL---------------HAFTPSGFKKTIGSFNEEFSGYDQQDSQE 360

                 ....*..
gi 521588939 410 FLKHLVD 416
Cdd:COG5560  361 FIAFLLD 367
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
623-660 1.60e-07

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


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 48.21  E-value: 1.60e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 521588939  623 FDAGAMSQLASMGFPEVRCQKALLATGNsDAEAAMNWL 660
Cdd:pfam00627   1 EDEEAIQRLVEMGFDREQVREALRATGN-NVERAAEYL 37
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
630-661 3.01e-07

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: 47.48  E-value: 3.01e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 521588939   630 QLASMGFPEVRCQKALLATGNsDAEAAMNWLF 661
Cdd:smart00165   7 QLLEMGFSREEALKALRAANG-NVERAAEYLL 37
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
703-734 1.01e-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: 45.94  E-value: 1.01e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 521588939   703 AMLEEMGFTRAQSLKALRLNHNNAEMAVAWLF 734
Cdd:smart00165   6 DQLLEMGFSREEALKALRAANGNVERAAEYLL 37
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
703-733 7.90e-06

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: 43.20  E-value: 7.90e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 521588939  703 AMLEEMGFTRAQSLKALRLNHNNAEMAVAWL 733
Cdd:pfam00627   7 QRLVEMGFDREQVREALRATGNNVERAAEYL 37
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
26-78 1.32e-04

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 40.43  E-value: 1.32e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 521588939    26 ECTLCfddhDTQNGIDVCLSCFNGACtGADNDrNHSQLHFQKTQHPIVVNIRR 78
Cdd:smart00290   1 RCSVC----GTIENLWLCLTCGQVGC-GRYQN-GHALEHFEETGHPLVVKLGT 47
 
Name Accession Description Interval E-value
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
309-875 1.81e-88

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: 283.44  E-value: 1.81e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 309 GLRNLGNSCYMASVLQSLFALPSFQSRYrDSYRPHTLACTAAPAACFD----------LGGQADVEMADPAAAAPadapi 378
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRY-DDLENKFPSDVVDPANDLNcqlikladglLSGRYSKPASLKSENDP----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 379 FQAGIRPSMFKALVGKGHEEFSTMRQQDADEFLKHLVDFIKRENRRLPAAaaaapanDPTAVFSFGLEQRLQCNSCKKVR 458
Cdd:cd02658   75 YQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGL-------NPNDLFKFMIEDRLECLSCKKVK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 459 YSVEaQDAGLGLPVPIRPRVKPSAGSsskqpaegvhapdaassakaasapVEYEAVSLVECLDLLTAPEEIEYHCPSCNA 538
Cdd:cd02658  148 YTSE-LSEILSLPVPKDEATEKEEGE------------------------LVYEPVPLEDCLKAYFAPETIEDFCSTCKE 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 539 KVSATKQTRFSSFPEVLAVQARRFQL-VNWVPTKVNVPVEVPlepfeldrylgkglqegEELLPeddaaaaaggsqggsa 617
Cdd:cd02658  203 KTTATKTTGFKTFPDYLVINMKRFQLlENWVPKKLDVPIDVP-----------------EELGP---------------- 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 618 agtvtfdagamsqlasmgfpevrcqkallatgnsdaeaamnwlfahmddadiddpidpsalfiggggggggafastsstt 697
Cdd:cd02658      --------------------------------------------------------------------------------
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 698 nkvdtamleemgftraqslkalrlnhnnaemavawlfehsddqgdvddaeepaagasaadaqpssaagagavvggtttlp 777
Cdd:cd02658      --------------------------------------------------------------------------------
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 778 ARYALKSFISHKGPSVHSGHYVAHIRRDVgagsgsgegegegeGAGEGWVFFNDEKVVKAplsakkpvADAEEHgdeveq 857
Cdd:cd02658  250 GKYELIAFISHKGTSVHSGHYVAHIKKEI--------------DGEGKWVLFNDEKVVAS--------QDPPEM------ 301
                        570
                 ....*....|....*...
gi 521588939 858 edvgvvglSKLAYEYFFE 875
Cdd:cd02658  302 --------KKLGYIYFYQ 311
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
308-602 2.41e-43

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 159.92  E-value: 2.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939  308 TGLRNLGNSCYMASVLQSLFALPSFQsRYRDSYRPHTLACTaapaacfdLGGQADVEMADPAAAAPADAPIFQAGIRPSM 387
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFR-DYLLRISPLSEDSR--------YNKDINLLCALRDLFKALQKNSKSSSVSPKM 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939  388 FKALVGKGHEEFSTMRQQDADEFLKHLVDFIKREnrrLPAAAAAAPANDPTAVFSFGLEQRLQCNSCKKVRYSVEAQdag 467
Cdd:pfam00443  72 FKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHED---LNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPF--- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939  468 LGLPVPIRPRVKPSAGSSSKQpaegvhapdaassakaasapvEYEAVSLVECLDlltapEEIEYHCPSCNAKVSATKQTR 547
Cdd:pfam00443 146 SDLSLPIPGDSAELKTASLQI---------------------CFLQFSKLEELD-----DEEKYYCDKCGCKQDAIKQLK 199
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 521588939  548 FSSFPEVLAVQARRFQLVNWVPTKVNVPVEVPLEpFELDRYLGKGLQEGEELLPE 602
Cdd:pfam00443 200 ISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNNLQD 253
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
309-598 6.81e-26

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: 107.57  E-value: 6.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 309 GLRNLGNSCYMASVLQSLFalpsfqsryrdsyrphtlactaapaacfdlggqadvemadpaaaapadapifqagirpsmf 388
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALF------------------------------------------------------------- 19
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 389 kalvgkgheefstMRQQDADEFLKHLVDFIKRENRRLPAAAAAAPAND--PTAVFSFGLEQRLQCNSCKKVRYSVEAQDa 466
Cdd:cd02257   20 -------------SEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKslIHDLFGGKLESTIVCLECGHESVSTEPEL- 85
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 467 GLGLPVPIRPRvkpsagssskqpaegvhapdaassakaasapveyEAVSLVECLDLLTAPEEIE----YHCpSCNAKVSA 542
Cdd:cd02257   86 FLSLPLPVKGL----------------------------------PQVSLEDCLEKFFKEEILEgdncYKC-EKKKKQEA 130
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 521588939 543 TKQTRFSSFPEVLAVQARRFQLVN-WVPTKVNVPVEVPLEpFELDRYLGKGLQEGEE 598
Cdd:cd02257  131 TKRLKIKKLPPVLIIHLKRFSFNEdGTKEKLNTKVSFPLE-LDLSPYLSEGEKDSDS 186
zf-UBP_var pfam17807
Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ...
16-82 4.26e-24

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: 96.13  E-value: 4.26e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521588939   16 PRPSQQVHKEECTLCFDDHDTQNGIDVCLSCFNGACtgadndRNHSQLHFQKTQHPIVVNIRRVPKP 82
Cdd:pfam17807   4 PSASDRVYKDECIFCFDTPESEGGLFVCLKCFLGFC------KKHAQLHFERTGHPVYLNIKRTKKE 64
UBA1_spUBP14_like cd14385
UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
624-664 3.54e-23

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: 92.86  E-value: 3.54e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 521588939 624 DAGAMSQLASMGFPEVRCQKALLATGNSDAEAAMNWLFAHM 664
Cdd:cd14385    1 NAEALAQLLGMGFPEVRCKKALLATGNSDAEAAMNWLFEHM 41
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
181-255 8.12e-23

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 92.32  E-value: 8.12e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521588939  181 CGKCDLTSNLWLCLTCGHLGCGRAQfggvggNSHGLAHFEETGHPVSVKQGTITaegtadIYCYACNDARIDPLL 255
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQ------NSHALEHYEETGHPLAVNLSTLT------VYCYPCDDYVHDPSL 63
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
309-589 5.86e-19

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 86.96  E-value: 5.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 309 GLRNLGNSCYMASVLQSLFAlpsfqsryrdsyrphtlactaapaacfdlggqadvemadpaaaapadapifqagirpsmf 388
Cdd:cd02674    1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 389 kalvgkgheefstmRQQDADEFLKHLVD----FIkrenrrlpaaaaaapandpTAVFSFGLEQRLQCNSCKKVRYSVEAQ 464
Cdd:cd02674   21 --------------DQQDAQEFLLFLLDglhsII-------------------VDLFQGQLKSRLTCLTCGKTSTTFEPF 67
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 465 DAglgLPVPIrprvkpsagssskqPAEGVHAPdaassakaasapveyeAVSLVECLDLLTAPEEIE----YHCPSCNAKV 540
Cdd:cd02674   68 TY---LSLPI--------------PSGSGDAP----------------KVTLEDCLRLFTKEETLDgdnaWKCPKCKKKR 114
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 521588939 541 SATKQTRFSSFPEVLAVQARRFQLVNWVPTKVNVPVEVPLEPFELDRYL 589
Cdd:cd02674  115 KATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYV 163
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
309-581 2.28e-18

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 87.04  E-value: 2.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 309 GLRNLGNSCYMASVLQSL--------FALPSFQSRYRDSYRPHT-LACTAAPAACfDLGGQADVEmadpaaaapadapif 379
Cdd:cd02660    2 GLINLGATCFMNVILQALlhnpllrnYFLSDRHSCTCLSCSPNScLSCAMDEIFQ-EFYYSGDRS--------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 380 qaGIRPSMFKALVGKGHEEFSTMRQQDADEFLKHLVDFIKREN-RRLPAAAAAAPANDPT-AVFSFGLEQRLQCNSCKKV 457
Cdd:cd02660   66 --PYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYgGDKNEANDESHCNCIIhQTFSGSLQSSVTCQRCGGV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 458 RYSVeaqDAGLGLPVPIRPRVKPSAGSSskqPAEGVHAPdaassakaasapveyeavSLVECLDLLTAPEEIE---YHCP 534
Cdd:cd02660  144 STTV---DPFLDLSLDIPNKSTPSWALG---ESGVSGTP------------------TLSDCLDRFTRPEKLGdfaYKCS 199
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 521588939 535 SCNAKVSATKQTRFSSFPEVLAVQARRFQ-LVNWVPTKVNVPVEVPLE 581
Cdd:cd02660  200 GCGSTQEATKQLSIKKLPPVLCFQLKRFEhSLNKTSRKIDTYVQFPLE 247
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
308-583 1.16e-17

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 84.63  E-value: 1.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 308 TGLRNLGNSCYMASVLQSL-------FALPSFQsryrdsyrpHTLACtAAPAACFDLGGQADVEMADPAAAAPADAPIFQ 380
Cdd:cd02661    2 AGLQNLGNTCFLNSVLQCLthtpplaNYLLSRE---------HSKDC-CNEGFCMMCALEAHVERALASSGPGSAPRIFS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 381 AGIRpsmfkaLVGKGheeFSTMRQQDADEFLKHLVDfiKRENRRLPAAAAAAPANDPTA-------VFSFGLEQRLQCNS 453
Cdd:cd02661   72 SNLK------QISKH---FRIGRQEDAHEFLRYLLD--AMQKACLDRFKKLKAVDPSSQettlvqqIFGGYLRSQVKCLN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 454 CKKV--RYsveaqDAGLGLPVPIRprvkpsagssskqpaegvhapdaassakaasapveyEAVSLVECLDLLTAPEEIE- 530
Cdd:cd02661  141 CKHVsnTY-----DPFLDLSLDIK------------------------------------GADSLEDALEQFTKPEQLDg 179
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 531 ---YHCPSCNAKVSATKQTRFSSFPEVLAVQARRFQLVNWvpTKVNVPVEVP----LEPF 583
Cdd:cd02661  180 enkYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRG--GKINKQISFPetldLSPY 237
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
180-234 9.96e-17

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 74.71  E-value: 9.96e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 521588939   180 SCGKCDLTSNLWLCLTCGHLGCGRAQfggvggNSHGLAHFEETGHPVSVKQGTIT 234
Cdd:smart00290   1 RCSVCGTIENLWLCLTCGQVGCGRYQ------NGHALEHFEETGHPLVVKLGTQR 49
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
627-663 3.61e-14

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: 66.89  E-value: 3.61e-14
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 521588939 627 AMSQLASMGFPEVRCQKALLATGNSDAEAAMNWLFAH 663
Cdd:cd14296    3 AVSQLMSMGFSENAAKRALYYTGNSSVEAAMNWLFEH 39
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
309-604 9.20e-14

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 73.45  E-value: 9.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 309 GLRNLGNSCYMASVLQSLFALPSF-QSRYRDSYRPHTLACTAAPAA---CFDLGGQADVEMadpaaaapadapifqagIR 384
Cdd:cd02659    4 GLKNQGATCYMNSLLQQLYMTPEFrNAVYSIPPTEDDDDNKSVPLAlqrLFLFLQLSESPV-----------------KT 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 385 PSMFKALVGKGHEEFSTMRQQDADEFLKHLVDFIKRENRRLPAAaaaapandptavfsfGLEQRLQCNS------CKKVR 458
Cdd:cd02659   67 TELTDKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQE---------------GLIKNLFGGKlvnyiiCKECP 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 459 YSVEAQDAGLGLPVPIRPRVkpsagssskqpaegvhapdaassakaasapveyeavSLVECLDLLTAPEEIE----YHCP 534
Cdd:cd02659  132 HESEREEYFLDLQVAVKGKK------------------------------------NLEESLDAYVQGETLEgdnkYFCE 175
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521588939 535 SCNAKVSATKQTRFSSFPEVLAVQARRFQlVNWVP---TKVNVPVEVPLEpFELDRYLGKGLQEGEELLPEDD 604
Cdd:cd02659  176 KCGKKVDAEKGVCFKKLPPVLTLQLKRFE-FDFETmmrIKINDRFEFPLE-LDMEPYTEKGLAKKEGDSEKKD 246
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
309-583 2.66e-13

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 71.26  E-value: 2.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 309 GLRNLGNSCYMASVLQSLFALPSFQSRYRDsyrphtlactaapaacfdlggqadvemadpaaaapadapifqagiRPSMF 388
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE---------------------------------------------TPKEL 35
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 389 KALVGKGHEEFSTMRQQDADEFLKHLVD----FIKRenrrlpaaaaaapandptaVFSFGLEQRLQCNSCKKVRYSVEAq 464
Cdd:cd02667   36 FSQVCRKAPQFKGYQQQDSHELLRYLLDglrtFIDS-------------------IFGGELTSTIMCESCGTVSLVYEP- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 465 DAGLGLPVPIRPRvkpsagssskqpaegvhapdaassakaasapveyEAVSLVECLDLLTAPEEIE----YHCPSCnakV 540
Cdd:cd02667   96 FLDLSLPRSDEIK----------------------------------SECSIESCLKQFTEVEILEgnnkFACENC---T 138
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 521588939 541 SATKQTRFSSFPEVLAVQARRF-QLVNWVPTKVNVPVEVP----LEPF 583
Cdd:cd02667  139 KAKKQYLISKLPPVLVIHLKRFqQPRSANLRKVSRHVSFPeildLAPF 186
UBA1_UBP5_like cd14294
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; ...
626-664 2.00e-12

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: 62.33  E-value: 2.00e-12
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 521588939 626 GAMSQLASMGFPEVRCQKALLATGNSDAEAAMNWLFAHM 664
Cdd:cd14294    2 AVVSQLAEMGFPLEACRKAVYHTNNSGLEAAMNWIMEHM 40
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
703-737 4.84e-12

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: 60.96  E-value: 4.84e-12
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 521588939 703 AMLEEMGFTRAQSLKALRLNHNNAEMAVAWLFEHS 737
Cdd:cd14297    5 KQLVDMGFTEAQARKALRKTNNNVERAVDWLFEGP 39
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
624-664 5.27e-12

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


Pssm-ID: 270481 [Multi-domain]  Cd Length: 45  Bit Score: 61.23  E-value: 5.27e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 521588939 624 DAGAMSQLASMGFPEVRCQKALLATGNSDAEAAMNWLFAHM 664
Cdd:cd14295    1 DQELVAQLMEMGFPKVRAEKALFFTQNKGLEEAMEWLEEHS 41
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
703-739 5.40e-11

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: 58.11  E-value: 5.40e-11
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 521588939 703 AMLEEMGFTRAQSLKALRLNHNNAEMAVAWLFEHSDD 739
Cdd:cd14386    7 AMLVSMGFTRDQAIKALKATDNNVERAADWIFSHPDE 43
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
269-416 1.23e-10

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 65.29  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 269 LSKTEKSMTELQLEQN---LKFDFTMTGEDGKRLEPLF--------GPGNTGLRNLGNSCYMASVLQSLFALPS----FQ 333
Cdd:COG5560  216 DGRVLHPLTRLELFEDrsvLLLSKITRNPDWLVDSIVDdhnrsinkEAGTCGLRNLGNTCYMNSALQCLMHTWElrdyFL 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 334 SR-YRDSY-RPHTLACTAAPAACF-DLGGQA-DVEMadpaaaapadapifqAGIRPSMFKALVGKGHEEFSTMRQQDADE 409
Cdd:COG5560  296 SDeYEESInEENPLGMHGSVASAYaDLIKQLyDGNL---------------HAFTPSGFKKTIGSFNEEFSGYDQQDSQE 360

                 ....*..
gi 521588939 410 FLKHLVD 416
Cdd:COG5560  361 FIAFLLD 367
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
510-590 3.77e-10

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 63.75  E-value: 3.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 510 EYEAVSLVECLDLLTAPEEIE----YHCPSCNAKVSATKQTRFSSFPEVLAVQARRFQLVNWVPTKVNVPVEVPLEPFEL 585
Cdd:COG5560  671 AERTITLQDCLNEFSKPEQLGlsdsWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDL 750

                 ....*
gi 521588939 586 DRYLG 590
Cdd:COG5560  751 SGVEY 755
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
630-664 4.03e-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: 4.03e-10
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 521588939 630 QLASMGFPEVRCQKALLATGNSDAEAAMNWLFAHM 664
Cdd:cd14302    5 TLIEMGFSRNRAEKALAKTGNQGVEAAMEWLLAHE 39
UBA_UBS3B cd14301
UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and ...
627-663 9.06e-10

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: 54.37  E-value: 9.06e-10
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 521588939 627 AMSQLASMGFPEVRCQKALLATGNSDAEAAMNWLFAH 663
Cdd:cd14301    2 ALEVLLSMGFPKHRAEKALAATGGRSVQLASDWLLSH 38
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
703-737 1.09e-09

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: 54.37  E-value: 1.09e-09
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 521588939 703 AMLEEMGFTRAQSLKALRLNHNNAEMAVAWLFEHS 737
Cdd:cd14306    2 AKLMELGFPEEDCIRALRACGGNVEEAANWLLENA 36
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
309-562 1.89e-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: 60.13  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 309 GLRNLGNSCYMASVLQSLFALPSFQSryrdsyrphtlactaapaACFDLGGQADVEMADPAAAAPADAP--------IF- 379
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRK------------------AVYECNSTEDAELKNMPPDKPHEPQtiidqlqlIFa 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 380 --QAG----IRPSMF-KALvgkgheEFSTMRQQDADEFLKHLVDFIKRenrRLPAAAAAAPANDPTAVFSFGLEQRLQCN 452
Cdd:cd02668   63 qlQFGnrsvVDPSGFvKAL------GLDTGQQQDAQEFSKLFLSLLEA---KLSKSKNPDLKNIVQDLFRGEYSYVTQCS 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 453 SCKKvRYSVEAQDAGLGLPVpirprvkpsagSSSKQpaegvhapdaassakaasapveyeavsLVECLDLLTAPEEIE-- 530
Cdd:cd02668  134 KCGR-ESSLPSKFYELELQL-----------KGHKT---------------------------LEECIDEFLKEEQLTgd 174
                        250       260       270
                 ....*....|....*....|....*....|....
gi 521588939 531 --YHCPSCNAKVSATKQTRFSSFPEVLAVQARRF 562
Cdd:cd02668  175 nqYFCESCNSKTDATRRIRLTTLPPTLNFQLLRF 208
UBA1_UBP5 cd14383
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
623-664 3.92e-09

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: 53.13  E-value: 3.92e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 521588939 623 FDAGAMSQLASMGFPEVRCQKALLATGNSDAEAAMNWLFAHM 664
Cdd:cd14383    2 LDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHM 43
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
309-588 7.14e-09

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 58.11  E-value: 7.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 309 GLRNLGNSCYMASVLQSLFALPSFQSRYRDSyrphTLACTAAPAACFDLGG---QADVEMADPaaaapadapifQAGIRP 385
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNY----NPARRGANQSSDNLTNalrDLFDTMDKK-----------QEPVPP 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 386 SMFKALVGKGHEEFSTM------RQQDADEFLKHLVDFIKREnrrLPAAAAAAPANDptAVFSFGLEQRLQCNSCKKVRY 459
Cdd:cd02657   66 IEFLQLLRMAFPQFAEKqnqggyAQQDAEECWSQLLSVLSQK---LPGAGSKGSFID--QLFGIELETKMKCTESPDEEE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 460 SVEAQDAGLGLPVPIRPRVKpsagssskqpaegvhapdaassakaasapveyeavSLVECLdLLTAPEEIEYHCPSCNAK 539
Cdd:cd02657  141 VSTESEYKLQCHISITTEVN-----------------------------------YLQDGL-KKGLEEEIEKHSPTLGRD 184
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 521588939 540 VSATKQTRFSSFPEVLAVQARRFQlvnW-----VPTKVNVPVEVplePFELDRY 588
Cdd:cd02657  185 AIYTKTSRISRLPKYLTVQFVRFF---WkrdiqKKAKILRKVKF---PFELDLY 232
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
628-664 3.07e-08

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: 50.13  E-value: 3.07e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 521588939 628 MSQLASMGFPEVRCQKALLATGNsDAEAAMNWLFAHM 664
Cdd:cd14306    1 VAKLMELGFPEEDCIRALRACGG-NVEEAANWLLENA 36
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
703-736 4.50e-08

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: 49.55  E-value: 4.50e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 521588939 703 AMLEEMGFTRAQSLKALRLNHN-NAEMAVAWLFEH 736
Cdd:cd14296    5 SQLMSMGFSENAAKRALYYTGNsSVEAAMNWLFEH 39
UBA1_KPC2 cd14303
UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
623-663 6.60e-08

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: 49.31  E-value: 6.60e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 521588939 623 FDAGAMSQLASMGFPEVRCQKALLATGNSdAEAAMNWLFAH 663
Cdd:cd14303    1 VDPEALKQLTEMGFPEARATKALLLNRMS-PTQAMEWLLEH 40
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
623-660 1.60e-07

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


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 48.21  E-value: 1.60e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 521588939  623 FDAGAMSQLASMGFPEVRCQKALLATGNsDAEAAMNWL 660
Cdd:pfam00627   1 EDEEAIQRLVEMGFDREQVREALRATGN-NVERAAEYL 37
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
630-661 3.01e-07

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: 47.48  E-value: 3.01e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 521588939   630 QLASMGFPEVRCQKALLATGNsDAEAAMNWLF 661
Cdd:smart00165   7 QLLEMGFSREEALKALRAANG-NVERAAEYLL 37
UBA1_UBP13 cd14384
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
624-664 3.08e-07

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: 47.71  E-value: 3.08e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 521588939 624 DAGAMSQLASMGFPEVRCQKALLATGNSDAEAAMNWLFAHM 664
Cdd:cd14384    3 DESSVMQLAEMGFPLEACRKAVYYTGNMGAEVAFNWIIAHM 43
UBA1_KPC2 cd14303
UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
704-737 4.08e-07

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: 47.00  E-value: 4.08e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 521588939 704 MLEEMGFTRAQSLKALRLNHNNAEMAVAWLFEHS 737
Cdd:cd14303    8 QLTEMGFPEARATKALLLNRMSPTQAMEWLLEHE 41
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
309-418 4.37e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 52.88  E-value: 4.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 309 GLRNLGNSCYMASVLQSLFALPSFqSRYRDSYRPHTLACTAAPAacFDLGGQADVEMADPAAAAPADAPIFQAgIRPsmf 388
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDF-RRQVLSLNLPRLGDSQSVM--KKLQLLQAHLMHTQRRAEAPPDYFLEA-SRP--- 73
                         90       100       110
                 ....*....|....*....|....*....|
gi 521588939 389 kalvgkghEEFSTMRQQDADEFLKHLVDFI 418
Cdd:cd02664   74 --------PWFTPGSQQDCSEYLRYLLDRL 95
UBA_PUB_plant cd14290
UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family ...
624-663 7.11e-07

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: 46.67  E-value: 7.11e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 521588939 624 DAGAMSQLASMGFPEVRCQKALLATGNSDAEAAMNWLFAH 663
Cdd:cd14290    3 NADLLKELEAMGFPRARAVRALHHTGNTSVEAAVNWIVEH 42
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
629-664 7.99e-07

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: 46.32  E-value: 7.99e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 521588939 629 SQLASMGFPEVRCQKALLATGNsDAEAAMNWLFAHM 664
Cdd:cd14297    5 KQLVDMGFTEAQARKALRKTNN-NVERAVDWLFEGP 39
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
703-734 1.01e-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: 45.94  E-value: 1.01e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 521588939   703 AMLEEMGFTRAQSLKALRLNHNNAEMAVAWLF 734
Cdd:smart00165   6 DQLLEMGFSREEALKALRAANGNVERAAEYLL 37
UBA_UBS3A_like cd14300
UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and ...
628-663 1.05e-06

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: 45.99  E-value: 1.05e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 521588939 628 MSQLASMGFPEVRCQKALLATGNSDAEAAMNWLFAH 663
Cdd:cd14300    1 LETLLAMGFPEDVARKALKATGGKSIEKATDWLLSH 36
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
309-565 1.72e-06

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 50.06  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 309 GLRNLGNSCYMASVLQSLFALPSFqSRYRDSYrphtlactaapaacfdlggqadvemadpaaaapadapifqagirpsmf 388
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSL-IEYLEEF------------------------------------------------ 31
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 389 kalvgkgheefstMRQQDADEFLKHLVDFIKREnrrlpaaaaaapandPTAVFSFGLEQRLQCNSCK---KVRYSveaQD 465
Cdd:cd02662   32 -------------LEQQDAHELFQVLLETLEQL---------------LKFPFDGLLASRIVCLQCGessKVRYE---SF 80
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 466 AGLGLPVPIRPRVKPSagssskqpaegvhapdaassakaasapveyeavSLVECLDLLTAPEEIE-YHCPSCNAKVSATK 544
Cdd:cd02662   81 TMLSLPVPNQSSGSGT---------------------------------TLEHCLDDFLSTEIIDdYKCDRCQTVIVRLP 127
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 521588939 545 QT------RFS--------------SFPEVLavQARRFQLV 565
Cdd:cd02662  128 QIlcihlsRSVfdgrgtstknsckvSFPERL--PKVLYRLR 166
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
627-663 2.81e-06

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: 44.60  E-value: 2.81e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 521588939 627 AMSQLASMGFPEVRCQKALLATGNSDAEAAMNWLFAH 663
Cdd:cd14327    2 AVAQLVEMGFSRERAEEALRAVGTNSVELAMEWLFTN 38
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
780-838 4.05e-06

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 49.73  E-value: 4.05e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 521588939 780 YALKSFISHKGPSVHSGHYVAHIRRDvgagsgsgegegegegAGEGWVFFNDEKVVKAP 838
Cdd:cd02668  246 YELSGVLIHQGVSAYSGHYIAHIKDE----------------QTGEWYKFNDEDVEEMP 288
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
702-736 6.74e-06

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: 43.44  E-value: 6.74e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 521588939 702 TAMLEEMGFTRAQSLKALR-LNHNNAEMAVAWLFEH 736
Cdd:cd14327    3 VAQLVEMGFSRERAEEALRaVGTNSVELAMEWLFTN 38
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
623-664 7.50e-06

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: 43.48  E-value: 7.50e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 521588939 623 FDAGAMSQLASMGFPEVRCQKALLATGNsDAEAAMNWLFAHM 664
Cdd:cd14386    1 VPEEAVAMLVSMGFTRDQAIKALKATDN-NVERAADWIFSHP 41
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
703-733 7.90e-06

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: 43.20  E-value: 7.90e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 521588939  703 AMLEEMGFTRAQSLKALRLNHNNAEMAVAWL 733
Cdd:pfam00627   7 QRLVEMGFDREQVREALRATGNNVERAAEYL 37
UBA cd14270
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ...
703-730 8.21e-06

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: 43.11  E-value: 8.21e-06
                         10        20
                 ....*....|....*....|....*...
gi 521588939 703 AMLEEMGFTRAQSLKALRLNHNNAEMAV 730
Cdd:cd14270    2 AQLVEMGFSREQARRALRATNGDVEAAV 29
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
700-739 1.91e-05

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


Pssm-ID: 270487 [Multi-domain]  Cd Length: 41  Bit Score: 42.28  E-value: 1.91e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 521588939 700 VDTAMleEMGFTRAQSLKAL-RLNHNNAEMAVAWLFEHSDD 739
Cdd:cd14302    3 LQTLI--EMGFSRNRAEKALaKTGNQGVEAAMEWLLAHEDD 41
UBA2_scUBP14_like cd14298
UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
626-663 2.03e-05

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: 42.06  E-value: 2.03e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 521588939 626 GAMSQLASMGFPEVRCQKALLATgNSDAEAAMNWLFAH 663
Cdd:cd14298    2 EALAQLVSMGFDPEVARKALILT-NGNVERAIEWLFSN 38
UBA1_NUB1_like cd14291
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ...
703-733 4.16e-05

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: 41.28  E-value: 4.16e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 521588939 703 AMLEEMGFTRAQSLKALRLNHNNAEMAVAWL 733
Cdd:cd14291    6 QQLMEMGFSEAEARLALRACNGNVERAVDYI 36
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
703-739 4.66e-05

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: 41.59  E-value: 4.66e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 521588939 703 AMLEEMGFTRAQSLKALRLNHNNA-EMAVAWLFEHSDD 739
Cdd:cd14295    6 AQLMEMGFPKVRAEKALFFTQNKGlEEAMEWLEEHSED 43
UBA_PUB_plant cd14290
UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family ...
705-739 5.09e-05

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: 41.27  E-value: 5.09e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 521588939 705 LEEMGFTRAQSLKALRLNHN-NAEMAVAWLFEHSDD 739
Cdd:cd14290   10 LEAMGFPRARAVRALHHTGNtSVEAAVNWIVEHEND 45
UBA2_UBP13 cd14387
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
703-733 7.07e-05

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: 40.44  E-value: 7.07e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 521588939 703 AMLEEMGFTRAQSLKALRLNHNNAEMAVAWL 733
Cdd:cd14387    5 AILMSMGFPRNRAIEALKRTNNNLDRALDWL 35
UBA cd14270
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ...
628-658 8.56e-05

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: 40.03  E-value: 8.56e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 521588939 628 MSQLASMGFPEVRCQKALLATGNsDAEAAMN 658
Cdd:cd14270    1 LAQLVEMGFSREQARRALRATNG-DVEAAVE 30
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
26-78 1.32e-04

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 40.43  E-value: 1.32e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 521588939    26 ECTLCfddhDTQNGIDVCLSCFNGACtGADNDrNHSQLHFQKTQHPIVVNIRR 78
Cdd:smart00290   1 RCSVC----GTIENLWLCLTCGQVGC-GRYQN-GHALEHFEETGHPLVVKLGT 47
UBA2_KPC2 cd14304
UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
704-733 1.47e-04

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: 39.93  E-value: 1.47e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 521588939 704 MLEEMGFTRAQSLKALRLNHNNAEMAVAWL 733
Cdd:cd14304    8 SLMEMGFEEEDVLEALRVTRNNQNAACEWL 37
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
309-580 1.73e-04

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 44.50  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 309 GLRNLGNSCYMASVLQSLFALPSFQSRYR------DSYRPHTLACTAAPaacfdlggqadvEMADPAAAAPADAPIFQAg 382
Cdd:cd02671   26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKhlvsliSSVEQLQSSFLLNP------------EKYNDELANQAPRRLLNA- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 383 IRP--SMFKAlvgkgheefstMRQQDADEFLKHLVDFIKrenrrlpaaaaaapaNDPTAVFSFGLEQRLQCNSCKKVrys 460
Cdd:cd02671   93 LREvnPMYEG-----------YLQHDAQEVLQCILGNIQ---------------ELVEKDFQGQLVLRTRCLECETF--- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521588939 461 VEAQDAGLGLPVPIrprvkPSAGSSSKQPAEGVHAPDAASSAKAASAPVEYEAVSLVECLDlltapeeiEYHCPSCNAKV 540
Cdd:cd02671  144 TERREDFQDISVPV-----QESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGED--------KYFCENCHHYT 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 521588939 541 SATKQTRFSSFPEVLAVQARRFQLVNWVP------TKVNVPVEVPL 580
Cdd:cd02671  211 EAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPL 256
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
780-834 1.82e-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: 44.63  E-value: 1.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 521588939 780 YALKSFISHKGPSVHSGHYVAHIRRDvgagsgsgegegegegAGEGWVFFNDEKV 834
Cdd:cd02657  241 YELVAVITHQGRSADSGHYVAWVRRK----------------NDGKWIKFDDDKV 279
UBA1_UBP5_like cd14294
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; ...
705-739 2.20e-04

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: 39.60  E-value: 2.20e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 521588939 705 LEEMGFTRAQSLKALRLNHNN-AEMAVAWLFEHSDD 739
Cdd:cd14294    7 LAEMGFPLEACRKAVYHTNNSgLEAAMNWIMEHMDD 42
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
309-334 2.41e-04

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 44.02  E-value: 2.41e-04
                         10        20
                 ....*....|....*....|....*..
gi 521588939 309 GLRNLGNSCYMASVLQSL-FALPSFQS 334
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILaLYLPKLDE 27
UBA1_Rad23_like cd14280
UBA1 domain of Rad23 proteins found in eukaryotes; The Rad23 family includes the yeast ...
705-734 3.90e-04

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: 38.75  E-value: 3.90e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 521588939 705 LEEMGFTRAQSLKALRLNHNNAEMAVAWLF 734
Cdd:cd14280    9 IMSMGFEREQVVRALRAAFNNPDRAVEYLL 38
UBA_RUP1p cd14307
UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ...
703-736 4.06e-04

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: 38.43  E-value: 4.06e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 521588939 703 AMLEEMGFTRAQSLKALRLNHNNAEMAVAWLFEH 736
Cdd:cd14307    5 ASLLEMGIPREVAIEALRETNGDVEAAANYIFSN 38
UBA_AAA_plant cd14389
UBA domain found in plant AAA-type ATPase-like proteins; This family includes some ...
628-663 6.13e-04

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: 38.10  E-value: 6.13e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 521588939 628 MSQLASMGFPEVRCQKALLATGNSDAEAAMNWLFAH 663
Cdd:cd14389    1 MEQLVDMGFSSDLAAEALAATGGKSTQKATEWILSH 36
UBA_RUP1p cd14307
UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ...
627-663 8.93e-04

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: 37.66  E-value: 8.93e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 521588939 627 AMSQLASMGFPEVRCQKALLATgNSDAEAAMNWLFAH 663
Cdd:cd14307    3 AVASLLEMGIPREVAIEALRET-NGDVEAAANYIFSN 38
UBA2_scUBP14_like cd14298
UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
703-736 1.74e-03

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: 36.67  E-value: 1.74e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 521588939 703 AMLEEMGFTRAQSLKALRLNHNNAEMAVAWLFEH 736
Cdd:cd14298    5 AQLVSMGFDPEVARKALILTNGNVERAIEWLFSN 38
UBA_TNR6C cd14283
UBA domain found in trinucleotide repeat-containing gene 6C protein (TNRC6C) and similar ...
705-735 1.76e-03

UBA domain found in trinucleotide repeat-containing gene 6C protein (TNRC6C) and similar proteins; TNRC6C is one of three GW182 paralogs in mammalian genomes. It is enriched in P-bodies and important for efficient miRNA-mediated repression. TNRC6C is composed of an N-terminal glycine/tryptophan (G/W)-rich region containing an Ago hook responsible for Ago protein-binding; a ubiquitin-associated (UBA) domain and a glutamine (Q)-rich region in the middle region; a middle G/W-rich region, a RNA recognition motif (RRM), also called RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal G/W-rich region, at the C-terminus. A bipartite C-terminal region including the middle and C-terminal G/W-rich regions is referred as silencing domain that triggers silencing of bound transcripts by inhibiting protein expression and promoting mRNA decay via deadenylation. The C-terminal half containing the RRM domain functions as a key effector domain mediating protein synthesis repression by TNRC6C.


Pssm-ID: 270469  Cd Length: 38  Bit Score: 36.71  E-value: 1.76e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 521588939 705 LEEMGFTRAQSLKALRLNHNNAEMAVAWLFE 735
Cdd:cd14283    7 LTDMGFKREPAEEALKSNNMNLEQAVSALLS 37
UBA_UBL7 cd14326
UBA domain found in ubiquitin-like protein 7 (UBL7) and similar proteins; UBL7, also called ...
627-661 2.48e-03

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


Pssm-ID: 270511  Cd Length: 38  Bit Score: 36.15  E-value: 2.48e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 521588939 627 AMSQLASMGFP-EVRCQKALLATGnSDAEAAMNWLF 661
Cdd:cd14326    4 QLQQLREMGITdDSLSLRALQATG-GDVQAALNLLF 38
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
306-333 6.36e-03

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 40.24  E-value: 6.36e-03
                          10        20
                  ....*....|....*....|....*...
gi 521588939  306 GNTGLRNLGNSCYMASVLQSLFALPSFQ 333
Cdd:COG5077   192 GYVGLRNQGATCYMNSLLQSLFFIAKFR 219
UBA1_NUB1_like cd14291
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ...
624-660 9.21e-03

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: 34.73  E-value: 9.21e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 521588939 624 DAGAMSQLASMGFPEVRCQKALLATGNsDAEAAMNWL 660
Cdd:cd14291    1 DEDKLQQLMEMGFSEAEARLALRACNG-NVERAVDYI 36
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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