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Conserved domains on  [gi|193083197|ref|NP_659486|]
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ubiquitin-like domain-containing CTD phosphatase 1 [Homo sapiens]

Protein Classification

ubiquitin-like domain-containing CTD phosphatase 1( domain architecture ID 10110641)

ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity

EC:  3.1.3.16
Gene Symbol:  UBLCP1
Gene Ontology:  GO:0004722|GO:0006470
PubMed:  21949367

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_IIID1 TIGR02245
HAD-superfamily subfamily IIID hydrolase, TIGR02245; This family of sequences appears to ...
 117-311 1.48e-129

HAD-superfamily subfamily IIID hydrolase, TIGR02245; This family of sequences appears to belong to the Haloacid Dehalogenase (HAD) superfamily of enzymes by virtue of the presence of three catalytic domains, in this case: LLVLD(ILV)D(YH)T, I(VMG)IWS, and (DN)(VC)K(PA)Lx{15-17}T(IL)(MH)(FV)DD(IL)(GRS)(RK)N. Since this family has no large "cap" domain between motifs 1 and 2 or between 2 and 3, it is formally a "class III" HAD.


:

Pssm-ID: 131299  Cd Length: 195  Bit Score: 367.22  E-value: 1.48e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197  117 KISRRVKEYKVEILNPPREGKKLLVLDVDYTLFDHRSCAETGVELMRPYLHEFLTSAYEDYDIVIWSATNMKWIEAKMKE 196
Cdd:TIGR02245   1 KLLRRIEQYKIKLLNPPREGKKLLVLDIDYTLFDHRSPAETGEELMRPYLHEFLTSAYEDYDIVIWSATSMKWIEIKMTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197  197 LGVSTNANYKITFMLDSAAMITVHTPRRGLIDVKPLGVIWGKFSEFYSKKNTIMFDDIGRNFLMNPQNGLKIRPFMKAHL 276
Cdd:TIGR02245  81 LGVLTNPNYKITFLLDSTAMITVHTPRRGKFDVKPLGVIWALLPEFYSMKNTIMFDDLRRNFLMNPKNGLKIRPFKKAHA 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 193083197  277 NRDKDKELLKLTQYLKEIAKLDDFLDLNHKYWERY 311
Cdd:TIGR02245 161 NRGTDQELLKLTQYLKTIAELEDFSSLDHKEWERY 195
Ubl_UBLCP1 cd01813
ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 ...
 3-77 4.63e-37

ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) and similar proteins; UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity. It is localized in the nucleus and it contains conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which directly interacts with the proteasome. Knockdown of UBLCP1 in cells promotes 26S proteasome assembly and selectively enhances nuclear proteasome activity. UBLCP1 may also play a role in the regulation of phosphorylation state of RNA polymerase II C-terminal domain, a key event during mRNA metabolism.


:

Pssm-ID: 340511  Cd Length: 74  Bit Score: 127.30  E-value: 4.63e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193083197   3 LPIIVKWGGQEYSVTTLSEDdTVLDLKQFLKTLTGVLPERQKLLGLKVKGKPAENDVKLGALKLKPNTKIMMMGT 77
Cdd:cd01813    1 ITLIVKWSGKEYPVTVLSSD-TVLDLKQRIFELTGVLPKRQKLLGLKVKGKPADDDVKLSSLKLKPNTKIMMMGT 74
 
Name Accession Description Interval E-value
HAD_IIID1 TIGR02245
HAD-superfamily subfamily IIID hydrolase, TIGR02245; This family of sequences appears to ...
 117-311 1.48e-129

HAD-superfamily subfamily IIID hydrolase, TIGR02245; This family of sequences appears to belong to the Haloacid Dehalogenase (HAD) superfamily of enzymes by virtue of the presence of three catalytic domains, in this case: LLVLD(ILV)D(YH)T, I(VMG)IWS, and (DN)(VC)K(PA)Lx{15-17}T(IL)(MH)(FV)DD(IL)(GRS)(RK)N. Since this family has no large "cap" domain between motifs 1 and 2 or between 2 and 3, it is formally a "class III" HAD.


Pssm-ID: 131299  Cd Length: 195  Bit Score: 367.22  E-value: 1.48e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197  117 KISRRVKEYKVEILNPPREGKKLLVLDVDYTLFDHRSCAETGVELMRPYLHEFLTSAYEDYDIVIWSATNMKWIEAKMKE 196
Cdd:TIGR02245   1 KLLRRIEQYKIKLLNPPREGKKLLVLDIDYTLFDHRSPAETGEELMRPYLHEFLTSAYEDYDIVIWSATSMKWIEIKMTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197  197 LGVSTNANYKITFMLDSAAMITVHTPRRGLIDVKPLGVIWGKFSEFYSKKNTIMFDDIGRNFLMNPQNGLKIRPFMKAHL 276
Cdd:TIGR02245  81 LGVLTNPNYKITFLLDSTAMITVHTPRRGKFDVKPLGVIWALLPEFYSMKNTIMFDDLRRNFLMNPKNGLKIRPFKKAHA 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 193083197  277 NRDKDKELLKLTQYLKEIAKLDDFLDLNHKYWERY 311
Cdd:TIGR02245 161 NRGTDQELLKLTQYLKTIAELEDFSSLDHKEWERY 195
Ubl_UBLCP1 cd01813
ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 ...
 3-77 4.63e-37

ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) and similar proteins; UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity. It is localized in the nucleus and it contains conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which directly interacts with the proteasome. Knockdown of UBLCP1 in cells promotes 26S proteasome assembly and selectively enhances nuclear proteasome activity. UBLCP1 may also play a role in the regulation of phosphorylation state of RNA polymerase II C-terminal domain, a key event during mRNA metabolism.


Pssm-ID: 340511  Cd Length: 74  Bit Score: 127.30  E-value: 4.63e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193083197   3 LPIIVKWGGQEYSVTTLSEDdTVLDLKQFLKTLTGVLPERQKLLGLKVKGKPAENDVKLGALKLKPNTKIMMMGT 77
Cdd:cd01813    1 ITLIVKWSGKEYPVTVLSSD-TVLDLKQRIFELTGVLPKRQKLLGLKVKGKPADDDVKLSSLKLKPNTKIMMMGT 74
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 138-300 1.15e-28

NLI interacting factor-like phosphatase; This family contains a number of NLI interacting factor isoforms and also an N-terminal regions of RNA polymerase II CTC phosphatase and FCP1 serine phosphatase. This region has been identified as the minimal phosphatase domain.


Pssm-ID: 397254  Cd Length: 160  Bit Score: 108.09  E-value: 1.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197  138 KLLVLDVDYTLFdHRSCAE---------------TGVELMRPYLHEFLTSAYEDYDIVIWSATNMKWIEAKMKELGvstN 202
Cdd:pfam03031   1 KTLVLDLDETLV-HSSFEPplksdfilpvpgethGGYVKKRPGLDEFLKELSKYYEIVIFTASSKEYADPVLDILD---P 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197  203 ANYKITFMLDSAAMITVhtprrGLIDVKPLGVIWgkfsefYSKKNTIMFDDIGRNFLMNPQNGLKIRPFMkahlNRDKDK 282
Cdd:pfam03031  77 NGKLFSHRLYRESCKFE-----DGVYVKDLSLLG------RDLSRVVIVDNSPDSFLLQPDNGIPIPPFF----GDPDDN 141

                         170
                  ....*....|....*...
gi 193083197  283 ELLKLTQYLKEIAKLDDF 300
Cdd:pfam03031 142 ELLKLLPFLEGLAGVDDV 159
CPDc smart00577
catalytic domain of ctd-like phosphatases;
136-271 7.27e-18

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 78.81  E-value: 7.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197   136 GKKLLVLDVDYTLF--DHRSCAETGVE-----------------LMRPYLHEFLTSAYEDYDIVIWSATNMKWIEAkmke 196
Cdd:smart00577   1 KKKTLVLDLDETLVhsTHRSFKEWTNRdfivpvlidghphgvyvKKRPGVDEFLKRASELFELVVFTAGLRMYADP---- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197   197 lgvstnanykITFMLDSAAMI------TVHTPRRGLIDVKPLGVIWGkfsefySKKNTIMFDDIGRNFLMNPQNGLKIRP 270
Cdd:smart00577  77 ----------VLDLLDPKKYFgyrrlfRDECVFVKGKYVKDLSLLNR------DLSKVIIIDDSPDSWPFHPENLIPIKP 140


                   .
gi 193083197   271 F 271
Cdd:smart00577 141 W 141
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 5-77 1.37e-11

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 59.19  E-value: 1.37e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193083197     5 IIVKWGGQEYSVTTLSEDDTVLDLKQFLKTLTGVLPERQKLLglkVKGKPAENDVKLGALKLKPNTKIMMMGT 77
Cdd:smart00213   3 LTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLI---YKGKVLEDDRTLADYGIQDGSTIHLVLR 72
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 5-77 8.26e-08

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 48.71  E-value: 8.26e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193083197    5 IIVK-WGGQEYSVTtLSEDDTVLDLKQFLKTLTGVLPERQKLLglkVKGKPAENDVKLGALKLKPNTKIMMMGT 77
Cdd:pfam00240   1 ITVKtLDGKKITLE-VDPTDTVLELKEKIAEKEGVPPEQQRLI---YSGKVLEDDQTLGEYGIEDGSTIHLVLR 70
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 137-188 7.20e-03

human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid dehalogenase-like superfamily; Human CTDP1/FCP1 is a protein phosphatase which dephosphorylates the phosphorylated C terminus (CTD) of RNA polymerase II. CTD phosphorylation is a key mechanism of regulation of gene expression in eukaryotes. CTDP1/FCP1 may have other roles in in transcription regulation independent of its phosphatase activity. This family also includes human translocase of inner mitochondrial membrane 50 (TIMM50), CTD small phosphatase like (CTDSPL) and CTD small phosphatase like 2 (CTDSPL2), Saccharomyces cerevisiae (nuclear envelope morphology protein 1) Nem1p, and Xenopus Dullard. Yeast Nem1p in complex with Spo7p dephosphorylates the nuclear membrane-associated phosphatidic acid phosphatase, Smp2p, which may be part of a signaling cascade playing a role in nuclear membrane biogenesis. Xenopus Dullard is a potential regulator of neural tube development. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319823  Cd Length: 134  Bit Score: 36.03  E-value: 7.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193083197 137 KKLLVLDVDYTLFdHRSCAETGVE-----------------LMRPYLHEFLTSAYEDYDIVIWSATNMK 188
Cdd:cd07521    1 KLTLVLDLDETLV-HSTWKPVLSEdfkipvlpdgrehgyyvKKRPGVDEFLERLSKLYEIVIFTAGTRA 68
 
Name Accession Description Interval E-value
HAD_IIID1 TIGR02245
HAD-superfamily subfamily IIID hydrolase, TIGR02245; This family of sequences appears to ...
 117-311 1.48e-129

HAD-superfamily subfamily IIID hydrolase, TIGR02245; This family of sequences appears to belong to the Haloacid Dehalogenase (HAD) superfamily of enzymes by virtue of the presence of three catalytic domains, in this case: LLVLD(ILV)D(YH)T, I(VMG)IWS, and (DN)(VC)K(PA)Lx{15-17}T(IL)(MH)(FV)DD(IL)(GRS)(RK)N. Since this family has no large "cap" domain between motifs 1 and 2 or between 2 and 3, it is formally a "class III" HAD.


Pssm-ID: 131299  Cd Length: 195  Bit Score: 367.22  E-value: 1.48e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197  117 KISRRVKEYKVEILNPPREGKKLLVLDVDYTLFDHRSCAETGVELMRPYLHEFLTSAYEDYDIVIWSATNMKWIEAKMKE 196
Cdd:TIGR02245   1 KLLRRIEQYKIKLLNPPREGKKLLVLDIDYTLFDHRSPAETGEELMRPYLHEFLTSAYEDYDIVIWSATSMKWIEIKMTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197  197 LGVSTNANYKITFMLDSAAMITVHTPRRGLIDVKPLGVIWGKFSEFYSKKNTIMFDDIGRNFLMNPQNGLKIRPFMKAHL 276
Cdd:TIGR02245  81 LGVLTNPNYKITFLLDSTAMITVHTPRRGKFDVKPLGVIWALLPEFYSMKNTIMFDDLRRNFLMNPKNGLKIRPFKKAHA 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 193083197  277 NRDKDKELLKLTQYLKEIAKLDDFLDLNHKYWERY 311
Cdd:TIGR02245 161 NRGTDQELLKLTQYLKTIAELEDFSSLDHKEWERY 195
Ubl_UBLCP1 cd01813
ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 ...
 3-77 4.63e-37

ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) and similar proteins; UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity. It is localized in the nucleus and it contains conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which directly interacts with the proteasome. Knockdown of UBLCP1 in cells promotes 26S proteasome assembly and selectively enhances nuclear proteasome activity. UBLCP1 may also play a role in the regulation of phosphorylation state of RNA polymerase II C-terminal domain, a key event during mRNA metabolism.


Pssm-ID: 340511  Cd Length: 74  Bit Score: 127.30  E-value: 4.63e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193083197   3 LPIIVKWGGQEYSVTTLSEDdTVLDLKQFLKTLTGVLPERQKLLGLKVKGKPAENDVKLGALKLKPNTKIMMMGT 77
Cdd:cd01813    1 ITLIVKWSGKEYPVTVLSSD-TVLDLKQRIFELTGVLPKRQKLLGLKVKGKPADDDVKLSSLKLKPNTKIMMMGT 74
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 138-300 1.15e-28

NLI interacting factor-like phosphatase; This family contains a number of NLI interacting factor isoforms and also an N-terminal regions of RNA polymerase II CTC phosphatase and FCP1 serine phosphatase. This region has been identified as the minimal phosphatase domain.


Pssm-ID: 397254  Cd Length: 160  Bit Score: 108.09  E-value: 1.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197  138 KLLVLDVDYTLFdHRSCAE---------------TGVELMRPYLHEFLTSAYEDYDIVIWSATNMKWIEAKMKELGvstN 202
Cdd:pfam03031   1 KTLVLDLDETLV-HSSFEPplksdfilpvpgethGGYVKKRPGLDEFLKELSKYYEIVIFTASSKEYADPVLDILD---P 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197  203 ANYKITFMLDSAAMITVhtprrGLIDVKPLGVIWgkfsefYSKKNTIMFDDIGRNFLMNPQNGLKIRPFMkahlNRDKDK 282
Cdd:pfam03031  77 NGKLFSHRLYRESCKFE-----DGVYVKDLSLLG------RDLSRVVIVDNSPDSFLLQPDNGIPIPPFF----GDPDDN 141

                         170
                  ....*....|....*...
gi 193083197  283 ELLKLTQYLKEIAKLDDF 300
Cdd:pfam03031 142 ELLKLLPFLEGLAGVDDV 159
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
 3-79 4.60e-18

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and similar proteins; USP14 (EC 3.4.19.12), also termed deubiquitinating enzyme 14, or ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, or ubiquitin carboxyl-terminal hydrolase 14, is a component of proteasome regulatory subunit 19S that regulates deubiquitinated proteins entering inside the proteasome core 20S, which plays an inhibitory role in protein degradation. USP14 is also associated with various signal transduction pathways and tumorigenesis, and thus plays an essential role in the development of various types of cancer. Moreover, USP14 mediates the development of cardiac hypertrophy by promoting GSK-3beta phosphorylation, suggesting a role in cardiac hypertrophy treatment. USP14 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal ubiquitin-specific protease (USP) domain.


Pssm-ID: 340521  Cd Length: 75  Bit Score: 77.27  E-value: 4.60e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193083197   3 LPIIVKWGGQEYSVTTLSEDDTVLDLKQFLKTLTGVLPERQKLLglkVKGKPAENDVKLGALKLKPNTKIMMMGTRE 79
Cdd:cd16104    2 YKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIM---VKGGVLKDDDDLSKLKLKDGQTLMLMGSAE 75
CPDc smart00577
catalytic domain of ctd-like phosphatases;
136-271 7.27e-18

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 78.81  E-value: 7.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197   136 GKKLLVLDVDYTLF--DHRSCAETGVE-----------------LMRPYLHEFLTSAYEDYDIVIWSATNMKWIEAkmke 196
Cdd:smart00577   1 KKKTLVLDLDETLVhsTHRSFKEWTNRdfivpvlidghphgvyvKKRPGVDEFLKRASELFELVVFTAGLRMYADP---- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197   197 lgvstnanykITFMLDSAAMI------TVHTPRRGLIDVKPLGVIWGkfsefySKKNTIMFDDIGRNFLMNPQNGLKIRP 270
Cdd:smart00577  77 ----------VLDLLDPKKYFgyrrlfRDECVFVKGKYVKDLSLLNR------DLSKVIIIDDSPDSWPFHPENLIPIKP 140


                   .
gi 193083197   271 F 271
Cdd:smart00577 141 W 141
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 5-77 1.37e-11

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 59.19  E-value: 1.37e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193083197     5 IIVKWGGQEYSVTTLSEDDTVLDLKQFLKTLTGVLPERQKLLglkVKGKPAENDVKLGALKLKPNTKIMMMGT 77
Cdd:smart00213   3 LTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLI---YKGKVLEDDRTLADYGIQDGSTIHLVLR 72
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 5-75 2.18e-09

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 52.98  E-value: 2.18e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193083197   5 IIVKW-GGQEYSVTtLSEDDTVLDLKQFLKTLTGVLPERQKLLglkVKGKPAENDVKLGALKLKPNTKIMMM 75
Cdd:cd17039    1 ITVKTlDGKTYTVE-VDPDDTVADLKEKIEEKTGIPVEQQRLI---YNGKELKDDKTLSDYGIKDGSTIHLV 68
Ubl_UBFD1 cd17047
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar ...
 5-77 4.18e-08

ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar proteins; UBFD1, also termed ubiquitin-binding protein homolog (UBPH), is a polyubiquitin binding protein containing a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. It may play a role as nuclear factor-kappaB (NF-kappaB) regulator.


Pssm-ID: 340567  Cd Length: 70  Bit Score: 49.55  E-value: 4.18e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193083197   5 IIVKWGGQEYSVTtLSEDDTVLDLKQFLKTLTGVLPERQKLLglkVKGKpAENDVKLGALKLKPNTKIMMMGT 77
Cdd:cd17047    3 FKVIWNKEKYDVK-FPLDSTIAELKEHIETLTGVPPAMQKLM---YKGL-LKDDKTLRELKVTKGAKVMVVGS 70
Ubl_BAG1 cd01812
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and ...
 3-78 4.72e-08

ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and similar proteins; BAG1, also termed Bcl-2-associated athanogene 1, or HAP, is a multifunctional protein involved in a variety of cellular functions such as apoptosis, transcription, and proliferative pathways, as well as in cell signaling and differentiation. It delivers chaperone-recognized unfolded substrates to the proteasome for degradation. BAG1 functions as a co-chaperone for Hsp70/Hsc70 to increase Hsp70 foldase activity. It also suppresses apoptosis and enhances neuronal differentiation. As an anti-apoptotic factor, BAG1 interacts with tau and regulates its proteasomal degradation. It also binds to BCR-ABL with a high affinity, and directly routes immature BCR-ABL for proteasomal degradation. It acts as a potential therapeutic target in Parkinson's disease. It also modulates huntingtin toxicity, aggregation, degradation, and subcellular distribution, suggesting a role in Huntington's disease. There are at least four isoforms of Bag1 protein that are formed by alternative initiation of translation within a common mRNA. BAG1 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal BAG domain.


Pssm-ID: 340510 [Multi-domain]  Cd Length: 77  Bit Score: 49.58  E-value: 4.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197   3 LPIIVKWGGQEYSVTTLSEDD---TVLDLKQFLKTLTGVLPERQKLLglkVKGKP-AENDVKLGALKLKPNTKIMMMGTR 78
Cdd:cd01812    1 LTVTVIHGSNKHTIELPSQDEdepTLQDLAEAIEEVTGVPVENQKLI---FKGKSlKDPEQPLSALGVKNGSKIMLIGKK 77
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 5-77 8.26e-08

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 48.71  E-value: 8.26e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193083197    5 IIVK-WGGQEYSVTtLSEDDTVLDLKQFLKTLTGVLPERQKLLglkVKGKPAENDVKLGALKLKPNTKIMMMGT 77
Cdd:pfam00240   1 ITVKtLDGKKITLE-VDPTDTVLELKEKIAEKEGVPPEQQRLI---YSGKVLEDDQTLGEYGIEDGSTIHLVLR 70
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 137-299 6.74e-05

Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a family of eukaryotic proteins including "Dullard", and the NLI interacting factor (NIF)-like phosphatases. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDNxPxxa) and aparrently lacking the last aspartate. This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in FCP1-like phosphatases (TIGR02250), and together both are detected by the pfam03031.


Pssm-ID: 274055  Cd Length: 162  Bit Score: 42.67  E-value: 6.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197  137 KKLLVLDVDYTLFD---HRSCAETGVELM--------------RPYLHEFLTSAYEDYDIVIWSA-------TNMKWIEA 192
Cdd:TIGR02251   1 KKTLVLDLDETLVHstfKMPKVDADFKVPvlidgkiiqvyvfkRPHVDEFLERVSKWYELVIFTAsleeyadPVLDILDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083197  193 KMKELG--------VSTNANYkitfmldsaamitvhtprrglidVKPLGVIWGKFSefyskkNTIMFDDIGRNFLMNPQN 264
Cdd:TIGR02251  81 GGKVISrrlyrescVFTNGKY-----------------------VKDLSLVGKDLS------KVIIIDNSPYSYSLQPDN 131

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 193083197  265 GLKIRPFMKAhlnrDKDKELLKLTQYLKEIAKLDD 299
Cdd:TIGR02251 132 AIPIKSWFSD----PNDTELLNLIPFLEGLRFEDD 162
Ubl_FUBI cd01793
ubiquitin-like (Ubl) domain found in ubiquitin-like protein FUBI and similar proteins; FUBI is ...
 11-62 8.84e-04

ubiquitin-like (Ubl) domain found in ubiquitin-like protein FUBI and similar proteins; FUBI is a pro-apoptotic regulatory gene FAU encoding ubiquitin-like protein with ribosomal protein S30 as a C-terminal extension. FUBI functions as a tumor suppressor protein that may be involved in the ATP-dependent proteolytic activity of ubiquitin. The N-terminal ubiquitin-like (Ubl) domain of FUBI has the beta-grasp Ubl fold, and it may act as a substitute or an inhibitor of ubiquitin or one of ubiquitin's close relatives UCRP, FAT10, and Nedd8.


Pssm-ID: 340491  Cd Length: 74  Bit Score: 37.26  E-value: 8.84e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 193083197  11 GQEYSVTTLSEDDTVLDLKQFLKTLTGVLPERQKLLglkVKGKPAENDVKLG 62
Cdd:cd01793    7 AQSLHTLEVSGNETVADIKAHIAALEGIAVEDQVLL---YAGAPLEDDVVLG 55
Ubl_OTU1 cd17059
ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 ...
 5-46 1.11e-03

ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 (EC 3.4.19.12), also termed YOD1, or DUBA-8, or HIV-1-induced protease 7 (HIN-7), or OTU domain-containing protein 2 (OTUD2), is a p97-associated deubiquitinylase that functions as a key player in endoplasmic reticulum-associated degradation (ERAD). Its deubiquitinylase activity is also required for negatively regulating cholera toxin A1 (CTA1) retro-translocation. OTU1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU domain.


Pssm-ID: 340579  Cd Length: 75  Bit Score: 37.19  E-value: 1.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 193083197   5 IIVKWGGQEYSVTTLSEDDTVLDLKQFLKTLTGVLPERQKLL 46
Cdd:cd17059    3 LRVRSKGGQHVLSLLTDTSTVGELQDRIAALTGIPPSSQKIL 44
Ubl_Dsk2p_like cd16106
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ...
 10-45 6.67e-03

ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein Dsk2p and similar proteins; The family contains several fungal multiubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (Ubl) and with ubiquitin (Ub) through their C-terminal Ub-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is an ubiquitin (Ub0 receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect Ub chains against disassembly by deubiquitinating enzymes.


Pssm-ID: 340523 [Multi-domain]  Cd Length: 73  Bit Score: 34.92  E-value: 6.67e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 193083197  10 GGQEYSVTtLSEDDTVLDLKQFLKTLTGVLPERQKL 45
Cdd:cd16106    9 NGKKFTVE-VEPDATVLELKELIAEKSDIPAEQQRL 43
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 137-188 7.20e-03

human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid dehalogenase-like superfamily; Human CTDP1/FCP1 is a protein phosphatase which dephosphorylates the phosphorylated C terminus (CTD) of RNA polymerase II. CTD phosphorylation is a key mechanism of regulation of gene expression in eukaryotes. CTDP1/FCP1 may have other roles in in transcription regulation independent of its phosphatase activity. This family also includes human translocase of inner mitochondrial membrane 50 (TIMM50), CTD small phosphatase like (CTDSPL) and CTD small phosphatase like 2 (CTDSPL2), Saccharomyces cerevisiae (nuclear envelope morphology protein 1) Nem1p, and Xenopus Dullard. Yeast Nem1p in complex with Spo7p dephosphorylates the nuclear membrane-associated phosphatidic acid phosphatase, Smp2p, which may be part of a signaling cascade playing a role in nuclear membrane biogenesis. Xenopus Dullard is a potential regulator of neural tube development. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319823  Cd Length: 134  Bit Score: 36.03  E-value: 7.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193083197 137 KKLLVLDVDYTLFdHRSCAETGVE-----------------LMRPYLHEFLTSAYEDYDIVIWSATNMK 188
Cdd:cd07521    1 KLTLVLDLDETLV-HSTWKPVLSEdfkipvlpdgrehgyyvKKRPGVDEFLERLSKLYEIVIFTAGTRA 68
Ubl_Rad23 cd01805
ubiquitin-like (Ubl) domain found in the Rad23 protein family; The Rad23 family includes the ...
 19-75 8.92e-03

ubiquitin-like (Ubl) domain found in the Rad23 protein family; 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 an ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and two ubiquitin-associated (UBA) domains, as well as a xeroderma pigmentosum group C (XPC) protein-binding domain. The Ubl domain is responsible for the binding to proteasome. The UBA domains are important for binding of ubiquitin (Ub) or multi-ubiquitinated substrates, which suggests Rad23 proteins might be involved in certain pathways of Ub metabolism. Both the Ubl domain and the XPC-binding domain are necessary for efficient NER function of Rad23 proteins.


Pssm-ID: 340503 [Multi-domain]  Cd Length: 72  Bit Score: 34.46  E-value: 8.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193083197  19 LSEDDTVLDLKQFLKTLTGVLP-ERQKLLglkVKGKPAENDVKLGALKLKPNTKIMMM 75
Cdd:cd01805   17 VEPSDTVLELKEKIEQEQGDFPaSGQKLI---YSGKVLKDDKTLSEYNIKEKDFVVVM 71
 
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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