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Conserved domains on  [gi|528504961|ref|XP_005158446|]
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OTU domain-containing protein 7B isoform X4 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OTU_OTUD7B cd22772
OTU (ovarian tumor) domain of OTU domain-containing protein 7B; OTU domain-containing protein ...
 152-356 6.61e-154

OTU (ovarian tumor) domain of OTU domain-containing protein 7B; OTU domain-containing protein 7B (OTUD7B) is also called cellular zinc finger anti-NF-kappa-B protein, zinc finger A20 domain-containing protein 1, or zinc finger protein Cezanne. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically targets Lys11-linked polyubiquitin. It functions as a negative regulator of the non-canonical NF-kappaB pathway by mediating the deubiquitination of TRAF3, an inhibitor of the NF-kappaB pathway, resulting in preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappaB. OTUD7B also deubiquitinates ZAP70, and thus, regulates T cell receptor (TCR) signaling. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS.


:

Pssm-ID: 438609  Cd Length: 207  Bit Score: 451.03  E-value: 6.61e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 152 QSMMVALEQAGRLNWWTRLGTGCQSLLPLATSGDGNCLLHAASLGMWGFHDRDLMLRKSLYALMDHGQEREALKRRWRWQ 231
Cdd:cd22772    1 QSMLVALEQAGRLNWWVSVDPTCQRLLPLATTGDGNCLLHAASLGMWGFHDRDLMLRKALYALMEKGVEKEALKRRWRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 232 QTMQNKESGLVYTEEEWQKEWNELLKLASSEPRIHYSTNGS--SGAESQEEPVYESLEEFHVFVLAHVLRRPIVVVADTM 309
Cdd:cd22772   81 QTQQNKESGLVYTEDEWQKEWNELIKLASSEPRMHYGTNGAncGGVESSEEPVYESLEEFHVFVLAHVLRRPIVVVADTM 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528504961 310 LRDSGGEAFAPIPFGGIYLPLEVPANKCHRSPLVLAYDQAHFSALVS 356
Cdd:cd22772  161 LRDSGGEAFAPIPFGGIYLPLEVPASKCHRSPLVLAYDQAHFSALVS 207
UBA_Cezanne_like cd14347
UBA-like domain found in OTU domain-containing proteins OTU7A, OTU7B and similar proteins; ...
 4-46 4.70e-25

UBA-like domain found in OTU domain-containing proteins OTU7A, OTU7B and similar proteins; OTU7A, also called zinc finger protein Cezanne 2, belongs to a family of proteins that have been characterized as highly specific ubiquitin iso-peptidases removing ubiquitin from proteins. OTU7B, also called cellular zinc finger anti-NF-kappaB protein, zinc finger A20 domain-containing protein 1, or zinc finger protein Cezanne, is a novel deubiquitinating enzyme that acts as a negative regulator of NF-kappaB and may play a role in the control of the inflammatory process. Both OTU7A and OTU7B contain an N-terminal ubiquitin-associated (UBA)-like domain, followed by an ovarian tumor (OTU) domain and a ubiquitin binding domain, A20-like zinc finger. In addition, they both display proteolytic activity.


:

Pssm-ID: 270532  Cd Length: 43  Bit Score: 98.10  E-value: 4.70e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 528504961   4 DMDAVLSDFVRSTGAEPGLARDLLEGKNWDLSAALSDFEQLRQ 46
Cdd:cd14347    1 DMDAVLSDFVRSTGAEPGLARDLLEGKNWDLTAALSDYEQLRQ 43
zf-A20 pfam01754
A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding ...
 879-903 4.10e-06

A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding Domain. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappa B activation.


:

Pssm-ID: 460313  Cd Length: 24  Bit Score: 44.03  E-value: 4.10e-06
                          10        20
                  ....*....|....*....|....*
gi 528504961  879 SKCRTPtCNYYGHPETGNYCSYCYR 903
Cdd:pfam01754   1 LLCRNG-CGFYGSPATNGLCSKCYK 24
SOBP super family cl25880
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
 720-826 3.24e-03

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


The actual alignment was detected with superfamily member pfam15279:

Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 40.57  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961  720 PPNFNALKSSSFSPVMYSGVVPIPRHTFIDHSPSPMTQHLHMHHGYMDTRRQlaggsPSSYPGLPSYATL-PRHCPLAQG 798
Cdd:pfam15279 175 GKPQQHPPPSPLPAFMEPSSMPPPFLRPPPSIPQPNSPLSNPMLPGIGPPPK-----PPRNLGPPSNPMHrPPFSPHHPP 249

                          90       100
                  ....*....|....*....|....*...
gi 528504961  799 PPHAQYHPPSASLGSPSRIITPcLTSFP 826
Cdd:pfam15279 250 PPPTPPGPPPGLPPPPPRGFTP-PFGPP 276
 
Name Accession Description Interval E-value
OTU_OTUD7B cd22772
OTU (ovarian tumor) domain of OTU domain-containing protein 7B; OTU domain-containing protein ...
 152-356 6.61e-154

OTU (ovarian tumor) domain of OTU domain-containing protein 7B; OTU domain-containing protein 7B (OTUD7B) is also called cellular zinc finger anti-NF-kappa-B protein, zinc finger A20 domain-containing protein 1, or zinc finger protein Cezanne. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically targets Lys11-linked polyubiquitin. It functions as a negative regulator of the non-canonical NF-kappaB pathway by mediating the deubiquitination of TRAF3, an inhibitor of the NF-kappaB pathway, resulting in preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappaB. OTUD7B also deubiquitinates ZAP70, and thus, regulates T cell receptor (TCR) signaling. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS.


Pssm-ID: 438609  Cd Length: 207  Bit Score: 451.03  E-value: 6.61e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 152 QSMMVALEQAGRLNWWTRLGTGCQSLLPLATSGDGNCLLHAASLGMWGFHDRDLMLRKSLYALMDHGQEREALKRRWRWQ 231
Cdd:cd22772    1 QSMLVALEQAGRLNWWVSVDPTCQRLLPLATTGDGNCLLHAASLGMWGFHDRDLMLRKALYALMEKGVEKEALKRRWRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 232 QTMQNKESGLVYTEEEWQKEWNELLKLASSEPRIHYSTNGS--SGAESQEEPVYESLEEFHVFVLAHVLRRPIVVVADTM 309
Cdd:cd22772   81 QTQQNKESGLVYTEDEWQKEWNELIKLASSEPRMHYGTNGAncGGVESSEEPVYESLEEFHVFVLAHVLRRPIVVVADTM 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528504961 310 LRDSGGEAFAPIPFGGIYLPLEVPANKCHRSPLVLAYDQAHFSALVS 356
Cdd:cd22772  161 LRDSGGEAFAPIPFGGIYLPLEVPASKCHRSPLVLAYDQAHFSALVS 207
UBA_Cezanne_like cd14347
UBA-like domain found in OTU domain-containing proteins OTU7A, OTU7B and similar proteins; ...
 4-46 4.70e-25

UBA-like domain found in OTU domain-containing proteins OTU7A, OTU7B and similar proteins; OTU7A, also called zinc finger protein Cezanne 2, belongs to a family of proteins that have been characterized as highly specific ubiquitin iso-peptidases removing ubiquitin from proteins. OTU7B, also called cellular zinc finger anti-NF-kappaB protein, zinc finger A20 domain-containing protein 1, or zinc finger protein Cezanne, is a novel deubiquitinating enzyme that acts as a negative regulator of NF-kappaB and may play a role in the control of the inflammatory process. Both OTU7A and OTU7B contain an N-terminal ubiquitin-associated (UBA)-like domain, followed by an ovarian tumor (OTU) domain and a ubiquitin binding domain, A20-like zinc finger. In addition, they both display proteolytic activity.


Pssm-ID: 270532  Cd Length: 43  Bit Score: 98.10  E-value: 4.70e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 528504961   4 DMDAVLSDFVRSTGAEPGLARDLLEGKNWDLSAALSDFEQLRQ 46
Cdd:cd14347    1 DMDAVLSDFVRSTGAEPGLARDLLEGKNWDLTAALSDYEQLRQ 43
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 184-351 1.01e-19

OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian Tumour (OTU) gene in Drosophila. Members include proteins from eukaryotes, viruses and pathogenic bacterium. The conserved cysteine and histidine, and possibly the aspartate, represent the catalytic residues in this putative group of proteases.


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 85.97  E-value: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961  184 GDGNCLLHAASLGMWGFHDrdlMLRKSLYalmdhgqerEALkrRWRWQQTMQNKESGlvyTEEEWQKEWNELLKLASSep 263
Cdd:pfam02338   2 GDGNCLYRSISHQLWGVHD---VLRKMLV---------QEL--RETLAEYMREHKEE---FEPFLEDDETGDIIEIEQ-- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961  264 rihystNGSSGaesqeepvyeslEEFHVFVLAHVLRRPIVVvadtmLRDSGGEAFAPIPFGGIYLPLEVPANKCHRSPLV 343
Cdd:pfam02338  63 ------TGAWG------------GEIEIFALAHILRRPIIV-----YKSEGGEELGGLKEYGIYLPLGWDPSLCLVYPRH 119


                  ....*...
gi 528504961  344 LAYDQAHF 351
Cdd:pfam02338 120 LYYLGGHY 127
zf-A20 pfam01754
A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding ...
 879-903 4.10e-06

A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding Domain. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappa B activation.


Pssm-ID: 460313  Cd Length: 24  Bit Score: 44.03  E-value: 4.10e-06
                          10        20
                  ....*....|....*....|....*
gi 528504961  879 SKCRTPtCNYYGHPETGNYCSYCYR 903
Cdd:pfam01754   1 LLCRNG-CGFYGSPATNGLCSKCYK 24
UBA_4 pfam14555
UBA-like domain;
6-41 2.07e-04

UBA-like domain;


Pssm-ID: 464207  Cd Length: 43  Bit Score: 39.36  E-value: 2.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 528504961    6 DAVLSDFVRSTGAEPGLARDLLEGKNWDLSAALSDF 41
Cdd:pfam14555   1 DELIAQFQAITGADEEVARQYLEAHNWDLEAAVNAF 36
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 879-903 3.73e-04

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


Pssm-ID: 128555  Cd Length: 26  Bit Score: 38.34  E-value: 3.73e-04
                           10        20
                   ....*....|....*....|....*
gi 528504961   879 SKCRTPTCNYYGHPETGNYCSYCYR 903
Cdd:smart00259   2 IKCRRPGCGFFGNPATEGLCSKCFK 26
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
 720-826 3.24e-03

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 40.57  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961  720 PPNFNALKSSSFSPVMYSGVVPIPRHTFIDHSPSPMTQHLHMHHGYMDTRRQlaggsPSSYPGLPSYATL-PRHCPLAQG 798
Cdd:pfam15279 175 GKPQQHPPPSPLPAFMEPSSMPPPFLRPPPSIPQPNSPLSNPMLPGIGPPPK-----PPRNLGPPSNPMHrPPFSPHHPP 249

                          90       100
                  ....*....|....*....|....*...
gi 528504961  799 PPHAQYHPPSASLGSPSRIITPcLTSFP 826
Cdd:pfam15279 250 PPPTPPGPPPGLPPPPPRGFTP-PFGPP 276
 
Name Accession Description Interval E-value
OTU_OTUD7B cd22772
OTU (ovarian tumor) domain of OTU domain-containing protein 7B; OTU domain-containing protein ...
 152-356 6.61e-154

OTU (ovarian tumor) domain of OTU domain-containing protein 7B; OTU domain-containing protein 7B (OTUD7B) is also called cellular zinc finger anti-NF-kappa-B protein, zinc finger A20 domain-containing protein 1, or zinc finger protein Cezanne. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically targets Lys11-linked polyubiquitin. It functions as a negative regulator of the non-canonical NF-kappaB pathway by mediating the deubiquitination of TRAF3, an inhibitor of the NF-kappaB pathway, resulting in preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappaB. OTUD7B also deubiquitinates ZAP70, and thus, regulates T cell receptor (TCR) signaling. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS.


Pssm-ID: 438609  Cd Length: 207  Bit Score: 451.03  E-value: 6.61e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 152 QSMMVALEQAGRLNWWTRLGTGCQSLLPLATSGDGNCLLHAASLGMWGFHDRDLMLRKSLYALMDHGQEREALKRRWRWQ 231
Cdd:cd22772    1 QSMLVALEQAGRLNWWVSVDPTCQRLLPLATTGDGNCLLHAASLGMWGFHDRDLMLRKALYALMEKGVEKEALKRRWRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 232 QTMQNKESGLVYTEEEWQKEWNELLKLASSEPRIHYSTNGS--SGAESQEEPVYESLEEFHVFVLAHVLRRPIVVVADTM 309
Cdd:cd22772   81 QTQQNKESGLVYTEDEWQKEWNELIKLASSEPRMHYGTNGAncGGVESSEEPVYESLEEFHVFVLAHVLRRPIVVVADTM 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528504961 310 LRDSGGEAFAPIPFGGIYLPLEVPANKCHRSPLVLAYDQAHFSALVS 356
Cdd:cd22772  161 LRDSGGEAFAPIPFGGIYLPLEVPASKCHRSPLVLAYDQAHFSALVS 207
OTU_OTUD7 cd22768
OTU (ovarian tumor) domain of OTU domain-containing proteins 7A, 7B, and similar proteins; ...
 152-356 1.38e-133

OTU (ovarian tumor) domain of OTU domain-containing proteins 7A, 7B, and similar proteins; This subfamily consists of OTU domain-containing protein 7A (OTUD7A), OTUD7B, and similar proteins. OTUD7A and OTUD7B are deubiquitinases (DUBs)/ubiquitin thioesterases (EC 3.4.19.12) that specifically target Lys11-linked polyubiquitin. OTUD7A, also called zinc finger protein Cezanne 2, has been identified as a critical gene for brain function. It localizes to dendritic and spine compartments in cortical neurons, and its reduced levels contributed to dendritic spine and dendrite outgrowth deficits. OTUD7B, also called zinc finger protein Cezanne, functions as a negative regulator of the non-canonical NF-kappaB pathway by mediating the deubiquitination of TRAF3, an inhibitor of the NF-kappaB pathway, resulting in preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappaB. OTUD7 proteins belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. They are classified as family C64 cysteine proteases by MEROPS.


Pssm-ID: 438605  Cd Length: 208  Bit Score: 398.22  E-value: 1.38e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 152 QSMMVALEQAGRLNWWTRLGTgCQSLLPLATSGDGNCLLHAASLGMWGFHDRDLMLRKSLYALMDHGQEREALKRRWRWQ 231
Cdd:cd22768    1 TSTLVSLEQAGRLNWWAKDGG-CQRLLPLATTGDGNCLLHAASLGMWGFHDRLLTLRKALYETLTSSAAKEALKRRWRWQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 232 QTMQNKESGLVYTEEEWQKEWNELLKLASSEPRIHYSTNGSSGA----ESQEEPVYESLEEFHVFVLAHVLRRPIVVVAD 307
Cdd:cd22768   80 QTQVNKEAGLVYSEEEWEREWKSLLKLASTEPRSQPSPSSGSELeeviENSSDPTYESLEEIHVFVLAHVLRRPIIVVAD 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 528504961 308 TMLRDSGGEAFAPIPFGGIYLPLEVPANKCHRSPLVLAYDQAHFSALVS 356
Cdd:cd22768  160 TMLRDSNGEPLAPIPFGGIYLPLECPPSECHRSPLVLAYDAAHFSALVP 208
OTU_OTUD7A cd22773
OTU (ovarian tumor) domain of OTU domain-containing protein 7A; OTU domain-containing protein ...
 152-356 4.02e-126

OTU (ovarian tumor) domain of OTU domain-containing protein 7A; OTU domain-containing protein 7A (OTUD7A), also called zinc finger protein Cezanne 2, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically targets Lys11-linked polyubiquitin. OTUD7A has been identified as a critical gene for brain function. It localizes to dendritic and spine compartments in cortical neurons, and its reduced levels contributed to dendritic spine and dendrite outgrowth deficits. A homozygous OTUD7A missense variant located within the OTU catalytic domain is linked to early-onset epileptic encephalopathy and proteasome dysfunction. OTUD7A belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS.


Pssm-ID: 438610  Cd Length: 207  Bit Score: 379.03  E-value: 4.02e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 152 QSMMVALEQAGRLNWWTRLGTGCQSLLPLATSGDGNCLLHAASLGMWGFHDRDLMLRKSLYALMDHGQEREALKRRWRWQ 231
Cdd:cd22773    1 QSTMVALEQAGRLNWWSTVCTSCKRLLPLATTGDGNCLLHAASLGMWGFHDRDLVLRKALYTMMKSGAEREALKRRWRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 232 QTMQNKESGLVYTEEEWQKEWNELLKLASSEPRIHYSTNGSS--GAESQEEPVYESLEEFHVFVLAHVLRRPIVVVADTM 309
Cdd:cd22773   81 QTQQNKESGLVYTEEEWEREWNELLKLASSEPRTHFSKNGGTggGVDNSEDPVYESLEEFHVFVLAHILRRPIVVVADTM 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528504961 310 LRDSGGEAFAPIPFGGIYLPLEVPANKCHRSPLVLAYDQAHFSALVS 356
Cdd:cd22773  161 LRDSGGEAFAPIPFGGIYLPLEVPPNRCHCSPLVLAYDQAHFSALVS 207
OTU_TNFAIP3 cd22766
OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis ...
 128-355 2.33e-82

OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis factor (TNF) alpha-induced protein 3 (TNFAIP3) is also called OTU domain-containing protein 7C (OTUD7C), DNA-binding protein A20, or zinc finger protein A20. It is a ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. It antagonizes IKK [IkappaB (inhibitor of kappaB) kinase] activation by modulating Lys63-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP1 (receptor-interacting protein 1). It can also inhibit IKK through a non-catalytic mechanism which involves polyubiquitin. In vitro, TNFAIP3 is able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. TNFAIP3 contains several A20-type zinc fingers that mediate the ubiquitin ligase activity and an OTU (ovarian tumor) domain that contains the DUB activity. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS.


Pssm-ID: 438603  Cd Length: 220  Bit Score: 264.51  E-value: 2.33e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 128 TFQLPDLTVYRDDFRGFIERDLIEQSMMVALEQAGRLNWWTRLgtgcQSLLPLATSGDGNCLLHAASLGMWGFHDRDLML 207
Cdd:cd22766    7 TLQLPRLCQFPPDFREFLQKALIDRNIQRTLEEAKKLNWCREV----RKLVPLKTTGDGNCLLHAVSLYMWGVQDTDLVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 208 RKSLYALMdHGQEREALKRRWR--WQQTMQNKESGLVYTEEEWQKEWNELLKLASSEPRihystngssgaESQEEPVYES 285
Cdd:cd22766   83 RKALYEAL-VETDTRNFKLRWQreRLKSQEFVGTGLRYDTREWEEEWDNVVKMASPESK-----------PAAGGLPYNS 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 286 LEEFHVFVLAHVLRRPIVVVADTMLRDSGGEAFAPIPFGGIYLPLEVPANKCHRSPLVLAYDQAHFSALV 355
Cdd:cd22766  151 LEEIHIFVLANILRRPIIVIADDMLRSLEGSSLAPLNFGGIYLPLHWPPQECYKYPIVLGYDSQHFTPLV 220
OTU_C64 cd22750
OTU (ovarian tumor) domain of family C64 cysteine proteases; This group includes proteins ...
 152-355 1.08e-77

OTU (ovarian tumor) domain of family C64 cysteine proteases; This group includes proteins classified as family C64 cysteine protease by MEROPS, such as tumor necrosis factor (TNF) alpha-induced protein 3 (TNFAIP3), ZRANB1, OTU domain-containing protein 7A (OTUD7A), and OTUD7B. It also includes VCIP135. These proteins are deubiquitinases (DUBs)/ubiquitin thioesterases (EC 3.4.19.12) that mediates the deubiquitination of protein substrates. TNFAIP3 also contains ubiquitin ligase activity. It antagonizes IKK [IkappaB (inhibitor of kappaB) kinase] activation by modulating Lys63-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP1 (receptor-interacting protein 1). ZRANB1 binds, deubiquitinates, and stabilizes EZH2, which is the catalytic component of the Polycomb repressive complex 2 (PRC2) that silences gene transcription by methylating histone H3 at lysine 27 and is mutated or highly expressed in many types of cancer, including lymphoma, melanoma, prostate cancer, ovarian cancer, and breast cancer. OTUD7A has been identified as a critical gene for brain function, while OTUD7B functions as a negative regulator of the non-canonical NF-kappaB pathway by mediating the deubiquitination of TRAF3, an inhibitor of the NF-kappaB pathway, resulting in preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappaB. VCIP135 controls Golgi membrane dynamics in the cell cycle and is required for Golgi and ER assembly. This group belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad.


Pssm-ID: 438587  Cd Length: 185  Bit Score: 250.72  E-value: 1.08e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 152 QSMMVALEQAGRLNWwtrlGTGCQSLLPLATSGDGNCLLHAASLGMWGFHDRDLMLRKSLYALMDHGQEReALKRRWRWQ 231
Cdd:cd22750    1 RDLKDDLESEKVINW----CRGVSRLVPLHTRGDGNCLLHAVSLALWGVEDRDLLLRSALHETLQNDQER-RFRARWRRQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 232 QTMQNKESGLVYTEEEWQKEWNELLKLASSEPRIHystngssgaesqeePVYESLEEFHVFVLAHVLRRPIVVVADTMLR 311
Cdd:cd22750   76 QLKSGQELGLSLDEEALQAEWEEILKAAETPTVPA--------------GPGSYLEEIHIFVLANVLRRPIIVLADDSAR 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 528504961 312 DSGGEAFAPIPFGGIYLPLEVPANKCHRSPLVLAYDQAHFSALV 355
Cdd:cd22750  142 SLEGSALQDNGMSGIYLPLLWPPSECSRSPLALGYSNGHFSPLV 185
OTU_ZRANB1 cd22767
OTU (ovarian tumor) domain of Ubiquitin thioesterase ZRANB1 and similar proteins; ZRANB1 is ...
 158-356 7.87e-41

OTU (ovarian tumor) domain of Ubiquitin thioesterase ZRANB1 and similar proteins; ZRANB1 is also called TRAF-binding domain-containing protein, Trabid, or zinc finger Ran-binding domain-containing protein 1. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin; it also cleaves 'Lys-63'-linked chains with less efficiency. ZRANB1 binds, deubiquitinates, and stabilizes EZH2, which is the catalytic component of the Polycomb repressive complex 2 (PRC2) that silences gene transcription by methylating histone H3 at lysine 27 and is mutated or highly expressed in many types of cancer, including lymphoma, melanoma, prostate cancer, ovarian cancer, and breast cancer. Drosophila Trabid interacts with TGF-beta Activating Kinase 1 (TAK1), which triggers both immunity and apoptosis, resulting in reduced immune signaling output and K63-linked ubiquitination. ZRANB1 belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. ZRANB1 does not contain the conserved aspartate, and uses cysteine and histidine as a catalytic dyad. It is classified as a family C64 cysteine protease by MEROPS.


Pssm-ID: 438604  Cd Length: 185  Bit Score: 148.22  E-value: 7.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 158 LEQAGR-LNWWTRLGTGCQS-LLPLATSGDGNCLLHAASLGMWGFHDRDLMLRKSLYALMDHGQEReaLKRRWRWQQTMQ 235
Cdd:cd22767    7 LEEESPiINWSLELTDRLGSrLYALWNRTAGDCLLDSVLQATWGVFDRDNVLRRALADSLHDCAHW--FYSRWKEYESWQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 236 NKESGLVYTEEEWQKEWNELLKLASSePRihystngssgaesqeepvyESLEEFHVFVLAHVLRRPIVVVADTMLRDSGG 315
Cdd:cd22767   85 AQSLGYSLEEEQWQKDWAFLLSLASQ-PG-------------------ASLEQTHIFALAHILRRPIIVYGVKYVKSFRG 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528504961 316 EAFAPIPFGGIYLPLEVPANKCHRSPLVLAYDQAHFSALVS 356
Cdd:cd22767  145 ETLGYARFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVP 185
UBA_Cezanne_like cd14347
UBA-like domain found in OTU domain-containing proteins OTU7A, OTU7B and similar proteins; ...
 4-46 4.70e-25

UBA-like domain found in OTU domain-containing proteins OTU7A, OTU7B and similar proteins; OTU7A, also called zinc finger protein Cezanne 2, belongs to a family of proteins that have been characterized as highly specific ubiquitin iso-peptidases removing ubiquitin from proteins. OTU7B, also called cellular zinc finger anti-NF-kappaB protein, zinc finger A20 domain-containing protein 1, or zinc finger protein Cezanne, is a novel deubiquitinating enzyme that acts as a negative regulator of NF-kappaB and may play a role in the control of the inflammatory process. Both OTU7A and OTU7B contain an N-terminal ubiquitin-associated (UBA)-like domain, followed by an ovarian tumor (OTU) domain and a ubiquitin binding domain, A20-like zinc finger. In addition, they both display proteolytic activity.


Pssm-ID: 270532  Cd Length: 43  Bit Score: 98.10  E-value: 4.70e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 528504961   4 DMDAVLSDFVRSTGAEPGLARDLLEGKNWDLSAALSDFEQLRQ 46
Cdd:cd14347    1 DMDAVLSDFVRSTGAEPGLARDLLEGKNWDLTAALSDYEQLRQ 43
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 184-351 1.01e-19

OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian Tumour (OTU) gene in Drosophila. Members include proteins from eukaryotes, viruses and pathogenic bacterium. The conserved cysteine and histidine, and possibly the aspartate, represent the catalytic residues in this putative group of proteases.


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 85.97  E-value: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961  184 GDGNCLLHAASLGMWGFHDrdlMLRKSLYalmdhgqerEALkrRWRWQQTMQNKESGlvyTEEEWQKEWNELLKLASSep 263
Cdd:pfam02338   2 GDGNCLYRSISHQLWGVHD---VLRKMLV---------QEL--RETLAEYMREHKEE---FEPFLEDDETGDIIEIEQ-- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961  264 rihystNGSSGaesqeepvyeslEEFHVFVLAHVLRRPIVVvadtmLRDSGGEAFAPIPFGGIYLPLEVPANKCHRSPLV 343
Cdd:pfam02338  63 ------TGAWG------------GEIEIFALAHILRRPIIV-----YKSEGGEELGGLKEYGIYLPLGWDPSLCLVYPRH 119


                  ....*...
gi 528504961  344 LAYDQAHF 351
Cdd:pfam02338 120 LYYLGGHY 127
OTU_VCIP135 cd22769
OTU (ovarian tumor) domain of deubiquitinating protein VCIP135; Deubiquitinating protein ...
 177-355 2.53e-07

OTU (ovarian tumor) domain of deubiquitinating protein VCIP135; Deubiquitinating protein VCIP135 is also called valosin-containing protein p97/p47 complex-interacting protein 1, valosin-containing protein p97/p47 complex-interacting protein p135, or VCP/p47 complex-interacting 135-kDa protein. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains. It is necessary for VCP-mediated reassembly of Golgi stacks after mitosis, and may play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). VCIP135 controls Golgi membrane dynamics in the cell cycle and is required for Golgi and ER assembly. It belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. Not all members of this subfamily contain the active site. It is closely related to proteins classified as family C64 cysteine protease by MEROPS, such as TNFAIP3, ZRANB1, and OTUD7A/B.


Pssm-ID: 438606  Cd Length: 197  Bit Score: 51.91  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 177 LLPLATSGDGNCLLHAASLGMWGfhdRDLM---LRKSLyalMDHGQEREAlkrrwRWQQTMQNkesglvYTEEEwqkEWN 253
Cdd:cd22769   45 LIPIHADGDGHCLVHAVSRALVG---RELFwhaLRENL---KQHFKENLD-----QYKALFQD------FIDDS---EWP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 254 ELLklASSEPRIHYSTNGSSGaesqeepvyesLEEFHVFVLAHVLRRPIVVVaDTM--LRDSGGeafapipFGGIYLPLE 331
Cdd:cd22769  105 DII--AECDPDFVPPEGEPLG-----------LRNIHIFGLANVLKRPIILL-DSLsgMQSSGD-------YSAIFLPGL 163

                        170       180       190
                 ....*....|....*....|....*....|...
gi 528504961 332 VPANKCH------RSPLVLAYDQA---HFSALV 355
Cdd:cd22769  164 VPPEKCRgkdgllNKPICIAWSSSgrnHFIPLV 196
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 182-354 5.58e-07

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 49.36  E-value: 5.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 182 TSGDGNCLLHAASLGMWGFHDRDLMLRKslyALMDHgqereaLKRRWrwqqtmqNKESGLVYTEEEWQKEWNELLKlass 261
Cdd:cd22744    5 VPGDGNCLFRALAHALYGDQESHRELRQ---EVVDY------LRENP-------DLYEPAELADEDDGEDFDEYLQ---- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961 262 epriHYSTNGSSGaesqeepvyeslEEFHVFVLAHVLRRPIVVVadtmlrDSGGEAFAPIPFGgiylplevPANKCHRSP 341
Cdd:cd22744   65 ----RMRKPGTWG------------GELELQALANALNVPIVVY------SEDGGFLPVSVFG--------PGPGPSGRP 114

                        170
                 ....*....|....
gi 528504961 342 LVLAYDQA-HFSAL 354
Cdd:cd22744  115 IHLLYTGGnHYDAL 128
zf-A20 pfam01754
A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding ...
 879-903 4.10e-06

A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding Domain. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappa B activation.


Pssm-ID: 460313  Cd Length: 24  Bit Score: 44.03  E-value: 4.10e-06
                          10        20
                  ....*....|....*....|....*
gi 528504961  879 SKCRTPtCNYYGHPETGNYCSYCYR 903
Cdd:pfam01754   1 LLCRNG-CGFYGSPATNGLCSKCYK 24
UBA_4 pfam14555
UBA-like domain;
6-41 2.07e-04

UBA-like domain;


Pssm-ID: 464207  Cd Length: 43  Bit Score: 39.36  E-value: 2.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 528504961    6 DAVLSDFVRSTGAEPGLARDLLEGKNWDLSAALSDF 41
Cdd:pfam14555   1 DELIAQFQAITGADEEVARQYLEAHNWDLEAAVNAF 36
UBA_TAP-C_like cd14273
UBA-like domain found in the NXF family of mRNA nuclear export factors and similar proteins; ...
 12-41 2.22e-04

UBA-like domain found in the NXF family of mRNA nuclear export factors and similar proteins; This family includes nuclear RNA export factors (NXF1/NXF2), FAS-associated factors (FAF1/2), tyrosyl-DNA phosphodiesterase 2 (TDP2), OTU domain-containing proteins (OTU7A/OTU7B), NSFL1 cofactor p47, defective in cullin neddylation protein 1 (DCN1)-like protein (DCNL1/DCNL2), yeast defective in cullin neddylation protein 1 (DCN1) and similar proteins. NXF proteins can stimulate nuclear export of mRNAs and facilitate the export of unspliced viral mRNA containing the constitutive transport element. FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF2 is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. Its biological function remains unclear. TDP2 is a 5'-Tyr-DNA phosphodiesterase required for the efficient repair of topoisomerase II-induced DNA double strand breaks. OTU7A and OTU7B are zinc finger proteins that function as deubiquitinating enzymes. p47 is a major cofactor of the cytosolic AAA ATPase p97. It is required for the p97-regulated membrane reassembly of the endoplasmic reticulum (ER), the nuclear envelope and the Golgi apparatus. DCNL1 plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. The biological function of DCNL2 remains unclear. Yeast DCN1 is a scaffold-type E3 ligase for cullin neddylation. It can bind directly to cullins and the ubiquitin-like protein Nedd8-specific E2 (Ubc12), and regulate cullin neddylation and thus display ubiquitin ligase activity.


Pssm-ID: 270459  Cd Length: 31  Bit Score: 39.31  E-value: 2.22e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 528504961  12 FVRSTGAEPGLARDLLEGKNWDLSAALSDF 41
Cdd:cd14273    1 FMEITGADPETARQYLESNNWDLEAAINLY 30
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 879-903 3.73e-04

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


Pssm-ID: 128555  Cd Length: 26  Bit Score: 38.34  E-value: 3.73e-04
                           10        20
                   ....*....|....*....|....*
gi 528504961   879 SKCRTPTCNYYGHPETGNYCSYCYR 903
Cdd:smart00259   2 IKCRRPGCGFFGNPATEGLCSKCFK 26
OTU_VRTN cd22791
OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU ...
 177-208 4.70e-04

OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU domain-containing protein that is required for the development of thoracic vertebrae in mammals. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. Vertnin and some subfamily members do not possess the conserved catalytic residues and may not have DUB activity. VRTN gene is associated with variations in vertebral number.


Pssm-ID: 438612  Cd Length: 137  Bit Score: 41.05  E-value: 4.70e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 528504961 177 LLPLATSGDGNCLLHAASLGMWGFHDRDLMLR 208
Cdd:cd22791    1 LEPLRVTGDGNCLFRAASLLLFGDESLHLELR 32
UBA_p47 cd14348
UBA-like domain found in NSFL1 cofactor p47 and similar proteins; p47, also called UBX ...
 6-41 1.33e-03

UBA-like domain found in NSFL1 cofactor p47 and similar proteins; p47, also called UBX domain-containing protein 2C, is a major cofactor of the cytosolic AAA ATPase p97. It is required for the p97-regulated membrane reassembly of the endoplasmic reticulum (ER), the nuclear envelope and the Golgi apparatus. p47, together with p97, forms the p97-p47 complex that plays an important role in regulation of membrane fusion events. p47 contains an N-terminal ubiquitin-associated (UBA)-like domain, a central SEP (named after shp1, eyc and p47) domain, and a ubiquitin-like (UBX) domain. UBA-like domain is responsible for forming a highly stable complex with ubiquitin. SEP domain and UBX domain may involve in p47 trimerization or forms a stable complex with the p97 N-terminal domain.


Pssm-ID: 270533  Cd Length: 40  Bit Score: 37.13  E-value: 1.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 528504961   6 DAVLSDFVRSTGAEPGLARDLLEGKNWDLSAALSDF 41
Cdd:cd14348    1 DELIAQFVSVTGADEDRAKFFLESAGWDLEAALSSF 36
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
 720-826 3.24e-03

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 40.57  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504961  720 PPNFNALKSSSFSPVMYSGVVPIPRHTFIDHSPSPMTQHLHMHHGYMDTRRQlaggsPSSYPGLPSYATL-PRHCPLAQG 798
Cdd:pfam15279 175 GKPQQHPPPSPLPAFMEPSSMPPPFLRPPPSIPQPNSPLSNPMLPGIGPPPK-----PPRNLGPPSNPMHrPPFSPHHPP 249

                          90       100
                  ....*....|....*....|....*...
gi 528504961  799 PPHAQYHPPSASLGSPSRIITPcLTSFP 826
Cdd:pfam15279 250 PPPTPPGPPPGLPPPPPRGFTP-PFGPP 276
 
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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