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Conserved domains on  [gi|1034608096|ref|XP_016882340|]
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nitric oxide synthase-interacting protein isoform X3 [Homo sapiens]

Protein Classification

nitric oxide synthase-interacting protein( domain architecture ID 12175296)

nitric oxide synthase-interacting protein (NOSIP) is an E3 ubiquitin-protein ligase implicated in the control of airway and vascular diameter, mucosal secretion, and NO synthesis in ciliated epithelium affecting mucociliary and bronchial function

EC:  2.3.2.27
Gene Symbol:  NOSIP
Gene Ontology:  GO:0061630|GO:0016567

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
zf-NOSIP pfam15906
Zinc-finger of nitric oxide synthase-interacting protein;
4-78 2.11e-52

Zinc-finger of nitric oxide synthase-interacting protein;


:

Pssm-ID: 318178  Cd Length: 75  Bit Score: 166.36  E-value: 2.11e-52
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034608096   4 HGKNCTAGAVYTYHEKKKDTAASGYGTQNIRLSRDAVKDFDCCCLSLQPCHDPVVTPDGYLYEREAILEYILHQK 78
Cdd:pfam15906   1 HGKNCTAGAVYTYHEKKKDTAASGYGTQNIQLGKDAIKDFDCCCLSLQACHDPVLTEDGYLYEKEAILEYILHQK 75
RING-Ubox2_NOSIP cd16662
U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein ...
220-287 2.90e-40

U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein (NOSIP) and similar proteins; NOSIP, also known as endothelial NO synthase (eNOS)-interacting protein, p33RUL, is an E3 ubiquitin-protein ligase implicated in the control of airway and vascular diameter, mucosal secretion, NO synthesis in ciliated epithelium, and, therefore, of mucociliary and bronchial function. The loss of NOSIP may cause holoprosencephaly and facial anomalies including cleft lip/palate, cyclopia and facial midline clefting. NOSIP interacts with neuronal nitric oxide synthase (nNOS) and eNOS by inhibiting nitric oxide (NO) production. It acts as a novel type of modulator that promotes translocation of eNOS from the plasma membrane to intracellular sites, thereby uncoupling eNOS from plasma membrane caveolae and inhibiting NO synthesis. NOSIP also interacts with protein phosphatase PP2A and mediates the monoubiquitination of the PP2A catalytic subunit. Thus, it is a critical modulator of brain and craniofacial development in mice and a candidate gene for holoprosencephaly in humans. Moreover, NOSIP associates with the erythropoietin (Epo) receptor (EpoR), mediates ubiquitination of EpoR, and plays an essential role in erythropoietin-induced proliferation. NOSIP contains an atypical N-terminal RING-like U-box domain that is split into two parts by an interjacent stretch of 104 amino acid residues, as well as a C-terminal RING-like U-box domain. This model corresponds to the second U-box domain.


:

Pssm-ID: 438324  Cd Length: 68  Bit Score: 134.73  E-value: 2.90e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034608096 220 RYVCAVTRDSLSNATPCAVLRPSGAVVTLECVEKLIRKDMVDPVTGDKLTDRDIIVLQRGGTGFAGSG 287
Cdd:cd16662     1 RYMCAVTKDVLTNSVPCAVLRPSGDVVTMECVEKLIKKDMIDPVTGKKLKEKDIIPLQRGGTGFAASN 68
 
Name Accession Description Interval E-value
zf-NOSIP pfam15906
Zinc-finger of nitric oxide synthase-interacting protein;
4-78 2.11e-52

Zinc-finger of nitric oxide synthase-interacting protein;


Pssm-ID: 318178  Cd Length: 75  Bit Score: 166.36  E-value: 2.11e-52
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034608096   4 HGKNCTAGAVYTYHEKKKDTAASGYGTQNIRLSRDAVKDFDCCCLSLQPCHDPVVTPDGYLYEREAILEYILHQK 78
Cdd:pfam15906   1 HGKNCTAGAVYTYHEKKKDTAASGYGTQNIQLGKDAIKDFDCCCLSLQACHDPVLTEDGYLYEKEAILEYILHQK 75
RING-Ubox2_NOSIP cd16662
U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein ...
220-287 2.90e-40

U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein (NOSIP) and similar proteins; NOSIP, also known as endothelial NO synthase (eNOS)-interacting protein, p33RUL, is an E3 ubiquitin-protein ligase implicated in the control of airway and vascular diameter, mucosal secretion, NO synthesis in ciliated epithelium, and, therefore, of mucociliary and bronchial function. The loss of NOSIP may cause holoprosencephaly and facial anomalies including cleft lip/palate, cyclopia and facial midline clefting. NOSIP interacts with neuronal nitric oxide synthase (nNOS) and eNOS by inhibiting nitric oxide (NO) production. It acts as a novel type of modulator that promotes translocation of eNOS from the plasma membrane to intracellular sites, thereby uncoupling eNOS from plasma membrane caveolae and inhibiting NO synthesis. NOSIP also interacts with protein phosphatase PP2A and mediates the monoubiquitination of the PP2A catalytic subunit. Thus, it is a critical modulator of brain and craniofacial development in mice and a candidate gene for holoprosencephaly in humans. Moreover, NOSIP associates with the erythropoietin (Epo) receptor (EpoR), mediates ubiquitination of EpoR, and plays an essential role in erythropoietin-induced proliferation. NOSIP contains an atypical N-terminal RING-like U-box domain that is split into two parts by an interjacent stretch of 104 amino acid residues, as well as a C-terminal RING-like U-box domain. This model corresponds to the second U-box domain.


Pssm-ID: 438324  Cd Length: 68  Bit Score: 134.73  E-value: 2.90e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034608096 220 RYVCAVTRDSLSNATPCAVLRPSGAVVTLECVEKLIRKDMVDPVTGDKLTDRDIIVLQRGGTGFAGSG 287
Cdd:cd16662     1 RYMCAVTKDVLTNSVPCAVLRPSGDVVTMECVEKLIKKDMIDPVTGKKLKEKDIIPLQRGGTGFAASN 68
RING-Ubox1_NOSIP cd16661
U-box domain 1, a modified RING finger, found in nitric oxide synthase-interacting protein ...
43-80 1.06e-24

U-box domain 1, a modified RING finger, found in nitric oxide synthase-interacting protein (NOSIP) and similar proteins; NOSIP, also known as endothelial NO synthase (eNOS)-interacting protein, p33RUL, is an E3 ubiquitin-protein ligase implicated in the control of airway and vascular diameter, mucosal secretion, NO synthesis in ciliated epithelium, and, therefore, of mucociliary and bronchial function. The loss of NOSIP may cause holoprosencephaly and facial anomalies, including cleft lip/palate, cyclopia, and facial midline clefting. NOSIP interacts with neuronal nitric oxide synthase (nNOS) and eNOS by inhibiting the nitric oxide (NO) production. It acts as a novel type of modulator that promotes translocation of eNOS from the plasma membrane to intracellular sites, thereby uncoupling eNOS from plasma membrane caveolae and inhibiting NO synthesis. NOSIP also interacts with protein phosphatase PP2A and mediates the monoubiquitination of the PP2A catalytic subunit. Thus, it is a critical modulator of brain and craniofacial development in mice and a candidate gene for holoprosencephaly in humans. Moreover, NOSIP associates with the erythropoietin (Epo) receptor (EpoR), mediates ubiquitination of EpoR, and plays an essential role in erythropoietin-induced proliferation. NOSIP contains an atypical N-terminal RING-like U-box domain that is split into two parts by an interjacent stretch of 104 amino acid residues, as well as a C-terminal RING-like U-box domain. This model corresponds to the first U-box domain.


Pssm-ID: 438323  Cd Length: 46  Bit Score: 93.54  E-value: 1.06e-24
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1034608096  43 FDCCCLSLQPCHDPVVTPDGYLYEREAILEYILHQKKE 80
Cdd:cd16661     1 FDCCCLTLQPCRDPVVTPDGYLYDKEAILEYILHQKKE 38
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
45-75 2.54e-07

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 46.84  E-value: 2.54e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1034608096   45 CCCLSLQPCHDPVVTPDGYLYEREAILEYIL 75
Cdd:smart00504   3 LCPISLEVMKDPVILPSGQTYERSAIEKWLL 33
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
227-274 2.59e-04

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 38.37  E-value: 2.59e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1034608096  227 RDSLSNATP-CAVLRPSGAVVTLECVEKLIRKDMVDPVTGDKLTDRDII 274
Cdd:smart00504   3 LCPISLEVMkDPVILPSGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLI 51
Rtf2 pfam04641
Rtf2 RING-finger; It is vital for effective cell-replication that replication is not stalled ...
194-276 7.00e-04

Rtf2 RING-finger; It is vital for effective cell-replication that replication is not stalled at any point by, for instance, damaged bases. Replication termination factor 2 (Rtf2) stabilizes the replication fork stalled at the site-specific replication barrier RTS1 by preventing replication restart until completion of DNA synthesis by a converging replication fork initiated at a flanking origin. The RTS1 element terminates replication forks that are moving in the cen2-distal direction while allowing forks moving in the cen2-proximal direction to pass through the region. Rtf2 contains a C2HC2 motif related to the C3HC4 RING-finger motif, and would appear to fold up, creating a RING finger-like structure but forming only one functional Zn2+ ion-binding site. This domain is also found at the N-terminus of peptidyl-prolyl cis-trans isomerase 4, a divergent cyclophilin family.


Pssm-ID: 398360 [Multi-domain]  Cd Length: 258  Bit Score: 40.42  E-value: 7.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608096 194 MSDLTPVHFTP-LDSSVDRVGLITRSERYVCAVTRDSLSNATPCAVLRPSGAVVTlecvEKLIR--KDMVDPVTGDKLTD 270
Cdd:pfam04641  83 LKDVVELKLTPnPAFEGSKVYDDTSEAPFICPVTGLEMNGKYKFVALWPCGCVFS----EKALKevKSKNCPVCGKPYSE 158

                  ....*.
gi 1034608096 271 RDIIVL 276
Cdd:pfam04641 159 EDVIPL 164
 
Name Accession Description Interval E-value
zf-NOSIP pfam15906
Zinc-finger of nitric oxide synthase-interacting protein;
4-78 2.11e-52

Zinc-finger of nitric oxide synthase-interacting protein;


Pssm-ID: 318178  Cd Length: 75  Bit Score: 166.36  E-value: 2.11e-52
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034608096   4 HGKNCTAGAVYTYHEKKKDTAASGYGTQNIRLSRDAVKDFDCCCLSLQPCHDPVVTPDGYLYEREAILEYILHQK 78
Cdd:pfam15906   1 HGKNCTAGAVYTYHEKKKDTAASGYGTQNIQLGKDAIKDFDCCCLSLQACHDPVLTEDGYLYEKEAILEYILHQK 75
RING-Ubox2_NOSIP cd16662
U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein ...
220-287 2.90e-40

U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein (NOSIP) and similar proteins; NOSIP, also known as endothelial NO synthase (eNOS)-interacting protein, p33RUL, is an E3 ubiquitin-protein ligase implicated in the control of airway and vascular diameter, mucosal secretion, NO synthesis in ciliated epithelium, and, therefore, of mucociliary and bronchial function. The loss of NOSIP may cause holoprosencephaly and facial anomalies including cleft lip/palate, cyclopia and facial midline clefting. NOSIP interacts with neuronal nitric oxide synthase (nNOS) and eNOS by inhibiting nitric oxide (NO) production. It acts as a novel type of modulator that promotes translocation of eNOS from the plasma membrane to intracellular sites, thereby uncoupling eNOS from plasma membrane caveolae and inhibiting NO synthesis. NOSIP also interacts with protein phosphatase PP2A and mediates the monoubiquitination of the PP2A catalytic subunit. Thus, it is a critical modulator of brain and craniofacial development in mice and a candidate gene for holoprosencephaly in humans. Moreover, NOSIP associates with the erythropoietin (Epo) receptor (EpoR), mediates ubiquitination of EpoR, and plays an essential role in erythropoietin-induced proliferation. NOSIP contains an atypical N-terminal RING-like U-box domain that is split into two parts by an interjacent stretch of 104 amino acid residues, as well as a C-terminal RING-like U-box domain. This model corresponds to the second U-box domain.


Pssm-ID: 438324  Cd Length: 68  Bit Score: 134.73  E-value: 2.90e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034608096 220 RYVCAVTRDSLSNATPCAVLRPSGAVVTLECVEKLIRKDMVDPVTGDKLTDRDIIVLQRGGTGFAGSG 287
Cdd:cd16662     1 RYMCAVTKDVLTNSVPCAVLRPSGDVVTMECVEKLIKKDMIDPVTGKKLKEKDIIPLQRGGTGFAASN 68
RING-Ubox1_NOSIP cd16661
U-box domain 1, a modified RING finger, found in nitric oxide synthase-interacting protein ...
43-80 1.06e-24

U-box domain 1, a modified RING finger, found in nitric oxide synthase-interacting protein (NOSIP) and similar proteins; NOSIP, also known as endothelial NO synthase (eNOS)-interacting protein, p33RUL, is an E3 ubiquitin-protein ligase implicated in the control of airway and vascular diameter, mucosal secretion, NO synthesis in ciliated epithelium, and, therefore, of mucociliary and bronchial function. The loss of NOSIP may cause holoprosencephaly and facial anomalies, including cleft lip/palate, cyclopia, and facial midline clefting. NOSIP interacts with neuronal nitric oxide synthase (nNOS) and eNOS by inhibiting the nitric oxide (NO) production. It acts as a novel type of modulator that promotes translocation of eNOS from the plasma membrane to intracellular sites, thereby uncoupling eNOS from plasma membrane caveolae and inhibiting NO synthesis. NOSIP also interacts with protein phosphatase PP2A and mediates the monoubiquitination of the PP2A catalytic subunit. Thus, it is a critical modulator of brain and craniofacial development in mice and a candidate gene for holoprosencephaly in humans. Moreover, NOSIP associates with the erythropoietin (Epo) receptor (EpoR), mediates ubiquitination of EpoR, and plays an essential role in erythropoietin-induced proliferation. NOSIP contains an atypical N-terminal RING-like U-box domain that is split into two parts by an interjacent stretch of 104 amino acid residues, as well as a C-terminal RING-like U-box domain. This model corresponds to the first U-box domain.


Pssm-ID: 438323  Cd Length: 46  Bit Score: 93.54  E-value: 1.06e-24
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1034608096  43 FDCCCLSLQPCHDPVVTPDGYLYEREAILEYILHQKKE 80
Cdd:cd16661     1 FDCCCLTLQPCRDPVVTPDGYLYDKEAILEYILHQKKE 38
RING-Ubox_PPIL2 cd16663
U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 ...
43-79 3.59e-10

U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 (PPIL2) and similar proteins; PPIL2 (EC 5.2.1.8), also known as PPIase, CYC4, cyclophilin-60 (Cyp60), cyclophilin-like protein Cyp-60, or Rotamase PPIL2, is a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c and regulates gene expression. PPIL2 belongs to the cyclophilin family of peptidylprolyl isomerases and catalyzes cis-trans isomerization of proline-peptide bonds, which is often a rate-limiting step in protein folding. It positively regulates beta-site amyloid precursor protein cleaving enzyme (BACE1) expression and beta-secretase activity. Moreover, PPIL2 plays an important role in the translocation of CD147 to the cell surface, and thus may present a novel target for therapeutic interventions in diseases where CD147 functions as a pathogenic factor in cancer, human immunodeficiency virus infection, or rheumatoid arthritis. PPIL2 contains an N-terminal RING-like U-box domain and a C-terminal cyclophilin (Cyp)-like chaperone domain.


Pssm-ID: 438325  Cd Length: 73  Bit Score: 55.26  E-value: 3.59e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1034608096  43 FDCCCLSLQPCHDPVVTPDGYLYEREAILEYILHQKK 79
Cdd:cd16663     2 FDCCALSLQPFENPVCTPDGIVFDLLNIVPYLKKYGK 38
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
45-78 6.05e-10

U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.


Pssm-ID: 438117 [Multi-domain]  Cd Length: 44  Bit Score: 53.71  E-value: 6.05e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1034608096  45 CCCLSLQPCHDPVVTPDGYLYEREAILEYILHQK 78
Cdd:cd16453     2 LCPISGELMKDPVITPSGITYDRSAIERWLLSDN 35
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
221-268 1.32e-07

U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.


Pssm-ID: 438117 [Multi-domain]  Cd Length: 44  Bit Score: 47.16  E-value: 1.32e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1034608096 221 YVCAVTRDSlsnaTPCAVLRPSGAVVTLECVEKLIRKDMVDPVTGDKL 268
Cdd:cd16453     1 FLCPISGEL----MKDPVITPSGITYDRSAIERWLLSDNTDPFTREPL 44
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
45-74 1.39e-07

U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis.


Pssm-ID: 438317 [Multi-domain]  Cd Length: 55  Bit Score: 47.50  E-value: 1.39e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 1034608096  45 CCCLSLQPCHDPVVTPDGYLYEREAILEYI 74
Cdd:cd16655     5 LCPITQELMRDPVVAADGHTYERSAIEEWL 34
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
45-75 2.54e-07

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 46.84  E-value: 2.54e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1034608096   45 CCCLSLQPCHDPVVTPDGYLYEREAILEYIL 75
Cdd:smart00504   3 LCPISLEVMKDPVILPSGQTYERSAIEKWLL 33
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
40-76 1.02e-06

U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins; CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins, thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (or apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase.


Pssm-ID: 438316 [Multi-domain]  Cd Length: 71  Bit Score: 45.64  E-value: 1.02e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1034608096  40 VKDFDCCCLSLQPCHDPVVTPDGYLYEREAILEYILH 76
Cdd:cd16654     1 VPDYLCCKISFELMRDPVITPSGITYERKDIEEHLQR 37
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
227-274 2.59e-04

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 38.37  E-value: 2.59e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1034608096  227 RDSLSNATP-CAVLRPSGAVVTLECVEKLIRKDMVDPVTGDKLTDRDII 274
Cdd:smart00504   3 LCPISLEVMkDPVILPSGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLI 51
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
41-74 2.87e-04

U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain.


Pssm-ID: 438326 [Multi-domain]  Cd Length: 53  Bit Score: 37.93  E-value: 2.87e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1034608096  41 KDFdCCCLSLQPCHDPVVTPDGYLYEREAILEYI 74
Cdd:cd16664     2 EEF-ICPISLELMKDPVILATGQTYERAAIEKWL 34
Rtf2 pfam04641
Rtf2 RING-finger; It is vital for effective cell-replication that replication is not stalled ...
194-276 7.00e-04

Rtf2 RING-finger; It is vital for effective cell-replication that replication is not stalled at any point by, for instance, damaged bases. Replication termination factor 2 (Rtf2) stabilizes the replication fork stalled at the site-specific replication barrier RTS1 by preventing replication restart until completion of DNA synthesis by a converging replication fork initiated at a flanking origin. The RTS1 element terminates replication forks that are moving in the cen2-distal direction while allowing forks moving in the cen2-proximal direction to pass through the region. Rtf2 contains a C2HC2 motif related to the C3HC4 RING-finger motif, and would appear to fold up, creating a RING finger-like structure but forming only one functional Zn2+ ion-binding site. This domain is also found at the N-terminus of peptidyl-prolyl cis-trans isomerase 4, a divergent cyclophilin family.


Pssm-ID: 398360 [Multi-domain]  Cd Length: 258  Bit Score: 40.42  E-value: 7.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608096 194 MSDLTPVHFTP-LDSSVDRVGLITRSERYVCAVTRDSLSNATPCAVLRPSGAVVTlecvEKLIR--KDMVDPVTGDKLTD 270
Cdd:pfam04641  83 LKDVVELKLTPnPAFEGSKVYDDTSEAPFICPVTGLEMNGKYKFVALWPCGCVFS----EKALKevKSKNCPVCGKPYSE 158

                  ....*.
gi 1034608096 271 RDIIVL 276
Cdd:pfam04641 159 EDVIPL 164
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
40-75 1.70e-03

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 36.52  E-value: 1.70e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1034608096  40 VKDFDCCCLSLQPCHDPVVTPDGYLYEREAILEYIL 75
Cdd:pfam04564   1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLL 36
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
55-80 7.72e-03

first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the first one.


Pssm-ID: 438511 [Multi-domain]  Cd Length: 55  Bit Score: 34.00  E-value: 7.72e-03
                          10        20
                  ....*....|....*....|....*.
gi 1034608096  55 DPVVTPDGYLYEREAILEYiLHQKKE 80
Cdd:cd23149    12 DPVITPSGFSYERSAIERW-LETKPE 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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