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Conserved domains on  [gi|767980118|ref|XP_011534892|]
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protein KHNYN isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RNase_Zc3h12a pfam11977
Zc3h12a-like Ribonuclease NYN domain; This domain is found in the Zc3h12a protein which has ...
479-632 5.57e-80

Zc3h12a-like Ribonuclease NYN domain; This domain is found in the Zc3h12a protein which has shown to be a ribonuclease that controls the stability of a set of inflammatory genes. It has been suggested that this domain belongs to the PIN domain superfamily. This domain has also been identified as part of the NYN domain family.


:

Pssm-ID: 403256  Cd Length: 154  Bit Score: 251.86  E-value: 5.57e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980118  479 DLRHIVIDGSNVAMVHGLQHYFSSRGIAIAVQYFWDRGHRDITVFVPQWRFSKDAKVRESHFLQKLYSLSLLSLTPSRVM 558
Cdd:pfam11977   1 GLRPIVIDGSNVAMSHGRQKKFSVRGLAIAVDYFVKRGHEEITVFVPQWRKEADEKITDQHELLELERLGLIVFTPSRTL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767980118  559 DGKRISSYDDRFMVKLAEETDGIIVSNDQFRDLAEESEKWMAIIRERLLPFTFVGNLFMVPDDPLGRNGPTLDE 632
Cdd:pfam11977  81 DGKRIVSYDDRFILKLAEETDGVIVSNDNFRDLADENPEWIDIVEERLLMYTFVGDKFMPPDDPLGRVGPSLED 154
KH-I_NYNRIN_like cd22477
type I K homology (KH) RNA-binding domain found in the subfamily of NYN domain and retroviral ...
119-184 5.25e-38

type I K homology (KH) RNA-binding domain found in the subfamily of NYN domain and retroviral integrase catalytic domain-containing protein (NYNRIN); The NYNRIN subfamily includes NYNRIN and KH and NYN domain-containing protein (KHNYN). NYNRIN, also known as CGIN1/Cousin of GIN1, may contribute to retroviral resistance in mammals by regulating the ubiquitination of viral proteins. KHNYN acts as a novel cofactor for zinc finger antiviral protein (ZAP) to target CpG-containing retroviral RNA for degradation.


:

Pssm-ID: 411905  Cd Length: 66  Bit Score: 135.22  E-value: 5.25e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767980118 119 PELQDEIHYPPKLHCIFLGAQGFFLDCLAWSTSAHLVPRAPGSLMISGLTEAFVMAQSRVEELAER 184
Cdd:cd22477    1 PELTKEVLYPRDLHCIFLGAKGLFLDCLIWGTSAHIVPGAPGSLLISGLTEAFVMAQSRIEDLVEK 66
KH-I_N4BP1_like_rpt1 cd09032
first type I K homology (KH) RNA-binding domain found in the family of NEDD4-binding protein 1 ...
55-117 6.98e-21

first type I K homology (KH) RNA-binding domain found in the family of NEDD4-binding protein 1 (N4BP1); The N4BP1 family includes N4BP1, NYN domain and retroviral integrase catalytic domain-containing protein (NYNRIN) and KH and NYN domain-containing protein (KHNYN). These proteins are probably of retroviral origin. N4BP1 interacts with and is a substrate of NEDD4 ubiquitin ligase (neural precursor cell expressed, developmentally downregulated 4, E3 ubiquitin protein ligase). It is also an inhibitor of the E3 ubiquitin-protein ligase ITCH, a NEDD4 structurally related E3. N4BP1 acts by interacting with the second WW domain of ITCH, leading to compete with ITCH's substrates and impairing ubiquitination of substrates. NYNRIN, also known as CGIN1/Cousin of GIN1, may contribute to retroviral resistance in mammals by regulating the ubiquitination of viral proteins. KHNYN acts as a novel cofactor for zinc finger antiviral protein (ZAP) to target CpG-containing retroviral RNA for degradation. Members of this family contains two type I K homology (KH) RNA-binding domain. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif.


:

Pssm-ID: 411808  Cd Length: 65  Bit Score: 86.57  E-value: 6.98e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767980118  55 DRFAVSAEAENKVREQQPHVERIFSVGVSVLPKDC--PDNPHIWLQLEGPKENASRAKEYLKGLC 117
Cdd:cd09032    1 DEFVVPAEKVPLLERSRPRIERLFGVKVSLLEELSkpKDGGKQWVQLEGDEEDVRKAKEYIKALC 65
 
Name Accession Description Interval E-value
RNase_Zc3h12a pfam11977
Zc3h12a-like Ribonuclease NYN domain; This domain is found in the Zc3h12a protein which has ...
479-632 5.57e-80

Zc3h12a-like Ribonuclease NYN domain; This domain is found in the Zc3h12a protein which has shown to be a ribonuclease that controls the stability of a set of inflammatory genes. It has been suggested that this domain belongs to the PIN domain superfamily. This domain has also been identified as part of the NYN domain family.


Pssm-ID: 403256  Cd Length: 154  Bit Score: 251.86  E-value: 5.57e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980118  479 DLRHIVIDGSNVAMVHGLQHYFSSRGIAIAVQYFWDRGHRDITVFVPQWRFSKDAKVRESHFLQKLYSLSLLSLTPSRVM 558
Cdd:pfam11977   1 GLRPIVIDGSNVAMSHGRQKKFSVRGLAIAVDYFVKRGHEEITVFVPQWRKEADEKITDQHELLELERLGLIVFTPSRTL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767980118  559 DGKRISSYDDRFMVKLAEETDGIIVSNDQFRDLAEESEKWMAIIRERLLPFTFVGNLFMVPDDPLGRNGPTLDE 632
Cdd:pfam11977  81 DGKRIVSYDDRFILKLAEETDGVIVSNDNFRDLADENPEWIDIVEERLLMYTFVGDKFMPPDDPLGRVGPSLED 154
PIN_N4BP1-like cd18728
PRORP-like PIN domain of NEDD4 binding protein 1 and related proteins; NEDD4-binding partner-1 ...
483-609 3.06e-75

PRORP-like PIN domain of NEDD4 binding protein 1 and related proteins; NEDD4-binding partner-1 (N4BP1) interacts with and is a substrate of NEDD4 ubiquitin ligase (neural precursor cell expressed, developmentally down-regulated 4, E3 ubiquitin protein ligase). It is also an inhibitor of the E3 ubiquitin-protein ligase ITCH, a NEDD4 structurally related E3. This subfamily additionally includes NYNRIN (NYN domain and retroviral integrase containing, also known as CGIN1/Cousin of GIN1), and KHNYN (KH and NYN domain containing) protein. N4BP1, CGIN1, and KHNYN proteins are probably of retroviral origin. This subfamily belongs to the Zc3h12a-N4BP1-like PIN subfamily of the PRORP-Zc3h12a-like PIN family, the latter of which additionally includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


Pssm-ID: 350295  Cd Length: 127  Bit Score: 238.16  E-value: 3.06e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980118 483 IVIDGSNVAMVHGLQHYFSSRGIAIAVQYFWDRGHRDITVFVPQWRFSKDAKVRESHFLQKLYSLSLLSLTPSRVMDGKR 562
Cdd:cd18728    1 IVIDGSNVAMVHGLQHFFSCRGIAIAVEYFWKRGHRNITVFVPQWRTKRDPNVTEQHFLTQLQELGILSLTPSRMVLGKR 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767980118 563 ISSYDDRFMVKLAEETDGIIVSNDQFRDLAEESEKWMAIIRERLLPF 609
Cdd:cd18728   81 IASHDDRFLLHLAEKTGGIIVTNDNFREFVNESPSWREIIKERLLQY 127
KH-I_NYNRIN_like cd22477
type I K homology (KH) RNA-binding domain found in the subfamily of NYN domain and retroviral ...
119-184 5.25e-38

type I K homology (KH) RNA-binding domain found in the subfamily of NYN domain and retroviral integrase catalytic domain-containing protein (NYNRIN); The NYNRIN subfamily includes NYNRIN and KH and NYN domain-containing protein (KHNYN). NYNRIN, also known as CGIN1/Cousin of GIN1, may contribute to retroviral resistance in mammals by regulating the ubiquitination of viral proteins. KHNYN acts as a novel cofactor for zinc finger antiviral protein (ZAP) to target CpG-containing retroviral RNA for degradation.


Pssm-ID: 411905  Cd Length: 66  Bit Score: 135.22  E-value: 5.25e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767980118 119 PELQDEIHYPPKLHCIFLGAQGFFLDCLAWSTSAHLVPRAPGSLMISGLTEAFVMAQSRVEELAER 184
Cdd:cd22477    1 PELTKEVLYPRDLHCIFLGAKGLFLDCLIWGTSAHIVPGAPGSLLISGLTEAFVMAQSRIEDLVEK 66
KH-I_N4BP1_like_rpt1 cd09032
first type I K homology (KH) RNA-binding domain found in the family of NEDD4-binding protein 1 ...
55-117 6.98e-21

first type I K homology (KH) RNA-binding domain found in the family of NEDD4-binding protein 1 (N4BP1); The N4BP1 family includes N4BP1, NYN domain and retroviral integrase catalytic domain-containing protein (NYNRIN) and KH and NYN domain-containing protein (KHNYN). These proteins are probably of retroviral origin. N4BP1 interacts with and is a substrate of NEDD4 ubiquitin ligase (neural precursor cell expressed, developmentally downregulated 4, E3 ubiquitin protein ligase). It is also an inhibitor of the E3 ubiquitin-protein ligase ITCH, a NEDD4 structurally related E3. N4BP1 acts by interacting with the second WW domain of ITCH, leading to compete with ITCH's substrates and impairing ubiquitination of substrates. NYNRIN, also known as CGIN1/Cousin of GIN1, may contribute to retroviral resistance in mammals by regulating the ubiquitination of viral proteins. KHNYN acts as a novel cofactor for zinc finger antiviral protein (ZAP) to target CpG-containing retroviral RNA for degradation. Members of this family contains two type I K homology (KH) RNA-binding domain. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411808  Cd Length: 65  Bit Score: 86.57  E-value: 6.98e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767980118  55 DRFAVSAEAENKVREQQPHVERIFSVGVSVLPKDC--PDNPHIWLQLEGPKENASRAKEYLKGLC 117
Cdd:cd09032    1 DEFVVPAEKVPLLERSRPRIERLFGVKVSLLEELSkpKDGGKQWVQLEGDEEDVRKAKEYIKALC 65
 
Name Accession Description Interval E-value
RNase_Zc3h12a pfam11977
Zc3h12a-like Ribonuclease NYN domain; This domain is found in the Zc3h12a protein which has ...
479-632 5.57e-80

Zc3h12a-like Ribonuclease NYN domain; This domain is found in the Zc3h12a protein which has shown to be a ribonuclease that controls the stability of a set of inflammatory genes. It has been suggested that this domain belongs to the PIN domain superfamily. This domain has also been identified as part of the NYN domain family.


Pssm-ID: 403256  Cd Length: 154  Bit Score: 251.86  E-value: 5.57e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980118  479 DLRHIVIDGSNVAMVHGLQHYFSSRGIAIAVQYFWDRGHRDITVFVPQWRFSKDAKVRESHFLQKLYSLSLLSLTPSRVM 558
Cdd:pfam11977   1 GLRPIVIDGSNVAMSHGRQKKFSVRGLAIAVDYFVKRGHEEITVFVPQWRKEADEKITDQHELLELERLGLIVFTPSRTL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767980118  559 DGKRISSYDDRFMVKLAEETDGIIVSNDQFRDLAEESEKWMAIIRERLLPFTFVGNLFMVPDDPLGRNGPTLDE 632
Cdd:pfam11977  81 DGKRIVSYDDRFILKLAEETDGVIVSNDNFRDLADENPEWIDIVEERLLMYTFVGDKFMPPDDPLGRVGPSLED 154
PIN_N4BP1-like cd18728
PRORP-like PIN domain of NEDD4 binding protein 1 and related proteins; NEDD4-binding partner-1 ...
483-609 3.06e-75

PRORP-like PIN domain of NEDD4 binding protein 1 and related proteins; NEDD4-binding partner-1 (N4BP1) interacts with and is a substrate of NEDD4 ubiquitin ligase (neural precursor cell expressed, developmentally down-regulated 4, E3 ubiquitin protein ligase). It is also an inhibitor of the E3 ubiquitin-protein ligase ITCH, a NEDD4 structurally related E3. This subfamily additionally includes NYNRIN (NYN domain and retroviral integrase containing, also known as CGIN1/Cousin of GIN1), and KHNYN (KH and NYN domain containing) protein. N4BP1, CGIN1, and KHNYN proteins are probably of retroviral origin. This subfamily belongs to the Zc3h12a-N4BP1-like PIN subfamily of the PRORP-Zc3h12a-like PIN family, the latter of which additionally includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


Pssm-ID: 350295  Cd Length: 127  Bit Score: 238.16  E-value: 3.06e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980118 483 IVIDGSNVAMVHGLQHYFSSRGIAIAVQYFWDRGHRDITVFVPQWRFSKDAKVRESHFLQKLYSLSLLSLTPSRVMDGKR 562
Cdd:cd18728    1 IVIDGSNVAMVHGLQHFFSCRGIAIAVEYFWKRGHRNITVFVPQWRTKRDPNVTEQHFLTQLQELGILSLTPSRMVLGKR 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767980118 563 ISSYDDRFMVKLAEETDGIIVSNDQFRDLAEESEKWMAIIRERLLPF 609
Cdd:cd18728   81 IASHDDRFLLHLAEKTGGIIVTNDNFREFVNESPSWREIIKERLLQY 127
PIN_Zc3h12a-N4BP1-like cd18719
PRORP-like PIN domain of ribonuclease Zc3h12a, NEDD4-binding partner-1, and related proteins; ...
483-609 1.44e-58

PRORP-like PIN domain of ribonuclease Zc3h12a, NEDD4-binding partner-1, and related proteins; Zc3h12a (zinc finger CCCH-type containing 12A, also known as MCPIP1/MCP induced protein 1 and Regnase-1) is a critical regulator of inflammatory response, with additional roles in defense against viruses and various stresses, cellular differentiation, and apoptosis. This subfamily also includes Caenorhabditis elegans REGE-1 (REGnasE-1), which also functions as a cytoplasmic endonuclease. Additionally, it includes three less-studied mammalian homologs: Zc3h12b-d/Regnase-2-4, as well as N4BP1 (NEDD4-binding partner-1), NYNRIN (NYN domain and retroviral integrase containing, also known as CGIN1/Cousin of GIN1), and KHNYN (KH and NYN domain containing) protein. N4BP1, CGIN1, and KHNYN proteins are probably of retroviral origin. This subfamily belongs to the PRORP-Zc3h12a-like PIN family which in addition includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


Pssm-ID: 350286  Cd Length: 127  Bit Score: 193.96  E-value: 1.44e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980118 483 IVIDGSNVAMVHGLQHYFSSRGIAIAVQYFWDRGHrDITVFVPQWRFSK-DAKVRESHFLQKLYSLSLLSLTPSRVMDGK 561
Cdd:cd18719    1 VVIDGSNVAMSHGNGKVFSCKGIQICVRYFLERGH-EVTAFVPQFRLESpNPNSTDQDILEELERLGILVFTPSRRVPGK 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767980118 562 RISSYDDRFMVKLAEETDGIIVSNDQFRDLAEESEKWMAIIRERLLPF 609
Cdd:cd18719   80 RISSYDDRFILQLAEETDGVIVSNDNFRDLLNENPDWREIIEERLLPF 127
PIN_Zc3h12-like cd18729
PRORP-like PIN domain of ribonuclease Zc3h12a and related proteins; Zc3h12a (zinc finger ...
483-610 4.28e-55

PRORP-like PIN domain of ribonuclease Zc3h12a and related proteins; Zc3h12a (zinc finger CCCH-type containing 12A, also known as MCPIP1/MCP induced protein 1 and Regnase-1) is a critical regulator of inflammatory response, with additional roles in defense against viruses and various stresses, cellular differentiation, and apoptosis. This subfamily also includes three less-studied mammalian homologs: Zc3h12b-d/Regnase-2-4. It belongs to the Zc3h12a-N4BP1-like PIN subfamily of the PRORP-Zc3h12a-like PIN family, the latter of which additionally includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


Pssm-ID: 350296  Cd Length: 131  Bit Score: 184.88  E-value: 4.28e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980118 483 IVIDGSNVAMVHGLQHYFSSRGIAIAVQYFWDRGHRDITVFVPQWRFSK---DAKVRESHFLQKLYSLSLLSLTPSRVMD 559
Cdd:cd18729    1 IVIDGSNVAMSHGNKEVFSCRGIQLAVDWFRERGHRDITVFVPSWRKEQprpDAPITDQEILRELEKEKILVFTPSRRVG 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767980118 560 GKRISSYDDRFMVKLAEETDGIIVSNDQFRDLAEESEKWMAIIRERLLPFT 610
Cdd:cd18729   81 GKRVVCYDDRFILKLAYESDGIVVSNDNYRDLQNEKPEWKKFIEERLLMYS 131
KH-I_NYNRIN_like cd22477
type I K homology (KH) RNA-binding domain found in the subfamily of NYN domain and retroviral ...
119-184 5.25e-38

type I K homology (KH) RNA-binding domain found in the subfamily of NYN domain and retroviral integrase catalytic domain-containing protein (NYNRIN); The NYNRIN subfamily includes NYNRIN and KH and NYN domain-containing protein (KHNYN). NYNRIN, also known as CGIN1/Cousin of GIN1, may contribute to retroviral resistance in mammals by regulating the ubiquitination of viral proteins. KHNYN acts as a novel cofactor for zinc finger antiviral protein (ZAP) to target CpG-containing retroviral RNA for degradation.


Pssm-ID: 411905  Cd Length: 66  Bit Score: 135.22  E-value: 5.25e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767980118 119 PELQDEIHYPPKLHCIFLGAQGFFLDCLAWSTSAHLVPRAPGSLMISGLTEAFVMAQSRVEELAER 184
Cdd:cd22477    1 PELTKEVLYPRDLHCIFLGAKGLFLDCLIWGTSAHIVPGAPGSLLISGLTEAFVMAQSRIEDLVEK 66
KH-I_N4BP1_like_rpt2 cd22388
second type I K homology (KH) RNA-binding domain found in the family of NEDD4-binding protein ...
120-181 3.23e-25

second type I K homology (KH) RNA-binding domain found in the family of NEDD4-binding protein 1 (N4BP1); The N4BP1 family includes N4BP1, NYN domain and retroviral integrase catalytic domain-containing protein (NYNRIN) and KH and NYN domain-containing protein (KHNYN). These proteins are probably of retroviral origin. N4BP1 interacts with and is a substrate of NEDD4 ubiquitin ligase (neural precursor cell expressed, developmentally downregulated 4, E3 ubiquitin protein ligase). It is also an inhibitor of the E3 ubiquitin-protein ligase ITCH, a NEDD4 structurally related E3. N4BP1 acts by interacting with the second WW domain of ITCH, leading to compete with ITCH's substrates and impairing ubiquitination of substrates. NYNRIN, also known as CGIN1/Cousin of GIN1, may contribute to retroviral resistance in mammals by regulating the ubiquitination of viral proteins. KHNYN acts as a novel cofactor for zinc finger antiviral protein (ZAP) to target CpG-containing retroviral RNA for degradation. Members of this family contains two type I K homology (KH) RNA-binding domain. The model corresponds to the second one.


Pssm-ID: 411816  Cd Length: 63  Bit Score: 99.16  E-value: 3.23e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767980118 120 ELQDEIHYPPKLHCIFLGAQGFFLDCLAWSTSAHLVPRAPGSLMISGLTEAFVMAQSRVEEL 181
Cdd:cd22388    1 ELWKEVRYPKDMHCIFLGAQGLFLDSLIWSTLAYLVPGPPGSLMIGGLTESVVMAQSWIQEF 62
PIN_PRORP-Zc3h12a-like cd18671
PIN domain of protein-only RNase P (PRORP), ribonuclease Zc3h12a, and related proteins; PRORPs ...
483-607 3.66e-22

PIN domain of protein-only RNase P (PRORP), ribonuclease Zc3h12a, and related proteins; PRORPs catalyze the maturation of the 5' end of precursor tRNAs in eukaryotes. This family includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3, PRORP1 localizes to the chloroplast and the mitochondria, and PRORP2 and PRORP3 localize to the nucleus. Zc3h12a (zinc finger CCCH-type containing 12A, also known as MCPIP1/MCP induced protein 1 and Regnase-1) is a critical regulator of inflammatory response, with additional roles in defense against viruses and various stresses, cellular differentiation, and apoptosis. This PIN_PRORP-Zc3h12a-like family also includes Caenorhabditis elegans REGE-1 (REGnasE-1), which also functions as a cytoplasmic endonuclease. Additionally, it includes three less-studied mammalian homologs: Zc3h12b-d/Regnase-2-4, as well as N4BP1 (NEDD4-binding partner-1), NYNRIN (NYN domain and retroviral integrase containing, also known as CGIN1/Cousin of GIN1), and KHNYN (KH and NYN domain containing) protein. N4BP1, CGIN1, and KHNYN proteins are probably of retroviral origin. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


Pssm-ID: 350238  Cd Length: 126  Bit Score: 92.31  E-value: 3.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980118 483 IVIDGSNVAMVHGLQHYFSSRGIAIAVQYFWDRGH--RDITVFVPQWRFSKDAKV--RESHFLQKLYSLSLLSLTPSrvm 558
Cdd:cd18671    1 AVIDGANVGLSHQNKESFSCRQLLLAVNWFLERSHnnTDPLVFLHKWRVEQPRPVppTDRHLLEEWEKKGILYATPP--- 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767980118 559 dgkriSSYDDRFMVKLAEETDGIIVSNDQFRDLAEE---SEKWMAIIRERLL 607
Cdd:cd18671   78 -----GSNDDWYWLYAAYESKCLLVTNDEMRDHQFEllgRQFFKRWKEEHQV 124
KH-I_N4BP1_like_rpt1 cd09032
first type I K homology (KH) RNA-binding domain found in the family of NEDD4-binding protein 1 ...
55-117 6.98e-21

first type I K homology (KH) RNA-binding domain found in the family of NEDD4-binding protein 1 (N4BP1); The N4BP1 family includes N4BP1, NYN domain and retroviral integrase catalytic domain-containing protein (NYNRIN) and KH and NYN domain-containing protein (KHNYN). These proteins are probably of retroviral origin. N4BP1 interacts with and is a substrate of NEDD4 ubiquitin ligase (neural precursor cell expressed, developmentally downregulated 4, E3 ubiquitin protein ligase). It is also an inhibitor of the E3 ubiquitin-protein ligase ITCH, a NEDD4 structurally related E3. N4BP1 acts by interacting with the second WW domain of ITCH, leading to compete with ITCH's substrates and impairing ubiquitination of substrates. NYNRIN, also known as CGIN1/Cousin of GIN1, may contribute to retroviral resistance in mammals by regulating the ubiquitination of viral proteins. KHNYN acts as a novel cofactor for zinc finger antiviral protein (ZAP) to target CpG-containing retroviral RNA for degradation. Members of this family contains two type I K homology (KH) RNA-binding domain. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411808  Cd Length: 65  Bit Score: 86.57  E-value: 6.98e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767980118  55 DRFAVSAEAENKVREQQPHVERIFSVGVSVLPKDC--PDNPHIWLQLEGPKENASRAKEYLKGLC 117
Cdd:cd09032    1 DEFVVPAEKVPLLERSRPRIERLFGVKVSLLEELSkpKDGGKQWVQLEGDEEDVRKAKEYIKALC 65
KH-I_N4BP1 cd22476
type I K homology (KH) RNA-binding domain found in NEDD4-binding protein 1 (N4BP1) and similar ...
119-182 1.07e-15

type I K homology (KH) RNA-binding domain found in NEDD4-binding protein 1 (N4BP1) and similar proteins; N4BP1 interacts with and is a substrate of NEDD4 ubiquitin ligase (neural precursor cell expressed, developmentally downregulated 4, E3 ubiquitin protein ligase). It is also an inhibitor of the E3 ubiquitin-protein ligase ITCH, a NEDD4 structurally related E3. N4BP1 acts by interacting with the second WW domain of ITCH, leading to compete with ITCH's substrates and impairing ubiquitination of substrates.


Pssm-ID: 411904  Cd Length: 68  Bit Score: 72.08  E-value: 1.07e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767980118 119 PELQDEIHYPPKLHCIFLGAQGFFLDCLAWSTSAHLVPRAPGSLMISGLTEAFVMAQSRVEELA 182
Cdd:cd22476    1 PELEEKEYYPKDMHCIFAGAQGLFLNSLIQDTCADVSVLDIGVLGIKGGAEAVVMAQSRIQQFV 64
 
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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