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Conserved domains on  [gi|1162503618|ref|NP_001336414|]
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E3 SUMO-protein ligase NSE2 isoform 1 [Homo sapiens]

Protein Classification

NSE2 family E3 SUMO-protein ligase( domain architecture ID 11616116)

NSE2 family E3 SUMO-protein ligase such as NSE2 and MMS2, which are required for DNA repair

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
167-237 9.89e-29

SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity.


:

Pssm-ID: 438313 [Multi-domain]  Cd Length: 67  Bit Score: 103.50  E-value: 9.89e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162503618 167 FTCPITKEEMKKPVKNKVCGHTYEEDAIVRMIesrQKRKKKAYCPQIGCSHTdIRKSDLIQDEALRRAIEN 237
Cdd:cd16651     1 LKCPITQQLMVDPVRNKKCGHTYEKAAILQYL---QSRKKKAKCPVAGCRNT-VSKSDLVPDPELKRRIER 67
 
Name Accession Description Interval E-value
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
167-237 9.89e-29

SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity.


Pssm-ID: 438313 [Multi-domain]  Cd Length: 67  Bit Score: 103.50  E-value: 9.89e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162503618 167 FTCPITKEEMKKPVKNKVCGHTYEEDAIVRMIesrQKRKKKAYCPQIGCSHTdIRKSDLIQDEALRRAIEN 237
Cdd:cd16651     1 LKCPITQQLMVDPVRNKKCGHTYEKAAILQYL---QSRKKKAKCPVAGCRNT-VSKSDLVPDPELKRRIER 67
zf-Nse pfam11789
Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the ...
156-216 3.80e-24

Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the fission yeast Smc5-6 DNA repair complex. This family is the zinc-finger domain similar to the MIZ type of zinc-finger.


Pssm-ID: 403098 [Multi-domain]  Cd Length: 57  Bit Score: 91.19  E-value: 3.80e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162503618 156 EDIIVTQSQTNFTCPITKEEMKKPVKNKVCGHTYEEDAIVRMIesrqKRKKKAYCPQIGCS 216
Cdd:pfam11789   1 DDLQIEGETISLTCPLTLQPFVEPVTSKKCNHVFEKDAILEML----KRNPTVKCPVIGCS 57
COG5627 COG5627
SUMO ligase MMS21, Smc5/6 complex, required for cell growth and DNA repair [Replication, ...
142-233 2.48e-06

SUMO ligase MMS21, Smc5/6 complex, required for cell growth and DNA repair [Replication, recombination and repair];


Pssm-ID: 227914  Cd Length: 275  Bit Score: 47.32  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503618 142 LQADREADGTEGVDEDIIVTQSQTNFTCPITKEEMKKPVKNKVCGHTYEEDAIVRMIESRQKRKkkayCPQIGCSHTDIR 221
Cdd:COG5627   165 NIVMKSPNPEEGLVDKILIHQELLSNRCPITLNPDFYPILSSKCNHKPEMDLINKKLQVECTRV----CPRLICSQKEVV 240
                          90
                  ....*....|..
gi 1162503618 222 kSDLIQDEALRR 233
Cdd:COG5627   241 -DPYVCDHILEK 251
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
167-236 2.58e-06

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: 43.76  E-value: 2.58e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503618  167 FTCPITKEEMKKPVKNKVcGHTYEEDAIVRMIESRQKrkkkayCPqigCSHTDIRKSDLIQDEALRRAIE 236
Cdd:smart00504   2 FLCPISLEVMKDPVILPS-GQTYERSAIEKWLLSHGT------DP---VTGQPLTHEDLIPNLALKSAIQ 61
 
Name Accession Description Interval E-value
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
167-237 9.89e-29

SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity.


Pssm-ID: 438313 [Multi-domain]  Cd Length: 67  Bit Score: 103.50  E-value: 9.89e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162503618 167 FTCPITKEEMKKPVKNKVCGHTYEEDAIVRMIesrQKRKKKAYCPQIGCSHTdIRKSDLIQDEALRRAIEN 237
Cdd:cd16651     1 LKCPITQQLMVDPVRNKKCGHTYEKAAILQYL---QSRKKKAKCPVAGCRNT-VSKSDLVPDPELKRRIER 67
zf-Nse pfam11789
Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the ...
156-216 3.80e-24

Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the fission yeast Smc5-6 DNA repair complex. This family is the zinc-finger domain similar to the MIZ type of zinc-finger.


Pssm-ID: 403098 [Multi-domain]  Cd Length: 57  Bit Score: 91.19  E-value: 3.80e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162503618 156 EDIIVTQSQTNFTCPITKEEMKKPVKNKVCGHTYEEDAIVRMIesrqKRKKKAYCPQIGCS 216
Cdd:pfam11789   1 DDLQIEGETISLTCPLTLQPFVEPVTSKKCNHVFEKDAILEML----KRNPTVKCPVIGCS 57
SP-RING-like cd16452
SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a ...
167-211 6.16e-14

SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a group of proteins with variants of RING fingers that are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. They include SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases and SPL-RING finger found in E3 SUMO-protein ligase NSE2. The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress.


Pssm-ID: 438116 [Multi-domain]  Cd Length: 45  Bit Score: 64.20  E-value: 6.16e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1162503618 167 FTCPITKEEMKKPVKNKVCGHTYEEDAIVRMIESRQKRKKkayCP 211
Cdd:cd16452     1 LKCPITQKRMKDPVRGKHCGHCFDLEAILQYLKRRKKKWK---CP 42
RING_Ubox cd00162
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
169-212 4.71e-10

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. 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. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438111 [Multi-domain]  Cd Length: 42  Bit Score: 53.62  E-value: 4.71e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1162503618 169 CPITKEEMKK--PVKNKVCGHTYEEDAIVRMIESrqkrkKKAYCPQ 212
Cdd:cd00162     1 CPICREEMNDrrPVVLLSCGHTFSRSAIARWLEG-----SKQKCPF 41
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
169-211 6.49e-07

RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.


Pssm-ID: 463881 [Multi-domain]  Cd Length: 38  Bit Score: 44.70  E-value: 6.49e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1162503618 169 CPITKEEMKKPVKNkvCGHTYEEDAIVRMiesRQKRKKKAYCP 211
Cdd:pfam13445   1 CPICLELFTDPVLP--CGHTFCRECLEEM---SQKKGGKFKCP 38
COG5627 COG5627
SUMO ligase MMS21, Smc5/6 complex, required for cell growth and DNA repair [Replication, ...
142-233 2.48e-06

SUMO ligase MMS21, Smc5/6 complex, required for cell growth and DNA repair [Replication, recombination and repair];


Pssm-ID: 227914  Cd Length: 275  Bit Score: 47.32  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503618 142 LQADREADGTEGVDEDIIVTQSQTNFTCPITKEEMKKPVKNKVCGHTYEEDAIVRMIESRQKRKkkayCPQIGCSHTDIR 221
Cdd:COG5627   165 NIVMKSPNPEEGLVDKILIHQELLSNRCPITLNPDFYPILSSKCNHKPEMDLINKKLQVECTRV----CPRLICSQKEVV 240
                          90
                  ....*....|..
gi 1162503618 222 kSDLIQDEALRR 233
Cdd:COG5627   241 -DPYVCDHILEK 251
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
167-236 2.58e-06

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: 43.76  E-value: 2.58e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503618  167 FTCPITKEEMKKPVKNKVcGHTYEEDAIVRMIESRQKrkkkayCPqigCSHTDIRKSDLIQDEALRRAIE 236
Cdd:smart00504   2 FLCPISLEVMKDPVILPS-GQTYERSAIEKWLLSHGT------DP---VTGQPLTHEDLIPNLALKSAIQ 61
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
167-201 2.73e-06

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: 43.64  E-value: 2.73e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1162503618 167 FTCPITKEEMKKPVknkVC--GHTYEEDAIVRMIESR 201
Cdd:cd16655     4 FLCPITQELMRDPV---VAadGHTYERSAIEEWLETH 37
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
167-200 4.46e-06

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: 42.94  E-value: 4.46e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1162503618 167 FTCPITKEEMKKPVknKVC-GHTYEEDAIVRMIES 200
Cdd:cd16664     4 FICPISLELMKDPV--ILAtGQTYERAAIEKWLDS 36
COG5222 COG5222
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
125-242 1.26e-04

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227547 [Multi-domain]  Cd Length: 427  Bit Score: 42.81  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503618 125 KFVQFKQQLKELKKQCGLQADREADGtegvDEDIIVTQSQTNFTCPITKEEMKKPVKNKVCGHTYEEDAIVRMIESRQKR 204
Cdd:COG5222   237 GYVVAQPDVQSWEKYQQRTKAVAEIP----DQVYKMQPPNISLKCPLCHCLLRNPMKTPCCGHTFCDECIGTALLDSDFK 312
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1162503618 205 kkkayCPQigCSHTDIRKSDLIQDEALRRAIENHNKKR 242
Cdd:COG5222   313 -----CPN--CSRKDVLLDGLTPDIDKKLEVEKALKKQ 343
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
167-201 2.33e-04

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: 38.23  E-value: 2.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1162503618 167 FTCPITKEEMKKPVKNKvCGHTYEEDAIVRMIESR 201
Cdd:cd23149     1 FTCPITSGFMEDPVITP-SGFSYERSAIERWLETK 34
dRING_Rmd5p-like cd16652
Degenerated RING (dRING) finger found in Saccharomyces cerevisiae required for meiotic nuclear ...
167-211 2.36e-04

Degenerated RING (dRING) finger found in Saccharomyces cerevisiae required for meiotic nuclear division protein 5 (Rmd5p) and similar proteins; Rmd5p, also known as glucose-induced degradation protein 2 (Gid2) or sporulation protein RMD5, is an E3 ubiquitin ligase containing a Lissencephaly type-1-like homology motif (LisH), a C-terminal to LisH motif (CTLH) domain, and a degenerated RING finger that is characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. It forms the heterodimeric E3 ligase unit of the glucose induced degradation deficient (GID) complex with Gid9 (also known as Fyv10), which has a degenerated RING finger as well. The GID complex triggers polyubiquitylation and subsequent proteasomal degradation of the gluconeogenic enzymes fructose-1, 6-bisphosphate by fructose-1, 6-bisphosphatase (FBPase), phosphoenolpyruvate carboxykinase (PEPCK), and cytoplasmic malate dehydrogenase (c-MDH). Moreover, Rmd5p can form the GID complex with the other six Gid proteins, including Gid1/Vid30, Gid4/Vid24, Gid5/Vid28, Gid7, Gid8, and Gid9/Fyv10. The GID complex in which the seven Gid proteins reside functions as a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism.


Pssm-ID: 438314  Cd Length: 49  Bit Score: 38.00  E-value: 2.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1162503618 167 FTCPITKEEMKK--PVKNKVCGHTYEEDAIVRMIESRQKRKKKAYCP 211
Cdd:cd16652     1 FACPVSREQSTEenPPMRLPCGHVISKDSLKKLSKNNGNKFKCPYCP 47
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
167-200 4.08e-04

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: 37.15  E-value: 4.08e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1162503618 167 FTCPITKEEMKKPVKNKvCGHTYEEDAIVRMIES 200
Cdd:cd16453     1 FLCPISGELMKDPVITP-SGITYDRSAIERWLLS 33
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
164-211 8.38e-04

RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by the tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus.


Pssm-ID: 438161 [Multi-domain]  Cd Length: 94  Bit Score: 37.66  E-value: 8.38e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1162503618 164 QTNFTCPITKEEMKKPVKNKvCGHTYEEDAIVRMIesrQKRKKKAYCP 211
Cdd:cd16498    14 QKNLECPICLELLKEPVSTK-CDHQFCRFCILKLL---QKKKKPAPCP 57
dRING_RMD5A cd16794
Degenerated RING finger found in protein RMD5 homolog A (RMD5A); RMD5A is one of the ...
167-211 5.68e-03

Degenerated RING finger found in protein RMD5 homolog A (RMD5A); RMD5A is one of the vertebrate homologs of yeast Rmd5p. The biological function of RMD5A remains unclear. RMD5A contains a Lissencephaly type-1-like homology motif (LisH), a C-terminal to LisH motif (CTLH) domain, and a degenerated RING finger that is characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers.


Pssm-ID: 438448  Cd Length: 60  Bit Score: 34.24  E-value: 5.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1162503618 167 FTCPITKEEMKK--PVKNKVCGHTYEEDAIVRMIESrqKRKKKAYCP 211
Cdd:cd16794     3 FACPILRQQTTEnnPPMKLVCGHIISRDALNKMFNG--SKLKCPYCP 47
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
169-212 7.40e-03

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 404756 [Multi-domain]  Cd Length: 40  Bit Score: 33.56  E-value: 7.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1162503618 169 CPITKEEMKKPVKNKVCGHTYEEDAIVRMIESRQKrkkkayCPQ 212
Cdd:pfam13923   2 CPICMDMLKDPSTTTPCGHVFCQDCILRALRAGNE------CPL 39
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
167-237 9.18e-03

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: 34.09  E-value: 9.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162503618 167 FTCPITKEEMKKPVKNKvCGHTYEEDAIVRMIesrqkRKKKAYCPqigCSHTDIRKSDLIQDEALRRAIEN 237
Cdd:cd16654     5 LCCKISFELMRDPVITP-SGITYERKDIEEHL-----QRVGHFDP---ITREPLTQDQLIPNLALKEAIEA 66
 
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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