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Conserved domains on  [gi|528474849|ref|XP_005164264|]
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non-structural maintenance of chromosomes element 1 homolog isoform X1 [Danio rerio]

Protein Classification

non-structural maintenance of chromosomes element 1( domain architecture ID 11698274)

non-structural maintenance of chromosomes element 1 homolog (NSE1) is a RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate

CATH:  3.30.40.10
EC:  2.3.2.27
Gene Symbol:  NSMCE1
Gene Ontology:  GO:0004842|GO:0061630|GO:0016567|GO:0008270
PubMed:  11007473|20864041|18667531|19489725
SCOP:  3000160

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RING-CH-C4HC3_NSE1 cd16493
RING-CH finger, H2 subclass (C4HC3-type), found in non-structural maintenance of chromosomes ...
 180-228 5.04e-21

RING-CH finger, H2 subclass (C4HC3-type), found in non-structural maintenance of chromosomes (SMC) element 1 homolog (NSE1) and similar proteins; NSE1, also known as non-SMC element 1 homolog (NSMCE1), is an E3 ubiquitin ligase that contains a C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger. Together with its partner proteins NSE3 and NSE4, it forms a tight subcomplex of the SMC5-6 complex, which includes another two subcomplexes, SMC6-SMC5-NSE2 and NSE5-NSE6. The vRING finger is essential for normal NSE1-NSE3-NSE4 trimer formation in vitro and for damage-induced recruitment of NSE4 and SMC5 to subnuclear foci in vivo. Thus it functions as a protein-protein interaction domain required for SMC5-6 holocomplex integrity and recruitment to, or retention at, DNA lesions. The C-terminal half of NSE1, including the vRING finger, is required for DNA damage resistance and mitotic fidelity of SMC5-6 complex in the fission yeast Schizosaccharomyces pombe. The RING-CH finger may play an important role in Rad52-dependent post-replication repair of UV-damaged DNA in Saccharomyces cerevisiae.


:

Pssm-ID: 438156  Cd Length: 49  Bit Score: 83.26  E-value: 5.04e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 528474849 180 KVCYVCHNIALQCQVCENPSCEIKVHLPCVARYFRARSDPHCPACNDFW 228
Cdd:cd16493    1 KSCNICHEIVIQGQSCPNEDCGIRLHLYCAKRYFRRRAEPRCPSCNTPW 49
SMC_Nse1 super family cl20339
Nse1 non-SMC component of SMC5-6 complex; S. cerevisiae Nse1 forms part of a complex with ...
 10-166 1.22e-15

Nse1 non-SMC component of SMC5-6 complex; S. cerevisiae Nse1 forms part of a complex with SMC5-SMC6. This non-structural maintenance of chromosomes (SMC) complex plays an essential role in genomic stability, being involved in DNA repair and DNA metabolism. It is conserved in eukaryotes from yeast to human. This domain lies immediately up-stream of the DNA-binding zinc-finger domain, zf-RING-like pfam08746.


The actual alignment was detected with superfamily member pfam07574:

Pssm-ID: 462214  Cd Length: 196  Bit Score: 73.03  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474849   10 RLFLQNMMTNGIVS--AAQAGMLHkkcceLHGG-------------QEKIDDFINVVNTHLQPLFMHIRKGMSEEDGQE- 73
Cdd:pfam07574   1 RAFLQALLARGTLTeeEAKPILAA-----IFSAdegepvdpndditQDDLNDYISTINVALSPLDYEIRSVRHQLGKERv 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474849   74 HFVLVNMAETDITRMAADYAENELELFRKIMDLIVESD-----------SGSASSTA-ILNSADKLISKKLKKK------ 135
Cdd:pfam07574  76 YYALVNTTSDPETQLATTFSPDEIAFIKRLLDAMFDTYntprmevmaitSMQAIKLArILAPPRRNRWSSYGYTagsgql 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 528474849  136 ---------EAELVLNKFVQDKWL-KEQDGEYTLSVRCIVE 166
Cdd:pfam07574 156 sqaaglthsEAEKLLTRLVEEGWLeRSREGFYGLSPRALLE 196
 
Name Accession Description Interval E-value
RING-CH-C4HC3_NSE1 cd16493
RING-CH finger, H2 subclass (C4HC3-type), found in non-structural maintenance of chromosomes ...
 180-228 5.04e-21

RING-CH finger, H2 subclass (C4HC3-type), found in non-structural maintenance of chromosomes (SMC) element 1 homolog (NSE1) and similar proteins; NSE1, also known as non-SMC element 1 homolog (NSMCE1), is an E3 ubiquitin ligase that contains a C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger. Together with its partner proteins NSE3 and NSE4, it forms a tight subcomplex of the SMC5-6 complex, which includes another two subcomplexes, SMC6-SMC5-NSE2 and NSE5-NSE6. The vRING finger is essential for normal NSE1-NSE3-NSE4 trimer formation in vitro and for damage-induced recruitment of NSE4 and SMC5 to subnuclear foci in vivo. Thus it functions as a protein-protein interaction domain required for SMC5-6 holocomplex integrity and recruitment to, or retention at, DNA lesions. The C-terminal half of NSE1, including the vRING finger, is required for DNA damage resistance and mitotic fidelity of SMC5-6 complex in the fission yeast Schizosaccharomyces pombe. The RING-CH finger may play an important role in Rad52-dependent post-replication repair of UV-damaged DNA in Saccharomyces cerevisiae.


Pssm-ID: 438156  Cd Length: 49  Bit Score: 83.26  E-value: 5.04e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 528474849 180 KVCYVCHNIALQCQVCENPSCEIKVHLPCVARYFRARSDPHCPACNDFW 228
Cdd:cd16493    1 KSCNICHEIVIQGQSCPNEDCGIRLHLYCAKRYFRRRAEPRCPSCNTPW 49
SMC_Nse1 pfam07574
Nse1 non-SMC component of SMC5-6 complex; S. cerevisiae Nse1 forms part of a complex with ...
 10-166 1.22e-15

Nse1 non-SMC component of SMC5-6 complex; S. cerevisiae Nse1 forms part of a complex with SMC5-SMC6. This non-structural maintenance of chromosomes (SMC) complex plays an essential role in genomic stability, being involved in DNA repair and DNA metabolism. It is conserved in eukaryotes from yeast to human. This domain lies immediately up-stream of the DNA-binding zinc-finger domain, zf-RING-like pfam08746.


Pssm-ID: 462214  Cd Length: 196  Bit Score: 73.03  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474849   10 RLFLQNMMTNGIVS--AAQAGMLHkkcceLHGG-------------QEKIDDFINVVNTHLQPLFMHIRKGMSEEDGQE- 73
Cdd:pfam07574   1 RAFLQALLARGTLTeeEAKPILAA-----IFSAdegepvdpndditQDDLNDYISTINVALSPLDYEIRSVRHQLGKERv 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474849   74 HFVLVNMAETDITRMAADYAENELELFRKIMDLIVESD-----------SGSASSTA-ILNSADKLISKKLKKK------ 135
Cdd:pfam07574  76 YYALVNTTSDPETQLATTFSPDEIAFIKRLLDAMFDTYntprmevmaitSMQAIKLArILAPPRRNRWSSYGYTagsgql 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 528474849  136 ---------EAELVLNKFVQDKWL-KEQDGEYTLSVRCIVE 166
Cdd:pfam07574 156 sqaaglthsEAEKLLTRLVEEGWLeRSREGFYGLSPRALLE 196
zf-RING-like pfam08746
RING-like domain; This is a zinc finger domain that is related to the C3HC4 RING finger domain ...
 182-224 4.45e-14

RING-like domain; This is a zinc finger domain that is related to the C3HC4 RING finger domain (pfam00097).


Pssm-ID: 430187  Cd Length: 43  Bit Score: 64.70  E-value: 4.45e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 528474849  182 CYVCHNIALQCQVCENPSCEIKVHLPCVARYFRARSDPHCPAC 224
Cdd:pfam08746   1 CEACKEIVTQGQRCPNEDCNVRLHDDCLRKYFRTRRSPKCPKC 43
 
Name Accession Description Interval E-value
RING-CH-C4HC3_NSE1 cd16493
RING-CH finger, H2 subclass (C4HC3-type), found in non-structural maintenance of chromosomes ...
 180-228 5.04e-21

RING-CH finger, H2 subclass (C4HC3-type), found in non-structural maintenance of chromosomes (SMC) element 1 homolog (NSE1) and similar proteins; NSE1, also known as non-SMC element 1 homolog (NSMCE1), is an E3 ubiquitin ligase that contains a C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger. Together with its partner proteins NSE3 and NSE4, it forms a tight subcomplex of the SMC5-6 complex, which includes another two subcomplexes, SMC6-SMC5-NSE2 and NSE5-NSE6. The vRING finger is essential for normal NSE1-NSE3-NSE4 trimer formation in vitro and for damage-induced recruitment of NSE4 and SMC5 to subnuclear foci in vivo. Thus it functions as a protein-protein interaction domain required for SMC5-6 holocomplex integrity and recruitment to, or retention at, DNA lesions. The C-terminal half of NSE1, including the vRING finger, is required for DNA damage resistance and mitotic fidelity of SMC5-6 complex in the fission yeast Schizosaccharomyces pombe. The RING-CH finger may play an important role in Rad52-dependent post-replication repair of UV-damaged DNA in Saccharomyces cerevisiae.


Pssm-ID: 438156  Cd Length: 49  Bit Score: 83.26  E-value: 5.04e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 528474849 180 KVCYVCHNIALQCQVCENPSCEIKVHLPCVARYFRARSDPHCPACNDFW 228
Cdd:cd16493    1 KSCNICHEIVIQGQSCPNEDCGIRLHLYCAKRYFRRRAEPRCPSCNTPW 49
SMC_Nse1 pfam07574
Nse1 non-SMC component of SMC5-6 complex; S. cerevisiae Nse1 forms part of a complex with ...
 10-166 1.22e-15

Nse1 non-SMC component of SMC5-6 complex; S. cerevisiae Nse1 forms part of a complex with SMC5-SMC6. This non-structural maintenance of chromosomes (SMC) complex plays an essential role in genomic stability, being involved in DNA repair and DNA metabolism. It is conserved in eukaryotes from yeast to human. This domain lies immediately up-stream of the DNA-binding zinc-finger domain, zf-RING-like pfam08746.


Pssm-ID: 462214  Cd Length: 196  Bit Score: 73.03  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474849   10 RLFLQNMMTNGIVS--AAQAGMLHkkcceLHGG-------------QEKIDDFINVVNTHLQPLFMHIRKGMSEEDGQE- 73
Cdd:pfam07574   1 RAFLQALLARGTLTeeEAKPILAA-----IFSAdegepvdpndditQDDLNDYISTINVALSPLDYEIRSVRHQLGKERv 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474849   74 HFVLVNMAETDITRMAADYAENELELFRKIMDLIVESD-----------SGSASSTA-ILNSADKLISKKLKKK------ 135
Cdd:pfam07574  76 YYALVNTTSDPETQLATTFSPDEIAFIKRLLDAMFDTYntprmevmaitSMQAIKLArILAPPRRNRWSSYGYTagsgql 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 528474849  136 ---------EAELVLNKFVQDKWL-KEQDGEYTLSVRCIVE 166
Cdd:pfam07574 156 sqaaglthsEAEKLLTRLVEEGWLeRSREGFYGLSPRALLE 196
zf-RING-like pfam08746
RING-like domain; This is a zinc finger domain that is related to the C3HC4 RING finger domain ...
 182-224 4.45e-14

RING-like domain; This is a zinc finger domain that is related to the C3HC4 RING finger domain (pfam00097).


Pssm-ID: 430187  Cd Length: 43  Bit Score: 64.70  E-value: 4.45e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 528474849  182 CYVCHNIALQCQVCENPSCEIKVHLPCVARYFRARSDPHCPAC 224
Cdd:pfam08746   1 CEACKEIVTQGQRCPNEDCNVRLHDDCLRKYFRTRRSPKCPKC 43
 
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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