NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15239202|ref|NP_196187|]
View 

nuclear pore complex protein-like protein [Arabidopsis thaliana]

Protein Classification

nucleoporin Nup88 family protein( domain architecture ID 708993)

nucleoporin Nup88 family protein is a component of the nuclear pore complex (NPC) and plays critical roles in maintaining the spindle stability and preventing aneuploidy formation during mitosis.

Gene Ontology:  GO:0005643|GO:0017056|GO:0006913
PubMed:  30883195

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Nup88 super family cl25737
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
29-249 6.55e-17

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


The actual alignment was detected with superfamily member pfam10168:

Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 85.10  E-value: 6.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202    29 LQSHPVFASLPSSQDEPAVSQLFP-RNFMAWDgDSRVYYWDSRRYLLhrLSLRLGEPEPSSVLAAVPSKVMQPDLQVTFS 107
Cdd:pfam10168   6 LNKHELFLKLREGLPTDGQQTRKIaRNLLDCK-DGDLYVWNSNDSCL--LTTNLRTLQSDEKDAKSSYQTLLCTNPPLFE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202   108 VSKISINKSGSAVLLAGSDGICVMYL---FGRASVIEDN---VICRVVSIGSEIYTSSDSaITLLQASWHPDS--DTHLG 179
Cdd:pfam10168  83 VDRVLVSPTGSHVALSGPRGVSVLELprrWGKDSEFEGGkpkITCRTYPVAERFFTSNPS-LELRQVRWHPSStsDSHLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202   180 ILSSDAVFRLFDLsSDTELPEQEYYLQPGEPGRSRTA--SSIYPA-------DFSFG-----GDHLWDRFT--------- 236
Cdd:pfam10168 162 LLTSDNTLRLYSL-KEPQNPAKLRHLWQVGPESVLSGsnRSLYDFslgetavDFDFAppvkkPSEEKELNGqtlkeekie 240
                         250
                  ....*....|....*
gi 15239202   237 --VFILFTDGSIYIL 249
Cdd:pfam10168 241 wpIYILRENGEVYIL 255
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
648-784 9.12e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 9.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202    648 NLKRIIDDQHQRLAEANEKISKVEKNQSFLEKRIDKAIERHDSLEQCLQRLrslpGTHKKPLTRAELDFKSELdqyAGVE 727
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL----QEELQRLSEELADLNAAI---AGIE 433
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239202    728 --VDALQSSIETLRARVKKSTQK-SHKGTVVAASQKKQYSKKNLIQDTQ--MSQLQSTLAKL 784
Cdd:TIGR02169  434 akINELEEEKEDKALEIKKQEWKlEQLAADLSKYEQELYDLKEEYDRVEkeLSKLQRELAEA 495
 
Name Accession Description Interval E-value
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
29-249 6.55e-17

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 85.10  E-value: 6.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202    29 LQSHPVFASLPSSQDEPAVSQLFP-RNFMAWDgDSRVYYWDSRRYLLhrLSLRLGEPEPSSVLAAVPSKVMQPDLQVTFS 107
Cdd:pfam10168   6 LNKHELFLKLREGLPTDGQQTRKIaRNLLDCK-DGDLYVWNSNDSCL--LTTNLRTLQSDEKDAKSSYQTLLCTNPPLFE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202   108 VSKISINKSGSAVLLAGSDGICVMYL---FGRASVIEDN---VICRVVSIGSEIYTSSDSaITLLQASWHPDS--DTHLG 179
Cdd:pfam10168  83 VDRVLVSPTGSHVALSGPRGVSVLELprrWGKDSEFEGGkpkITCRTYPVAERFFTSNPS-LELRQVRWHPSStsDSHLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202   180 ILSSDAVFRLFDLsSDTELPEQEYYLQPGEPGRSRTA--SSIYPA-------DFSFG-----GDHLWDRFT--------- 236
Cdd:pfam10168 162 LLTSDNTLRLYSL-KEPQNPAKLRHLWQVGPESVLSGsnRSLYDFslgetavDFDFAppvkkPSEEKELNGqtlkeekie 240
                         250
                  ....*....|....*
gi 15239202   237 --VFILFTDGSIYIL 249
Cdd:pfam10168 241 wpIYILRENGEVYIL 255
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
648-784 9.12e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 9.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202    648 NLKRIIDDQHQRLAEANEKISKVEKNQSFLEKRIDKAIERHDSLEQCLQRLrslpGTHKKPLTRAELDFKSELdqyAGVE 727
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL----QEELQRLSEELADLNAAI---AGIE 433
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239202    728 --VDALQSSIETLRARVKKSTQK-SHKGTVVAASQKKQYSKKNLIQDTQ--MSQLQSTLAKL 784
Cdd:TIGR02169  434 akINELEEEKEDKALEIKKQEWKlEQLAADLSKYEQELYDLKEEYDRVEkeLSKLQRELAEA 495
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
648-785 3.23e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 3.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202 648 NLKRIIDDQHQRLAEANEKISKVEKNQSFLEKRIDKAIERHDSLEQCL--------QRLRSLPGTHKKPLTRAELDFKSE 719
Cdd:COG4942  52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELeaqkeelaELLRALYRLGRQPPLALLLSPEDF 131
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239202 720 LD-----QYAGVEVDALQSSIETLRARVK-----KSTQKSHKGTVVAASQKKQYSKKNLiqDTQMSQLQSTLAKLS 785
Cdd:COG4942 132 LDavrrlQYLKYLAPARREQAEELRADLAelaalRAELEAERAELEALLAELEEERAAL--EALKAERQKLLARLE 205
 
Name Accession Description Interval E-value
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
29-249 6.55e-17

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 85.10  E-value: 6.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202    29 LQSHPVFASLPSSQDEPAVSQLFP-RNFMAWDgDSRVYYWDSRRYLLhrLSLRLGEPEPSSVLAAVPSKVMQPDLQVTFS 107
Cdd:pfam10168   6 LNKHELFLKLREGLPTDGQQTRKIaRNLLDCK-DGDLYVWNSNDSCL--LTTNLRTLQSDEKDAKSSYQTLLCTNPPLFE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202   108 VSKISINKSGSAVLLAGSDGICVMYL---FGRASVIEDN---VICRVVSIGSEIYTSSDSaITLLQASWHPDS--DTHLG 179
Cdd:pfam10168  83 VDRVLVSPTGSHVALSGPRGVSVLELprrWGKDSEFEGGkpkITCRTYPVAERFFTSNPS-LELRQVRWHPSStsDSHLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202   180 ILSSDAVFRLFDLsSDTELPEQEYYLQPGEPGRSRTA--SSIYPA-------DFSFG-----GDHLWDRFT--------- 236
Cdd:pfam10168 162 LLTSDNTLRLYSL-KEPQNPAKLRHLWQVGPESVLSGsnRSLYDFslgetavDFDFAppvkkPSEEKELNGqtlkeekie 240
                         250
                  ....*....|....*
gi 15239202   237 --VFILFTDGSIYIL 249
Cdd:pfam10168 241 wpIYILRENGEVYIL 255
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
648-784 9.12e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 9.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202    648 NLKRIIDDQHQRLAEANEKISKVEKNQSFLEKRIDKAIERHDSLEQCLQRLrslpGTHKKPLTRAELDFKSELdqyAGVE 727
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL----QEELQRLSEELADLNAAI---AGIE 433
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239202    728 --VDALQSSIETLRARVKKSTQK-SHKGTVVAASQKKQYSKKNLIQDTQ--MSQLQSTLAKL 784
Cdd:TIGR02169  434 akINELEEEKEDKALEIKKQEWKlEQLAADLSKYEQELYDLKEEYDRVEkeLSKLQRELAEA 495
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
648-785 3.23e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 3.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202 648 NLKRIIDDQHQRLAEANEKISKVEKNQSFLEKRIDKAIERHDSLEQCL--------QRLRSLPGTHKKPLTRAELDFKSE 719
Cdd:COG4942  52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELeaqkeelaELLRALYRLGRQPPLALLLSPEDF 131
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239202 720 LD-----QYAGVEVDALQSSIETLRARVK-----KSTQKSHKGTVVAASQKKQYSKKNLiqDTQMSQLQSTLAKLS 785
Cdd:COG4942 132 LDavrrlQYLKYLAPARREQAEELRADLAelaalRAELEAERAELEALLAELEEERAAL--EALKAERQKLLARLE 205
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
649-748 1.63e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239202  649 LKRIIDDQHQRLAEANEKISKVEKNQSFLEKRIDKAIERHDSLEQCLQRLRSLPGTHkkPLTRAELDFKSEL-DQYAGVE 727
Cdd:COG4913  690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE--LRALLEERFAAALgDAVEREL 767
                         90       100
                 ....*....|....*....|.
gi 15239202  728 VDALQSSIETLRARVKKSTQK 748
Cdd:COG4913  768 RENLEERIDALRARLNRAEEE 788
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH