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Conserved domains on  [gi|564328266|ref|XP_006229213|]
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nuclear pore glycoprotein p62 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Nsp1_C pfam05064
Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region ...
318-432 1.10e-46

Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region of Nsp1 is involved in binding Nup82.


:

Pssm-ID: 461540 [Multi-domain]  Cd Length: 114  Bit Score: 158.63  E-value: 1.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266  318 ASSTAVGTTTgPAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELD 397
Cdd:pfam05064   1 LSAKPVEPPP-SALKNKTLDDIINKWSTQLSKQSKEFETQAAKVNEWDRVLVENGDKISKLYSETLEAEQDQNRIDQQLD 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564328266  398 FILSQQKELEDLLSPLEESVKEQSGTIYLQHADEE 432
Cdd:pfam05064  80 YVESQQDELESLLDNYEEQLEELLGDITSQNSDEE 114
Nucleoporin_FG2 super family cl37900
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
1-188 1.66e-04

Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.


The actual alignment was detected with superfamily member pfam15967:

Pssm-ID: 435043 [Multi-domain]  Cd Length: 586  Bit Score: 44.27  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266    1 MSGFNFGG----TGAPAGGFTFGTAKTATTTPATGFSFSASGTGtggfnfgtpsqPAATTpstslfslATQTSTTQTPGF 76
Cdd:pfam15967   1 MSGFSFGGgpgsTATAGGGFSFGAAAASNPGSTGGFSFGTLGAA-----------PAATA--------TTTTATLGLGGG 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266   77 NFGTTPASG---GTGFSLGISTPKLSLSSTAATPATANTGSFGLGSSTLTNAISGASTSSQGTAPTGFVFGSSTTSapst 153
Cdd:pfam15967  62 LFGQKPATGftfGTPASSTAATGPTGLTLGTPAATTAASTGFSLGFNKPAASATPFSLPASSTSGGGLSLGSVLTS---- 137
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 564328266  154 gttgfsftsgSASQPGASGFNIGSVGSLAQPTALS 188
Cdd:pfam15967 138 ----------TAAQQGATGFTLNLGGTPATTTAVS 162
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
346-525 4.75e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 4.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 346 ELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEESVKEqsgtiy 425
Cdd:COG4372   67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE------ 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 426 LQHADEEREKTyklAENIDAQLKRMAQDLKDiIEHLNMAGGPADTSDPLQQICKILNAHMDSLQWVDqssaLLQRRVEEA 505
Cdd:COG4372  141 LQSEIAEREEE---LKELEEQLESLQEELAA-LEQELQALSEAEAEQALDELLKEANRNAEKEEELA----EAEKLIESL 212
                        170       180
                 ....*....|....*....|
gi 564328266 506 SRVCESRRKEQERSLRIAFD 525
Cdd:COG4372  213 PRELAEELLEAKDSLEAKLG 232
 
Name Accession Description Interval E-value
Nsp1_C pfam05064
Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region ...
318-432 1.10e-46

Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region of Nsp1 is involved in binding Nup82.


Pssm-ID: 461540 [Multi-domain]  Cd Length: 114  Bit Score: 158.63  E-value: 1.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266  318 ASSTAVGTTTgPAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELD 397
Cdd:pfam05064   1 LSAKPVEPPP-SALKNKTLDDIINKWSTQLSKQSKEFETQAAKVNEWDRVLVENGDKISKLYSETLEAEQDQNRIDQQLD 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564328266  398 FILSQQKELEDLLSPLEESVKEQSGTIYLQHADEE 432
Cdd:pfam05064  80 YVESQQDELESLLDNYEEQLEELLGDITSQNSDEE 114
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
1-188 1.66e-04

Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.


Pssm-ID: 435043 [Multi-domain]  Cd Length: 586  Bit Score: 44.27  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266    1 MSGFNFGG----TGAPAGGFTFGTAKTATTTPATGFSFSASGTGtggfnfgtpsqPAATTpstslfslATQTSTTQTPGF 76
Cdd:pfam15967   1 MSGFSFGGgpgsTATAGGGFSFGAAAASNPGSTGGFSFGTLGAA-----------PAATA--------TTTTATLGLGGG 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266   77 NFGTTPASG---GTGFSLGISTPKLSLSSTAATPATANTGSFGLGSSTLTNAISGASTSSQGTAPTGFVFGSSTTSapst 153
Cdd:pfam15967  62 LFGQKPATGftfGTPASSTAATGPTGLTLGTPAATTAASTGFSLGFNKPAASATPFSLPASSTSGGGLSLGSVLTS---- 137
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 564328266  154 gttgfsftsgSASQPGASGFNIGSVGSLAQPTALS 188
Cdd:pfam15967 138 ----------TAAQQGATGFTLNLGGTPATTTAVS 162
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
346-525 4.75e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 4.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 346 ELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEESVKEqsgtiy 425
Cdd:COG4372   67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE------ 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 426 LQHADEEREKTyklAENIDAQLKRMAQDLKDiIEHLNMAGGPADTSDPLQQICKILNAHMDSLQWVDqssaLLQRRVEEA 505
Cdd:COG4372  141 LQSEIAEREEE---LKELEEQLESLQEELAA-LEQELQALSEAEAEQALDELLKEANRNAEKEEELA----EAEKLIESL 212
                        170       180
                 ....*....|....*....|
gi 564328266 506 SRVCESRRKEQERSLRIAFD 525
Cdd:COG4372  213 PRELAEELLEAKDSLEAKLG 232
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
334-461 5.97e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 5.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 334 AQLESLINKWSlELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPL 413
Cdd:PRK03918 200 KELEEVLREIN-EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564328266 414 EESVKE-----QSGTIYLQhADEEREKTYKLAENIDAQLKRMAQDLKDIIEHL 461
Cdd:PRK03918 279 EEKVKElkelkEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
334-462 6.51e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 334 AQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSqQKELEDLLSPL 413
Cdd:COG1579   20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-NKEYEALQKEI 98
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 564328266 414 EESVKEQSgtiylQHADEEREKTYKLaENIDAQLKRMAQDLKDIIEHLN 462
Cdd:COG1579   99 ESLKRRIS-----DLEDEILELMERI-EELEEELAELEAELAELEAELE 141
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
334-517 1.07e-03

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: 41.98  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266   334 AQLESLINKwsLELEDQERHFLQQATQVNAWDRTLIEN-----GEKITSLHREVEKVKLDQKRLDQELDFILSQQKELED 408
Cdd:TIGR02169  688 RELSSLQSE--LRRIENRLDELSQELSDASRKIGEIEKeieqlEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266   409 LLSPLEE---SVKEQSGTIYLQHADEEREKTYKLAENIDAQLKRmaqdLKDIIEHLNmaggpadtsdplqqicKILNAHM 485
Cdd:TIGR02169  766 RIEELEEdlhKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSR----IEARLREIE----------------QKLNRLT 825
                          170       180       190
                   ....*....|....*....|....*....|..
gi 564328266   486 DSLQWVDQSSALLQRRVEEASRVCESRRKEQE 517
Cdd:TIGR02169  826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
CENP-Q pfam13094
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles ...
378-499 1.14e-03

CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles onto the CENPA-nucleosome distal (CAD) centromere. The centromere, which is the basic element of chromosome inheritance, is epigenetically determined in mammals. CENP-A, the centromere-specific histone H3 variant, assembles an array of nucleosomes and it is this that seems to be the prime candidate for specifying centromere identity. CENPA nucleosomes directly recruit a proximal CENPA-nucleosome-associated complex (NAC) comprised of CENP-M, CENP-N and CENP-T, CENP-U(50), CENP-C and CENP-H. Assembly of the CENPA NAC at centromeres is dependent on CENP-M, CENP-N and CENP-T. Additionally, there are seven other subunits which make up the CENPA-nucleosome distal (CAD) centromere, CENP-K, CENP-L, CENP-O, CENP-P, CENP-Q, CENP-R and CENP-S, also assembling on the CENP-A NAC. Fta7 is the equivalent component of the fission yeast Sim4 complex.


Pssm-ID: 432970 [Multi-domain]  Cd Length: 159  Bit Score: 39.58  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266  378 LHREVEKVKLDQKRLDQELDF--ILSQQKELEDLLSPLEESV--------KEQSGTI----YLQ--------HADEEREK 435
Cdd:pfam13094   1 LLRRLARLPFPPGGKEKVLDFekLLDRNKALEAQLSAELHSLelleeeieKEEALLEsdeeYLEeleknakaEARERKEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266  436 TyKLAENIDAQLKRMAQDLKDIIEHLNMAGGPADTSDP-----LQQICKILNAHMDSLQ-----------WVDQSSALLQ 499
Cdd:pfam13094  81 L-KKEHPLLQEDDSGVLSLPELSSDLGLGDTDFSLFDPtldeeLLPLLEQLQKHLESMQgnlaqleglneAIERAYAALD 159
 
Name Accession Description Interval E-value
Nsp1_C pfam05064
Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region ...
318-432 1.10e-46

Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region of Nsp1 is involved in binding Nup82.


Pssm-ID: 461540 [Multi-domain]  Cd Length: 114  Bit Score: 158.63  E-value: 1.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266  318 ASSTAVGTTTgPAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELD 397
Cdd:pfam05064   1 LSAKPVEPPP-SALKNKTLDDIINKWSTQLSKQSKEFETQAAKVNEWDRVLVENGDKISKLYSETLEAEQDQNRIDQQLD 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564328266  398 FILSQQKELEDLLSPLEESVKEQSGTIYLQHADEE 432
Cdd:pfam05064  80 YVESQQDELESLLDNYEEQLEELLGDITSQNSDEE 114
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
1-188 1.66e-04

Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.


Pssm-ID: 435043 [Multi-domain]  Cd Length: 586  Bit Score: 44.27  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266    1 MSGFNFGG----TGAPAGGFTFGTAKTATTTPATGFSFSASGTGtggfnfgtpsqPAATTpstslfslATQTSTTQTPGF 76
Cdd:pfam15967   1 MSGFSFGGgpgsTATAGGGFSFGAAAASNPGSTGGFSFGTLGAA-----------PAATA--------TTTTATLGLGGG 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266   77 NFGTTPASG---GTGFSLGISTPKLSLSSTAATPATANTGSFGLGSSTLTNAISGASTSSQGTAPTGFVFGSSTTSapst 153
Cdd:pfam15967  62 LFGQKPATGftfGTPASSTAATGPTGLTLGTPAATTAASTGFSLGFNKPAASATPFSLPASSTSGGGLSLGSVLTS---- 137
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 564328266  154 gttgfsftsgSASQPGASGFNIGSVGSLAQPTALS 188
Cdd:pfam15967 138 ----------TAAQQGATGFTLNLGGTPATTTAVS 162
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
346-525 4.75e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 4.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 346 ELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEESVKEqsgtiy 425
Cdd:COG4372   67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE------ 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 426 LQHADEEREKTyklAENIDAQLKRMAQDLKDiIEHLNMAGGPADTSDPLQQICKILNAHMDSLQWVDqssaLLQRRVEEA 505
Cdd:COG4372  141 LQSEIAEREEE---LKELEEQLESLQEELAA-LEQELQALSEAEAEQALDELLKEANRNAEKEEELA----EAEKLIESL 212
                        170       180
                 ....*....|....*....|
gi 564328266 506 SRVCESRRKEQERSLRIAFD 525
Cdd:COG4372  213 PRELAEELLEAKDSLEAKLG 232
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
334-461 5.97e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 5.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 334 AQLESLINKWSlELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPL 413
Cdd:PRK03918 200 KELEEVLREIN-EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564328266 414 EESVKE-----QSGTIYLQhADEEREKTYKLAENIDAQLKRMAQDLKDIIEHL 461
Cdd:PRK03918 279 EEKVKElkelkEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
334-462 6.51e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 334 AQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSqQKELEDLLSPL 413
Cdd:COG1579   20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-NKEYEALQKEI 98
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 564328266 414 EESVKEQSgtiylQHADEEREKTYKLaENIDAQLKRMAQDLKDIIEHLN 462
Cdd:COG1579   99 ESLKRRIS-----DLEDEILELMERI-EELEEELAELEAELAELEAELE 141
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
334-517 1.07e-03

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: 41.98  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266   334 AQLESLINKwsLELEDQERHFLQQATQVNAWDRTLIEN-----GEKITSLHREVEKVKLDQKRLDQELDFILSQQKELED 408
Cdd:TIGR02169  688 RELSSLQSE--LRRIENRLDELSQELSDASRKIGEIEKeieqlEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266   409 LLSPLEE---SVKEQSGTIYLQHADEEREKTYKLAENIDAQLKRmaqdLKDIIEHLNmaggpadtsdplqqicKILNAHM 485
Cdd:TIGR02169  766 RIEELEEdlhKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSR----IEARLREIE----------------QKLNRLT 825
                          170       180       190
                   ....*....|....*....|....*....|..
gi 564328266   486 DSLQWVDQSSALLQRRVEEASRVCESRRKEQE 517
Cdd:TIGR02169  826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
334-462 1.09e-03

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: 41.98  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266   334 AQLESLINKWSLELEDQERhflQQATQVNAWDRTLiengEKITSLHREVEKVKLDQKRLDQELDfilSQQKELEDLLSPL 413
Cdd:TIGR02169  304 ASLERSIAEKERELEDAEE---RLAKLEAEIDKLL----AEIEELEREIEEERKRRDKLTEEYA---ELKEELEDLRAEL 373
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564328266   414 EEsVKEQSGTIYLQHADEERE----------------KTYKLAENIDAQLKRMAQDLKDIIEHLN 462
Cdd:TIGR02169  374 EE-VDKEFAETRDELKDYREKleklkreinelkreldRLQEELQRLSEELADLNAAIAGIEAKIN 437
CENP-Q pfam13094
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles ...
378-499 1.14e-03

CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles onto the CENPA-nucleosome distal (CAD) centromere. The centromere, which is the basic element of chromosome inheritance, is epigenetically determined in mammals. CENP-A, the centromere-specific histone H3 variant, assembles an array of nucleosomes and it is this that seems to be the prime candidate for specifying centromere identity. CENPA nucleosomes directly recruit a proximal CENPA-nucleosome-associated complex (NAC) comprised of CENP-M, CENP-N and CENP-T, CENP-U(50), CENP-C and CENP-H. Assembly of the CENPA NAC at centromeres is dependent on CENP-M, CENP-N and CENP-T. Additionally, there are seven other subunits which make up the CENPA-nucleosome distal (CAD) centromere, CENP-K, CENP-L, CENP-O, CENP-P, CENP-Q, CENP-R and CENP-S, also assembling on the CENP-A NAC. Fta7 is the equivalent component of the fission yeast Sim4 complex.


Pssm-ID: 432970 [Multi-domain]  Cd Length: 159  Bit Score: 39.58  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266  378 LHREVEKVKLDQKRLDQELDF--ILSQQKELEDLLSPLEESV--------KEQSGTI----YLQ--------HADEEREK 435
Cdd:pfam13094   1 LLRRLARLPFPPGGKEKVLDFekLLDRNKALEAQLSAELHSLelleeeieKEEALLEsdeeYLEeleknakaEARERKEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266  436 TyKLAENIDAQLKRMAQDLKDIIEHLNMAGGPADTSDP-----LQQICKILNAHMDSLQ-----------WVDQSSALLQ 499
Cdd:pfam13094  81 L-KKEHPLLQEDDSGVLSLPELSSDLGLGDTDFSLFDPtldeeLLPLLEQLQKHLESMQgnlaqleglneAIERAYAALD 159
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
330-523 1.73e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 330 AMTYAQL-----ESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELD------F 398
Cdd:COG1196  212 AERYRELkeelkELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeY 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 399 ILSQQKE-LEDLLSPLEESVKEQSGTiyLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLNMAggpADTSDPLQQi 477
Cdd:COG1196  292 ELLAELArLEQDIARLEERRRELEER--LEELEEELAELEEELEELEEELEELEEELEEAEEELEEA---EAELAEAEE- 365
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564328266 478 cKILNAHMDSLQWVDQSSALLQRRVEEASRVCESRRKEQERSLRIA 523
Cdd:COG1196  366 -ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
335-454 3.24e-03

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266   335 QLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHR-------EVEKVKldqkrldQELDFILSQQKELE 407
Cdd:TIGR02168  941 LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPvnlaaieEYEELK-------ERYDFLTAQKEDLT 1013
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 564328266   408 DLLSPLEESVKEqsgtiylqhADEEREKTYKLA-ENIDAQLKRMAQDL 454
Cdd:TIGR02168 1014 EAKETLEEAIEE---------IDREARERFKDTfDQVNENFQRVFPKL 1052
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
330-462 4.02e-03

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 4.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266   330 AMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELdfilsQQKELEDL 409
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL-----EEAELKEL 438
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 564328266   410 LSPLEESVKEQSGtiyLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLN 462
Cdd:TIGR02168  439 QAELEELEEELEE---LQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
336-463 4.23e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266  336 LESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEE 415
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564328266  416 SVKEQSGTIYLQHADEEREK---TYKLAENIDAQLKRMAQDL----KDIIEHLNM 463
Cdd:TIGR04523 553 ELKKENLEKEIDEKNKEIEElkqTQKSLKKKQEEKQELIDQKekekKDLIKEIEE 607
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
334-521 4.41e-03

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 4.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266   334 AQLESLINkwslELEDQERHFLQQA----------TQVNAWDRTLIenGEKITSLHREVEKVKLDQKRLDQELDFILSQQ 403
Cdd:TIGR02168  189 DRLEDILN----ELERQLKSLERQAekaerykelkAELRELELALL--VLRLEELREELEELQEELKEAEEELEELTAEL 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266   404 K-------ELEDLLSPLEESVKEQSGTIY------------LQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLNMA 464
Cdd:TIGR02168  263 QeleekleELRLEVSELEEEIEELQKELYalaneisrleqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564328266   465 ggpADTSDPLQQICKILNAHMDSLQWVDQSsalLQRRVEEASRVCESRR------KEQERSLR 521
Cdd:TIGR02168  343 ---EEKLEELKEELESLEAELEELEAELEE---LESRLEELEEQLETLRskvaqlELQIASLN 399
FmiP_Thoc5 pfam09766
Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues ...
390-464 5.51e-03

Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues of the FmiP (Fms interacting protein). A member of the THO (suppressors of the transcriptional defects of hpr1delta by overexpression) complex which is a subcomplex of the transcription/export (TREX) complex. It is essential for the binding of the protein to the cytoplasmic domain of activated Fms-molecules in M-CSF induced haematopoietic differentiation of macrophages. Fmip is also known as THOC5 (THO complex subunit 5) a 683 amino acids long protein which contains a nuclear localization sequence (NLS), a leucine zipper and a PEST like sequence (aa. 303-319) that carries three ataxia-telangiectasia mutated (ATM) kinase specific phosphorylation sites. The C-terminus contains a THOC1 binding site. The level of FMIP/Thoc5 expression might form a threshold that determines whether cells differentiate into macrophages or into granulocytes.


Pssm-ID: 462889  Cd Length: 347  Bit Score: 39.22  E-value: 5.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564328266  390 KRLDQELDfilsQQKELEDLLSPLEESVKEqsgtiyLQHADEEREKTYKlaeNIDAQLKRMAQDLKDIIEHLNMA 464
Cdd:pfam09766  87 ARLEWELE----QRKELAKQLKELEQSKKK------LLQEIESKKKRLS---SLPPALKSLLKATKPLQEALGLP 148
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
335-461 6.32e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 6.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 335 QLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDfilSQQKELEDLLSPLE 414
Cdd:COG4372   42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE---SLQEEAEELQEELE 118
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 564328266 415 ESVKEQSG-TIYLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHL 461
Cdd:COG4372  119 ELQKERQDlEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
313-521 6.65e-03

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: 38.98  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 313 ATALPASSTAVGTTTGPAMTYAQLESLINkwslELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRL 392
Cdd:COG4942    6 LLALLLALAAAAQADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266 393 DQELDFILSQQKELEDLLSPLEESVKEQSGTIYlQHADEEREKTYKLAENIdAQLKRMAQDLKDIIEHL-NMAGGPADTS 471
Cdd:COG4942   82 EAELAELEKEIAELRAELEAQKEELAELLRALY-RLGRQPPLALLLSPEDF-LDAVRRLQYLKYLAPARrEQAEELRADL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 564328266 472 DPLQQICKILNAHMDSLQwvdqssALLQRRVEEASRVcESRRKEQERSLR 521
Cdd:COG4942  160 AELAALRAELEAERAELE------ALLAELEEERAAL-EALKAERQKLLA 202
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
334-524 8.91e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 8.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266  334 AQLESLINKWSLELEDQERHFLQQATQVNAWDR--TLIENGEKITSLHREVEkvkldqkRLDQELDFILSQQKELEDLLS 411
Cdd:COG4913   620 AELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIA-------ELEAELERLDASSDDLAALEE 692
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328266  412 PLEESVKEqsgtiyLQHADEEREKTYKLAENIDAQLKRMA---QDLKDIIEHLNMAGGPADTSDplqqickiLNAHMDSL 488
Cdd:COG4913   693 QLEELEAE------LEELEEELDELKGEIGRLEKELEQAEeelDELQDRLEAAEDLARLELRAL--------LEERFAAA 758
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 564328266  489 QwVDQSSALLQRRVEEASRVCESRRKEQERSLRIAF 524
Cdd:COG4913   759 L-GDAVERELRENLEERIDALRARLNRAEEELERAM 793
 
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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