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Conserved domains on  [gi|16716349|ref|NP_444304|]
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nuclear pore glycoprotein p62 [Mus musculus]

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 ...
319-433 6.23e-47

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: 159.01  E-value: 6.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349   319 ASSTAAGTATgPAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELD 398
Cdd:pfam05064   1 LSAKPVEPPP-SALKNKTLDDIINKWSTQLSKQSKEFETQAAKVNEWDRVLVENGDKISKLYSETLEAEQDQNRIDQQLD 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 16716349   399 FILSQQKELEDLLSPLEESVKEQSGTIYLQHADEE 433
Cdd:pfam05064  80 YVESQQDELESLLDNYEEQLEELLGDITSQNSDEE 114
Nucleoporin_FG2 super family cl37900
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
75-267 1.99e-05

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: 47.35  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349    75 GFNFGTTPASG---GTGFSLGISTpklslsnaaaTPATANTGSFGLGS---------STLTNAISSGSTSNQGTAPTGFV 142
Cdd:pfam15967   3 GFSFGGGPGSTataGGGFSFGAAA----------ASNPGSTGGFSFGTlgaapaataTTTTATLGLGGGLFGQKPATGFT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349   143 FGSSTTSAPSTGSTGFSFTSGSASQPGASGFSLGsvgsSAQPTAlSGSPFT-PATLVTTTAGATQPAAAAPTAATTSAGS 221
Cdd:pfam15967  73 FGTPASSTAATGPTGLTLGTPAATTAASTGFSLG----FNKPAA-SATPFSlPASSTSGGGLSLGSVLTSTAAQQGATGF 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16716349   222 TLFASIAAAPASSSATGLSLPAPVTT----------AATPSAGTLGFSLKAPGAAP 267
Cdd:pfam15967 148 TLNLGGTPATTTAVSTGLSLGSTLTSlggslfqntnSTGLGQTTLGLTLLATSTAP 203
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
347-526 1.54e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 1.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349 347 ELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEESVKEqsgtiy 426
Cdd:COG4372  67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE------ 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349 427 LQHADEEREKTyklAENIDAQLKRMAQDLKDiIEHLNMAGGPADTSDPLQQICKILNAHMDSLQWVDqssaLLQRRVEEA 506
Cdd:COG4372 141 LQSEIAEREEE---LKELEEQLESLQEELAA-LEQELQALSEAEAEQALDELLKEANRNAEKEEELA----EAEKLIESL 212
                       170       180
                ....*....|....*....|
gi 16716349 507 SRVCEGRRKEQERSLRIAFD 526
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 ...
319-433 6.23e-47

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: 159.01  E-value: 6.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349   319 ASSTAAGTATgPAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELD 398
Cdd:pfam05064   1 LSAKPVEPPP-SALKNKTLDDIINKWSTQLSKQSKEFETQAAKVNEWDRVLVENGDKISKLYSETLEAEQDQNRIDQQLD 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 16716349   399 FILSQQKELEDLLSPLEESVKEQSGTIYLQHADEE 433
Cdd:pfam05064  80 YVESQQDELESLLDNYEEQLEELLGDITSQNSDEE 114
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
75-267 1.99e-05

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: 47.35  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349    75 GFNFGTTPASG---GTGFSLGISTpklslsnaaaTPATANTGSFGLGS---------STLTNAISSGSTSNQGTAPTGFV 142
Cdd:pfam15967   3 GFSFGGGPGSTataGGGFSFGAAA----------ASNPGSTGGFSFGTlgaapaataTTTTATLGLGGGLFGQKPATGFT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349   143 FGSSTTSAPSTGSTGFSFTSGSASQPGASGFSLGsvgsSAQPTAlSGSPFT-PATLVTTTAGATQPAAAAPTAATTSAGS 221
Cdd:pfam15967  73 FGTPASSTAATGPTGLTLGTPAATTAASTGFSLG----FNKPAA-SATPFSlPASSTSGGGLSLGSVLTSTAAQQGATGF 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16716349   222 TLFASIAAAPASSSATGLSLPAPVTT----------AATPSAGTLGFSLKAPGAAP 267
Cdd:pfam15967 148 TLNLGGTPATTTAVSTGLSLGSTLTSlggslfqntnSTGLGQTTLGLTLLATSTAP 203
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
347-526 1.54e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 1.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349 347 ELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEESVKEqsgtiy 426
Cdd:COG4372  67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE------ 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349 427 LQHADEEREKTyklAENIDAQLKRMAQDLKDiIEHLNMAGGPADTSDPLQQICKILNAHMDSLQWVDqssaLLQRRVEEA 506
Cdd:COG4372 141 LQSEIAEREEE---LKELEEQLESLQEELAA-LEQELQALSEAEAEQALDELLKEANRNAEKEEELA----EAEKLIESL 212
                       170       180
                ....*....|....*....|
gi 16716349 507 SRVCEGRRKEQERSLRIAFD 526
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLG 232
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
335-462 5.99e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 5.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349  335 AQLESLINKWSlELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPL 414
Cdd:PRK03918 200 KELEEVLREIN-EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16716349  415 EESVKE-----QSGTIYLQhADEEREKTYKLAENIDAQLKRMAQDLKDIIEHL 462
Cdd:PRK03918 279 EEKVKElkelkEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
335-463 6.53e-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: 6.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349 335 AQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSqQKELEDLLSPL 414
Cdd:COG1579  20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-NKEYEALQKEI 98
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 16716349 415 EESVKEQSgtiylQHADEEREKTYKLaENIDAQLKRMAQDLKDIIEHLN 463
Cdd:COG1579  99 ESLKRRIS-----DLEDEILELMERI-EELEEELAELEAELAELEAELE 141
CENP-Q pfam13094
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles ...
379-500 9.02e-04

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: 39.96  E-value: 9.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349   379 LHREVEKVKLDQKRLDQELDF--ILSQQKELEDLLSPLEESV--------KEQSGTI----YLQ--------HADEEREK 436
Cdd:pfam13094   1 LLRRLARLPFPPGGKEKVLDFekLLDRNKALEAQLSAELHSLelleeeieKEEALLEsdeeYLEeleknakaEARERKEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349   437 TyKLAENIDAQLKRMAQDLKDIIEHLNMAGGPADTSDP-----LQQICKILNAHMDSLQ-----------WVDQSSALLQ 500
Cdd:pfam13094  81 L-KKEHPLLQEDDSGVLSLPELSSDLGLGDTDFSLFDPtldeeLLPLLEQLQKHLESMQgnlaqleglneAIERAYAALD 159
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
335-463 1.10e-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: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349    335 AQLESLINKWSLELEDQERhflQQATQVNAWDRTLiengEKITSLHREVEKVKLDQKRLDQELDfilSQQKELEDLLSPL 414
Cdd:TIGR02169  304 ASLERSIAEKERELEDAEE---RLAKLEAEIDKLL----AEIEELEREIEEERKRRDKLTEEYA---ELKEELEDLRAEL 373
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16716349    415 EEsVKEQSGTIYLQHADEERE----------------KTYKLAENIDAQLKRMAQDLKDIIEHLN 463
Cdd:TIGR02169  374 EE-VDKEFAETRDELKDYREKleklkreinelkreldRLQEELQRLSEELADLNAAIAGIEAKIN 437
 
Name Accession Description Interval E-value
Nsp1_C pfam05064
Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region ...
319-433 6.23e-47

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: 159.01  E-value: 6.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349   319 ASSTAAGTATgPAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELD 398
Cdd:pfam05064   1 LSAKPVEPPP-SALKNKTLDDIINKWSTQLSKQSKEFETQAAKVNEWDRVLVENGDKISKLYSETLEAEQDQNRIDQQLD 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 16716349   399 FILSQQKELEDLLSPLEESVKEQSGTIYLQHADEE 433
Cdd:pfam05064  80 YVESQQDELESLLDNYEEQLEELLGDITSQNSDEE 114
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
75-267 1.99e-05

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: 47.35  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349    75 GFNFGTTPASG---GTGFSLGISTpklslsnaaaTPATANTGSFGLGS---------STLTNAISSGSTSNQGTAPTGFV 142
Cdd:pfam15967   3 GFSFGGGPGSTataGGGFSFGAAA----------ASNPGSTGGFSFGTlgaapaataTTTTATLGLGGGLFGQKPATGFT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349   143 FGSSTTSAPSTGSTGFSFTSGSASQPGASGFSLGsvgsSAQPTAlSGSPFT-PATLVTTTAGATQPAAAAPTAATTSAGS 221
Cdd:pfam15967  73 FGTPASSTAATGPTGLTLGTPAATTAASTGFSLG----FNKPAA-SATPFSlPASSTSGGGLSLGSVLTSTAAQQGATGF 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16716349   222 TLFASIAAAPASSSATGLSLPAPVTT----------AATPSAGTLGFSLKAPGAAP 267
Cdd:pfam15967 148 TLNLGGTPATTTAVSTGLSLGSTLTSlggslfqntnSTGLGQTTLGLTLLATSTAP 203
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
1-257 1.22e-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: 44.66  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349     1 MSGFNFGG----TGAPAGGFTFGTAKTATTTPATGFSFSASGTGTGGFnfgtpsqpaATTPSTSLFSLTTQTPTTQTPGF 76
Cdd:pfam15967   1 MSGFSFGGgpgsTATAGGGFSFGAAAASNPGSTGGFSFGTLGAAPAAT---------ATTTTATLGLGGGLFGQKPATGF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349    77 NFGT----TPASGGTGFSLGisTPKLSLSNAAatpatantgSFGLGSSTLTNAISSGSTSNQGTAPTGFVFGSSTTSaps 152
Cdd:pfam15967  72 TFGTpassTAATGPTGLTLG--TPAATTAAST---------GFSLGFNKPAASATPFSLPASSTSGGGLSLGSVLTS--- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349   153 tgstgfsftsgSASQPGASGFSLGSVGSSAQPTALSGSPFTPATLvtttagatqpaaaaptaatTSAGSTLFASIAAAPA 232
Cdd:pfam15967 138 -----------TAAQQGATGFTLNLGGTPATTTAVSTGLSLGSTL-------------------TSLGGSLFQNTNSTGL 187
                         250       260
                  ....*....|....*....|....*
gi 16716349   233 SSSATGLSLPAPVTTAATPSAGTLG 257
Cdd:pfam15967 188 GQTTLGLTLLATSTAPVSAPAASEG 212
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
347-526 1.54e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 1.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349 347 ELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEESVKEqsgtiy 426
Cdd:COG4372  67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE------ 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349 427 LQHADEEREKTyklAENIDAQLKRMAQDLKDiIEHLNMAGGPADTSDPLQQICKILNAHMDSLQWVDqssaLLQRRVEEA 506
Cdd:COG4372 141 LQSEIAEREEE---LKELEEQLESLQEELAA-LEQELQALSEAEAEQALDELLKEANRNAEKEEELA----EAEKLIESL 212
                       170       180
                ....*....|....*....|
gi 16716349 507 SRVCEGRRKEQERSLRIAFD 526
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLG 232
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
335-462 5.99e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 5.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349  335 AQLESLINKWSlELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPL 414
Cdd:PRK03918 200 KELEEVLREIN-EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16716349  415 EESVKE-----QSGTIYLQhADEEREKTYKLAENIDAQLKRMAQDLKDIIEHL 462
Cdd:PRK03918 279 EEKVKElkelkEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
335-463 6.53e-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: 6.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349 335 AQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSqQKELEDLLSPL 414
Cdd:COG1579  20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-NKEYEALQKEI 98
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 16716349 415 EESVKEQSgtiylQHADEEREKTYKLaENIDAQLKRMAQDLKDIIEHLN 463
Cdd:COG1579  99 ESLKRRIS-----DLEDEILELMERI-EELEEELAELEAELAELEAELE 141
CENP-Q pfam13094
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles ...
379-500 9.02e-04

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: 39.96  E-value: 9.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349   379 LHREVEKVKLDQKRLDQELDF--ILSQQKELEDLLSPLEESV--------KEQSGTI----YLQ--------HADEEREK 436
Cdd:pfam13094   1 LLRRLARLPFPPGGKEKVLDFekLLDRNKALEAQLSAELHSLelleeeieKEEALLEsdeeYLEeleknakaEARERKEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349   437 TyKLAENIDAQLKRMAQDLKDIIEHLNMAGGPADTSDP-----LQQICKILNAHMDSLQ-----------WVDQSSALLQ 500
Cdd:pfam13094  81 L-KKEHPLLQEDDSGVLSLPELSSDLGLGDTDFSLFDPtldeeLLPLLEQLQKHLESMQgnlaqleglneAIERAYAALD 159
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
335-463 1.10e-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: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349    335 AQLESLINKWSLELEDQERhflQQATQVNAWDRTLiengEKITSLHREVEKVKLDQKRLDQELDfilSQQKELEDLLSPL 414
Cdd:TIGR02169  304 ASLERSIAEKERELEDAEE---RLAKLEAEIDKLL----AEIEELEREIEEERKRRDKLTEEYA---ELKEELEDLRAEL 373
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16716349    415 EEsVKEQSGTIYLQHADEERE----------------KTYKLAENIDAQLKRMAQDLKDIIEHLN 463
Cdd:TIGR02169  374 EE-VDKEFAETRDELKDYREKleklkreinelkreldRLQEELQRLSEELADLNAAIAGIEAKIN 437
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
331-524 2.07e-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: 2.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349 331 AMTYAQL-----ESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELD------F 399
Cdd:COG1196 212 AERYRELkeelkELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeY 291
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349 400 ILSQQKE-LEDLLSPLEESVKEQSGTiyLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLNMAggpADTSDPLQQi 478
Cdd:COG1196 292 ELLAELArLEQDIARLEERRRELEER--LEELEEELAELEEELEELEEELEELEEELEEAEEELEEA---EAELAEAEE- 365
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 16716349 479 cKILNAHMDSLQWVDQSSALLQRRVEEASRVCEGRRKEQERSLRIA 524
Cdd:COG1196 366 -ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
336-455 2.43e-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: 40.81  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349    336 QLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHR-------EVEKVKldqkrldQELDFILSQQKELE 408
Cdd:TIGR02168  941 LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPvnlaaieEYEELK-------ERYDFLTAQKEDLT 1013
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 16716349    409 DLLSPLEESVKEqsgtiylqhADEEREKTYKLA-ENIDAQLKRMAQDL 455
Cdd:TIGR02168 1014 EAKETLEEAIEE---------IDREARERFKDTfDQVNENFQRVFPKL 1052
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
336-462 2.76e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349 336 QLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDfilSQQKELEDLLSPLE 415
Cdd:COG4372  42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE---SLQEEAEELQEELE 118
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 16716349 416 ESVKEQSG-TIYLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHL 462
Cdd:COG4372 119 ELQKERQDlEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
331-463 3.20e-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: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349    331 AMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELdfilsQQKELEDL 410
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL-----EEAELKEL 438
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 16716349    411 LSPLEESVKEQSGtiyLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLN 463
Cdd:TIGR02168  439 QAELEELEEELEE---LQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
337-464 4.25e-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: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349   337 LESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEE 416
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16716349   417 SVKEQSGTIYLQHADEEREK---TYKLAENIDAQLKRMAQDL----KDIIEHLNM 464
Cdd:TIGR04523 553 ELKKENLEKEIDEKNKEIEElkqTQKSLKKKQEEKQELIDQKekekKDLIKEIEE 607
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
335-522 4.54e-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: 4.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349    335 AQLESLINkwslELEDQERHFLQQA----------TQVNAWDRTLIenGEKITSLHREVEKVKLDQKRLDQELDFILSQQ 404
Cdd:TIGR02168  189 DRLEDILN----ELERQLKSLERQAekaerykelkAELRELELALL--VLRLEELREELEELQEELKEAEEELEELTAEL 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349    405 K-------ELEDLLSPLEESVKEQSGTIY------------LQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLNMA 465
Cdd:TIGR02168  263 QeleekleELRLEVSELEEEIEELQKELYalaneisrleqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16716349    466 ggpADTSDPLQQICKILNAHMDSLQWVDQSsalLQRRVEEASRVCEGRR------KEQERSLR 522
Cdd:TIGR02168  343 ---EEKLEELKEELESLEAELEELEAELEE---LESRLEELEEQLETLRskvaqlELQIASLN 399
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
314-522 4.78e-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: 39.36  E-value: 4.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349 314 ATALPASSTAAGTATGPAMTYAQLESLINkwslELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRL 393
Cdd:COG4942   6 LLALLLALAAAAQADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716349 394 DQELDFILSQQKELEDLLSPLEESVKEQSGTIYlQHADEEREKTYKLAENIdAQLKRMAQDLKDIIEHL-NMAGGPADTS 472
Cdd:COG4942  82 EAELAELEKEIAELRAELEAQKEELAELLRALY-RLGRQPPLALLLSPEDF-LDAVRRLQYLKYLAPARrEQAEELRADL 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16716349 473 DPLQQICKILNAHMDSLQwvdqssALLQRRVEEASRVcEGRRKEQERSLR 522
Cdd:COG4942 160 AELAALRAELEAERAELE------ALLAELEEERAAL-EALKAERQKLLA 202
FmiP_Thoc5 pfam09766
Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues ...
391-465 5.52e-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: 5.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16716349   391 KRLDQELDfilsQQKELEDLLSPLEESVKEqsgtiyLQHADEEREKTYKlaeNIDAQLKRMAQDLKDIIEHLNMA 465
Cdd:pfam09766  87 ARLEWELE----QRKELAKQLKELEQSKKK------LLQEIESKKKRLS---SLPPALKSLLKATKPLQEALGLP 148
 
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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