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Conserved domains on  [gi|2462524671|ref|XP_054224493|]
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EF-hand calcium-binding domain-containing protein 4A isoform X13 [Homo sapiens]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 1000101)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-89 8.82e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.95  E-value: 8.82e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462524671  27 RAAILEQAEELFLLCDKEAKGFITKHDLQGLQSDLPLTPEQLEAVFESLDRAHTGFLTAREFC 89
Cdd:COG5126    64 EATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFV 126
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-324 1.44e-07

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 159 RQRAVRTLWARLQRERPELLGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppSQN 238
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA--AAE 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 239 FArgERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGR 318
Cdd:COG1196   398 LA--AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475


                  ....*.
gi 2462524671 319 QEQTQR 324
Cdd:COG1196   476 EAALAE 481
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-89 8.82e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.95  E-value: 8.82e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462524671  27 RAAILEQAEELFLLCDKEAKGFITKHDLQGLQSDLPLTPEQLEAVFESLDRAHTGFLTAREFC 89
Cdd:COG5126    64 EATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFV 126
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-324 1.44e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 159 RQRAVRTLWARLQRERPELLGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppSQN 238
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA--AAE 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 239 FArgERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGR 318
Cdd:COG1196   398 LA--AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475


                  ....*.
gi 2462524671 319 QEQTQR 324
Cdd:COG1196   476 EAALAE 481
PRK12309 PRK12309
transaldolase;
28-93 2.99e-05

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 45.88  E-value: 2.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462524671  28 AAILEQAEELFLLCDKEAKGFITKHDLQGlqSDlpltpeqleAVFESLDRAHTGFLTAREFCLGLG 93
Cdd:PRK12309  330 EAFTHAAQEIFRLYDLDGDGFITREEWLG--SD---------AVFDALDLNHDGKITPEEMRAGLG 384
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 159-321 3.54e-05

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: 46.20  E-value: 3.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671  159 RQRAVRTLWARLQRERPELLG---SFEDVLIRASACLEEAARERDGLEQALRRREseherevralyEETEQLREQSRRPP 235
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAeieELEERLEEAEEELAEAEAEIEELEAQIEQLK-----------EELKALREALDELR 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671  236 SQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEA 315
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889


                   ....*.
gi 2462524671  316 RGRQEQ 321
Cdd:TIGR02168  890 ALLRSE 895
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 245-315 6.02e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.54  E-value: 6.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462524671 245 RSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQ-------AQNSQLWRAHEALRTQLEGAQEQIRRLESEA 315
Cdd:pfam07926   3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQqnyerelVLHAEDIKALQALREELNELKAEIAELKAEA 80
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 35-92 3.14e-03

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 36.87  E-value: 3.14e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671   35 EELFLLCDKEAKGFITKHDLQG--LQSDLPltPEQLEAVFESLDRAHTGFLTAREFCLGL 92
Cdd:smart00027  13 EQIFRSLDKNQDGTVTGAQAKPilLKSGLP--QTLLAKIWNLADIDNDGELDKDEFALAM 70
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
169-329 6.19e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 169 RLQRERPELLGS--FEDVLIRA-SACLEEAARERDGLEQALRRRESEHErevrALYEETEQLREQSRRPPSQNFARGERR 245
Cdd:PRK02224  290 ELEEERDDLLAEagLDDADAEAvEARREELEDRDEELRDRLEECRVAAQ----AHNEEAESLREDADDLEERAEELREEA 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 246 SRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE---SEARGRQEQT 322
Cdd:PRK02224  366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlRTARERVEEA 445


                  ....*..
gi 2462524671 323 QRCRGTG 329
Cdd:PRK02224  446 EALLEAG 452
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-89 8.82e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.95  E-value: 8.82e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462524671  27 RAAILEQAEELFLLCDKEAKGFITKHDLQGLQSDLPLTPEQLEAVFESLDRAHTGFLTAREFC 89
Cdd:COG5126    64 EATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFV 126
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-324 1.44e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 159 RQRAVRTLWARLQRERPELLGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppSQN 238
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA--AAE 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 239 FArgERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGR 318
Cdd:COG1196   398 LA--AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475


                  ....*.
gi 2462524671 319 QEQTQR 324
Cdd:COG1196   476 EAALAE 481
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 161-326 2.22e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 161 RAVRTLWARLQRERPELlgsfEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppsqnfa 240
Cdd:COG1196   235 RELEAELEELEAELEEL----EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD------- 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 241 rgerRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQE 320
Cdd:COG1196   304 ----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379


                  ....*.
gi 2462524671 321 QTQRCR 326
Cdd:COG1196   380 ELEELA 385
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 168-321 5.88e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 5.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 168 ARLQRERPELLGSfEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRrppsQNFARGERRSR 247
Cdd:COG1196   344 EELEEAEEELEEA-EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE----AEEALLERLER 418

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462524671 248 LELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQ 321
Cdd:COG1196   419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
222-326 1.90e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 222 EETEQLREQSRRPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQL 301
Cdd:COG4372    52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131

                          90       100
                  ....*....|....*....|....*
gi 2462524671 302 EGAQEQIRRLESEARGRQEQTQRCR 326
Cdd:COG4372   132 KQLEAQIAELQSEIAEREEELKELE 156
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
167-324 1.98e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 167 WARLQRERPELlgsfEDVLIRASACLEEAARERDGLEQALRRReseherevrALYEETEQLREQSRRPPSQ---NFARGE 243
Cdd:COG4717    90 YAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLL---------PLYQELEALEAELAELPERleeLEERLE 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 244 RRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQN-SQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQT 322
Cdd:COG4717   157 ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236


                  ..
gi 2462524671 323 QR 324
Cdd:COG4717   237 EA 238
PRK12309 PRK12309
transaldolase;
28-93 2.99e-05

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 45.88  E-value: 2.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462524671  28 AAILEQAEELFLLCDKEAKGFITKHDLQGlqSDlpltpeqleAVFESLDRAHTGFLTAREFCLGLG 93
Cdd:PRK12309  330 EAFTHAAQEIFRLYDLDGDGFITREEWLG--SD---------AVFDALDLNHDGKITPEEMRAGLG 384
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
192-326 3.21e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 3.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671  192 LEEAARERDGLEQALRrreseherevrALYEETEQLREQSRrppsQNFARGERRSRLElELQSREQDLERAGLRQRELEQ 271
Cdd:COG4913    612 LAALEAELAELEEELA-----------EAEERLEALEAELD----ALQERREALQRLA-EYSWDEIDVASAEREIAELEA 675

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462524671  272 QLH---AQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQTQRCR 326
Cdd:COG4913    676 ELErldASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 159-321 3.54e-05

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: 46.20  E-value: 3.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671  159 RQRAVRTLWARLQRERPELLG---SFEDVLIRASACLEEAARERDGLEQALRRREseherevralyEETEQLREQSRRPP 235
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAeieELEERLEEAEEELAEAEAEIEELEAQIEQLK-----------EELKALREALDELR 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671  236 SQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEA 315
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889


                   ....*.
gi 2462524671  316 RGRQEQ 321
Cdd:TIGR02168  890 ALLRSE 895
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 158-324 8.78e-05

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: 45.05  E-value: 8.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671  158 SRQRAVRTLWARLQRerpellgsFEDVLIRASACLEEAARERDGLEQA---LRRRESEHEREVRALYEETEQLREQSRRP 234
Cdd:TIGR02168  674 ERRREIEELEEKIEE--------LEEKIAELEKALAELRKELEELEEEleqLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671  235 PSQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQL----EGAQEQIRR 310
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllnEEAANLRER 825

                          170
                   ....*....|....
gi 2462524671  311 LESEARGRQEQTQR 324
Cdd:TIGR02168  826 LESLERRIAATERR 839
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
185-326 1.45e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671  185 LIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSrrppsqnfarGERRSRLELELQSREQDLERAGL 264
Cdd:COG4913    290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG----------GDRLEQLEREIERLERELEERER 359

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462524671  265 RQRELEQQ---LHAQAAEHLEAQAQNSQLWRAH-EALRTQLEGAQEQIRRLESEARGRQEQTQRCR 326
Cdd:COG4913    360 RRARLEALlaaLGLPLPASAEEFAALRAEAAALlEALEEELEALEEALAEAEAALRDLRRELRELE 425
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
159-313 2.03e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671  159 RQRAVRTLWARLQRERpELLGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQsRRPPSQN 238
Cdd:COG4913    286 AQRRLELLEAELEELR-AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE-RERRRAR 363

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462524671  239 FArgERRSRLELELQSREQDLERAglrQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLES 313
Cdd:COG4913    364 LE--ALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-324 2.21e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 158 SRQRAVRTLWARLQRERpELLGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRrppsQ 237
Cdd:COG1196   257 ELEAELAELEAELEELR-LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE----E 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 238 NFARGERRSRLELELQSREQDLERAglrQRELEQ---QLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESE 314
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEA---EAELAEaeeALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                         170
                  ....*....|
gi 2462524671 315 ARGRQEQTQR 324
Cdd:COG1196   409 EEALLERLER 418
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
192-321 2.74e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671  192 LEEAARERDGLEQALRRRESEHEREVrALYEETEQLREQSRRPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQ 271
Cdd:COG4913    663 VASAEREIAELEAELERLDASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462524671  272 ----QLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQ 321
Cdd:COG4913    742 larlELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
176-326 2.91e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 2.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671  176 ELLGSFEDvLIRASACLEEAARERDGLEQAlrrreseherevRALYEETEQLREQsrrppsqnfargerrsRLELELQSR 255
Cdd:COG4913    229 ALVEHFDD-LERAHEALEDAREQIELLEPI------------RELAERYAAARER----------------LAELEYLRA 279

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462524671  256 EQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIR--------RLESEARGRQEQTQRCR 326
Cdd:COG4913    280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELEERE 358
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 192-327 2.97e-04

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: 43.12  E-value: 2.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671  192 LEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppsqNFARGERRSRLELELQSREQDLERAGLRQRELEQ 271
Cdd:TIGR02168  346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK----VAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462524671  272 QLHAQAAEHLEAQAQNSQ------------LWRAHEALRTQLEGAQEQIRRLESEARGRQEQTQRCRG 327
Cdd:TIGR02168  422 EIEELLKKLEEAELKELQaeleeleeeleeLQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 245-315 6.02e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.54  E-value: 6.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462524671 245 RSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQ-------AQNSQLWRAHEALRTQLEGAQEQIRRLESEA 315
Cdd:pfam07926   3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQqnyerelVLHAEDIKALQALREELNELKAEIAELKAEA 80
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 167-316 7.93e-04

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: 7.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671  167 WARLQRERPELLGSFEDVLIRASAC---LEEAARERDGLEQALRRRESEHEREVRALyEETEQLREQSRRPPSQNFARG- 242
Cdd:TIGR02169  725 IEQLEQEEEKLKERLEELEEDLSSLeqeIENVKSELKELEARIEELEEDLHKLEEAL-NDLEARLSHSRIPEIQAELSKl 803

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462524671  243 -ERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEAR 316
Cdd:TIGR02169  804 eEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
222-326 1.00e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 222 EETEQLREQSRRPPSQNfargERRSRLELELQSREQDLERAGLRQRELEQQLhaqaaEHLEAQAQNSQLWRAHEALRTQL 301
Cdd:COG4717    71 KELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREEL-----EKLEKLLQLLPLYQELEALEAEL 141

                          90       100
                  ....*....|....*....|....*
gi 2462524671 302 EGAQEQIRRLESEARGRQEQTQRCR 326
Cdd:COG4717   142 AELPERLEELEERLEELRELEEELE 166
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 128-312 1.41e-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: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 128 LDEEEEEEERFHTVLEQLGVAPVLGNSRPPSRQRAVRTLWARLQRERPELlgsfeDVLIRASACLEEAARERDGLEQALR 207
Cdd:COG1196   604 VASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG-----EGGSAGGSLTGGSRRELLAALLEAE 678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 208 RRESEHEREVRALYEETEQLREQSRRppsQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQN 287
Cdd:COG1196   679 AELEELAERLAEEELELEEALLAEEE---EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                         170       180
                  ....*....|....*....|....*
gi 2462524671 288 SQLWRAHEALRTQLEGAQEQIRRLE 312
Cdd:COG1196   756 LPEPPDLEELERELERLEREIEALG 780
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 35-92 3.14e-03

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 36.87  E-value: 3.14e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671   35 EELFLLCDKEAKGFITKHDLQG--LQSDLPltPEQLEAVFESLDRAHTGFLTAREFCLGL 92
Cdd:smart00027  13 EQIFRSLDKNQDGTVTGAQAKPilLKSGLP--QTLLAKIWNLADIDNDGELDKDEFALAM 70
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
169-329 6.19e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 169 RLQRERPELLGS--FEDVLIRA-SACLEEAARERDGLEQALRRRESEHErevrALYEETEQLREQSRRPPSQNFARGERR 245
Cdd:PRK02224  290 ELEEERDDLLAEagLDDADAEAvEARREELEDRDEELRDRLEECRVAAQ----AHNEEAESLREDADDLEERAEELREEA 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524671 246 SRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE---SEARGRQEQT 322
Cdd:PRK02224  366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlRTARERVEEA 445


                  ....*..
gi 2462524671 323 QRCRGTG 329
Cdd:PRK02224  446 EALLEAG 452
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 253-307 6.34e-03

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 38.40  E-value: 6.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462524671 253 QSREQDLERAgLRQRELEQQLH----AQAAEHLEAQAQNSQLWRAHEaLRTQLEGAQEQ 307
Cdd:pfam09728 148 ELRELHFEKL-LKTKELEVQLAeaklQQATEEEEKKAQEKEVAKARE-LKAQVQTLSET 204
PRK09039 PRK09039
peptidoglycan -binding protein;
245-323 9.52e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.02  E-value: 9.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462524671 245 RSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRrlESEARGRQEQTQ 323
Cdd:PRK09039   97 RSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD--ASEKRDRESQAK 173
 
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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