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Conserved domains on  [gi|2462524677|ref|XP_054224496|]
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EF-hand calcium-binding domain-containing protein 4A isoform X14 [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 1.05e-07

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: 50.56  E-value: 1.05e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462524677  27 RAAILEQAEELFLLCDKEAKGFITKHDLQGLQSDLPLTPEQLEAVFESLDRAHTGFLTAREFC 89
Cdd:COG5126    64 EATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFV 126
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 155-320 2.52e-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: 53.02  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 155 RAVRTLWARLQRERPELlgsfEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppsqnfa 234
Cdd:COG1196   235 RELEAELEELEAELEEL----EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD------- 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 235 rgerRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQE 314
Cdd:COG1196   304 ----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379


                  ....*.
gi 2462524677 315 QTQRCR 320
Cdd:COG1196   380 ELEELA 385
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-89 1.05e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.56  E-value: 1.05e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462524677  27 RAAILEQAEELFLLCDKEAKGFITKHDLQGLQSDLPLTPEQLEAVFESLDRAHTGFLTAREFC 89
Cdd:COG5126    64 EATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFV 126
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 155-320 2.52e-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: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 155 RAVRTLWARLQRERPELlgsfEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppsqnfa 234
Cdd:COG1196   235 RELEAELEELEAELEEL----EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD------- 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 235 rgerRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQE 314
Cdd:COG1196   304 ----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379


                  ....*.
gi 2462524677 315 QTQRCR 320
Cdd:COG1196   380 ELEELA 385
PRK12309 PRK12309
transaldolase;
28-93 2.97e-05

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 45.88  E-value: 2.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462524677  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 ...
 153-315 4.07e-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: 45.82  E-value: 4.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  153 KQRAVRTLWARLQRERPELLG---SFEDVLIRASACLEEAARERDGLEQALRRREseherevralyEETEQLREQSRRPP 229
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAeieELEERLEEAEEELAEAEAEIEELEAQIEQLK-----------EELKALREALDELR 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  230 SQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEA 309
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889


                   ....*.
gi 2462524677  310 RGRQEQ 315
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 ...
 239-309 8.36e-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: 39.16  E-value: 8.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462524677 239 RSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQ-------AQNSQLWRAHEALRTQLEGAQEQIRRLESEA 309
Cdd:pfam07926   3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQqnyerelVLHAEDIKALQALREELNELKAEIAELKAEA 80
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 35-92 3.09e-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: 3.09e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677   35 EELFLLCDKEAKGFITKHDLQG--LQSDLPltPEQLEAVFESLDRAHTGFLTAREFCLGL 92
Cdd:smart00027  13 EQIFRSLDKNQDGTVTGAQAKPilLKSGLP--QTLLAKIWNLADIDNDGELDKDEFALAM 70
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
163-323 6.89e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 6.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 163 RLQRERPELLGS--FEDVLIRA-SACLEEAARERDGLEQALRRRESEHErevrALYEETEQLREQSRRPPSQNFARGERR 239
Cdd:PRK02224  290 ELEEERDDLLAEagLDDADAEAvEARREELEDRDEELRDRLEECRVAAQ----AHNEEAESLREDADDLEERAEELREEA 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 240 SRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE---SEARGRQEQT 316
Cdd:PRK02224  366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlRTARERVEEA 445


                  ....*..
gi 2462524677 317 QRCRGTG 323
Cdd:PRK02224  446 EALLEAG 452
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-89 1.05e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.56  E-value: 1.05e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462524677  27 RAAILEQAEELFLLCDKEAKGFITKHDLQGLQSDLPLTPEQLEAVFESLDRAHTGFLTAREFC 89
Cdd:COG5126    64 EATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFV 126
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 155-320 2.52e-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: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 155 RAVRTLWARLQRERPELlgsfEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppsqnfa 234
Cdd:COG1196   235 RELEAELEELEAELEEL----EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD------- 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 235 rgerRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQE 314
Cdd:COG1196   304 ----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379


                  ....*.
gi 2462524677 315 QTQRCR 320
Cdd:COG1196   380 ELEELA 385
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 162-318 2.63e-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: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 162 ARLQRERPEL---LGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYE---ETEQLREQSRRPPSQNFAR 235
Cdd:COG1196   319 EELEEELAELeeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaeeELEELAEELLEALRAAAEL 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 236 GERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQ 315
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478


                  ...
gi 2462524677 316 TQR 318
Cdd:COG1196   479 LAE 481
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 162-315 6.86e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 6.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 162 ARLQRERPELLGSfEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRrppsQNFARGERRSR 241
Cdd:COG1196   344 EELEEAEEELEEA-EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE----AEEALLERLER 418

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462524677 242 LELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQ 315
Cdd:COG1196   419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
151-318 1.97e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 151 LGKQRAVRTLWARLQRERPELlgsfEDVLIRASACLEEAARERDGLEQALRRReseherevrALYEETEQLREQSRRPPS 230
Cdd:COG4717    80 LKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLL---------PLYQELEALEAELAELPE 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 231 Q---NFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQN-SQLWRAHEALRTQLEGAQEQIRRLE 306
Cdd:COG4717   147 RleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEElEELQQRLAELEEELEEAQEELEELE 226

                         170
                  ....*....|..
gi 2462524677 307 SEARGRQEQTQR 318
Cdd:COG4717   227 EELEQLENELEA 238
PRK12309 PRK12309
transaldolase;
28-93 2.97e-05

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 45.88  E-value: 2.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462524677  28 AAILEQAEELFLLCDKEAKGFITKHDLQGlqSDlpltpeqleAVFESLDRAHTGFLTAREFCLGLG 93
Cdd:PRK12309  330 EAFTHAAQEIFRLYDLDGDGFITREEWLG--SD---------AVFDALDLNHDGKITPEEMRAGLG 384
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
216-320 3.02e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 216 EETEQLREQSRRPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQL 295
Cdd:COG4372    52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131

                          90       100
                  ....*....|....*....|....*
gi 2462524677 296 EGAQEQIRRLESEARGRQEQTQRCR 320
Cdd:COG4372   132 KQLEAQIAELQSEIAEREEELKELE 156
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
186-320 3.95e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 3.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  186 LEEAARERDGLEQALRrreseherevrALYEETEQLREQSRrppsQNFARGERRSRLElELQSREQDLERAGLRQRELEQ 265
Cdd:COG4913    612 LAALEAELAELEEELA-----------EAEERLEALEAELD----ALQERREALQRLA-EYSWDEIDVASAEREIAELEA 675

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462524677  266 QLH---AQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQTQRCR 320
Cdd:COG4913    676 ELErldASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 153-315 4.07e-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: 45.82  E-value: 4.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  153 KQRAVRTLWARLQRERPELLG---SFEDVLIRASACLEEAARERDGLEQALRRREseherevralyEETEQLREQSRRPP 229
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAeieELEERLEEAEEELAEAEAEIEELEAQIEQLK-----------EELKALREALDELR 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  230 SQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEA 309
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889


                   ....*.
gi 2462524677  310 RGRQEQ 315
Cdd:TIGR02168  890 ALLRSE 895
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 150-318 6.11e-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: 45.43  E-value: 6.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  150 VLGKQRAVRTLWARLQRerpellgsFEDVLIRASACLEEAARERDGLEQA---LRRRESEHEREVRALYEETEQLREQSR 226
Cdd:TIGR02168  672 ILERRREIEELEEKIEE--------LEEKIAELEKALAELRKELEELEEEleqLRKELEELSRQISALRKDLARLEAEVE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  227 RPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQL----EGAQEQI 302
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllnEEAANLR 823

                          170
                   ....*....|....*.
gi 2462524677  303 RRLESEARGRQEQTQR 318
Cdd:TIGR02168  824 ERLESLERRIAATERR 839
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
148-320 1.09e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  148 APVLGKQRAVRTLWARL--QRERPELLGSFEDV--LIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLRE 223
Cdd:COG4913    255 EPIRELAERYAAARERLaeLEYLRAALRLWFAQrrLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  224 QSrrppsqnfarGERRSRLELELQSREQDLERAGLRQRELEQQ---LHAQAAEHLEAQAQNSQLWRAH-EALRTQLEGAQ 299
Cdd:COG4913    335 NG----------GDRLEQLEREIERLERELEERERRRARLEALlaaLGLPLPASAEEFAALRAEAAALlEALEEELEALE 404

                          170       180
                   ....*....|....*....|.
gi 2462524677  300 EQIRRLESEARGRQEQTQRCR 320
Cdd:COG4913    405 EALAEAEAALRDLRRELRELE 425
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
148-308 1.64e-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: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  148 APVLGKQRAVRTLWARLQRERpELLGSFEDVLIRASACLEEAARERDGLEQALRRREseherevralYEETEQLREQSRR 227
Cdd:COG4913    281 LRLWFAQRRLELLEAELEELR-AELARLEAELERLEARLDALREELDELEAQIRGNG----------GDRLEQLEREIER 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  228 ppsqnfaRGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHE----ALRTQLEGAQEQIR 303
Cdd:COG4913    350 -------LERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaEAEAALRDLRRELR 422


                   ....*
gi 2462524677  304 RLESE 308
Cdd:COG4913    423 ELEAE 427
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 154-318 2.92e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 154 QRAVRTLWARLQRERpELLGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRrppsQNF 233
Cdd:COG1196   259 EAELAELEAELEELR-LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE----ELE 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 234 ARGERRSRLELELQSREQDLERAglrQRELEQ---QLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEAR 310
Cdd:COG1196   334 ELEEELEELEEELEEAEEELEEA---EAELAEaeeALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410


                  ....*...
gi 2462524677 311 GRQEQTQR 318
Cdd:COG1196   411 ALLERLER 418
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 108-306 3.03e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 108 RTPEETFESGGLDVQGTAGSLDEEEEEEERFHTVLEQLGVAPVLGKQRAVRTLWARLQRERPELLGSFEDVLIRASACLE 187
Cdd:COG1196   585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 188 EAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppsQNFARGERRSRLELELQSREQDLERAGLRQRELEQQL 267
Cdd:COG1196   665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE---EERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462524677 268 HAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE 306
Cdd:COG1196   742 LEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 186-321 3.27e-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: 3.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  186 LEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppsqNFARGERRSRLELELQSREQDLERAGLRQRELEQ 265
Cdd:TIGR02168  346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK----VAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462524677  266 QLHAQAAEHLEAQAQNSQ------------LWRAHEALRTQLEGAQEQIRRLESEARGRQEQTQRCRG 321
Cdd:TIGR02168  422 EIEELLKKLEEAELKELQaeleeleeeleeLQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
170-320 3.29e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 3.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  170 ELLGSFEDvLIRASACLEEAARERDGLEQAlrrreseherevRALYEETEQLREQsrrppsqnfargerrsRLELELQSR 249
Cdd:COG4913    229 ALVEHFDD-LERAHEALEDAREQIELLEPI------------RELAERYAAARER----------------LAELEYLRA 279

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462524677  250 EQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIR--------RLESEARGRQEQTQRCR 320
Cdd:COG4913    280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELEERE 358
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
186-315 3.32e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  186 LEEAARERDGLEQALRRRESEHEREVrALYEETEQLREQSRRPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQ 265
Cdd:COG4913    663 VASAEREIAELEAELERLDASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462524677  266 ----QLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQ 315
Cdd:COG4913    742 larlELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 152-310 7.88e-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: 7.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  152 GKQRAVRTLWARLQRERPELLGSFEDVLIRASAC---LEEAARERDGLEQALRRRESEHEREVRALyEETEQLREQSRRP 228
Cdd:TIGR02169  716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLeqeIENVKSELKELEARIEELEEDLHKLEEAL-NDLEARLSHSRIP 794

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677  229 PSQNFARG--ERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE 306
Cdd:TIGR02169  795 EIQAELSKleEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874


                   ....
gi 2462524677  307 SEAR 310
Cdd:TIGR02169  875 AALR 878
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 239-309 8.36e-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: 39.16  E-value: 8.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462524677 239 RSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQ-------AQNSQLWRAHEALRTQLEGAQEQIRRLESEA 309
Cdd:pfam07926   3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQqnyerelVLHAEDIKALQALREELNELKAEIAELKAEA 80
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
216-320 1.32e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 216 EETEQLREQSRRPPSQNfargERRSRLELELQSREQDLERAGLRQRELEQQLhaqaaEHLEAQAQNSQLWRAHEALRTQL 295
Cdd:COG4717    71 KELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREEL-----EKLEKLLQLLPLYQELEALEAEL 141

                          90       100
                  ....*....|....*....|....*
gi 2462524677 296 EGAQEQIRRLESEARGRQEQTQRCR 320
Cdd:COG4717   142 AELPERLEELEERLEELRELEEELE 166
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 35-92 3.09e-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: 3.09e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677   35 EELFLLCDKEAKGFITKHDLQG--LQSDLPltPEQLEAVFESLDRAHTGFLTAREFCLGL 92
Cdd:smart00027  13 EQIFRSLDKNQDGTVTGAQAKPilLKSGLP--QTLLAKIWNLADIDNDGELDKDEFALAM 70
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
163-323 6.89e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 6.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 163 RLQRERPELLGS--FEDVLIRA-SACLEEAARERDGLEQALRRRESEHErevrALYEETEQLREQSRRPPSQNFARGERR 239
Cdd:PRK02224  290 ELEEERDDLLAEagLDDADAEAvEARREELEDRDEELRDRLEECRVAAQ----AHNEEAESLREDADDLEERAEELREEA 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462524677 240 SRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE---SEARGRQEQT 316
Cdd:PRK02224  366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlRTARERVEEA 445


                  ....*..
gi 2462524677 317 QRCRGTG 323
Cdd:PRK02224  446 EALLEAG 452
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 247-301 9.09e-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: 37.63  E-value: 9.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462524677 247 QSREQDLERAgLRQRELEQQLH----AQAAEHLEAQAQNSQLWRAHEaLRTQLEGAQEQ 301
Cdd:pfam09728 148 ELRELHFEKL-LKTKELEVQLAeaklQQATEEEEKKAQEKEVAKARE-LKAQVQTLSET 204
PRK09039 PRK09039
peptidoglycan -binding protein;
239-317 9.49e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.02  E-value: 9.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462524677 239 RSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRrlESEARGRQEQTQ 317
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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