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Conserved domains on  [gi|1635401214|ref|WP_137119166|]
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hypothetical protein [Azospirillum argentinense]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CALCOCO1 super family cl37761
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
194-446 2.30e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


The actual alignment was detected with superfamily member pfam07888:

Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 44.12  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214 194 ETRGWDGALKKLEGERTELKGRWAEVSGE-AFGDQKIQDW--KPTGWTPDLAEVSADglQAIVTAANAALET-------- 262
Cdd:pfam07888  60 EKERYKRDREQWERQRRELESRVAELKEElRQSREKHEELeeKYKELSASSEELSEE--KDALLAQRAAHEArireleed 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214 263 --VVAEQAVD-QSELDRLRVDAGKLDALKEVEQaASKKKLDAEVAVVDAENAHRAAEQAVANLPPAEQDSglscphcqgk 339
Cdd:pfam07888 138 ikTLTQRVLErETELERMKERAKKAGAQRKEEE-AERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT---------- 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214 340 vhyhkgqdgerldKAERLSDDVLK-QRRLDritvegTFNRAKTALSAARTDLQSAQRALDDAQRAVAGAESakrkltDLE 418
Cdd:pfam07888 207 -------------QVLQLQDTITTlTQKLT------TAHRKEAENEALLEELRSLQERLNASERKVEGLGE------ELS 261
                         250       260
                  ....*....|....*....|....*...
gi 1635401214 419 VQSAGKSGSAEAVQKARDAAAVAQLRLS 446
Cdd:pfam07888 262 SMAAQRDRTQAELHQARLQAAQLTLQLA 289
SbcC super family cl33865
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
6-75 4.57e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG0419:

Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 41.92  E-value: 4.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214   6 NVRAFQilERADITFGEGVTLIAAENSHGKSSVAKAIAGAMAGDplHGYLKKDVKALVKDGAKSGSVMVT 75
Cdd:COG0419     9 NFRSYR--DTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGK--ARSRSKLRSDLINVGSEEASVELE 74
 
Name Accession Description Interval E-value
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
194-446 2.30e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 44.12  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214 194 ETRGWDGALKKLEGERTELKGRWAEVSGE-AFGDQKIQDW--KPTGWTPDLAEVSADglQAIVTAANAALET-------- 262
Cdd:pfam07888  60 EKERYKRDREQWERQRRELESRVAELKEElRQSREKHEELeeKYKELSASSEELSEE--KDALLAQRAAHEArireleed 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214 263 --VVAEQAVD-QSELDRLRVDAGKLDALKEVEQaASKKKLDAEVAVVDAENAHRAAEQAVANLPPAEQDSglscphcqgk 339
Cdd:pfam07888 138 ikTLTQRVLErETELERMKERAKKAGAQRKEEE-AERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT---------- 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214 340 vhyhkgqdgerldKAERLSDDVLK-QRRLDritvegTFNRAKTALSAARTDLQSAQRALDDAQRAVAGAESakrkltDLE 418
Cdd:pfam07888 207 -------------QVLQLQDTITTlTQKLT------TAHRKEAENEALLEELRSLQERLNASERKVEGLGE------ELS 261
                         250       260
                  ....*....|....*....|....*...
gi 1635401214 419 VQSAGKSGSAEAVQKARDAAAVAQLRLS 446
Cdd:pfam07888 262 SMAAQRDRTQAELHQARLQAAQLTLQLA 289
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
240-460 3.08e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214 240 DLAEVSADGLQAIVTAANAALETVVAEQAVDQSELDRLRVDAGKLDALKEVEQA------ASKKKLDAEVAVVDAENAHR 313
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyellAELARLEQDIARLEERRREL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214 314 AAEQAVANlppAEQDSglscphcQGKVHYHKGQDGERLDKAERLSDDVLKQRRLDRITVEGTFNRAKTALSAARTDLQSA 393
Cdd:COG1196   315 EERLEELE---EELAE-------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1635401214 394 QRALDDAQRAVAGAESAKRKLTDLEVQSAGKSGSAEAVQKARDAAAVAQLRLSLFQTKARADALARQ 460
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
6-75 4.57e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 41.92  E-value: 4.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214   6 NVRAFQilERADITFGEGVTLIAAENSHGKSSVAKAIAGAMAGDplHGYLKKDVKALVKDGAKSGSVMVT 75
Cdd:COG0419     9 NFRSYR--DTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGK--ARSRSKLRSDLINVGSEEASVELE 74
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
6-72 1.69e-03

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 40.28  E-value: 1.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1635401214   6 NVRAFQilERADITFGEGVTLIAAENSHGKSSVAKAIAGAMAGD-PLHGYLKKDVKALVKDGAKSGSV 72
Cdd:cd03240     8 NIRSFH--ERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGElPPNSKGGAHDPKLIREGEVRAQV 73
AAA_23 pfam13476
AAA domain;
6-50 2.40e-03

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 39.40  E-value: 2.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1635401214   6 NVRAFqilERADITFGEGVTLIAAENSHGKSSVAKAIAGAMAGDP 50
Cdd:pfam13476   5 NFRSF---RDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKT 46
PRK01156 PRK01156
chromosome segregation protein; Provisional
7-74 4.01e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 4.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1635401214   7 VRAFQILERADITFGEGVTLIAAENSHGKSSVAKAIAGAMAGDPlhgyLKKDVKALVKDGAKSGSVMV 74
Cdd:PRK01156    8 LKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMIKKGKNNLEVEL 71
 
Name Accession Description Interval E-value
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
194-446 2.30e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 44.12  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214 194 ETRGWDGALKKLEGERTELKGRWAEVSGE-AFGDQKIQDW--KPTGWTPDLAEVSADglQAIVTAANAALET-------- 262
Cdd:pfam07888  60 EKERYKRDREQWERQRRELESRVAELKEElRQSREKHEELeeKYKELSASSEELSEE--KDALLAQRAAHEArireleed 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214 263 --VVAEQAVD-QSELDRLRVDAGKLDALKEVEQaASKKKLDAEVAVVDAENAHRAAEQAVANLPPAEQDSglscphcqgk 339
Cdd:pfam07888 138 ikTLTQRVLErETELERMKERAKKAGAQRKEEE-AERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT---------- 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214 340 vhyhkgqdgerldKAERLSDDVLK-QRRLDritvegTFNRAKTALSAARTDLQSAQRALDDAQRAVAGAESakrkltDLE 418
Cdd:pfam07888 207 -------------QVLQLQDTITTlTQKLT------TAHRKEAENEALLEELRSLQERLNASERKVEGLGE------ELS 261
                         250       260
                  ....*....|....*....|....*...
gi 1635401214 419 VQSAGKSGSAEAVQKARDAAAVAQLRLS 446
Cdd:pfam07888 262 SMAAQRDRTQAELHQARLQAAQLTLQLA 289
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
240-460 3.08e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214 240 DLAEVSADGLQAIVTAANAALETVVAEQAVDQSELDRLRVDAGKLDALKEVEQA------ASKKKLDAEVAVVDAENAHR 313
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyellAELARLEQDIARLEERRREL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214 314 AAEQAVANlppAEQDSglscphcQGKVHYHKGQDGERLDKAERLSDDVLKQRRLDRITVEGTFNRAKTALSAARTDLQSA 393
Cdd:COG1196   315 EERLEELE---EELAE-------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1635401214 394 QRALDDAQRAVAGAESAKRKLTDLEVQSAGKSGSAEAVQKARDAAAVAQLRLSLFQTKARADALARQ 460
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
6-75 4.57e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 41.92  E-value: 4.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214   6 NVRAFQilERADITFGEGVTLIAAENSHGKSSVAKAIAGAMAGDplHGYLKKDVKALVKDGAKSGSVMVT 75
Cdd:COG0419     9 NFRSYR--DTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGK--ARSRSKLRSDLINVGSEEASVELE 74
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
6-72 1.69e-03

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 40.28  E-value: 1.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1635401214   6 NVRAFQilERADITFGEGVTLIAAENSHGKSSVAKAIAGAMAGD-PLHGYLKKDVKALVKDGAKSGSV 72
Cdd:cd03240     8 NIRSFH--ERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGElPPNSKGGAHDPKLIREGEVRAQV 73
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
20-75 1.79e-03

ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213244 [Multi-domain]  Cd Length: 213  Bit Score: 40.27  E-value: 1.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1635401214  20 FGEGVTLIAAENSHGKSSVAKAIAGAMAGDPLHGYLKKDVKALVKDGAKSGSVMVT 75
Cdd:cd03277    21 PGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIE 76
AAA_23 pfam13476
AAA domain;
6-50 2.40e-03

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 39.40  E-value: 2.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1635401214   6 NVRAFqilERADITFGEGVTLIAAENSHGKSSVAKAIAGAMAGDP 50
Cdd:pfam13476   5 NFRSF---RDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKT 46
PRK01156 PRK01156
chromosome segregation protein; Provisional
7-74 4.01e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 4.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1635401214   7 VRAFQILERADITFGEGVTLIAAENSHGKSSVAKAIAGAMAGDPlhgyLKKDVKALVKDGAKSGSVMV 74
Cdd:PRK01156    8 LKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMIKKGKNNLEVEL 71
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
249-464 9.74e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 9.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214  249 LQAIVtAANAALETVVAEQAVDQSELDRLRVDAG--KLDALKEVEQAASKKKLDAEVAVVDAENAHRAAEQAVANLppaE 326
Cdd:COG4913    254 LEPIR-ELAERYAAARERLAELEYLRAALRLWFAqrRLELLEAELEELRAELARLEAELERLEARLDALREELDEL---E 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635401214  327 QDsglscphcqgkvhyHKGQDGERLDKAERLSDDV---LKQRRLDRITVEGTFNRAKTALSAARTDLQSAQRALDDAQRA 403
Cdd:COG4913    330 AQ--------------IRGNGGDRLEQLEREIERLereLEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1635401214  404 VAGAEsakrkltdlevqsagksgsaEAVQKARDAAAVAQLRLslfqtKARADALARQITSM 464
Cdd:COG4913    396 LEEEL--------------------EALEEALAEAEAALRDL-----RRELRELEAEIASL 431
 
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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