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Conserved domains on  [gi|530360374|ref|XP_005244833|]
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ski oncogene isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 250-421 1.17e-08

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.37  E-value: 1.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   250 LEAELEHLRQALEGG-LDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEI 328
Cdd:TIGR02168  218 LKAELRELELALLVLrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   329 ERLraenEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREARE 408
Cdd:TIGR02168  298 SRL----EQQKQILRERLANLERQLEELEAQLE-----ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368

                          170
                   ....*....|...
gi 530360374   409 HLEKVVKELQEQL 421
Cdd:TIGR02168  369 ELESRLEELEEQL 381
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
85-193 5.29e-03

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14951:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 618  Bit Score: 39.31  E-value: 5.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  85 RLSAFRPWSPAVSASEKELSPHLPAlirdsfysyksfeTAVAPNVALAPPAQQKVVSSPPCAAAVSRAPEPLATCTQPRK 164
Cdd:PRK14951 360 RLLAFKPAAAAEAAAPAEKKTPARP-------------EAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPV 426

                         90       100
                 ....*....|....*....|....*....
gi 530360374 165 RKLTVDTPGAPETLAPVAAPEEDKDSEAE 193
Cdd:PRK14951 427 AAPAAAAPAAAPAAAPAAVALAPAPPAQA 455
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 250-421 1.17e-08

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: 57.37  E-value: 1.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   250 LEAELEHLRQALEGG-LDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEI 328
Cdd:TIGR02168  218 LKAELRELELALLVLrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   329 ERLraenEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREARE 408
Cdd:TIGR02168  298 SRL----EQQKQILRERLANLERQLEELEAQLE-----ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368

                          170
                   ....*....|...
gi 530360374   409 HLEKVVKELQEQL 421
Cdd:TIGR02168  369 ELESRLEELEEQL 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 250-439 3.80e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 3.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 250 LEAELEHLRQALEGG-LDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEI 328
Cdd:COG1196  218 LKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 329 ERLRAENEKKMKEANESRLRLKRELEQARQARVCDKGCEAGRLRAKysAQIEDLQVKLQHAEADREQLRADLLREREARE 408
Cdd:COG1196  298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE--EELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190
                 ....*....|....*....|....*....|.
gi 530360374 409 HLEKVVKELQEQlwpRARPEAAGSEGAAELE 439
Cdd:COG1196  376 EAEEELEELAEE---LLEALRAAAELAAQLE 403
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
251-419 2.91e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 251 EAELEHLRQALEGGLDTKEAK-EKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRnLRKEIE 329
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEElAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK-LEEELD 629

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 330 RLRAENEKKMKEANESRLR---LKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA 406
Cdd:PRK03918 630 KAFEELAETEKRLEELRKEleeLEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709

                        170
                 ....*....|...
gi 530360374 407 REHLEKVVKELQE 419
Cdd:PRK03918 710 KKELEKLEKALER 722
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 322-420 5.08e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 37.96  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  322 RNLRKEIERLR---AENEKKMKEANESRLRLKRELEQARQarvcdkgceagrlrakysaQIEDLQVKLQHAEADREQLRA 398
Cdd:pfam13851  29 KSLKEEIAELKkkeERNEKLMSEIQQENKRLTEPLQKAQE-------------------EVEELRKQLENYEKDKQSLKN 89

                          90       100
                  ....*....|....*....|..
gi 530360374  399 dlLREReaREHLEKVVKELQEQ 420
Cdd:pfam13851  90 --LKAR--LKVLEKELKDLKWE 107
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 85-193 5.29e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 39.31  E-value: 5.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  85 RLSAFRPWSPAVSASEKELSPHLPAlirdsfysyksfeTAVAPNVALAPPAQQKVVSSPPCAAAVSRAPEPLATCTQPRK 164
Cdd:PRK14951 360 RLLAFKPAAAAEAAAPAEKKTPARP-------------EAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPV 426

                         90       100
                 ....*....|....*....|....*....
gi 530360374 165 RKLTVDTPGAPETLAPVAAPEEDKDSEAE 193
Cdd:PRK14951 427 AAPAAAAPAAAPAAAPAAVALAPAPPAQA 455
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
 255-317 8.98e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A1 (or endophilin-1) is also referred to as SH3P4 (SH3 domain containing protein 4) or SH3GL2 (SH3 domain containing Grb2-like protein 2). It is localized in presynaptic nerve terminals. It plays many roles in clathrin-dependent endocytosis of synaptic vesicles including early vesicle formation, ubiquitin-dependent sorting of plasma membrane proteins, and regulation of calcium influx into neurons. The BAR domain of endophilin-A1 forms crescent-shaped dimers that can detect membrane curvature and drive membrane bending, while its SH3 domain binds the endocytic proteins, dynamin 1, synaptojanin 1, and amphiphysins.


Pssm-ID: 153297  Cd Length: 223  Bit Score: 37.68  E-value: 8.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360374 255 EHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQE----LEFLRVAKKEKLREA 317
Cdd:cd07613  157 EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQatqiLQQVTVKLEDRIREA 223
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 250-421 1.17e-08

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: 57.37  E-value: 1.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   250 LEAELEHLRQALEGG-LDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEI 328
Cdd:TIGR02168  218 LKAELRELELALLVLrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   329 ERLraenEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREARE 408
Cdd:TIGR02168  298 SRL----EQQKQILRERLANLERQLEELEAQLE-----ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368

                          170
                   ....*....|...
gi 530360374   409 HLEKVVKELQEQL 421
Cdd:TIGR02168  369 ELESRLEELEEQL 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 250-439 3.80e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 3.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 250 LEAELEHLRQALEGG-LDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEI 328
Cdd:COG1196  218 LKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 329 ERLRAENEKKMKEANESRLRLKRELEQARQARVCDKGCEAGRLRAKysAQIEDLQVKLQHAEADREQLRADLLREREARE 408
Cdd:COG1196  298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE--EELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190
                 ....*....|....*....|....*....|.
gi 530360374 409 HLEKVVKELQEQlwpRARPEAAGSEGAAELE 439
Cdd:COG1196  376 EAEEELEELAEE---LLEALRAAAELAAQLE 403
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 250-421 8.99e-07

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: 51.60  E-value: 8.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   250 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKL-----------------SAALQAKRSLHQELEFLRVAKKE 312
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELaeleekleelkeeleslEAELEELEAELEELESRLEELEE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   313 KLREATEAKRNLRKEIERLRAE---NEKKMKEANESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHA 389
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459

                          170       180       190
                   ....*....|....*....|....*....|..
gi 530360374   390 EADREQLRADLLREREAREHLEKVVKELQEQL 421
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARL 491
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
253-422 6.43e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 6.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 253 ELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFL-----RVAKKEKLREATEAKRNLRKE 327
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqeLEALEAELAELPERLEELEER 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 328 IERLRaENEKKMKEANESRLRLKRELEQARQarvcdkgceagRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAR 407
Cdd:COG4717  155 LEELR-ELEEELEELEAELAELQEELEELLE-----------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222

                        170
                 ....*....|....*
gi 530360374 408 EHLEKVVKELQEQLW 422
Cdd:COG4717  223 EELEEELEQLENELE 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 285-421 7.09e-06

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: 48.51  E-value: 7.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   285 QEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRLRLKRELEQarqarvcdk 364
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE--------- 762

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530360374   365 gceagrlRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 421
Cdd:TIGR02168  763 -------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 250-421 1.28e-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: 47.74  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   250 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFL---RVAKKEKLREATEAKRNLRK 326
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELeaeIEELEERLEEAEEELAEAEA 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   327 EIERLRAENEKKMKEANESRLRLKRELEQARQARvcDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA 406
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860

                          170
                   ....*....|....*
gi 530360374   407 REHLEKVVKELQEQL 421
Cdd:TIGR02168  861 IEELEELIEELESEL 875
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
249-439 1.59e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  249 GLEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEI 328
Cdd:COG4913   239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  329 ERLRAE---NEKKMKEANESRL-RLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKlqhAEADREQLRADLLRER 404
Cdd:COG4913   319 DALREEldeLEAQIRGNGGDRLeQLEREIERLERELE-----ERERRRARLEALLAALGLP---LPASAEEFAALRAEAA 390

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 530360374  405 EAREHLEKVVKELQEQLWPRARPEAAGSEGAAELE 439
Cdd:COG4913   391 ALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
251-419 2.91e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 251 EAELEHLRQALEGGLDTKEAK-EKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRnLRKEIE 329
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEElAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK-LEEELD 629

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 330 RLRAENEKKMKEANESRLR---LKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA 406
Cdd:PRK03918 630 KAFEELAETEKRLEELRKEleeLEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709

                        170
                 ....*....|...
gi 530360374 407 REHLEKVVKELQE 419
Cdd:PRK03918 710 KKELEKLEKALER 722
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 250-440 5.43e-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: 5.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   250 LEAELEHLRQALEGGLDTKEAKEKFLHEVvKMRVKQeekLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIE 329
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDEL-RAELTL---LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   330 RLRAENEKKMKEANESRLRLKRELEQARQARVCDKgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREH 409
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLNERASLEEALA--LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933

                          170       180       190
                   ....*....|....*....|....*....|.
gi 530360374   410 LEKVVKELQEQLWPRARPEAagsEGAAELEP 440
Cdd:TIGR02168  934 LEVRIDNLQERLSEEYSLTL---EEAEALEN 961
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 250-439 6.67e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 6.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 250 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRvakkEKLREATEAKRNLRKEIE 329
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE----AELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 330 RLRAENEKKMKEA--------------------NESRLRLKRELEQARQARVcdkgceagrlrAKYSAQIEDLQVKLQHA 389
Cdd:COG4942  101 AQKEELAELLRALyrlgrqpplalllspedfldAVRRLQYLKYLAPARREQA-----------EELRADLAELAALRAEL 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 530360374 390 EADREQLRADLLREREAREHLEKVVKELQEQLWPRARPEAAGSEGAAELE 439
Cdd:COG4942  170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 284-421 6.85e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 6.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 284 KQEEKLSA-ALQAKR--SLHQELEFLRV-AKKEKLREATEAKRNLRKEIERLRAENEKKMK-----EANESRLRLKRELE 354
Cdd:COG1196  200 RQLEPLERqAEKAERyrELKEELKELEAeLLLLKLRELEAELEELEAELEELEAELEELEAelaelEAELEELRLELEEL 279

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360374 355 QARQArvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 421
Cdd:COG1196  280 ELELE-------EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
268-419 8.03e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.85  E-value: 8.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 268 KEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAK-----RNLRKEIERLRAEN---EKKM 339
Cdd:COG2433  357 KKVPPDVDRDEVKARVIRGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEeeeeiRRLEEQVERLEAEVeelEAEL 436

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 340 KEANESRLRLKRELEQARQARvcdkgceagRLRAKYSAQIEDLQVKLqhaeadrEQLRADLLREREAREHLEKVVKELQE 419
Cdd:COG2433  437 EEKDERIERLERELSEARSEE---------RREIRKDREISRLDREI-------ERLERELEEERERIEELKRKLERLKE 500
PTZ00121 PTZ00121
MAEBL; Provisional
 186-415 1.38e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  186 EDKDSEAEVEVESREECTFTSSLSSLSSPSFTSSSSAKDLGSPGARALPSAVPDAAAPADAPSGLEAELEHLRQALEGGL 265
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  266 DTKEAKEKflHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAK--KEKLREATEAKRNLRKEIERLRAENEKKMKEAN 343
Cdd:PTZ00121 1392 KADEAKKK--AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADeaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530360374  344 ESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVK 415
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK 1541
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 288-421 1.39e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.99  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 288 KLSAALQAKRSLHQELEFLRvAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRLRLKRELEQARQARvcdkgce 367
Cdd:COG1579   18 ELDRLEHRLKELPAELAELE-DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK------- 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530360374 368 agrlrakysaQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 421
Cdd:COG1579   90 ----------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL 133
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
259-421 1.49e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 259 QALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKK--EKLREATEAKRNLRKEIERLRA--E 334
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEEleE 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 335 NEKKMKEANESRLRLKRELEQARQARVcdkgceagRLRAKYSAQIEDlqvKLQHAEADREQLRADLLREREAREHLEKVV 414
Cdd:COG4717  154 RLEELRELEEELEELEAELAELQEELE--------ELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEEL 222


                 ....*..
gi 530360374 415 KELQEQL 421
Cdd:COG4717  223 EELEEEL 229
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
282-408 1.68e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 43.71  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 282 RVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRlRLKRELEQARQARV 361
Cdd:COG2268  213 EIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAER-EVQRQLEIAERERE 291

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530360374 362 CD-KGCEAGRLRAKYSAQIE-----DLQVKLQHAEADREQLRADLLREREARE 408
Cdd:COG2268  292 IElQEKEAEREEAELEADVRkpaeaEKQAAEAEAEAEAEAIRAKGLAEAEGKR 344
PTZ00121 PTZ00121
MAEBL; Provisional
 250-433 3.03e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  250 LEAELEHLRQALEGGLDTKEAKEKflheVVKMRVKQEEKLSAALQAKRSLHQELEFLRVA----KKEKLREATEAKR--- 322
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKK----ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAeeakKADEAKKAEEKKKade 1550

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  323 -----NLRKEIERLRAENEKKMKEANESRLRLKRELEQARQAR---VCDKGCEAGRLRAKYSAQIEDLQVK---LQHAEA 391
Cdd:PTZ00121 1551 lkkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieeVMKLYEEEKKMKAEEAKKAEEAKIKaeeLKKAEE 1630

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 530360374  392 DREQLRADLLREREAREHLEKVVKElQEQLWPRARPEAAGSE 433
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAE 1671
PRK12704 PRK12704
phosphodiesterase; Provisional
 309-420 3.28e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 3.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 309 AKKEKLREATEAKRNLRKEIERLRAENEKKMKEAN------ESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDL 382
Cdd:PRK12704  47 AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRnelqklEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQEL 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 530360374 383 QVKLQHAEADREQLRADLLR-----EREAREH-LEKVVKELQEQ 420
Cdd:PRK12704 127 EKKEEELEELIEEQLQELERisgltAEEAKEIlLEKVEEEARHE 170
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
250-418 5.12e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 5.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 250 LEAELEHLRQALEGGLDTKEAKEKF--LHEVVKMRVKQEEKLSAAL--QAKRSLHQELEFLRVAKKE---KLREATEAKR 322
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERheLYEEAKAKKEELERLKKRLtgLTPEKLEKELEELEKAKEEieeEISKITARIG 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 323 NLRKEIERLRaENEKKMKEANESRLRLKRELEQArqarvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLR 402
Cdd:PRK03918 416 ELKKEIKELK-KAIEELKKAKGKCPVCGRELTEE----------HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484

                        170
                 ....*....|....*.
gi 530360374 403 EREAREHLEKVVKELQ 418
Cdd:PRK03918 485 LEKVLKKESELIKLKE 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 250-410 8.41e-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: 41.97  E-value: 8.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   250 LEAELEHLRQALEgglDTKEAKEKFLHEVVKMRVkQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIE 329
Cdd:TIGR02168  836 TERRLEDLEEQIE---ELSEDIESLAAEIEELEE-LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   330 RLRAENEKKMKEANESRLRLKR-ELEQARQarvcdkgceAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREARE 408
Cdd:TIGR02168  912 ELRRELEELREKLAQLELRLEGlEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982


                   ..
gi 530360374   409 HL 410
Cdd:TIGR02168  983 EL 984
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 301-434 1.06e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 301 QELEFLRVAKKEKLREATEakrnLRKEIERLRAENEKKMKEANESRLRLKRELEQARQARVcdkgCEAGRLRAKYSAQIE 380
Cdd:PRK00409 523 ASLEELERELEQKAEEAEA----LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAI----KEAKKEADEIIKELR 594

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530360374 381 DLQvKLQHAEADREQLradllreREAREHLEKVVKELQEQLWPRARPEAAGSEG 434
Cdd:PRK00409 595 QLQ-KGGYASVKAHEL-------IEARKRLNKANEKKEKKKKKQKEKQEELKVG 640
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
250-421 1.36e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  250 LEAELEHLRQALEGgLDTKEA---KEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEkLREATEAKRNLRK 326
Cdd:COG4913   622 LEEELAEAEERLEA-LEAELDalqERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD-LAALEEQLEELEA 699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  327 EIERLRAEnekkMKEANESRLRLKRELEQARQarvcdkgceagrlrakysaQIEDLQVKLQHAEADREQLRADLLREREA 406
Cdd:COG4913   700 ELEELEEE----LDELKGEIGRLEKELEQAEE-------------------ELDELQDRLEAAEDLARLELRALLEERFA 756

                         170
                  ....*....|....*
gi 530360374  407 REHLEKVVKELQEQL 421
Cdd:COG4913   757 AALGDAVERELRENL 771
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
252-421 1.73e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 252 AELEHLRQALEGGLDTKEAKekflHEVVKMRVKQEEKLSAaLQAKRSLHQELeflRVAKKEKLREATEAKRNLRKEIERL 331
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEER----LERAEDLVEAEDRIER-LEERREDLEEL---IAERRETIEEKRERAEELRERAAEL 549

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 332 RAENEKKMKEANESRlrlkrelEQARQARVCDKGCEagRLRAKYSAQIEDLQvKLQHAEADREQLRADLLREREAREHLE 411
Cdd:PRK02224 550 EAEAEEKREAAAEAE-------EEAEEAREEVAELN--SKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALA 619

                        170
                 ....*....|
gi 530360374 412 KVVKELQEQL 421
Cdd:PRK02224 620 ELNDERRERL 629
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
276-439 2.76e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 276 HEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLR-----AENEKKMKEANESRLRLK 350
Cdd:COG4717   66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqlLPLYQELEALEAELAELP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 351 RELEQARQARvcdkgceagrlrakysAQIEDLQVKLQHAEADREQLRADLLRERE-----AREHLEKVVKELQEQLWPRA 425
Cdd:COG4717  146 ERLEELEERL----------------EELRELEEELEELEAELAELQEELEELLEqlslaTEEELQDLAEELEELQQRLA 209

                        170
                 ....*....|....
gi 530360374 426 RPEAAGSEGAAELE 439
Cdd:COG4717  210 ELEEELEEAQEELE 223
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 249-421 4.16e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   249 GLEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAK-RSLHQELEFLRVAKKEKLREATEAKRNLRK- 326
Cdd:TIGR02169  248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKl 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374   327 --EIERLRAENEKkmkeanesrlrLKRELEQaRQARVCDKGCEAGRLRAKYsaqiEDLQVKLQHAEADREQLRADLLRER 404
Cdd:TIGR02169  328 eaEIDKLLAEIEE-----------LEREIEE-ERKRRDKLTEEYAELKEEL----EDLRAELEEVDKEFAETRDELKDYR 391

                          170
                   ....*....|....*..
gi 530360374   405 EAREHLEKVVKELQEQL 421
Cdd:TIGR02169  392 EKLEKLKREINELKREL 408
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 322-420 5.08e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 37.96  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  322 RNLRKEIERLR---AENEKKMKEANESRLRLKRELEQARQarvcdkgceagrlrakysaQIEDLQVKLQHAEADREQLRA 398
Cdd:pfam13851  29 KSLKEEIAELKkkeERNEKLMSEIQQENKRLTEPLQKAQE-------------------EVEELRKQLENYEKDKQSLKN 89

                          90       100
                  ....*....|....*....|..
gi 530360374  399 dlLREReaREHLEKVVKELQEQ 420
Cdd:pfam13851  90 --LKAR--LKVLEKELKDLKWE 107
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 85-193 5.29e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 39.31  E-value: 5.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  85 RLSAFRPWSPAVSASEKELSPHLPAlirdsfysyksfeTAVAPNVALAPPAQQKVVSSPPCAAAVSRAPEPLATCTQPRK 164
Cdd:PRK14951 360 RLLAFKPAAAAEAAAPAEKKTPARP-------------EAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPV 426

                         90       100
                 ....*....|....*....|....*....
gi 530360374 165 RKLTVDTPGAPETLAPVAAPEEDKDSEAE 193
Cdd:PRK14951 427 AAPAAAAPAAAPAAAPAAVALAPAPPAQA 455
PRK11020 PRK11020
YibL family ribosome-associated protein;
281-359 7.68e-03

YibL family ribosome-associated protein;


Pssm-ID: 182904 [Multi-domain]  Cd Length: 118  Bit Score: 36.15  E-value: 7.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 281 MRVKQE-EKLSAALQAKRslHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKM-KEANE-SRLRLKRELEQAR 357
Cdd:PRK11020   1 MVEKNEiKRLSDRLDAIR--HKLAAASLRGDAEKYAQFEKEKATLEAEIARLKEVQSQKLsKEAQKlMKLPFSRAITKKE 78


                 ..
gi 530360374 358 QA 359
Cdd:PRK11020  79 QA 80
PTZ00121 PTZ00121
MAEBL; Provisional
 255-406 7.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  255 EHLRQALEGGLDTKEAKEKFLHEVVK---MRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERL 331
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360374  332 RAENEKKMKEANESRLRLKRELEQARQARV--CDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA 406
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAeeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
PTZ00121 PTZ00121
MAEBL; Provisional
 253-420 7.76e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 7.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  253 ELEHLRQALEGGLDTKEAKEKFLHEVvkMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRN-----LRKE 327
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEV--MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKkeaeeKKKA 1649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374  328 IERLRAENEKKMKEANESRL--RLKRELEQARQARVCD-KGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADllrER 404
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKaeEDKKKAEEAKKAEEDEkKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA---EE 1726

                         170
                  ....*....|....*.
gi 530360374  405 EAREHLEKVVKELQEQ 420
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEED 1742
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 284-421 8.08e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.60  E-value: 8.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 284 KQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRA---ENEKKMKEANESR--LRLKRELEQARQ 358
Cdd:COG1579   24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikKYEEQLGNVRNNKeyEALQKEIESLKR 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530360374 359 ARvcdKGCEAGRLRAKysAQIEDLQVKLQHAEADREQLRADLlreREAREHLEKVVKELQEQL 421
Cdd:COG1579  104 RI---SDLEDEILELM--ERIEELEEELAELEAELAELEAEL---EEKKAELDEELAELEAEL 158
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 250-438 8.92e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 8.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 250 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEflrvAKKEKLREATEAKRNLRKEIE 329
Cdd:COG1196  377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA----ELEEEEEEEEEALEEAAEEEA 452

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 330 RLRAENEkkmkEANESRLRLKRELEQARQArvcdkgceagRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREH 409
Cdd:COG1196  453 ELEEEEE----ALLELLAELLEEAALLEAA----------LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518

                        170       180
                 ....*....|....*....|....*....
gi 530360374 410 LEKVVKELQEQLWPRARPEAAGSEGAAEL 438
Cdd:COG1196  519 LRGLAGAVAVLIGVEAAYEAALEAALAAA 547
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
 255-317 8.98e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A1 (or endophilin-1) is also referred to as SH3P4 (SH3 domain containing protein 4) or SH3GL2 (SH3 domain containing Grb2-like protein 2). It is localized in presynaptic nerve terminals. It plays many roles in clathrin-dependent endocytosis of synaptic vesicles including early vesicle formation, ubiquitin-dependent sorting of plasma membrane proteins, and regulation of calcium influx into neurons. The BAR domain of endophilin-A1 forms crescent-shaped dimers that can detect membrane curvature and drive membrane bending, while its SH3 domain binds the endocytic proteins, dynamin 1, synaptojanin 1, and amphiphysins.


Pssm-ID: 153297  Cd Length: 223  Bit Score: 37.68  E-value: 8.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360374 255 EHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQE----LEFLRVAKKEKLREA 317
Cdd:cd07613  157 EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQatqiLQQVTVKLEDRIREA 223
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 250-421 9.59e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.60  E-value: 9.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 250 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRvAKKEKLREATEAKRNLR---- 325
Cdd:COG1579   15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-ARIKKYEEQLGNVRNNKeyea 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360374 326 --KEIERLRAEN---EKKMKEANESRLRLKRELEQARqarvcdkgceagrlrakysAQIEDLQVKLQHAEADREQLRADL 400
Cdd:COG1579   94 lqKEIESLKRRIsdlEDEILELMERIEELEEELAELE-------------------AELAELEAELEEKKAELDEELAEL 154

                        170       180
                 ....*....|....*....|..
gi 530360374 401 LREREA-REHLEKVVKELQEQL 421
Cdd:COG1579  155 EAELEElEAEREELAAKIPPEL 176
 
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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