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Conserved domains on  [gi|320544532|ref|NP_001188690|]
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quick-to-court, isoform H [Drosophila melanogaster]

Protein Classification

AAA family ATPase( domain architecture ID 1003843)

AAA family ATPase containing an AAA (ATPases Associated with various cellular Activities) domain, may function as an ATP-dependent endonuclease or the ATPase component of an ABC-type transporter; similar to Bacillus subtilis protein YhaN

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  15037234|18208389|16828312|18466635|15037233

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
320-490 1.65e-06

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 320 ASNLENYELQRQELISmYEHRIEELIRSQDSATSDLKR-SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 398
Cdd:COG4717   84 EEKEEEYAELQEELEE-LEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 399 EDLQRKLIEHEEKQNKMYLHMYQQGQE--------AERISRADQALDLAQRQPES-KVSINELLHQLQSTQDELENI--- 466
Cdd:COG4717  163 EELEELEAELAELQEELEELLEQLSLAteeelqdlAEELEELQQRLAELEEELEEaQEELEELEEELEQLENELEAAale 242

                        170       180
                 ....*....|....*....|....*
gi 320544532 467 -RVRFFNIFLILFSVLFCVLHFVAS 490
Cdd:COG4717  243 eRLKEARLLLLIAAALLALLGLGGS 267
 
Name Accession Description Interval E-value
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
320-490 1.65e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 320 ASNLENYELQRQELISmYEHRIEELIRSQDSATSDLKR-SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 398
Cdd:COG4717   84 EEKEEEYAELQEELEE-LEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 399 EDLQRKLIEHEEKQNKMYLHMYQQGQE--------AERISRADQALDLAQRQPES-KVSINELLHQLQSTQDELENI--- 466
Cdd:COG4717  163 EELEELEAELAELQEELEELLEQLSLAteeelqdlAEELEELQQRLAELEEELEEaQEELEELEEELEQLENELEAAale 242

                        170       180
                 ....*....|....*....|....*
gi 320544532 467 -RVRFFNIFLILFSVLFCVLHFVAS 490
Cdd:COG4717  243 eRLKEARLLLLIAAALLALLGLGGS 267
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 162-483 1.05e-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: 48.13  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532   162 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 241
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532   242 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 311
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532   312 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 382
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532   383 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKMYLHMYQQGQEAERISRADQAL------------DLAQRQ---PESK 446
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaieeyeELKERYdflTAQK 1009

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 320544532   447 VSINELLHQLQSTQDEL-ENIRVRFFNIF-LI------LFSVLFC 483
Cdd:TIGR02168 1010 EDLTEAKETLEEAIEEIdREARERFKDTFdQVnenfqrVFPKLFG 1054
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 324-415 8.91e-05

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 42.79  E-value: 8.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532   324 ENYELQRqELISMYEHRIEELIRS-QDSATSDLKRSHNDKVEALLQKLA-ECNTRYSDMVPDYEQAKQRIRELEKQLEDL 401
Cdd:smart01071  49 KNLKYEL-IMNDHLNKRIDKLLKGlREEELSPETPTYNEMLAELQDQLKkELEEANGDSEGLLEELKKHRDKLKKEQKEL 127

                           90
                   ....*....|....
gi 320544532   402 QRKLIEHEEKQNKM 415
Cdd:smart01071 128 RKKLDELEKEEKKK 141
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 360-465 3.89e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 3.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 360 NDKVEALLQKLAECNTRYSDmvpDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISR--ADQAL- 436
Cdd:PRK00409 515 KEKLNELIASLEELERELEQ---KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKkeADEIIk 591

                         90       100
                 ....*....|....*....|....*....
gi 320544532 437 DLAQRQPESKVSINEllHQLQSTQDELEN 465
Cdd:PRK00409 592 ELRQLQKGGYASVKA--HELIEARKRLNK 618
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 358-470 6.68e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.98  E-value: 6.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532  358 SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEK-------QNKMYLHMYQQGQEAERIS 430
Cdd:pfam05622 301 SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKaedssllKQKLEEHLEKLHEAQSELQ 380

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 320544532  431 RADQALD-LAQRQPESK-VSINELLHQLQSTQDELENIRVRF 470
Cdd:pfam05622 381 KKKEQIEeLEPKQDSNLaQKIDELQEALRKKDEDMKAMEERY 422
 
Name Accession Description Interval E-value
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
320-490 1.65e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 320 ASNLENYELQRQELISmYEHRIEELIRSQDSATSDLKR-SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 398
Cdd:COG4717   84 EEKEEEYAELQEELEE-LEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 399 EDLQRKLIEHEEKQNKMYLHMYQQGQE--------AERISRADQALDLAQRQPES-KVSINELLHQLQSTQDELENI--- 466
Cdd:COG4717  163 EELEELEAELAELQEELEELLEQLSLAteeelqdlAEELEELQQRLAELEEELEEaQEELEELEEELEQLENELEAAale 242

                        170       180
                 ....*....|....*....|....*
gi 320544532 467 -RVRFFNIFLILFSVLFCVLHFVAS 490
Cdd:COG4717  243 eRLKEARLLLLIAAALLALLGLGGS 267
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 162-483 1.05e-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: 48.13  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532   162 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 241
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532   242 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 311
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532   312 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 382
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532   383 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKMYLHMYQQGQEAERISRADQAL------------DLAQRQ---PESK 446
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaieeyeELKERYdflTAQK 1009

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 320544532   447 VSINELLHQLQSTQDEL-ENIRVRFFNIF-LI------LFSVLFC 483
Cdd:TIGR02168 1010 EDLTEAKETLEEAIEEIdREARERFKDTFdQVnenfqrVFPKLFG 1054
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
321-470 3.01e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.55  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 321 SNLENYELQRQELISMYEhRIEELIRSQDSATSDLKRSHN-----DKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELE 395
Cdd:COG3206  226 SQLAEARAELAEAEARLA-ALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALR 304

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544532 396 KQLEDLQRKLIEHEEKQNKMylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRVRF 470
Cdd:COG3206  305 AQLQQEAQRILASLEAELEA-----LQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL 374
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
321-467 3.91e-05

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 45.67  E-value: 3.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 321 SNLENYELQRQELISMYEHRIEEL--IRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 398
Cdd:COG1340    8 SSLEELEEKIEELREEIEELKEKRdeLNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 399 EDLQRKLIEHEEKQNKM---------------YLHMYQQ----GQEAER-----ISRADQALDLAQRQPESKVSINELLH 454
Cdd:COG1340   88 NELREELDELRKELAELnkaggsidklrkeieRLEWRQQtevlSPEEEKelvekIKELEKELEKAKKALEKNEKLKELRA 167

                        170
                 ....*....|...
gi 320544532 455 QLQSTQDELENIR 467
Cdd:COG1340  168 ELKELRKEAEEIH 180
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 334-470 5.58e-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: 5.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532   334 ISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQN 413
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320544532   414 KMYLHMYQQGQEAERISR-----------ADQALDLAQRQ------PESKVSINELLHQLQSTQDELENIRVRF 470
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDrrerlqqeieeLLKKLEEAELKelqaelEELEEELEELQEELERLEEALEELREEL 470
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 329-467 8.79e-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: 8.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 329 QRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEA------LLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQ 402
Cdd:COG1196  285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELeeelaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544532 403 RKLIEHEEKqnkmylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIR 467
Cdd:COG1196  365 EALLEAEAE---------LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 324-415 8.91e-05

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 42.79  E-value: 8.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532   324 ENYELQRqELISMYEHRIEELIRS-QDSATSDLKRSHNDKVEALLQKLA-ECNTRYSDMVPDYEQAKQRIRELEKQLEDL 401
Cdd:smart01071  49 KNLKYEL-IMNDHLNKRIDKLLKGlREEELSPETPTYNEMLAELQDQLKkELEEANGDSEGLLEELKKHRDKLKKEQKEL 127

                           90
                   ....*....|....
gi 320544532   402 QRKLIEHEEKQNKM 415
Cdd:smart01071 128 RKKLDELEKEEKKK 141
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
338-474 1.39e-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: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532  338 EHRIEELIRSQDSATSDlkrshNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRkliehEEKQNKMYL 417
Cdd:COG4913   667 EREIAELEAELERLDAS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE-----ELDELQDRL 736

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 320544532  418 HMYQQGQEAERISRADQALD-LAQRQPESKVSiNELLHQLQSTQDELENIRVRFFNIF 474
Cdd:COG4913   737 EAAEDLARLELRALLEERFAaALGDAVERELR-ENLEERIDALRARLNRAEEELERAM 793
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 315-467 1.58e-04

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: 43.98  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 315 AGGDSASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYsdmvpdyEQAKQRIREL 394
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQEL-------AALEAELAEL 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320544532 395 EKQLEDLQRKLIEHEEKQNKMYLHMYQQGQ--EAERISRADQALDLAQRQPESKV---SINELLHQLQSTQDELENIR 467
Cdd:COG4942   89 EKEIAELRAELEAQKEELAELLRALYRLGRqpPLALLLSPEDFLDAVRRLQYLKYlapARREQAEELRADLAELAALR 166
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 360-465 3.89e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 3.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 360 NDKVEALLQKLAECNTRYSDmvpDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISR--ADQAL- 436
Cdd:PRK00409 515 KEKLNELIASLEELERELEQ---KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKkeADEIIk 591

                         90       100
                 ....*....|....*....|....*....
gi 320544532 437 DLAQRQPESKVSINEllHQLQSTQDELEN 465
Cdd:PRK00409 592 ELRQLQKGGYASVKA--HELIEARKRLNK 618
PRK05563 PRK05563
DNA polymerase III subunits gamma and tau; Validated
 319-467 5.37e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235505 [Multi-domain]  Cd Length: 559  Bit Score: 42.55  E-value: 5.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 319 SASNLENYELQRQEL-ISMYEHRIEELIRSQdsatSDLKRSHNDKV--EALLQKLAECNTRYSDMVPDYEQAKQRIRELE 395
Cdd:PRK05563 307 STENDELFKELSEKLdIERLYRMIDILNDAQ----QQIKWTNQPRIylEVALVKLCEQAAASPEYDTELEVLLQRVEQLE 382

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320544532 396 KQLEDLQrklieheekqnkmylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQL-QSTQDELENIR 467
Cdd:PRK05563 383 QELKQLK------------------AQPVGVAPEQKEKKKEKKKNKKKKYKVPRGKIYKVLkEATRQDLELLK 437
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 355-470 6.46e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 6.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 355 LKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQ-----NKMYLHMYQQ--GQEAE 427
Cdd:COG1579   25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYEALQKEieSLKRR 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 320544532 428 RISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRVRF 470
Cdd:COG1579  105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 358-470 6.68e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.98  E-value: 6.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532  358 SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEK-------QNKMYLHMYQQGQEAERIS 430
Cdd:pfam05622 301 SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKaedssllKQKLEEHLEKLHEAQSELQ 380

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 320544532  431 RADQALD-LAQRQPESK-VSINELLHQLQSTQDELENIRVRF 470
Cdd:pfam05622 381 KKKEQIEeLEPKQDSNLaQKIDELQEALRKKDEDMKAMEERY 422
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
338-473 1.22e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532  338 EHRIEELIRSQDSATSDLKRsHNDKVEALLQKLAECNTRYSDMVPDYEQAK-QRIRELEKQLEDLQRKLIEHEEKQNKMY 416
Cdd:COG4913   287 QRRLELLEAELEELRAELAR-LEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLE 365

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320544532  417 LHMYQQGQE--------AERISRADQALD--------LAQRQPESKVSINELLHQLQSTQDELENIRVRFFNI 473
Cdd:COG4913   366 ALLAALGLPlpasaeefAALRAEAAALLEaleeeleaLEEALAEAEAALRDLRRELRELEAEIASLERRKSNI 438
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 360-467 1.24e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 360 NDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQE-------------A 426
Cdd:COG3883   36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvllgsesfS 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 320544532 427 ERISRADQALDLAQRQpeskvsiNELLHQLQSTQDELENIR 467
Cdd:COG3883  116 DFLDRLSALSKIADAD-------ADLLEELKADKAELEAKK 149
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 318-464 2.33e-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: 40.82  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532   318 DSASNLENYELQRQELISMYEHRIEELirsqdsatsdlkrshNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQ 397
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKEIENL---------------NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320544532   398 LEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELE 464
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVE 964
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 323-465 3.97e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 39.84  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532  323 LENYELQRQELismYEHRIEELIRsqdsatsdlkrshndKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDL- 401
Cdd:pfam06160 323 LNENELERVRG---LEKQLEELEK---------------RYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFk 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532  402 -------------QRKLIE-----HE-----EKQN-----KMYLHMYQQGQeaERISRADQALDlaqrqpESKVSINELL 453
Cdd:pfam06160 385 eslqslrkdeleaREKLDEfklelREikrlvEKSNlpglpESYLDYFFDVS--DEIEDLADELN------EVPLNMDEVN 456

                         170
                  ....*....|..
gi 320544532  454 HQLQSTQDELEN 465
Cdd:pfam06160 457 RLLDEAQDDVDT 468
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
317-467 4.87e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 4.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 317 GDSASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEK 396
Cdd:COG4372    9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQL-REELEQAREELEQLEEELEQARSELEQLEEELEELNE 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320544532 397 QLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISRADQalDLAQRQPESKVSINELLHQLQSTQDELENIR 467
Cdd:COG4372   88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ--DLEQQRKQLEAQIAELQSEIAEREEELKELE 156
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
330-467 5.15e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 5.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532 330 RQELISMYEHRIEELIRSQDSATSdLKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHE 409
Cdd:COG4717   44 RAMLLERLEKEADELFKPQGRKPE-LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 320544532 410 EKQNkmYLHMYQQGQEAE-RISRADQALDLAQRQPEskvSINELLHQLQSTQDELENIR 467
Cdd:COG4717  123 KLLQ--LLPLYQELEALEaELAELPERLEELEERLE---ELRELEEELEELEAELAELQ 176
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 382-467 6.19e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.33  E-value: 6.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532   382 PDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQ-----QGQEAERISRADQALDLAQRQPESKvsiNELLHQL 456
Cdd:pfam15921   71 PGKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidlQTKLQEMQMERDAMADIRRRESQSQ---EDLRNQL 147

                           90
                   ....*....|.
gi 320544532   457 QSTQDELENIR 467
Cdd:pfam15921  148 QNTVHELEAAK 158
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
 393-466 7.72e-03

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.


Pssm-ID: 431235 [Multi-domain]  Cd Length: 185  Bit Score: 37.57  E-value: 7.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544532  393 ELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQE--AERISRADQALDLA-QRQP---ESKVSINELLHQLQSTQDELENI 466
Cdd:pfam10368  15 ELEKPFEEQQEPLVELEKKEQELYEEIIELGMDefDEIKKLSDEALENVeEREElleKEKESIEEAKEEFKKIKEIIEEI 94
 
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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