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Conserved domains on  [gi|442626127|ref|NP_723058|]
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quick-to-court, isoform J [Drosophila melanogaster]

Protein Classification

GRIP domain-containing protein( domain architecture ID 10477838)

GRIP domain-containing protein

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];
352-500 4.17e-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: 49.77  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 352 ASNLENYELQRQELISmYEHRIEELIRSQDSATSDLKR-SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 430
Cdd:COG4717   84 EEKEEEYAELQEELEE-LEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626127 431 EDLQRKLIEHEEKQNKMYLHMYQQGQEAE-RISRADQALDLAQRQpeskvsINELLHQLQSTQDELENIRA 500
Cdd:COG4717  163 EELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQR------LAELEEELEEAQEELEELEE 227
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
549-590 1.16e-05

GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.


:

Pssm-ID: 460221 [Multi-domain]  Cd Length: 44  Bit Score: 42.73  E-value: 1.16e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 442626127  549 EVTLQFLKSAIFYFLTDKENS-QGHL-QAIESILEFTDAEKQKI 590
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSeRKQLlPVIATLLKFSPEEEQKI 44
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
194-469 2.19e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   194 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 273
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   274 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 343
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   344 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 414
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 442626127   415 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKmyLHMYQQGQEaERISRADQALD 469
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLsEEYSLTLEEAEALENK--IEDDEEEAR-RRLKRLENKIK 982
 
Name Accession Description Interval E-value
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
352-500 4.17e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 352 ASNLENYELQRQELISmYEHRIEELIRSQDSATSDLKR-SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 430
Cdd:COG4717   84 EEKEEEYAELQEELEE-LEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626127 431 EDLQRKLIEHEEKQNKMYLHMYQQGQEAE-RISRADQALDLAQRQpeskvsINELLHQLQSTQDELENIRA 500
Cdd:COG4717  163 EELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQR------LAELEEELEEAQEELEELEE 227
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
549-590 1.16e-05

GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.


Pssm-ID: 460221 [Multi-domain]  Cd Length: 44  Bit Score: 42.73  E-value: 1.16e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 442626127  549 EVTLQFLKSAIFYFLTDKENS-QGHL-QAIESILEFTDAEKQKI 590
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSeRKQLlPVIATLLKFSPEEEQKI 44
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
366-544 1.99e-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: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   366 ISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQN 445
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   446 KMYLHMYQQGQEAERISRADQALDLAQRQPESKVS-------------INELLHQLQSTQDELENiRASECRMRECGSNH 512
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkelqaeleeLEEELEELQEELERLEE-ALEELREELEEAEQ 475
                          170       180       190
                   ....*....|....*....|....*....|..
gi 442626127   513 ALLTAKEaiSLWVLGARKTIYRRLLEAQKNRT 544
Cdd:TIGR02168  476 ALDAAER--ELAQLQARLDSLERLQENLEGFS 505
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
356-447 1.91e-04

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: 42.02  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   356 ENYELQRqELISMYEHRIEELIRS-QDSATSDLKRSHNDKVEALLQKLA-ECNTRYSDMVPDYEQAKQRIRELEKQLEDL 433
Cdd:smart01071  49 KNLKYEL-IMNDHLNKRIDKLLKGlREEELSPETPTYNEMLAELQDQLKkELEEANGDSEGLLEELKKHRDKLKKEQKEL 127
                           90
                   ....*....|....
gi 442626127   434 QRKLIEHEEKQNKM 447
Cdd:smart01071 128 RKKLDELEKEEKKK 141
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
194-469 2.19e-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: 44.66  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   194 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 273
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   274 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 343
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   344 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 414
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 442626127   415 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKmyLHMYQQGQEaERISRADQALD 469
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLsEEYSLTLEEAEALENK--IEDDEEEAR-RRLKRLENKIK 982
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
390-508 3.60e-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: 43.52  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127  390 SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEK-------QNKMYLHMYQQGQEAERIS 462
Cdd:pfam05622 301 SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKaedssllKQKLEEHLEKLHEAQSELQ 380
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 442626127  463 RADQALD-LAQRQPESK-VSINELLHQLQSTQDELeniRASECRMREC 508
Cdd:pfam05622 381 KKKEQIEeLEPKQDSNLaQKIDELQEALRKKDEDM---KAMEERYKKY 425
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
392-497 8.66e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 8.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 392 NDKVEALLQKLAECNTRYSDmvpDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISR--ADQAL- 468
Cdd:PRK00409 515 KEKLNELIASLEELERELEQ---KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKkeADEIIk 591
                         90       100
                 ....*....|....*....|....*....
gi 442626127 469 DLAQRQPESKVSINEllHQLQSTQDELEN 497
Cdd:PRK00409 592 ELRQLQKGGYASVKA--HELIEARKRLNK 618
 
Name Accession Description Interval E-value
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
352-500 4.17e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 352 ASNLENYELQRQELISmYEHRIEELIRSQDSATSDLKR-SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 430
Cdd:COG4717   84 EEKEEEYAELQEELEE-LEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626127 431 EDLQRKLIEHEEKQNKMYLHMYQQGQEAE-RISRADQALDLAQRQpeskvsINELLHQLQSTQDELENIRA 500
Cdd:COG4717  163 EELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQR------LAELEEELEEAQEELEELEE 227
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
549-590 1.16e-05

GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.


Pssm-ID: 460221 [Multi-domain]  Cd Length: 44  Bit Score: 42.73  E-value: 1.16e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 442626127  549 EVTLQFLKSAIFYFLTDKENS-QGHL-QAIESILEFTDAEKQKI 590
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSeRKQLlPVIATLLKFSPEEEQKI 44
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
366-544 1.99e-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: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   366 ISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQN 445
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   446 KMYLHMYQQGQEAERISRADQALDLAQRQPESKVS-------------INELLHQLQSTQDELENiRASECRMRECGSNH 512
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkelqaeleeLEEELEELQEELERLEE-ALEELREELEEAEQ 475
                          170       180       190
                   ....*....|....*....|....*....|..
gi 442626127   513 ALLTAKEaiSLWVLGARKTIYRRLLEAQKNRT 544
Cdd:TIGR02168  476 ALDAAER--ELAQLQARLDSLERLQENLEGFS 505
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
353-500 6.08e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 6.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 353 SNLENYELQRQELISMYEhRIEELIRSQDSATSDLKRSHN-----DKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELE 427
Cdd:COG3206  226 SQLAEARAELAEAEARLA-ALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALR 304
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626127 428 KQLEDLQRKLIEHEEKQNKMylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRA 500
Cdd:COG3206  305 AQLQQEAQRILASLEAELEA-----LQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
361-543 1.04e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 361 QRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEA------LLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQ 434
Cdd:COG1196  285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELeeelaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 435 RKLIEHEEKqnkmylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRASECRMREcgSNHAL 514
Cdd:COG1196  365 EALLEAEAE---------LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE--ALAEL 433
                        170       180
                 ....*....|....*....|....*....
gi 442626127 515 LTAKEAISLWVLGARKTIYRRLLEAQKNR 543
Cdd:COG1196  434 EEEEEEEEEALEEAAEEEAELEEEEEALL 462
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
356-447 1.91e-04

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: 42.02  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   356 ENYELQRqELISMYEHRIEELIRS-QDSATSDLKRSHNDKVEALLQKLA-ECNTRYSDMVPDYEQAKQRIRELEKQLEDL 433
Cdd:smart01071  49 KNLKYEL-IMNDHLNKRIDKLLKGlREEELSPETPTYNEMLAELQDQLKkELEEANGDSEGLLEELKKHRDKLKKEQKEL 127
                           90
                   ....*....|....
gi 442626127   434 QRKLIEHEEKQNKM 447
Cdd:smart01071 128 RKKLDELEKEEKKK 141
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
194-469 2.19e-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: 44.66  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   194 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 273
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   274 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 343
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   344 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 414
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 442626127   415 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKmyLHMYQQGQEaERISRADQALD 469
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLsEEYSLTLEEAEALENK--IEDDEEEAR-RRLKRLENKIK 982
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
347-501 2.30e-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: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 347 AGGDSASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYsdmvpdyEQAKQRIREL 426
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQEL-------AALEAELAEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 427 EKQLEDLQRKLIEHEEKQNKMYLHMYQQGQ--EAERISRADQALDLAQRQPESKV---SINELLHQLQSTQDELENIRAS 501
Cdd:COG4942   89 EKEIAELRAELEAQKEELAELLRALYRLGRqpPLALLLSPEDFLDAVRRLQYLKYlapARREQAEELRADLAELAALRAE 168
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
353-499 3.29e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.98  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 353 SNLENYELQRQELISMYEHRIEEL--IRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 430
Cdd:COG1340    8 SSLEELEEKIEELREEIEELKEKRdeLNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 431 EDLQRKLIEHEEKQNKM---------------YLHMYQQ----GQEAER-----ISRADQALDLAQRQPESKVSINELLH 486
Cdd:COG1340   88 NELREELDELRKELAELnkaggsidklrkeieRLEWRQQtevlSPEEEKelvekIKELEKELEKAKKALEKNEKLKELRA 167
                        170
                 ....*....|...
gi 442626127 487 QLQSTQDELENIR 499
Cdd:COG1340  168 ELKELRKEAEEIH 180
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
390-508 3.60e-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: 43.52  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127  390 SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEK-------QNKMYLHMYQQGQEAERIS 462
Cdd:pfam05622 301 SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKaedssllKQKLEEHLEKLHEAQSELQ 380
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 442626127  463 RADQALD-LAQRQPESK-VSINELLHQLQSTQDELeniRASECRMREC 508
Cdd:pfam05622 381 KKKEQIEeLEPKQDSNLaQKIDELQEALRKKDEDM---KAMEERYKKY 425
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
393-543 5.09e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 5.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 393 DKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNkmYLHMYQQGQEAE-RISRADQALDLA 471
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEaELAELPERLEEL 151
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626127 472 QRQPEskvSINELLHQLQSTQDELENIRASECRMRECGSNHALLTAKEAI-SLWVLGARKTIYRRLLEAQKNR 543
Cdd:COG4717  152 EERLE---ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAeELEELQQRLAELEEELEEAQEE 221
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
361-471 6.15e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 361 QRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEH 440
Cdd:COG4717  146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
                         90       100       110
                 ....*....|....*....|....*....|.
gi 442626127 441 EEKQNKMYLHMYQQgQEAERISRADQALDLA 471
Cdd:COG4717  226 EEELEQLENELEAA-ALEERLKEARLLLLIA 255
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
392-501 6.20e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 6.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 392 NDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQE-------------A 458
Cdd:COG3883   36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvllgsesfS 115
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 442626127 459 ERISRADQALDLAQRQpeskvsiNELLHQLQSTQDELENIRAS 501
Cdd:COG3883  116 DFLDRLSALSKIADAD-------ADLLEELKADKAELEAKKAE 151
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
392-497 8.66e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 8.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 392 NDKVEALLQKLAECNTRYSDmvpDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISR--ADQAL- 468
Cdd:PRK00409 515 KEKLNELIASLEELERELEQ---KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKkeADEIIk 591
                         90       100
                 ....*....|....*....|....*....
gi 442626127 469 DLAQRQPESKVSINEllHQLQSTQDELEN 497
Cdd:PRK00409 592 ELRQLQKGGYASVKA--HELIEARKRLNK 618
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
387-500 1.01e-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: 41.06  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 387 LKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQ-----NKMYLHMYQQ--GQEAE 459
Cdd:COG1579   25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYEALQKEieSLKRR 104
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 442626127 460 RISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRA 500
Cdd:COG1579  105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
PRK05563 PRK05563
DNA polymerase III subunits gamma and tau; Validated
351-499 1.01e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235505 [Multi-domain]  Cd Length: 559  Bit Score: 42.17  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127 351 SASNLENYELQRQEL-ISMYEHRIEELIRSQdsatSDLKRSHNDKV--EALLQKLAECNTRYSDMVPDYEQAKQRIRELE 427
Cdd:PRK05563 307 STENDELFKELSEKLdIERLYRMIDILNDAQ----QQIKWTNQPRIylEVALVKLCEQAAASPEYDTELEVLLQRVEQLE 382
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626127 428 KQLEDLQrklieheekqnkmylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQL-QSTQDELENIR 499
Cdd:PRK05563 383 QELKQLK------------------AQPVGVAPEQKEKKKEKKKNKKKKYKVPRGKIYKVLkEATRQDLELLK 437
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
370-496 1.19e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127  370 EHRIEELIRSQDSATSDlkrshNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQnkmyl 449
Cdd:COG4913   667 EREIAELEAELERLDAS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL----- 736
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 442626127  450 hmyqqgQEAERISRADQALDLAQRQPESKV--SINELLHQLQSTQDELE 496
Cdd:COG4913   737 ------EAAEDLARLELRALLEERFAAALGdaVERELRENLEERIDALR 779
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
414-588 1.89e-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: 41.64  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   414 PDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQ-----QGQEAERISRADQALDLAQRQPESKvsiNELLHQL 488
Cdd:pfam15921   71 PGKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidlQTKLQEMQMERDAMADIRRRESQSQ---EDLRNQL 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   489 QSTQDELENIRASECRMRECGSNHALLTAKEAISL-WVLGARKTIYRRLLEAQKNRTHV-DPEVTLQF--LKSAIFYFLT 564
Cdd:pfam15921  148 QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHeGVLQEIRSILVDFEEASGKKIYEhDSMSTMHFrsLGSAISKILR 227
                          170       180
                   ....*....|....*....|....*...
gi 442626127   565 --DKENS--QGHLQAIESILEFTDAEKQ 588
Cdd:pfam15921  228 elDTEISylKGRIFPVEDQLEALKSESQ 255
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
370-521 2.76e-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: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127  370 EHRIEELIRSQDSATSDLKRsHNDKVEALLQKLAECNTRYSDMVPDYEQAK-QRIRELEKQLEDLQRKLIEHEEKQNKMY 448
Cdd:COG4913   287 QRRLELLEAELEELRAELAR-LEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLE 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127  449 LHMYQQGQE--------AERISRADQALD--------LAQRQPESKVSINELLHQLQSTQDELENIRASecrmrecGSN- 511
Cdd:COG4913   366 ALLAALGLPlpasaeefAALRAEAAALLEaleeeleaLEEALAEAEAALRDLRRELRELEAEIASLERR-------KSNi 438
                         170
                  ....*....|.
gi 442626127  512 -HALLTAKEAI 521
Cdd:COG4913   439 pARLLALRDAL 449
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
350-496 4.04e-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: 40.44  E-value: 4.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127   350 DSASNLENYELQRQELISMYEHRIEELirsqdsatsdlkrshNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQ 429
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKEIENL---------------NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626127   430 LEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELE 496
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVE 964
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
355-497 6.85e-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: 39.45  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127  355 LENYELQRQELismYEHRIEELIRsqdsatsdlkrshndKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDL- 433
Cdd:pfam06160 323 LNENELERVRG---LEKQLEELEK---------------RYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFk 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626127  434 -------------QRKLIE-----HE-----EKQN-----KMYLHMYQQGQeaERISRADQALDlaqrqpESKVSINELL 485
Cdd:pfam06160 385 eslqslrkdeleaREKLDEfklelREikrlvEKSNlpglpESYLDYFFDVS--DEIEDLADELN------EVPLNMDEVN 456
                         170
                  ....*....|..
gi 442626127  486 HQLQSTQDELEN 497
Cdd:pfam06160 457 RLLDEAQDDVDT 468
 
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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