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Conserved domains on  [gi|24581856|ref|NP_723057|]
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quick-to-court, isoform B [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];
320-468 5.98e-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: 49.00  E-value: 5.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856 320 ASNLENYELQRQELISmYEHRIEELIRSQDSATSDLKR-SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 398
Cdd:COG4717  84 EEKEEEYAELQEELEE-LEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581856 399 EDLQRKLIEHEEKQNKMYLHMYQQGQEAE-RISRADQALDLAQRQpeskvsINELLHQLQSTQDELENIRA 468
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQR------LAELEEELEEAQEELEELEE 227
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
517-558 8.32e-06

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: 8.32e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 24581856   517 EVTLQFLKSAIFYFLTDKENS-QGHL-QAIESILEFTDAEKQKI 558
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSeRKQLlPVIATLLKFSPEEEQKI 44
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
162-437 4.29e-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: 43.51  E-value: 4.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    162 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 241
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    242 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 311
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    312 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 382
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24581856    383 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKmyLHMYQQGQEaERISRADQALD 437
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLsEEYSLTLEEAEALENK--IEDDEEEAR-RRLKRLENKIK 982
 
Name Accession Description Interval E-value
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
320-468 5.98e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 5.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856 320 ASNLENYELQRQELISmYEHRIEELIRSQDSATSDLKR-SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 398
Cdd:COG4717  84 EEKEEEYAELQEELEE-LEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581856 399 EDLQRKLIEHEEKQNKMYLHMYQQGQEAE-RISRADQALDLAQRQpeskvsINELLHQLQSTQDELENIRA 468
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQR------LAELEEELEEAQEELEELEE 227
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
517-558 8.32e-06

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: 8.32e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 24581856   517 EVTLQFLKSAIFYFLTDKENS-QGHL-QAIESILEFTDAEKQKI 558
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSeRKQLlPVIATLLKFSPEEEQKI 44
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
334-512 2.95e-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: 46.97  E-value: 2.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    334 ISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQN 413
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    414 KMYLHMYQQGQEAERISRADQALDLAQRQPESKVS-------------INELLHQLQSTQDELENiRASECRMRECGSNH 480
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkelqaeleeLEEELEELQEELERLEE-ALEELREELEEAEQ 475
                          170       180       190
                   ....*....|....*....|....*....|..
gi 24581856    481 ALLTAKEaiSLWVLGARKTIYRRLLEAQKNRT 512
Cdd:TIGR02168  476 ALDAAER--ELAQLQARLDSLERLQENLEGFS 505
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
324-415 1.98e-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: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    324 ENYELQRqELISMYEHRIEELIRS-QDSATSDLKRSHNDKVEALLQKLA-ECNTRYSDMVPDYEQAKQRIRELEKQLEDL 401
Cdd:smart01071  49 KNLKYEL-IMNDHLNKRIDKLLKGlREEELSPETPTYNEMLAELQDQLKkELEEANGDSEGLLEELKKHRDKLKKEQKEL 127
                           90
                   ....*....|....
gi 24581856    402 QRKLIEHEEKQNKM 415
Cdd:smart01071 128 RKKLDELEKEEKKK 141
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
162-437 4.29e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 4.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    162 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 241
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    242 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 311
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    312 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 382
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24581856    383 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKmyLHMYQQGQEaERISRADQALD 437
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 ...
358-476 5.69e-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: 42.75  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856   358 SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEK-------QNKMYLHMYQQGQEAERIS 430
Cdd:pfam05622 301 SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKaedssllKQKLEEHLEKLHEAQSELQ 380
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 24581856   431 RADQALD-LAQRQPESK-VSINELLHQLQSTQDELeniRASECRMREC 476
Cdd:pfam05622 381 KKKEQIEeLEPKQDSNLaQKIDELQEALRKKDEDM---KAMEERYKKY 425
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
360-465 7.17e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 7.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856  360 NDKVEALLQKLAECNTRYSDmvpDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISR--ADQAL- 436
Cdd:PRK00409 515 KEKLNELIASLEELERELEQ---KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKkeADEIIk 591
                         90       100
                 ....*....|....*....|....*....
gi 24581856  437 DLAQRQPESKVSINEllHQLQSTQDELEN 465
Cdd:PRK00409 592 ELRQLQKGGYASVKA--HELIEARKRLNK 618
 
Name Accession Description Interval E-value
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
320-468 5.98e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 5.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856 320 ASNLENYELQRQELISmYEHRIEELIRSQDSATSDLKR-SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 398
Cdd:COG4717  84 EEKEEEYAELQEELEE-LEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581856 399 EDLQRKLIEHEEKQNKMYLHMYQQGQEAE-RISRADQALDLAQRQpeskvsINELLHQLQSTQDELENIRA 468
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQR------LAELEEELEEAQEELEELEE 227
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
517-558 8.32e-06

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: 8.32e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 24581856   517 EVTLQFLKSAIFYFLTDKENS-QGHL-QAIESILEFTDAEKQKI 558
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSeRKQLlPVIATLLKFSPEEEQKI 44
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
334-512 2.95e-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: 46.97  E-value: 2.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    334 ISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQN 413
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    414 KMYLHMYQQGQEAERISRADQALDLAQRQPESKVS-------------INELLHQLQSTQDELENiRASECRMRECGSNH 480
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkelqaeleeLEEELEELQEELERLEE-ALEELREELEEAEQ 475
                          170       180       190
                   ....*....|....*....|....*....|..
gi 24581856    481 ALLTAKEaiSLWVLGARKTIYRRLLEAQKNRT 512
Cdd:TIGR02168  476 ALDAAER--ELAQLQARLDSLERLQENLEGFS 505
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
321-468 9.07e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 9.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856 321 SNLENYELQRQELISMYEhRIEELIRSQDSATSDLKRSHN-----DKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELE 395
Cdd:COG3206 226 SQLAEARAELAEAEARLA-ALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALR 304
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581856 396 KQLEDLQRKLIEHEEKQNKMylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRA 468
Cdd:COG3206 305 AQLQQEAQRILASLEAELEA-----LQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
329-511 1.55e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856 329 QRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEA------LLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQ 402
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELeeelaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856 403 RKLIEHEEKqnkmylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRASECRMREcgSNHAL 482
Cdd:COG1196 365 EALLEAEAE---------LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE--ALAEL 433
                       170       180
                ....*....|....*....|....*....
gi 24581856 483 LTAKEAISLWVLGARKTIYRRLLEAQKNR 511
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALL 462
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
324-415 1.98e-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: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    324 ENYELQRqELISMYEHRIEELIRS-QDSATSDLKRSHNDKVEALLQKLA-ECNTRYSDMVPDYEQAKQRIRELEKQLEDL 401
Cdd:smart01071  49 KNLKYEL-IMNDHLNKRIDKLLKGlREEELSPETPTYNEMLAELQDQLKkELEEANGDSEGLLEELKKHRDKLKKEQKEL 127
                           90
                   ....*....|....
gi 24581856    402 QRKLIEHEEKQNKM 415
Cdd:smart01071 128 RKKLDELEKEEKKK 141
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
315-469 2.52e-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: 43.60  E-value: 2.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856 315 AGGDSASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYsdmvpdyEQAKQRIREL 394
Cdd:COG4942  17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQEL-------AALEAELAEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856 395 EKQLEDLQRKLIEHEEKQNKMYLHMYQQGQ--EAERISRADQALDLAQRQPESKV---SINELLHQLQSTQDELENIRAS 469
Cdd:COG4942  89 EKEIAELRAELEAQKEELAELLRALYRLGRqpPLALLLSPEDFLDAVRRLQYLKYlapARREQAEELRADLAELAALRAE 168
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
321-467 3.63e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.59  E-value: 3.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856 321 SNLENYELQRQELISMYEHRIEEL--IRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 398
Cdd:COG1340   8 SSLEELEEKIEELREEIEELKEKRdeLNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856 399 EDLQRKLIEHEEKQNKM---------------YLHMYQQ----GQEAER-----ISRADQALDLAQRQPESKVSINELLH 454
Cdd:COG1340  88 NELREELDELRKELAELnkaggsidklrkeieRLEWRQQtevlSPEEEKelvekIKELEKELEKAKKALEKNEKLKELRA 167
                       170
                ....*....|...
gi 24581856 455 QLQSTQDELENIR 467
Cdd:COG1340 168 ELKELRKEAEEIH 180
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
162-437 4.29e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 4.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    162 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 241
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    242 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 311
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    312 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 382
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24581856    383 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKmyLHMYQQGQEaERISRADQALD 437
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 ...
358-476 5.69e-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: 42.75  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856   358 SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEK-------QNKMYLHMYQQGQEAERIS 430
Cdd:pfam05622 301 SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKaedssllKQKLEEHLEKLHEAQSELQ 380
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 24581856   431 RADQALD-LAQRQPESK-VSINELLHQLQSTQDELeniRASECRMREC 476
Cdd:pfam05622 381 KKKEQIEeLEPKQDSNLaQKIDELQEALRKKDEDM---KAMEERYKKY 425
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
361-511 6.64e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 6.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856 361 DKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNkmYLHMYQQGQEAE-RISRADQALDLA 439
Cdd:COG4717  74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEaELAELPERLEEL 151
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581856 440 QRQPEskvSINELLHQLQSTQDELENIRASECRMRECGSNHALLTAKEAI-SLWVLGARKTIYRRLLEAQKNR 511
Cdd:COG4717 152 EERLE---ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAeELEELQQRLAELEEELEEAQEE 221
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
360-465 7.17e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 7.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856  360 NDKVEALLQKLAECNTRYSDmvpDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISR--ADQAL- 436
Cdd:PRK00409 515 KEKLNELIASLEELERELEQ---KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKkeADEIIk 591
                         90       100
                 ....*....|....*....|....*....
gi 24581856  437 DLAQRQPESKVSINEllHQLQSTQDELEN 465
Cdd:PRK00409 592 ELRQLQKGGYASVKA--HELIEARKRLNK 618
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
329-439 7.63e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 7.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856 329 QRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEH 408
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
                        90       100       110
                ....*....|....*....|....*....|.
gi 24581856 409 EEKQNKMYLHMYQQgQEAERISRADQALDLA 439
Cdd:COG4717 226 EEELEQLENELEAA-ALEERLKEARLLLLIA 255
PRK05563 PRK05563
DNA polymerase III subunits gamma and tau; Validated
319-467 9.64e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235505 [Multi-domain]  Cd Length: 559  Bit Score: 41.78  E-value: 9.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856  319 SASNLENYELQRQEL-ISMYEHRIEELIRSQdsatSDLKRSHNDKV--EALLQKLAECNTRYSDMVPDYEQAKQRIRELE 395
Cdd:PRK05563 307 STENDELFKELSEKLdIERLYRMIDILNDAQ----QQIKWTNQPRIylEVALVKLCEQAAASPEYDTELEVLLQRVEQLE 382
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581856  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 ...
355-468 1.20e-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: 40.68  E-value: 1.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856 355 LKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQ-----NKMYLHMYQQ--GQEAE 427
Cdd:COG1579  25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYEALQKEieSLKRR 104
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 24581856 428 RISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRA 468
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
338-464 1.55e-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: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856  338 EHRIEELIRSQDSATSDlkrshNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQnkmyl 417
Cdd:COG4913  667 EREIAELEAELERLDAS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL----- 736
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 24581856  418 hmyqqgQEAERISRADQALDLAQRQPESKV--SINELLHQLQSTQDELE 464
Cdd:COG4913  737 ------EAAEDLARLELRALLEERFAAALGdaVERELRENLEERIDALR 779
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
360-469 1.96e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 1.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856 360 NDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQE-------------A 426
Cdd:COG3883  36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvllgsesfS 115
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 24581856 427 ERISRADQALDLAQRQpeskvsiNELLHQLQSTQDELENIRAS 469
Cdd:COG3883 116 DFLDRLSALSKIADAD-------ADLLEELKADKAELEAKKAE 151
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
382-556 3.13e-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: 40.49  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    382 PDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQ-----QGQEAERISRADQALDLAQRQPESKvsiNELLHQL 456
Cdd:pfam15921   71 PGKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidlQTKLQEMQMERDAMADIRRRESQSQ---EDLRNQL 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    457 QSTQDELENIRASECRMRECGSNHALLTAKEAISL-WVLGARKTIYRRLLEAQKNRTHV-DPEVTLQF--LKSAIFYFLT 532
Cdd:pfam15921  148 QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHeGVLQEIRSILVDFEEASGKKIYEhDSMSTMHFrsLGSAISKILR 227
                          170       180
                   ....*....|....*....|....*...
gi 24581856    533 --DKENS--QGHLQAIESILEFTDAEKQ 556
Cdd:pfam15921  228 elDTEISylKGRIFPVEDQLEALKSESQ 255
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
338-489 3.99e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856  338 EHRIEELIRSQDSATSDLKRsHNDKVEALLQKLAECNTRYSDMVPDYEQAK-QRIRELEKQLEDLQRKLIEHEEKQNKMY 416
Cdd:COG4913  287 QRRLELLEAELEELRAELAR-LEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLE 365
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856  417 LHMYQQGQE--------AERISRADQALD--------LAQRQPESKVSINELLHQLQSTQDELENIRASecrmrecGSN- 479
Cdd:COG4913  366 ALLAALGLPlpasaeefAALRAEAAALLEaleeeleaLEEALAEAEAALRDLRRELRELEAEIASLERR-------KSNi 438
                        170
                 ....*....|.
gi 24581856  480 -HALLTAKEAI 489
Cdd:COG4913  439 pARLLALRDAL 449
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
318-464 5.15e-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: 40.05  E-value: 5.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581856    318 DSASNLENYELQRQELISMYEHRIEELirsqdsatsdlkrshNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQ 397
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKEIENL---------------NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581856    398 LEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELE 464
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVE 964
 
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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