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Conserved domains on  [gi|442626131|ref|NP_001260084|]
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quick-to-court, isoform L [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
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
 494-535 9.15e-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: 9.15e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 442626131  494 EVTLQFLKSAIFYFLTDKENS-QGHL-QAIESILEFTDAEKQKI 535
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSeRKQLlPVIATLLKFSPEEEQKI 44
GumC super family cl34566
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
329-486 1.05e-05

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


The actual alignment was detected with superfamily member COG3206:

Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.47  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 329 SNLENYELQRQELISMYEhRIEELIRSQDSATSDLKRSHN-----DKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELE 403
Cdd:COG3206  226 SQLAEARAELAEAEARLA-ALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALR 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 404 KQLEDLQRKLIEHEEKQNKMylhmyQQGQEAERISRADQALDLAQRQPESKVSINELlhqlqstQDELENIRTIYRRLLE 483
Cdd:COG3206  305 AQLQQEAQRILASLEAELEA-----LQAREASLQAQLAQLEARLAELPELEAELRRL-------EREVEVARELYESLLQ 372


                 ...
gi 442626131 484 AQK 486
Cdd:COG3206  373 RLE 375
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-445 4.37e-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: 43.12  E-value: 4.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   170 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 249
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   250 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 319
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   320 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 390
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 442626131   391 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKmyLHMYQQGQEaERISRADQALD 445
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLsEEYSLTLEEAEALENK--IEDDEEEAR-RRLKRLENKIK 982
 
Name Accession Description Interval E-value
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
 494-535 9.15e-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: 9.15e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 442626131  494 EVTLQFLKSAIFYFLTDKENS-QGHL-QAIESILEFTDAEKQKI 535
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSeRKQLlPVIATLLKFSPEEEQKI 44
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
329-486 1.05e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.47  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 329 SNLENYELQRQELISMYEhRIEELIRSQDSATSDLKRSHN-----DKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELE 403
Cdd:COG3206  226 SQLAEARAELAEAEARLA-ALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALR 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 404 KQLEDLQRKLIEHEEKQNKMylhmyQQGQEAERISRADQALDLAQRQPESKVSINELlhqlqstQDELENIRTIYRRLLE 483
Cdd:COG3206  305 AQLQQEAQRILASLEAELEA-----LQAREASLQAQLAQLEARLAELPELEAELRRL-------EREVEVARELYESLLQ 372


                 ...
gi 442626131 484 AQK 486
Cdd:COG3206  373 RLE 375
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 342-540 2.04e-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: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   342 ISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQN 421
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   422 KMYLHMYQQGQEAERISRADQALDLAQRQPESKVS---INELLHQLQSTQDELENIRTIYRRLLEAQKNRthvdpEVTLQ 498
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaeLKELQAELEELEEELEELQEELERLEEALEEL-----REELE 471

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 442626131   499 FLKSAIFYFLTDKENSQGHLQAIESILE----FTDAEKQKISAANR 540
Cdd:TIGR02168  472 EAEQALDAAERELAQLQARLDSLERLQEnlegFSEGVKALLKNQSG 517
PRK05563 PRK05563
DNA polymerase III subunits gamma and tau; Validated
 327-492 6.20e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235505 [Multi-domain]  Cd Length: 559  Bit Score: 45.63  E-value: 6.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 327 SASNLENYELQRQEL-ISMYEHRIEELIRSQdsatSDLKRSHNDKV--EALLQKLAECNTRYSDMVPDYEQAKQRIRELE 403
Cdd:PRK05563 307 STENDELFKELSEKLdIERLYRMIDILNDAQ----QQIKWTNQPRIylEVALVKLCEQAAASPEYDTELEVLLQRVEQLE 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 404 KQLEDLQrklieheekqnkmylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQL-QSTQDELENIRTIYRRLL 482
Cdd:PRK05563 383 QELKQLK------------------AQPVGVAPEQKEKKKEKKKNKKKKYKVPRGKIYKVLkEATRQDLELLKNVWGEIL 444

                        170
                 ....*....|
gi 442626131 483 EAQKNRTHVD 492
Cdd:PRK05563 445 ESLKAQRKSL 454
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 366-487 1.05e-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: 45.07  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131  366 SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEK-------QNKMYLHMYQQGQEAERIS 438
Cdd:pfam05622 301 SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKaedssllKQKLEEHLEKLHEAQSELQ 380

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442626131  439 RADQALD-LAQRQPESK-VSINELLHQLQSTQDELENIRTIYRRLLEAQKN 487
Cdd:pfam05622 381 KKKEQIEeLEPKQDSNLaQKIDELQEALRKKDEDMKAMEERYKKYVEKAKS 431
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 332-423 2.30e-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: 41.63  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   332 ENYELQRqELISMYEHRIEELIRS-QDSATSDLKRSHNDKVEALLQKLA-ECNTRYSDMVPDYEQAKQRIRELEKQLEDL 409
Cdd:smart01071  49 KNLKYEL-IMNDHLNKRIDKLLKGlREEELSPETPTYNEMLAELQDQLKkELEEANGDSEGLLEELKKHRDKLKKEQKEL 127

                           90
                   ....*....|....
gi 442626131   410 QRKLIEHEEKQNKM 423
Cdd:smart01071 128 RKKLDELEKEEKKK 141
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-445 4.37e-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: 43.12  E-value: 4.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   170 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 249
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   250 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 319
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   320 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 390
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 442626131   391 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKmyLHMYQQGQEaERISRADQALD 445
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLsEEYSLTLEEAEALENK--IEDDEEEAR-RRLKRLENKIK 982
 
Name Accession Description Interval E-value
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
 494-535 9.15e-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: 9.15e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 442626131  494 EVTLQFLKSAIFYFLTDKENS-QGHL-QAIESILEFTDAEKQKI 535
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSeRKQLlPVIATLLKFSPEEEQKI 44
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
329-486 1.05e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.47  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 329 SNLENYELQRQELISMYEhRIEELIRSQDSATSDLKRSHN-----DKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELE 403
Cdd:COG3206  226 SQLAEARAELAEAEARLA-ALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALR 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 404 KQLEDLQRKLIEHEEKQNKMylhmyQQGQEAERISRADQALDLAQRQPESKVSINELlhqlqstQDELENIRTIYRRLLE 483
Cdd:COG3206  305 AQLQQEAQRILASLEAELEA-----LQAREASLQAQLAQLEARLAELPELEAELRRL-------EREVEVARELYESLLQ 372


                 ...
gi 442626131 484 AQK 486
Cdd:COG3206  373 RLE 375
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 342-540 2.04e-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: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   342 ISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQN 421
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   422 KMYLHMYQQGQEAERISRADQALDLAQRQPESKVS---INELLHQLQSTQDELENIRTIYRRLLEAQKNRthvdpEVTLQ 498
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaeLKELQAELEELEEELEELQEELERLEEALEEL-----REELE 471

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 442626131   499 FLKSAIFYFLTDKENSQGHLQAIESILE----FTDAEKQKISAANR 540
Cdd:TIGR02168  472 EAEQALDAAERELAQLQARLDSLERLQEnlegFSEGVKALLKNQSG 517
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 337-486 2.67e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 337 QRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEA------LLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQ 410
Cdd:COG1196  285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELeeelaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626131 411 RKLIEHEEKqnkmylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRTIYRRLLEAQK 486
Cdd:COG1196  365 EALLEAEAE---------LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 323-488 5.02e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 5.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 323 AGGDSASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYsdmvpdyEQAKQRIREL 402
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQEL-------AALEAELAEL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 403 EKQLEDLQRKLIEHEEKQNKMYLHMYQQGQ-----------EAERISRADQALD-LAQRQPESKVSINELLHQLQSTQDE 470
Cdd:COG4942   89 EKEIAELRAELEAQKEELAELLRALYRLGRqpplalllspeDFLDAVRRLQYLKyLAPARREQAEELRADLAELAALRAE 168

                        170
                 ....*....|....*...
gi 442626131 471 LENIRTIYRRLLEAQKNR 488
Cdd:COG4942  169 LEAERAELEALLAELEEE 186
PRK05563 PRK05563
DNA polymerase III subunits gamma and tau; Validated
 327-492 6.20e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235505 [Multi-domain]  Cd Length: 559  Bit Score: 45.63  E-value: 6.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 327 SASNLENYELQRQEL-ISMYEHRIEELIRSQdsatSDLKRSHNDKV--EALLQKLAECNTRYSDMVPDYEQAKQRIRELE 403
Cdd:PRK05563 307 STENDELFKELSEKLdIERLYRMIDILNDAQ----QQIKWTNQPRIylEVALVKLCEQAAASPEYDTELEVLLQRVEQLE 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 404 KQLEDLQrklieheekqnkmylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQL-QSTQDELENIRTIYRRLL 482
Cdd:PRK05563 383 QELKQLK------------------AQPVGVAPEQKEKKKEKKKNKKKKYKVPRGKIYKVLkEATRQDLELLKNVWGEIL 444

                        170
                 ....*....|
gi 442626131 483 EAQKNRTHVD 492
Cdd:PRK05563 445 ESLKAQRKSL 454
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 366-487 1.05e-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: 45.07  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131  366 SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEK-------QNKMYLHMYQQGQEAERIS 438
Cdd:pfam05622 301 SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKaedssllKQKLEEHLEKLHEAQSELQ 380

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442626131  439 RADQALD-LAQRQPESK-VSINELLHQLQSTQDELENIRTIYRRLLEAQKN 487
Cdd:pfam05622 381 KKKEQIEeLEPKQDSNLaQKIDELQEALRKKDEDMKAMEERYKKYVEKAKS 431
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 332-423 2.30e-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: 41.63  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   332 ENYELQRqELISMYEHRIEELIRS-QDSATSDLKRSHNDKVEALLQKLA-ECNTRYSDMVPDYEQAKQRIRELEKQLEDL 409
Cdd:smart01071  49 KNLKYEL-IMNDHLNKRIDKLLKGlREEELSPETPTYNEMLAELQDQLKkELEEANGDSEGLLEELKKHRDKLKKEQKEL 127

                           90
                   ....*....|....
gi 442626131   410 QRKLIEHEEKQNKM 423
Cdd:smart01071 128 RKKLDELEKEEKKK 141
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 390-535 2.52e-04

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: 43.95  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   390 PDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQ-----QGQEAERISRADQALDLAQRQPESKvsiNELLHQL 464
Cdd:pfam15921   71 PGKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidlQTKLQEMQMERDAMADIRRRESQSQ---EDLRNQL 147

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626131   465 QSTQDELENIRTIYRRLLEaqknrthvDPEVTLQFLKSAIFyfltdkeNSQGHLQAIESIL-EFTDAEKQKI 535
Cdd:pfam15921  148 QNTVHELEAAKCLKEDMLE--------DSNTQIEQLRKMML-------SHEGVLQEIRSILvDFEEASGKKI 204
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
329-475 3.85e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.59  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 329 SNLENYELQRQELISMYEHRIEEL--IRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 406
Cdd:COG1340    8 SSLEELEEKIEELREEIEELKEKRdeLNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 407 EDLQRKLIEHEEKQNKM---------------YLHMYQQ----GQEAER-----ISRADQALDLAQRQPESKVSINELLH 462
Cdd:COG1340   88 NELREELDELRKELAELnkaggsidklrkeieRLEWRQQtevlSPEEEKelvekIKELEKELEKAKKALEKNEKLKELRA 167

                        170
                 ....*....|...
gi 442626131 463 QLQSTQDELENIR 475
Cdd:COG1340  168 ELKELRKEAEEIH 180
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-445 4.37e-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: 43.12  E-value: 4.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   170 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 249
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   250 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 319
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   320 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 390
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 442626131   391 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKmyLHMYQQGQEaERISRADQALD 445
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLsEEYSLTLEEAEALENK--IEDDEEEAR-RRLKRLENKIK 982
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
338-537 5.01e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 5.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 338 RQELISMYEHRIEELIRSQDSatsdLKRSHNDKVEALLQKLAEcntrYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHE 417
Cdd:COG4717   44 RAMLLERLEKEADELFKPQGR----KPELNLKELKELEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 418 EKQNKM-----YLHMYQQGQEAE-RISRADQALDLAQRQPEskvSINELLHQLQSTQDELENIrtiyRRLLEAQKNRTHV 491
Cdd:COG4717  116 EELEKLekllqLLPLYQELEALEaELAELPERLEELEERLE---ELRELEEELEELEAELAEL----QEELEELLEQLSL 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 442626131 492 DPEVTLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISA 537
Cdd:COG4717  189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
346-488 5.69e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131  346 EHRIEELIRSQDSATSDlkrshNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRkliehEEKQNKMYL 425
Cdd:COG4913   667 EREIAELEAELERLDAS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE-----ELDELQDRL 736

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626131  426 HMYQQGQEAERISRADQALD-LAQRQPESKVSiNELLHQLQSTQDELENIRTIYRRLLEAQKNR 488
Cdd:COG4913   737 EAAEDLARLELRALLEERFAaALGDAVERELR-ENLEERIDALRARLNRAEEELERAMRAFNRE 799
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
337-447 6.84e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 6.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 337 QRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEH 416
Cdd:COG4717  146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225

                         90       100       110
                 ....*....|....*....|....*....|.
gi 442626131 417 EEKQNKMYLHMYQQgQEAERISRADQALDLA 447
Cdd:COG4717  226 EEELEQLENELEAA-ALEERLKEARLLLLIA 255
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 368-473 7.50e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 7.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 368 NDKVEALLQKLAECNTRYSDmvpDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISR--ADQAL- 444
Cdd:PRK00409 515 KEKLNELIASLEELERELEQ---KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKkeADEIIk 591

                         90       100
                 ....*....|....*....|....*....
gi 442626131 445 DLAQRQPESKVSINEllHQLQSTQDELEN 473
Cdd:PRK00409 592 ELRQLQKGGYASVKA--HELIEARKRLNK 618
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 363-476 2.07e-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: 39.91  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 363 LKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQ-----NKMYLHMYQQ--GQEAE 435
Cdd:COG1579   25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYEALQKEieSLKRR 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 442626131 436 RISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRT 476
Cdd:COG1579  105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 329-537 2.33e-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: 40.87  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   329 SNLENYELQRQELISMYEHRIEELIRSQDSATSDL---KRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQ 405
Cdd:pfam15921  299 SQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELreaKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQ 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   406 LEDL------QRKLIEHEEKQNK---------------MYLHMYQQGQEAERISRADQAL-DLAQRQPESKVSI----NE 459
Cdd:pfam15921  379 LQKLladlhkREKELSLEKEQNKrlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMkSECQGQMERQMAAiqgkNE 458

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   460 LLHQLQSTQDELENIRTIYRRLLE--AQKNRTHVDPEVTLQFLKSAifyfltdkensqghLQAIESILEFTDAEKQKISA 537
Cdd:pfam15921  459 SLEKVSSLTAQLESTKEMLRKVVEelTAKKMTLESSERTVSDLTAS--------------LQEKERAIEATNAEITKLRS 524
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
325-540 2.36e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 325 GDSASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEK 404
Cdd:COG4372    9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQL-REELEQAREELEQLEEELEQARSELEQLEEELEELNE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 405 QLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISRADQalDLAQRQPESKVSINELLHQLQSTQDELENIRTIYRRLLEA 484
Cdd:COG4372   88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ--DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442626131 485 QKNRTHVDPEVTLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISAANR 540
Cdd:COG4372  166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 323-501 2.68e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 39.98  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131  323 AGGD-SASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVP--------DYE 393
Cdd:pfam03961  73 AGGNiSAKFIQNAEVEAGGDILVEKQILHSLVKAGGSIIVGGRKGKIIGGNIKAGKGVKAKELGSPAGTkteievgvDFP 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131  394 QAKQRIRELEKQLEDLQRKLIEHEEKQNKmyLHMYQQGQEAERISraDQALDLAQRQPESKVSINELLHQLQSTQDELEN 473
Cdd:pfam03961 153 ELKEKLEELEKELEELEEELEKLKKRLKK--LPKKARGQLPPEKR--EQLEKLLETKNKLSEELEELEEELKELKEELES 228

                         170       180
                  ....*....|....*....|....*...
gi 442626131  474 IRTIYRrlLEAQKnrtHVDPEVTLQFLK 501
Cdd:pfam03961 229 LLGEGK--ISVNK---TIYPGVTIQIGN 251
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 368-487 4.06e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 368 NDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQE-------------A 434
Cdd:COG3883   36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvllgsesfS 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442626131 435 ERISRADQALDLAQRQpeskvsiNELLHQLQSTQDELENIRTIYRRLLEAQKN 487
Cdd:COG3883  116 DFLDRLSALSKIADAD-------ADLLEELKADKAELEAKKAELEAKLAELEA 161
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 326-472 4.82e-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: 4.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131   326 DSASNLENYELQRQELISMYEHRIEELirsqdsatsdlkrshNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQ 405
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKEIENL---------------NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626131   406 LEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELE 472
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVE 964
PRK11281 PRK11281
mechanosensitive channel MscK;
364-541 8.05e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.12  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131  364 KRSHNDKVEALLQKLAEcNTRysDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMylhmyqqgqEAERISRADQA 443
Cdd:PRK11281   50 KQKLLEAEDKLVQQDLE-QTL--ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL---------KDDNDEETRET 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131  444 LD-LAQRQPESKVsiNELLHQLQSTQDELENirtiYRRLLEAQKNRthvdPEVTlqflKSAIFyfltdkENSQgHLQAIE 522
Cdd:PRK11281  118 LStLSLRQLESRL--AQTLDQLQNAQNDLAE----YNSQLVSLQTQ----PERA----QAALY------ANSQ-RLQQIR 176

                         170
                  ....*....|....*....
gi 442626131  523 SILEFTDAEKQKISAANRT 541
Cdd:PRK11281  177 NLLKGGKVGGKALRPSQRV 195
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 349-533 8.25e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.05  E-value: 8.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 349 IEELIRSQDSATSDLKRSHndkveallqklAECNTRYSDMVPDYEQAKQRI-----------RELEKQLEDLQRKLIEHE 417
Cdd:PRK04778 117 IEEDIEQILEELQELLESE-----------EKNREEVEQLKDLYRELRKSLlanrfsfgpalDELEKQLENLEEEFSQFV 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 418 E-KQNKMYLhmyqqgQEAERISRADQALDLAQRQPESkvsINELLHQLQST-QDELENIRTIYRRLLEAQKNRTHVDPEV 495
Cdd:PRK04778 186 ElTESGDYV------EAREILDQLEEELAALEQIMEE---IPELLKELQTElPDQLQELKAGYRELVEEGYHLDHLDIEK 256

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 442626131 496 TLQFLKSAIfyfltdKENsqghLQAIESiLEFTDAEKQ 533
Cdd:PRK04778 257 EIQDLKEQI------DEN----LALLEE-LDLDEAEEK 283
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 337-537 8.60e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 38.79  E-value: 8.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 337 QRQELISMYEHRIEELIRsqdsATSDLKRSHNDKVEALLQKLAECNtrySDMVPDYEQAKQRIRELEKQLEDLQ------ 410
Cdd:COG5185  243 SELEDLAQTSDKLEKLVE----QNTDLRLEKLGENAESSKRLNENA---NNLIKQFENTKEKIAEYTKSIDIKKatesle 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 411 ------RKLIEHEEKQNKMYLHMYQQ----GQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRtiyRR 480
Cdd:COG5185  316 eqlaaaEAEQELEESKRETETGIQNLtaeiEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTK---ES 392

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442626131 481 LLEAQKNRTHVDPEVtLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISA 537
Cdd:COG5185  393 LDEIPQNQRGYAQEI-LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELIS 448
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
348-487 9.85e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.35  E-value: 9.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626131 348 RIEELIRSQDsaTSDLKRSHNDKveaLLQKLAECNTRYSDMVP------DYEQAKQRIRELEKQLEDLQRKLIEHEEKQN 421
Cdd:COG1340  117 EIERLEWRQQ--TEVLSPEEEKE---LVEKIKELEKELEKAKKalekneKLKELRAELKELRKEAEEIHKKIKELAEEAQ 191

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626131 422 KMYLHMYQQGQEAERISraDQALDLAQRQPESKVSINELLHQLQSTQDELENIRTIYRRLLEAQKN 487
Cdd:COG1340  192 ELHEEMIELYKEADELR--KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRA 255
 
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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