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Conserved domains on  [gi|665404327|ref|NP_001285612|]
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quick-to-court, isoform N [Drosophila melanogaster]

Protein Classification

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];
330-562 4.70e-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: 49.38  E-value: 4.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 330 RQELISMYEHRIEELIRSQDSatsdLKRSHNDKVEALLQKLAEcntrYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHE 409
Cdd:COG4717   44 RAMLLERLEKEADELFKPQGR----KPELNLKELKELEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 410 EKQNKM-----YLHMYQQGQEAE-RISRADQALDLAQRQPEskvSINELLHQLQSTQDELENIrtiyRRLLEAQKNRTHV 483
Cdd:COG4717  116 EELEKLekllqLLPLYQELEALEaELAELPERLEELEERLE---ELRELEEELEELEAELAEL----QEELEELLEQLSL 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665404327 484 DPEVTLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISAANRTPKLHAKMSKTMSTILVRAKLHCFQLIGWR 562
Cdd:COG4717  189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 162-437 2.34e-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: 44.28  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   162 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 241
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   242 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 311
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   312 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 382
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 665404327   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];
330-562 4.70e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 4.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 330 RQELISMYEHRIEELIRSQDSatsdLKRSHNDKVEALLQKLAEcntrYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHE 409
Cdd:COG4717   44 RAMLLERLEKEADELFKPQGR----KPELNLKELKELEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 410 EKQNKM-----YLHMYQQGQEAE-RISRADQALDLAQRQPEskvSINELLHQLQSTQDELENIrtiyRRLLEAQKNRTHV 483
Cdd:COG4717  116 EELEKLekllqLLPLYQELEALEaELAELPERLEELEERLE---ELRELEEELEELEAELAEL----QEELEELLEQLSL 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665404327 484 DPEVTLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISAANRTPKLHAKMSKTMSTILVRAKLHCFQLIGWR 562
Cdd:COG4717  189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 334-546 9.22e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 9.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   334 ISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQN 413
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   414 KMYLHMYQQGQEAERISRADQALDLAQRQPESKVS---INELLHQLQSTQDELENIRTIYRRLLEAQKNRthvdpEVTLQ 490
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaeLKELQAELEELEEELEELQEELERLEEALEEL-----REELE 471

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   491 FLKSAIFYFLTDKENSQGHLQAIESILE----FTDAEKQKISAANRTPKLHAKMSKTMST 546
Cdd:TIGR02168  472 EAEQALDAAERELAQLQARLDSLERLQEnlegFSEGVKALLKNQSGLSGILGVLSELISV 531
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
 486-527 1.03e-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: 1.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 665404327  486 EVTLQFLKSAIFYFLTDKENS-QGHL-QAIESILEFTDAEKQKI 527
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSeRKQLlPVIATLLKFSPEEEQKI 44
PRK05563 PRK05563
DNA polymerase III subunits gamma and tau; Validated
 319-484 5.99e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235505 [Multi-domain]  Cd Length: 559  Bit Score: 46.02  E-value: 5.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 319 SASNLENYELQRQEL-ISMYEHRIEELIRSQdsatSDLKRSHNDKV--EALLQKLAECNTRYSDMVPDYEQAKQRIRELE 395
Cdd:PRK05563 307 STENDELFKELSEKLdIERLYRMIDILNDAQ----QQIKWTNQPRIylEVALVKLCEQAAASPEYDTELEVLLQRVEQLE 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 396 KQLEDLQrklieheekqnkmylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQL-QSTQDELENIRTIYRRLL 474
Cdd:PRK05563 383 QELKQLK------------------AQPVGVAPEQKEKKKEKKKNKKKKYKVPRGKIYKVLkEATRQDLELLKNVWGEIL 444

                        170
                 ....*....|
gi 665404327 475 EAQKNRTHVD 484
Cdd:PRK05563 445 ESLKAQRKSL 454
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 324-415 2.16e-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: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   324 ENYELQRqELISMYEHRIEELIRS-QDSATSDLKRSHNDKVEALLQKLA-ECNTRYSDMVPDYEQAKQRIRELEKQLEDL 401
Cdd:smart01071  49 KNLKYEL-IMNDHLNKRIDKLLKGlREEELSPETPTYNEMLAELQDQLKkELEEANGDSEGLLEELKKHRDKLKKEQKEL 127

                           90
                   ....*....|....
gi 665404327   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 2.34e-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: 44.28  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   162 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 241
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   242 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 311
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   312 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 382
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 665404327   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];
330-562 4.70e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 4.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 330 RQELISMYEHRIEELIRSQDSatsdLKRSHNDKVEALLQKLAEcntrYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHE 409
Cdd:COG4717   44 RAMLLERLEKEADELFKPQGR----KPELNLKELKELEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 410 EKQNKM-----YLHMYQQGQEAE-RISRADQALDLAQRQPEskvSINELLHQLQSTQDELENIrtiyRRLLEAQKNRTHV 483
Cdd:COG4717  116 EELEKLekllqLLPLYQELEALEaELAELPERLEELEERLE---ELRELEEELEELEAELAEL----QEELEELLEQLSL 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665404327 484 DPEVTLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISAANRTPKLHAKMSKTMSTILVRAKLHCFQLIGWR 562
Cdd:COG4717  189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
321-478 7.05e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 7.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 321 SNLENYELQRQELISMYEhRIEELIRSQDSATSDLKRSHN-----DKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELE 395
Cdd:COG3206  226 SQLAEARAELAEAEARLA-ALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALR 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 396 KQLEDLQRKLIEHEEKQNKMylhmyQQGQEAERISRADQALDLAQRQPESKVSINELlhqlqstQDELENIRTIYRRLLE 475
Cdd:COG3206  305 AQLQQEAQRILASLEAELEA-----LQAREASLQAQLAQLEARLAELPELEAELRRL-------EREVEVARELYESLLQ 372


                 ...
gi 665404327 476 AQK 478
Cdd:COG3206  373 RLE 375
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 334-546 9.22e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 9.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   334 ISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQN 413
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   414 KMYLHMYQQGQEAERISRADQALDLAQRQPESKVS---INELLHQLQSTQDELENIRTIYRRLLEAQKNRthvdpEVTLQ 490
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaeLKELQAELEELEEELEELQEELERLEEALEEL-----REELE 471

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   491 FLKSAIFYFLTDKENSQGHLQAIESILE----FTDAEKQKISAANRTPKLHAKMSKTMST 546
Cdd:TIGR02168  472 EAEQALDAAERELAQLQARLDSLERLQEnlegFSEGVKALLKNQSGLSGILGVLSELISV 531
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
 486-527 1.03e-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: 1.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 665404327  486 EVTLQFLKSAIFYFLTDKENS-QGHL-QAIESILEFTDAEKQKI 527
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSeRKQLlPVIATLLKFSPEEEQKI 44
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 315-541 1.80e-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: 47.07  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 315 AGGDSASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYsdmvpdyEQAKQRIREL 394
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQEL-------AALEAELAEL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 395 EKQLEDLQRKLIEHEEKQNKMYLHMYQQGQ--------------EAERI---------SRADQALDLAQRQPESKVSINE 451
Cdd:COG4942   89 EKEIAELRAELEAQKEELAELLRALYRLGRqpplalllspedflDAVRRlqylkylapARREQAEELRADLAELAALRAE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 452 LLHQLQSTQDELENIRTIYRRLLEAQKNRTHVDPEVTLQFLKSAIfyFLTDKENSQGHLQAIESILEFTDAEKQKISAAN 531
Cdd:COG4942  169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA--ELAELQQEAEELEALIARLEAEAAAAAERTPAA 246

                        250
                 ....*....|
gi 665404327 532 RTPKLHAKMS 541
Cdd:COG4942  247 GFAALKGKLP 256
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 329-478 2.02e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 329 QRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEA------LLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQ 402
Cdd:COG1196  285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELeeelaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665404327 403 RKLIEHEEKqnkmylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRTIYRRLLEAQK 478
Cdd:COG1196  365 EALLEAEAE---------LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 382-548 2.89e-05

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: 47.04  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   382 PDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQ-----QGQEAERISRADQALDLAQRQPESKvsiNELLHQL 456
Cdd:pfam15921   71 PGKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidlQTKLQEMQMERDAMADIRRRESQSQ---EDLRNQL 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   457 QSTQDELENIRTIYRRLLEaqknrthvDPEVTLQFLKSAIFyfltdkeNSQGHLQAIESIL-EFTDAEKQKISAANRTPK 535
Cdd:pfam15921  148 QNTVHELEAAKCLKEDMLE--------DSNTQIEQLRKMML-------SHEGVLQEIRSILvDFEEASGKKIYEHDSMST 212

                          170
                   ....*....|....
gi 665404327   536 LHAK-MSKTMSTIL 548
Cdd:pfam15921  213 MHFRsLGSAISKIL 226
PRK05563 PRK05563
DNA polymerase III subunits gamma and tau; Validated
 319-484 5.99e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235505 [Multi-domain]  Cd Length: 559  Bit Score: 46.02  E-value: 5.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 319 SASNLENYELQRQEL-ISMYEHRIEELIRSQdsatSDLKRSHNDKV--EALLQKLAECNTRYSDMVPDYEQAKQRIRELE 395
Cdd:PRK05563 307 STENDELFKELSEKLdIERLYRMIDILNDAQ----QQIKWTNQPRIylEVALVKLCEQAAASPEYDTELEVLLQRVEQLE 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 396 KQLEDLQrklieheekqnkmylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQL-QSTQDELENIRTIYRRLL 474
Cdd:PRK05563 383 QELKQLK------------------AQPVGVAPEQKEKKKEKKKNKKKKYKVPRGKIYKVLkEATRQDLELLKNVWGEIL 444

                        170
                 ....*....|
gi 665404327 475 EAQKNRTHVD 484
Cdd:PRK05563 445 ESLKAQRKSL 454
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 358-479 8.66e-05

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: 45.45  E-value: 8.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327  358 SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEK-------QNKMYLHMYQQGQEAERIS 430
Cdd:pfam05622 301 SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKaedssllKQKLEEHLEKLHEAQSELQ 380

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 665404327  431 RADQALD-LAQRQPESK-VSINELLHQLQSTQDELENIRTIYRRLLEAQKN 479
Cdd:pfam05622 381 KKKEQIEeLEPKQDSNLaQKIDELQEALRKKDEDMKAMEERYKKYVEKAKS 431
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 324-415 2.16e-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: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   324 ENYELQRqELISMYEHRIEELIRS-QDSATSDLKRSHNDKVEALLQKLA-ECNTRYSDMVPDYEQAKQRIRELEKQLEDL 401
Cdd:smart01071  49 KNLKYEL-IMNDHLNKRIDKLLKGlREEELSPETPTYNEMLAELQDQLKkELEEANGDSEGLLEELKKHRDKLKKEQKEL 127

                           90
                   ....*....|....
gi 665404327   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 2.34e-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: 44.28  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   162 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 241
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   242 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 311
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   312 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 382
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 665404327   383 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKmyLHMYQQGQEaERISRADQALD 437
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLsEEYSLTLEEAEALENK--IEDDEEEAR-RRLKRLENKIK 982
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
321-467 2.50e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.36  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 321 SNLENYELQRQELISMYEHRIEEL--IRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 398
Cdd:COG1340    8 SSLEELEEKIEELREEIEELKEKRdeLNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 399 EDLQRKLIEHEEKQNKM---------------YLHMYQQ----GQEAER-----ISRADQALDLAQRQPESKVSINELLH 454
Cdd:COG1340   88 NELREELDELRKELAELnkaggsidklrkeieRLEWRQQtevlSPEEEKelvekIKELEKELEKAKKALEKNEKLKELRA 167

                        170
                 ....*....|...
gi 665404327 455 QLQSTQDELENIR 467
Cdd:COG1340  168 ELKELRKEAEEIH 180
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
338-480 4.92e-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: 4.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327  338 EHRIEELIRSQDSATSDlkrshNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRkliehEEKQNKMYL 417
Cdd:COG4913   667 EREIAELEAELERLDAS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE-----ELDELQDRL 736

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665404327  418 HMYQQGQEAERISRADQALD-LAQRQPESKVSiNELLHQLQSTQDELENIRTIYRRLLEAQKNR 480
Cdd:COG4913   737 EAAEDLARLELRALLEERFAaALGDAVERELR-ENLEERIDALRARLNRAEEELERAMRAFNRE 799
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
329-439 6.16e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 6.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 329 QRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEH 408
Cdd:COG4717  146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225

                         90       100       110
                 ....*....|....*....|....*....|.
gi 665404327 409 EEKQNKMYLHMYQQgQEAERISRADQALDLA 439
Cdd:COG4717  226 EEELEQLENELEAA-ALEERLKEARLLLLIA 255
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 360-465 7.37e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 7.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 360 NDKVEALLQKLAECNTRYSDmvpDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISR--ADQAL- 436
Cdd:PRK00409 515 KEKLNELIASLEELERELEQ---KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKkeADEIIk 591

                         90       100
                 ....*....|....*....|....*....
gi 665404327 437 DLAQRQPESKVSINEllHQLQSTQDELEN 465
Cdd:PRK00409 592 ELRQLQKGGYASVKA--HELIEARKRLNK 618
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
317-532 8.23e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 8.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 317 GDSASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEK 396
Cdd:COG4372    9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQL-REELEQAREELEQLEEELEQARSELEQLEEELEELNE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 397 QLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISRADQalDLAQRQPESKVSINELLHQLQSTQDELENIRTIYRRLLEA 476
Cdd:COG4372   88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ--DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 665404327 477 QKNRTHVDPEVTLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISAANR 532
Cdd:COG4372  166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 321-529 1.49e-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: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   321 SNLENYELQRQELISMYEHRIEELIRSQDSATSDL---KRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQ 397
Cdd:pfam15921  299 SQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELreaKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQ 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   398 LEDL------QRKLIEHEEKQNK---------------MYLHMYQQGQEAERISRADQAL-DLAQRQPESKVSI----NE 451
Cdd:pfam15921  379 LQKLladlhkREKELSLEKEQNKrlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMkSECQGQMERQMAAiqgkNE 458

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   452 LLHQLQSTQDELENIRTIYRRLLE--AQKNRTHVDPEVTLQFLKSAifyfltdkensqghLQAIESILEFTDAEKQKISA 529
Cdd:pfam15921  459 SLEKVSSLTAQLESTKEMLRKVVEelTAKKMTLESSERTVSDLTAS--------------LQEKERAIEATNAEITKLRS 524
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 360-479 1.59e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 360 NDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQE-------------A 426
Cdd:COG3883   36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvllgsesfS 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 665404327 427 ERISRADQALDLAQRQpeskvsiNELLHQLQSTQDELENIRTIYRRLLEAQKN 479
Cdd:COG3883  116 DFLDRLSALSKIADAD-------ADLLEELKADKAELEAKKAELEAKLAELEA 161
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 355-468 1.67e-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: 40.29  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 355 LKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQ-----NKMYLHMYQQ--GQEAE 427
Cdd:COG1579   25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYEALQKEieSLKRR 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 665404327 428 RISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRT 468
Cdd:COG1579  105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 315-493 2.80e-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: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327  315 AGGD-SASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVP--------DYE 385
Cdd:pfam03961  73 AGGNiSAKFIQNAEVEAGGDILVEKQILHSLVKAGGSIIVGGRKGKIIGGNIKAGKGVKAKELGSPAGTkteievgvDFP 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327  386 QAKQRIRELEKQLEDLQRKLIEHEEKQNKmyLHMYQQGQEAERISraDQALDLAQRQPESKVSINELLHQLQSTQDELEN 465
Cdd:pfam03961 153 ELKEKLEELEKELEELEEELEKLKKRLKK--LPKKARGQLPPEKR--EQLEKLLETKNKLSEELEELEEELKELKEELES 228

                         170       180
                  ....*....|....*....|....*...
gi 665404327  466 IRTIYRrlLEAQKnrtHVDPEVTLQFLK 493
Cdd:pfam03961 229 LLGEGK--ISVNK---TIYPGVTIQIGN 251
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 329-529 3.75e-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: 39.94  E-value: 3.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 329 QRQELISMYEHRIEELIRsqdsATSDLKRSHNDKVEALLQKLAECNtrySDMVPDYEQAKQRIRELEKQLEDLQ------ 402
Cdd:COG5185  243 SELEDLAQTSDKLEKLVE----QNTDLRLEKLGENAESSKRLNENA---NNLIKQFENTKEKIAEYTKSIDIKKatesle 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 403 ------RKLIEHEEKQNKMYLHMYQQ----GQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRtiyRR 472
Cdd:COG5185  316 eqlaaaEAEQELEESKRETETGIQNLtaeiEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTK---ES 392

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 665404327 473 LLEAQKNRTHVDPEVtLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISA 529
Cdd:COG5185  393 LDEIPQNQRGYAQEI-LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELIS 448
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 318-464 3.85e-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: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327   318 DSASNLENYELQRQELISMYEHRIEELirsqdsatsdlkrshNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQ 397
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKEIENL---------------NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665404327   398 LEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELE 464
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVE 964
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 341-525 5.83e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.43  E-value: 5.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 341 IEELIRSQDSATSDLKRSHndkveallQKLAEcntRYSDMVPDYEQAKQRI-----------RELEKQLEDLQRKLIEHE 409
Cdd:PRK04778 117 IEEDIEQILEELQELLESE--------EKNRE---EVEQLKDLYRELRKSLlanrfsfgpalDELEKQLENLEEEFSQFV 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 410 E-KQNKMYLhmyqqgQEAERISRADQALDLAQRQPESkvsINELLHQLQST-QDELENIRTIYRRLLEAQKNRTHVDPEV 487
Cdd:PRK04778 186 ElTESGDYV------EAREILDQLEEELAALEQIMEE---IPELLKELQTElPDQLQELKAGYRELVEEGYHLDHLDIEK 256

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 665404327 488 TLQFLKSAIfyfltdKENsqghLQAIESiLEFTDAEKQ 525
Cdd:PRK04778 257 EIQDLKEQI------DEN----LALLEE-LDLDEAEEK 283
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
340-479 7.00e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.74  E-value: 7.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327 340 RIEELIRSQDsaTSDLKRSHNDKveaLLQKLAECNTRYSDMVP------DYEQAKQRIRELEKQLEDLQRKLIEHEEKQN 413
Cdd:COG1340  117 EIERLEWRQQ--TEVLSPEEEKE---LVEKIKELEKELEKAKKalekneKLKELRAELKELRKEAEEIHKKIKELAEEAQ 191

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665404327 414 KMYLHMYQQGQEAERISraDQALDLAQRQPESKVSINELLHQLQSTQDELENIRTIYRRLLEAQKN 479
Cdd:COG1340  192 ELHEEMIELYKEADELR--KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRA 255
PRK11281 PRK11281
mechanosensitive channel MscK;
356-533 8.53e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.12  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327  356 KRSHNDKVEALLQKLAEcNTRysDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMylhmyqqgqEAERISRADQA 435
Cdd:PRK11281   50 KQKLLEAEDKLVQQDLE-QTL--ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL---------KDDNDEETRET 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404327  436 LD-LAQRQPESKVsiNELLHQLQSTQDELENirtiYRRLLEAQKNRthvdPEVTlqflKSAIFyfltdkENSQgHLQAIE 514
Cdd:PRK11281  118 LStLSLRQLESRL--AQTLDQLQNAQNDLAE----YNSQLVSLQTQ----PERA----QAALY------ANSQ-RLQQIR 176

                         170
                  ....*....|....*....
gi 665404327  515 SILEFTDAEKQKISAANRT 533
Cdd:PRK11281  177 NLLKGGKVGGKALRPSQRV 195
 
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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