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Conserved domains on  [gi|665404325|ref|NP_001285611|]
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quick-to-court, isoform M [Drosophila melanogaster]

Protein Classification

GRIP domain-containing protein( domain architecture ID 10477838)

GRIP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
362-594 4.33e-06

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 4.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 362 RQELISMYEHRIEELIRSQDSatsdLKRSHNDKVEALLQKLAEcntrYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHE 441
Cdd:COG4717   44 RAMLLERLEKEADELFKPQGR----KPELNLKELKELEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 442 EKQNKM-----YLHMYQQGQEAE-RISRADQALDLAQRQPEskvSINELLHQLQSTQDELENIrtiyRRLLEAQKNRTHV 515
Cdd:COG4717  116 EELEKLekllqLLPLYQELEALEaELAELPERLEELEERLE---ELRELEEELEELEAELAEL----QEELEELLEQLSL 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665404325 516 DPEVTLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISAANRTPKLHAKMSKTMSTILVRAKLHCFQLIGWR 594
Cdd:COG4717  189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-469 2.24e-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: 2.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   194 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 273
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   274 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 343
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   344 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 414
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 665404325   415 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKmyLHMYQQGQEaERISRADQALD 469
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLsEEYSLTLEEAEALENK--IEDDEEEAR-RRLKRLENKIK 982
 
Name Accession Description Interval E-value
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
362-594 4.33e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 4.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 362 RQELISMYEHRIEELIRSQDSatsdLKRSHNDKVEALLQKLAEcntrYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHE 441
Cdd:COG4717   44 RAMLLERLEKEADELFKPQGR----KPELNLKELKELEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 442 EKQNKM-----YLHMYQQGQEAE-RISRADQALDLAQRQPEskvSINELLHQLQSTQDELENIrtiyRRLLEAQKNRTHV 515
Cdd:COG4717  116 EELEKLekllqLLPLYQELEALEaELAELPERLEELEERLE---ELRELEEELEELEAELAEL----QEELEELLEQLSL 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665404325 516 DPEVTLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISAANRTPKLHAKMSKTMSTILVRAKLHCFQLIGWR 594
Cdd:COG4717  189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 366-578 9.43e-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: 9.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   366 ISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQN 445
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   446 KMYLHMYQQGQEAERISRADQALDLAQRQPESKVS---INELLHQLQSTQDELENIRTIYRRLLEAQKNRthvdpEVTLQ 522
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaeLKELQAELEELEEELEELQEELERLEEALEEL-----REELE 471

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   523 FLKSAIFYFLTDKENSQGHLQAIESILE----FTDAEKQKISAANRTPKLHAKMSKTMST 578
Cdd:TIGR02168  472 EAEQALDAAERELAQLQARLDSLERLQEnlegFSEGVKALLKNQSGLSGILGVLSELISV 531
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
 518-559 1.35e-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: 42.34  E-value: 1.35e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 665404325  518 EVTLQFLKSAIFYFLTDKENS-QGHL-QAIESILEFTDAEKQKI 559
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSeRKQLlPVIATLLKFSPEEEQKI 44
PRK05563 PRK05563
DNA polymerase III subunits gamma and tau; Validated
 351-516 6.94e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235505 [Multi-domain]  Cd Length: 559  Bit Score: 45.63  E-value: 6.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 351 SASNLENYELQRQEL-ISMYEHRIEELIRSQdsatSDLKRSHNDKV--EALLQKLAECNTRYSDMVPDYEQAKQRIRELE 427
Cdd:PRK05563 307 STENDELFKELSEKLdIERLYRMIDILNDAQ----QQIKWTNQPRIylEVALVKLCEQAAASPEYDTELEVLLQRVEQLE 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 428 KQLEDLQrklieheekqnkmylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQL-QSTQDELENIRTIYRRLL 506
Cdd:PRK05563 383 QELKQLK------------------AQPVGVAPEQKEKKKEKKKNKKKKYKVPRGKIYKVLkEATRQDLELLKNVWGEIL 444

                        170
                 ....*....|
gi 665404325 507 EAQKNRTHVD 516
Cdd:PRK05563 445 ESLKAQRKSL 454
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-469 2.24e-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: 2.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   194 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 273
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   274 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 343
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   344 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 414
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 665404325   415 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKmyLHMYQQGQEaERISRADQALD 469
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLsEEYSLTLEEAEALENK--IEDDEEEAR-RRLKRLENKIK 982
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 356-447 2.29e-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: 2.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   356 ENYELQRqELISMYEHRIEELIRS-QDSATSDLKRSHNDKVEALLQKLA-ECNTRYSDMVPDYEQAKQRIRELEKQLEDL 433
Cdd:smart01071  49 KNLKYEL-IMNDHLNKRIDKLLKGlREEELSPETPTYNEMLAELQDQLKkELEEANGDSEGLLEELKKHRDKLKKEQKEL 127

                           90
                   ....*....|....
gi 665404325   434 QRKLIEHEEKQNKM 447
Cdd:smart01071 128 RKKLDELEKEEKKK 141
 
Name Accession Description Interval E-value
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
362-594 4.33e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 4.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 362 RQELISMYEHRIEELIRSQDSatsdLKRSHNDKVEALLQKLAEcntrYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHE 441
Cdd:COG4717   44 RAMLLERLEKEADELFKPQGR----KPELNLKELKELEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 442 EKQNKM-----YLHMYQQGQEAE-RISRADQALDLAQRQPEskvSINELLHQLQSTQDELENIrtiyRRLLEAQKNRTHV 515
Cdd:COG4717  116 EELEKLekllqLLPLYQELEALEaELAELPERLEELEERLE---ELRELEEELEELEAELAEL----QEELEELLEQLSL 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665404325 516 DPEVTLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISAANRTPKLHAKMSKTMSTILVRAKLHCFQLIGWR 594
Cdd:COG4717  189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
353-510 7.45e-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: 7.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 353 SNLENYELQRQELISMYEhRIEELIRSQDSATSDLKRSHN-----DKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELE 427
Cdd:COG3206  226 SQLAEARAELAEAEARLA-ALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALR 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 428 KQLEDLQRKLIEHEEKQNKMylhmyQQGQEAERISRADQALDLAQRQPESKVSINELlhqlqstQDELENIRTIYRRLLE 507
Cdd:COG3206  305 AQLQQEAQRILASLEAELEA-----LQAREASLQAQLAQLEARLAELPELEAELRRL-------EREVEVARELYESLLQ 372


                 ...
gi 665404325 508 AQK 510
Cdd:COG3206  373 RLE 375
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 366-578 9.43e-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: 9.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   366 ISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQN 445
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   446 KMYLHMYQQGQEAERISRADQALDLAQRQPESKVS---INELLHQLQSTQDELENIRTIYRRLLEAQKNRthvdpEVTLQ 522
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaeLKELQAELEELEEELEELQEELERLEEALEEL-----REELE 471

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   523 FLKSAIFYFLTDKENSQGHLQAIESILE----FTDAEKQKISAANRTPKLHAKMSKTMST 578
Cdd:TIGR02168  472 EAEQALDAAERELAQLQARLDSLERLQEnlegFSEGVKALLKNQSGLSGILGVLSELISV 531
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
 518-559 1.35e-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: 42.34  E-value: 1.35e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 665404325  518 EVTLQFLKSAIFYFLTDKENS-QGHL-QAIESILEFTDAEKQKI 559
Cdd:pfam01465   1 GANLEYLKNVLLQFLESKESSeRKQLlPVIATLLKFSPEEEQKI 44
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 361-510 1.89e-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: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 361 QRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEA------LLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQ 434
Cdd:COG1196  285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELeeelaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665404325 435 RKLIEHEEKqnkmylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRTIYRRLLEAQK 510
Cdd:COG1196  365 EALLEAEAE---------LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 347-573 2.17e-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: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 347 AGGDSASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYsdmvpdyEQAKQRIREL 426
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQEL-------AALEAELAEL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 427 EKQLEDLQRKLIEHEEKQNKMYLHMYQQGQ--------------EAERI---------SRADQALDLAQRQPESKVSINE 483
Cdd:COG4942   89 EKEIAELRAELEAQKEELAELLRALYRLGRqpplalllspedflDAVRRlqylkylapARREQAEELRADLAELAALRAE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 484 LLHQLQSTQDELENIRTIYRRLLEAQKNRTHVDPEVTLQFLKSAIfyFLTDKENSQGHLQAIESILEFTDAEKQKISAAN 563
Cdd:COG4942  169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA--ELAELQQEAEELEALIARLEAEAAAAAERTPAA 246

                        250
                 ....*....|
gi 665404325 564 RTPKLHAKMS 573
Cdd:COG4942  247 GFAALKGKLP 256
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 414-580 2.66e-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: 47.42  E-value: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   414 PDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQ-----QGQEAERISRADQALDLAQRQPESKvsiNELLHQL 488
Cdd:pfam15921   71 PGKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidlQTKLQEMQMERDAMADIRRRESQSQ---EDLRNQL 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   489 QSTQDELENIRTIYRRLLEaqknrthvDPEVTLQFLKSAIFyfltdkeNSQGHLQAIESIL-EFTDAEKQKISAANRTPK 567
Cdd:pfam15921  148 QNTVHELEAAKCLKEDMLE--------DSNTQIEQLRKMML-------SHEGVLQEIRSILvDFEEASGKKIYEHDSMST 212

                          170
                   ....*....|....
gi 665404325   568 LHAK-MSKTMSTIL 580
Cdd:pfam15921  213 MHFRsLGSAISKIL 226
PRK05563 PRK05563
DNA polymerase III subunits gamma and tau; Validated
 351-516 6.94e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235505 [Multi-domain]  Cd Length: 559  Bit Score: 45.63  E-value: 6.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 351 SASNLENYELQRQEL-ISMYEHRIEELIRSQdsatSDLKRSHNDKV--EALLQKLAECNTRYSDMVPDYEQAKQRIRELE 427
Cdd:PRK05563 307 STENDELFKELSEKLdIERLYRMIDILNDAQ----QQIKWTNQPRIylEVALVKLCEQAAASPEYDTELEVLLQRVEQLE 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 428 KQLEDLQrklieheekqnkmylhmyQQGQEAERISRADQALDLAQRQPESKVSINELLHQL-QSTQDELENIRTIYRRLL 506
Cdd:PRK05563 383 QELKQLK------------------AQPVGVAPEQKEKKKEKKKNKKKKYKVPRGKIYKVLkEATRQDLELLKNVWGEIL 444

                        170
                 ....*....|
gi 665404325 507 EAQKNRTHVD 516
Cdd:PRK05563 445 ESLKAQRKSL 454
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 390-511 7.61e-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: 7.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325  390 SHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEK-------QNKMYLHMYQQGQEAERIS 462
Cdd:pfam05622 301 SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKaedssllKQKLEEHLEKLHEAQSELQ 380

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 665404325  463 RADQALD-LAQRQPESK-VSINELLHQLQSTQDELENIRTIYRRLLEAQKN 511
Cdd:pfam05622 381 KKKEQIEeLEPKQDSNLaQKIDELQEALRKKDEDMKAMEERYKKYVEKAKS 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-469 2.24e-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: 2.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   194 AQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSAssDAVTVREAELKTSQDVSPIVDMVDEGN 273
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   274 AKGSPRHLSRQQQQQAnhslQAMQMSAEMQSSYADSGHFED---LTMSSVHSK-----DSQTQSEACGTATPD--GEADV 343
Cdd:TIGR02168  774 EEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAeltLLNEEAANLrerleSLERRIAATERRLEDleEQIEE 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   344 GCGAGGDSASNLENYELQRQELISMYEH------RIEELIRSQDSATSDLK---RSHNDKVEALLQKLAECNTRYSDMVP 414
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLEL 929

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 665404325   415 DYEQAKQRIRELEKQL-EDLQRKLIEHEEKQNKmyLHMYQQGQEaERISRADQALD 469
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLsEEYSLTLEEAEALENK--IEDDEEEAR-RRLKRLENKIK 982
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 356-447 2.29e-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: 2.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   356 ENYELQRqELISMYEHRIEELIRS-QDSATSDLKRSHNDKVEALLQKLA-ECNTRYSDMVPDYEQAKQRIRELEKQLEDL 433
Cdd:smart01071  49 KNLKYEL-IMNDHLNKRIDKLLKGlREEELSPETPTYNEMLAELQDQLKkELEEANGDSEGLLEELKKHRDKLKKEQKEL 127

                           90
                   ....*....|....
gi 665404325   434 QRKLIEHEEKQNKM 447
Cdd:smart01071 128 RKKLDELEKEEKKK 141
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
353-499 4.05e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.59  E-value: 4.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 353 SNLENYELQRQELISMYEHRIEEL--IRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQL 430
Cdd:COG1340    8 SSLEELEEKIEELREEIEELKEKRdeLNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 431 EDLQRKLIEHEEKQNKM---------------YLHMYQQ----GQEAER-----ISRADQALDLAQRQPESKVSINELLH 486
Cdd:COG1340   88 NELREELDELRKELAELnkaggsidklrkeieRLEWRQQtevlSPEEEKelvekIKELEKELEKAKKALEKNEKLKELRA 167

                        170
                 ....*....|...
gi 665404325 487 QLQSTQDELENIR 499
Cdd:COG1340  168 ELKELRKEAEEIH 180
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
370-512 4.60e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325  370 EHRIEELIRSQDSATSDlkrshNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRkliehEEKQNKMYL 449
Cdd:COG4913   667 EREIAELEAELERLDAS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE-----ELDELQDRL 736

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665404325  450 HMYQQGQEAERISRADQALD-LAQRQPESKVSiNELLHQLQSTQDELENIRTIYRRLLEAQKNR 512
Cdd:COG4913   737 EAAEDLARLELRALLEERFAaALGDAVERELR-ENLEERIDALRARLNRAEEELERAMRAFNRE 799
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
361-471 5.89e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 361 QRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEH 440
Cdd:COG4717  146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225

                         90       100       110
                 ....*....|....*....|....*....|.
gi 665404325 441 EEKQNKMYLHMYQQgQEAERISRADQALDLA 471
Cdd:COG4717  226 EEELEQLENELEAA-ALEERLKEARLLLLIA 255
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
349-564 8.40e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 8.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 349 GDSASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRShNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEK 428
Cdd:COG4372    9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQL-REELEQAREELEQLEEELEQARSELEQLEEELEELNE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 429 QLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISRADQalDLAQRQPESKVSINELLHQLQSTQDELENIRTIYRRLLEA 508
Cdd:COG4372   88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ--DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 665404325 509 QKNRTHVDPEVTLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISAANR 564
Cdd:COG4372  166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 392-497 9.44e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.12  E-value: 9.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 392 NDKVEALLQKLAECNTRYSDmvpDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISR--ADQAL- 468
Cdd:PRK00409 515 KEKLNELIASLEELERELEQ---KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKkeADEIIk 591

                         90       100
                 ....*....|....*....|....*....
gi 665404325 469 DLAQRQPESKVSINEllHQLQSTQDELEN 497
Cdd:PRK00409 592 ELRQLQKGGYASVKA--HELIEARKRLNK 618
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 353-561 1.33e-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: 42.03  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   353 SNLENYELQRQELISMYEHRIEELIRSQDSATSDL---KRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQ 429
Cdd:pfam15921  299 SQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELreaKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQ 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   430 LEDL------QRKLIEHEEKQNK---------------MYLHMYQQGQEAERISRADQAL-DLAQRQPESKVSI----NE 483
Cdd:pfam15921  379 LQKLladlhkREKELSLEKEQNKrlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMkSECQGQMERQMAAiqgkNE 458

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   484 LLHQLQSTQDELENIRTIYRRLLE--AQKNRTHVDPEVTLQFLKSAifyfltdkensqghLQAIESILEFTDAEKQKISA 561
Cdd:pfam15921  459 SLEKVSSLTAQLESTKEMLRKVVEelTAKKMTLESSERTVSDLTAS--------------LQEKERAIEATNAEITKLRS 524
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 392-511 1.38e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 392 NDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQE-------------A 458
Cdd:COG3883   36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvllgsesfS 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 665404325 459 ERISRADQALDLAQRQpeskvsiNELLHQLQSTQDELENIRTIYRRLLEAQKN 511
Cdd:COG3883  116 DFLDRLSALSKIADAD-------ADLLEELKADKAELEAKKAELEAKLAELEA 161
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 387-500 1.86e-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: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 387 LKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQ-----NKMYLHMYQQ--GQEAE 459
Cdd:COG1579   25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYEALQKEieSLKRR 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 665404325 460 RISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRT 500
Cdd:COG1579  105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 347-525 3.01e-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: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325  347 AGGD-SASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVP--------DYE 417
Cdd:pfam03961  73 AGGNiSAKFIQNAEVEAGGDILVEKQILHSLVKAGGSIIVGGRKGKIIGGNIKAGKGVKAKELGSPAGTkteievgvDFP 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325  418 QAKQRIRELEKQLEDLQRKLIEHEEKQNKmyLHMYQQGQEAERISraDQALDLAQRQPESKVSINELLHQLQSTQDELEN 497
Cdd:pfam03961 153 ELKEKLEELEKELEELEEELEKLKKRLKK--LPKKARGQLPPEKR--EQLEKLLETKNKLSEELEELEEELKELKEELES 228

                         170       180
                  ....*....|....*....|....*...
gi 665404325  498 IRTIYRrlLEAQKnrtHVDPEVTLQFLK 525
Cdd:pfam03961 229 LLGEGK--ISVNK---TIYPGVTIQIGN 251
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 350-496 4.15e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 4.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325   350 DSASNLENYELQRQELISMYEHRIEELirsqdsatsdlkrshNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQ 429
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKEIENL---------------NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665404325   430 LEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELE 496
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVE 964
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 361-561 4.44e-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: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 361 QRQELISMYEHRIEELIRsqdsATSDLKRSHNDKVEALLQKLAECNtrySDMVPDYEQAKQRIRELEKQLEDLQ------ 434
Cdd:COG5185  243 SELEDLAQTSDKLEKLVE----QNTDLRLEKLGENAESSKRLNENA---NNLIKQFENTKEKIAEYTKSIDIKKatesle 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 435 ------RKLIEHEEKQNKMYLHMYQQ----GQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRtiyRR 504
Cdd:COG5185  316 eqlaaaEAEQELEESKRETETGIQNLtaeiEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTK---ES 392

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 665404325 505 LLEAQKNRTHVDPEVtLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISA 561
Cdd:COG5185  393 LDEIPQNQRGYAQEI-LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELIS 448
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 373-557 5.51e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.82  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 373 IEELIRSQDSATSDLKRSHND---KVEALLQKlaecntrysdmvpdYEQAKQRI-----------RELEKQLEDLQRKLI 438
Cdd:PRK04778 117 IEEDIEQILEELQELLESEEKnreEVEQLKDL--------------YRELRKSLlanrfsfgpalDELEKQLENLEEEFS 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325 439 EHEE-KQNKMYLhmyqqgQEAERISRADQALDLAQRQPESkvsINELLHQLQST-QDELENIRTIYRRLLEAQKNRTHVD 516
Cdd:PRK04778 183 QFVElTESGDYV------EAREILDQLEEELAALEQIMEE---IPELLKELQTElPDQLQELKAGYRELVEEGYHLDHLD 253

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 665404325 517 PEVTLQFLKSAIfyfltdKENsqghLQAIESiLEFTDAEKQ 557
Cdd:PRK04778 254 IEKEIQDLKEQI------DEN----LALLEE-LDLDEAEEK 283
PRK11281 PRK11281
mechanosensitive channel MscK;
388-565 9.18e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.12  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325  388 KRSHNDKVEALLQKLAEcNTRysDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMylhmyqqgqEAERISRADQA 467
Cdd:PRK11281   50 KQKLLEAEDKLVQQDLE-QTL--ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL---------KDDNDEETRET 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325  468 LD-LAQRQPESKVsiNELLHQLQSTQDELENirtiYRRLLEAQKNRthvdPEVTlqflKSAIFyfltdkENSQgHLQAIE 546
Cdd:PRK11281  118 LStLSLRQLESRL--AQTLDQLQNAQNDLAE----YNSQLVSLQTQ----PERA----QAALY------ANSQ-RLQQIR 176

                         170
                  ....*....|....*....
gi 665404325  547 SILEFTDAEKQKISAANRT 565
Cdd:PRK11281  177 NLLKGGKVGGKALRPSQRV 195
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 355-497 9.78e-03

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 38.68  E-value: 9.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325  355 LENYELQRQELismYEHRIEELIRsqdsatsdlkrshndKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDL- 433
Cdd:pfam06160 323 LNENELERVRG---LEKQLEELEK---------------RYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFk 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404325  434 -------------QRKLIE-----HE-----EKQN-----KMYLHMYQQGQeaERISRADQALDlaqrqpESKVSINELL 485
Cdd:pfam06160 385 eslqslrkdeleaREKLDEfklelREikrlvEKSNlpglpESYLDYFFDVS--DEIEDLADELN------EVPLNMDEVN 456

                         170
                  ....*....|..
gi 665404325  486 HQLQSTQDELEN 497
Cdd:pfam06160 457 RLLDEAQDDVDT 468
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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