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Conserved domains on  [gi|24582425|ref|NP_723249|]
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milton, isoform A [Drosophila melanogaster]

Protein Classification

trafficking kinesin-binding protein( domain architecture ID 12058656)

trafficking kinesin-binding protein such as human trafficking kinesin-binding protein 1 (TRAK1) that is involved in the regulation of endosome-to-lysosome trafficking, including endocytic trafficking of EGF-EGFR complexes and GABA-A receptors

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 76-375 3.14e-127

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


:

Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 390.93  E-value: 3.14e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425     76 EEQIPKYKVRNDFLtnFSGYANEDWFVPAPALPIPPEGLGLTKEQTRECLNYFLLCGNRVSQMTRAYDDIEAVTRLLEEK 155
Cdd:pfam04849    1 EEQIPPYKLRADTL--GTGYANQDWKIPSPAGRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    156 EKDLELTVQIGKELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVL-----------TNDADDGTDTDTP 224
Cdd:pfam04849   79 ERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYsndaeesetesSCSTPLRRNESFS 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    225 TMSKSITLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLMADISAQLNDANSQYDNLSLELERQREENRLQHE 304
Cdd:pfam04849  159 SLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQE 238

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582425    305 QIVNLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKR 375
Cdd:pfam04849  239 EITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 474-652 1.48e-34

Kinesin associated protein; This domain family is found in eukaryotes, and is typically between 143 and 173 amino acids in length. The family is found in association with pfam04849. This family is a region of the protein milton. Milton recruits the heavy chain of kinesin to mitochondria to allow the motor movement function of kinesin.


:

Pssm-ID: 463588  Cd Length: 171  Bit Score: 130.09  E-value: 1.48e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    474 RCAGKSGNYMDSGNVSmTQLGAmsmssssgPRMASMAYPAGSYYRG-GSNQSLGVKTLSSESLNSQSDDG---YPAQPsG 549
Cdd:pfam12448    3 RSLTPSPMNIPGSNQS-SSLTS--------MRSSSSSTPRSSYYGGdGSSISLDNRTNSILSETSSSQDSgydRPKKP-G 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    550 VPGAPGAKELEAALKRLTPA-----------EVLARRAMLSYapAGTYNYDEPMGHGTGnvrnsdlplgvrTPDSIMSTG 618
Cdd:pfam12448   73 TPGTPGARDLEAALRRLSLRrqnylserrffEEERERKLLAL--AGTYNYDEGEHGGSL------------TPNDSIMSL 138

                          170       180       190
                   ....*....|....*....|....*....|....
gi 24582425    619 SSGMSGSTNHMSASMTHQwRLPEKLQIIKPMEGS 652
Cdd:pfam12448  139 GSNHSGSSSHSSGFSSRS-YLPEKLQIVKPLEGS 171
 
Name Accession Description Interval E-value
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 76-375 3.14e-127

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 390.93  E-value: 3.14e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425     76 EEQIPKYKVRNDFLtnFSGYANEDWFVPAPALPIPPEGLGLTKEQTRECLNYFLLCGNRVSQMTRAYDDIEAVTRLLEEK 155
Cdd:pfam04849    1 EEQIPPYKLRADTL--GTGYANQDWKIPSPAGRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    156 EKDLELTVQIGKELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVL-----------TNDADDGTDTDTP 224
Cdd:pfam04849   79 ERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYsndaeesetesSCSTPLRRNESFS 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    225 TMSKSITLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLMADISAQLNDANSQYDNLSLELERQREENRLQHE 304
Cdd:pfam04849  159 SLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQE 238

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582425    305 QIVNLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKR 375
Cdd:pfam04849  239 EITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 474-652 1.48e-34

Kinesin associated protein; This domain family is found in eukaryotes, and is typically between 143 and 173 amino acids in length. The family is found in association with pfam04849. This family is a region of the protein milton. Milton recruits the heavy chain of kinesin to mitochondria to allow the motor movement function of kinesin.


Pssm-ID: 463588  Cd Length: 171  Bit Score: 130.09  E-value: 1.48e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    474 RCAGKSGNYMDSGNVSmTQLGAmsmssssgPRMASMAYPAGSYYRG-GSNQSLGVKTLSSESLNSQSDDG---YPAQPsG 549
Cdd:pfam12448    3 RSLTPSPMNIPGSNQS-SSLTS--------MRSSSSSTPRSSYYGGdGSSISLDNRTNSILSETSSSQDSgydRPKKP-G 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    550 VPGAPGAKELEAALKRLTPA-----------EVLARRAMLSYapAGTYNYDEPMGHGTGnvrnsdlplgvrTPDSIMSTG 618
Cdd:pfam12448   73 TPGTPGARDLEAALRRLSLRrqnylserrffEEERERKLLAL--AGTYNYDEGEHGGSL------------TPNDSIMSL 138

                          170       180       190
                   ....*....|....*....|....*....|....
gi 24582425    619 SSGMSGSTNHMSASMTHQwRLPEKLQIIKPMEGS 652
Cdd:pfam12448  139 GSNHSGSSSHSSGFSSRS-YLPEKLQIVKPLEGS 171
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 136-375 3.50e-10

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: 64.69  E-value: 3.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    136 SQMTRAYDDIEAVTRLLEEKEKDLEltvqigkELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVLTNDA 215
Cdd:TIGR02168  246 EELKEAEEELEELTAELQELEEKLE-------ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    216 DDGTDTDTPTMSKSIT-----------LDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEH---ERQLMADISAQLNDA 281
Cdd:TIGR02168  319 EELEAQLEELESKLDElaeelaeleekLEELKEELESLEAELEELEAELEELESRLEELEEQletLRSKVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    282 NSQYDNLSLELERQREENRLQHEQIVNLTARLAEAEMRLHQltQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLAL 361
Cdd:TIGR02168  399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ--AELEELEEELEELQEELERLEEALEELREELEEAEQA 476

                          250
                   ....*....|....
gi 24582425    362 LHSAQDQLKQQRKR 375
Cdd:TIGR02168  477 LDAAERELAQLQAR 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 232-382 2.68e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 2.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  232 LDLLQRKVNSLLDENKSLKCEATQLAHQTDEVE---EHERQLMADISAQLNDANSQYDNLSLELERQREENRLQHEQIVN 308
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582425  309 LTARLAEAEMRLHQLTQDNDEHlsllhvtKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKRSQPQARS 382
Cdd:COG1196  314 LEERLEELEEELAELEEELEEL-------EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
143-375 1.49e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.19  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425   143 DDIEAVTRLLEEKEKDLEltvqigkELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVLtndaddgtdtd 222
Cdd:PRK02224  370 SELEEAREAVEDRREEIE-------ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL----------- 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425   223 tptmskSITLDLLQRKVN---SLLDENKSLKCE--------ATQLAHQTDEVEEHERQLmADISAQLNDANSQYDNLS-- 289
Cdd:PRK02224  432 ------EATLRTARERVEeaeALLEAGKCPECGqpvegsphVETIEEDRERVEELEAEL-EDLEEEVEEVEERLERAEdl 504

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425   290 LELERQREENRLQHEQIVNLTA----RLAEAEMRLHQLTQDNDEHLSllhvTKENQNALALELVEFKQRYEEVLALLHSA 365
Cdd:PRK02224  505 VEAEDRIERLEERREDLEELIAerreTIEEKRERAEELRERAAELEA----EAEEKREAAAEAEEEAEEAREEVAELNSK 580

                         250
                  ....*....|
gi 24582425   366 QDQLKQQRKR 375
Cdd:PRK02224  581 LAELKERIES 590
 
Name Accession Description Interval E-value
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 76-375 3.14e-127

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 390.93  E-value: 3.14e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425     76 EEQIPKYKVRNDFLtnFSGYANEDWFVPAPALPIPPEGLGLTKEQTRECLNYFLLCGNRVSQMTRAYDDIEAVTRLLEEK 155
Cdd:pfam04849    1 EEQIPPYKLRADTL--GTGYANQDWKIPSPAGRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    156 EKDLELTVQIGKELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVL-----------TNDADDGTDTDTP 224
Cdd:pfam04849   79 ERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYsndaeesetesSCSTPLRRNESFS 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    225 TMSKSITLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLMADISAQLNDANSQYDNLSLELERQREENRLQHE 304
Cdd:pfam04849  159 SLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQE 238

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582425    305 QIVNLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKR 375
Cdd:pfam04849  239 EITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 474-652 1.48e-34

Kinesin associated protein; This domain family is found in eukaryotes, and is typically between 143 and 173 amino acids in length. The family is found in association with pfam04849. This family is a region of the protein milton. Milton recruits the heavy chain of kinesin to mitochondria to allow the motor movement function of kinesin.


Pssm-ID: 463588  Cd Length: 171  Bit Score: 130.09  E-value: 1.48e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    474 RCAGKSGNYMDSGNVSmTQLGAmsmssssgPRMASMAYPAGSYYRG-GSNQSLGVKTLSSESLNSQSDDG---YPAQPsG 549
Cdd:pfam12448    3 RSLTPSPMNIPGSNQS-SSLTS--------MRSSSSSTPRSSYYGGdGSSISLDNRTNSILSETSSSQDSgydRPKKP-G 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    550 VPGAPGAKELEAALKRLTPA-----------EVLARRAMLSYapAGTYNYDEPMGHGTGnvrnsdlplgvrTPDSIMSTG 618
Cdd:pfam12448   73 TPGTPGARDLEAALRRLSLRrqnylserrffEEERERKLLAL--AGTYNYDEGEHGGSL------------TPNDSIMSL 138

                          170       180       190
                   ....*....|....*....|....*....|....
gi 24582425    619 SSGMSGSTNHMSASMTHQwRLPEKLQIIKPMEGS 652
Cdd:pfam12448  139 GSNHSGSSSHSSGFSSRS-YLPEKLQIVKPLEGS 171
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 136-375 3.50e-10

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: 64.69  E-value: 3.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    136 SQMTRAYDDIEAVTRLLEEKEKDLEltvqigkELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVLTNDA 215
Cdd:TIGR02168  246 EELKEAEEELEELTAELQELEEKLE-------ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    216 DDGTDTDTPTMSKSIT-----------LDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEH---ERQLMADISAQLNDA 281
Cdd:TIGR02168  319 EELEAQLEELESKLDElaeelaeleekLEELKEELESLEAELEELEAELEELESRLEELEEQletLRSKVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    282 NSQYDNLSLELERQREENRLQHEQIVNLTARLAEAEMRLHQltQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLAL 361
Cdd:TIGR02168  399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ--AELEELEEELEELQEELERLEEALEELREELEEAEQA 476

                          250
                   ....*....|....
gi 24582425    362 LHSAQDQLKQQRKR 375
Cdd:TIGR02168  477 LDAAERELAQLQAR 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 232-382 2.68e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 2.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  232 LDLLQRKVNSLLDENKSLKCEATQLAHQTDEVE---EHERQLMADISAQLNDANSQYDNLSLELERQREENRLQHEQIVN 308
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582425  309 LTARLAEAEMRLHQLTQDNDEHlsllhvtKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKRSQPQARS 382
Cdd:COG1196  314 LEERLEELEEELAELEEELEEL-------EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 153-381 2.86e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 2.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  153 EEKEKDLELTVQIGKELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVLTNDADDGTDTDTPTMSKSITL 232
Cdd:COG1196  221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  233 dllQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLmadiSAQLNDANSQYDNLSLELERQREENRLQHEQIVNLTAR 312
Cdd:COG1196  301 ---EQDIARLEERRRELEERLEELEEELAELEEELEEL----EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24582425  313 LAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKRSQPQAR 381
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 136-356 3.27e-07

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: 54.68  E-value: 3.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    136 SQMTRAYDDIEAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVLtnda 215
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL---- 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    216 ddgtdtdtptmskSITLDLLQRKVNSLLDENKSLKCEAtqlahQTDEVEEHERQLmADISAQLNDANSQYDNLSLELERQ 295
Cdd:TIGR02168  406 -------------EARLERLEDRRERLQQEIEELLKKL-----EEAELKELQAEL-EELEEELEELQEELERLEEALEEL 466

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    296 REENRLQHEQIVNLTARLAEAEMRLHQLTQDNDEHLSLLHVTKE---NQNALA------LELVEFKQRYE 356
Cdd:TIGR02168  467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllkNQSGLSgilgvlSELISVDEGYE 536
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 152-374 5.45e-07

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 53.87  E-value: 5.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    152 LEEKEKDLEltvQIGKELlTQNN----ALEARVADLETDLKASNDDRAQLVHELHKKNELISVLtndaddgtdtdtptms 227
Cdd:TIGR04523  316 LKNQEKKLE---EIQNQI-SQNNkiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKL---------------- 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    228 ksitldllQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLmaDIsaQLNDANSQYDNLSLELERQREENRLQHEQIV 307
Cdd:TIGR04523  376 --------KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK--DE--QIKKLQQEKELLEKEIERLKETIIKNNSEIK 443

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582425    308 NLTARLAEAEM---RLHQLTQDNDEHLSLL--HVTKENQNalaLELV--EFKQRYEEVLAlLHSAQDQLKQQRK 374
Cdd:TIGR04523  444 DLTNQDSVKELiikNLDNTRESLETQLKVLsrSINKIKQN---LEQKqkELKSKEKELKK-LNEEKKELEEKVK 513
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 146-382 7.03e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 7.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  146 EAVTRLLEEKEKDLELTVQIgKELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVLTNDADDGTDTDTPT 225
Cdd:COG1196  264 ELEAELEELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  226 MSKSITLD-LLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLMADISAQLNDAN------SQYDNLSLELERQREE 298
Cdd:COG1196  343 EEELEEAEeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleeleEAEEALLERLERLEEE 422

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  299 NRLQHEQIVNLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELvefkQRYEEVLALLHSAQDQLKQQRKRSQP 378
Cdd:COG1196  423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA----ALLEAALAELLEELAEAAARLLLLLE 498


                 ....
gi 24582425  379 QARS 382
Cdd:COG1196  499 AEAD 502
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 143-371 1.09e-06

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: 53.15  E-value: 1.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    143 DDIEAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVADLETDL----KASNDDRAQLVHE-LHKKNELISVLTndadd 217
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhkleEALNDLEARLSHSrIPEIQAELSKLE----- 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    218 gtdtdtptmsksitlDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQlMADISAQLNDANSQYDNLSLELERQRE 297
Cdd:TIGR02169  805 ---------------EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLNGKKEELEE 868

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582425    298 EnrlqheqIVNLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQ 371
Cdd:TIGR02169  869 E-------LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
232-382 1.28e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  232 LDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLMADIsaqlndANSQYDNLSlELERQREENRLQHEQIVNLTA 311
Cdd:COG4913  290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI------RGNGGDRLE-QLEREIERLERELEERERRRA 362

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582425  312 RLAEAemrLHQLtqdndeHLSLLHvTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKRSQPQARS 382
Cdd:COG4913  363 RLEAL---LAAL------GLPLPA-SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 147-402 8.95e-06

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: 49.38  E-value: 8.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  147 AVTRLLEEKEKDLELTVQIGKELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVLTNdaddgtdtdtptm 226
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA------------- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  227 sksiTLDLLQRKVNSLldeNKSLKCEATQLAHQTDEVEEHERQ------LMADISAQLNDANSQYDNLSLELERQREENR 300
Cdd:COG4942   84 ----ELAELEKEIAEL---RAELEAQKEELAELLRALYRLGRQpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  301 LQHEQIVNLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKRSQPQA 380
Cdd:COG4942  157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236

                        250       260
                 ....*....|....*....|..
gi 24582425  381 RSSFLGGLGTSGAGMGGSLFPP 402
Cdd:COG4942  237 AAAAERTPAAGFAALKGKLPWP 258
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
133-372 9.00e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 9.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  133 NRVSQMTRAYDDIEAVTRLLEEKEK---DLELTVQIGKELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELIs 209
Cdd:COG4913  651 QRLAEYSWDEIDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL- 729

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  210 vltndaddgtdtdtptmsksitlDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLMADISAQLNDANSQYDNLS 289
Cdd:COG4913  730 -----------------------DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAE 786

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  290 LELERQREE-NRLQHEQIVNLTARLAEAEM---RLHQLTQDNdehlsllhvtkenqnalaleLVEFKQRYEEvlaLLHSA 365
Cdd:COG4913  787 EELERAMRAfNREWPAETADLDADLESLPEylaLLDRLEEDG--------------------LPEYEERFKE---LLNEN 843


                 ....*..
gi 24582425  366 QDQLKQQ 372
Cdd:COG4913  844 SIEFVAD 850
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
172-379 9.81e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 9.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  172 QNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVLTNDAddgtdtdtptmsKSITLDLLQRKVNSLLDENK--SL 249
Cdd:COG4717  317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE------------EELQLEELEQEIAALLAEAGveDE 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  250 KcEATQLAHQTDEVEEHERQLmADISAQLNDANS---------QYDNLSLELERQREENRLQHEQIVNLTARLAEAEMRL 320
Cdd:COG4717  385 E-ELRAALEQAEEYQELKEEL-EELEEQLEELLGeleellealDEEELEEELEELEEELEELEEELEELREELAELEAEL 462

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24582425  321 HQLTQDNDehLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRkrsQPQ 379
Cdd:COG4717  463 EQLEEDGE--LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER---LPP 516
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 245-377 1.19e-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: 49.30  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    245 ENKSLKCEAtqlahqtdevEEHERQLMADISAQLNDANSQYDNLslelerqREENRLQHEQIVNLTARLAEAEMRLHQLT 324
Cdd:pfam05622  290 ENKMLRLGQ----------EGSYRERLTELQQLLEDANRRKNEL-------ETQNRLANQRILELQQQVEELQKALQEQG 352

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 24582425    325 QDNDEHLSLlhvtkenqnalalelvefKQRYEEVLALLHSAQDQLkqQRKRSQ 377
Cdd:pfam05622  353 SKAEDSSLL------------------KQKLEEHLEKLHEAQSEL--QKKKEQ 385
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
135-362 2.99e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  135 VSQMTRAYDDIEAVTRLLEEKEKDLEltvQIGKELLTQNN---ALEARVADLETDLKASNDDRAQLVHELHKKNElisvl 211
Cdd:COG4372   37 LFELDKLQEELEQLREELEQAREELE---QLEEELEQARSeleQLEEELEELNEQLQAAQAELAQAQEELESLQE----- 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  212 tndaddgtdtdtptmsksiTLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEeherQLMADISAQLNDANSQYDNLSLE 291
Cdd:COG4372  109 -------------------EAEELQEELEELQKERQDLEQQRKQLEAQIAELQ----SEIAEREEELKELEEQLESLQEE 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582425  292 LERQREENRlqheqivnlTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALL 362
Cdd:COG4372  166 LAALEQELQ---------ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
157-341 3.08e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 3.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  157 KDLELTVQIGKELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVLTNDADDGTDTDtptmsksiTLDLLQ 236
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA--------ELAELP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  237 RKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLmADISAQLNDANSQydnlslELERQREENRLQHEQIVNLTARLAEA 316
Cdd:COG4717  146 ERLEELEERLEELRELEEELEELEAELAELQEEL-EELLEQLSLATEE------ELQDLAEELEELQQRLAELEEELEEA 218

                        170       180
                 ....*....|....*....|....*
gi 24582425  317 EMRLHQLTQDNDEHLSLLHVTKENQ 341
Cdd:COG4717  219 QEELEELEEELEQLENELEAAALEE 243
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 232-375 3.95e-05

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: 46.46  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  232 LDLLQRKVNSLLDENKSLKceaTQLAHQTDEVEEHeRQLMADISAQLNDANS--QYDNLSLELERQREENRLQHEQIVNL 309
Cdd:COG1579   40 LAALEARLEAAKTELEDLE---KEIKRLELEIEEV-EARIKKYEEQLGNVRNnkEYEALQKEIESLKRRISDLEDEILEL 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582425  310 TARLAEAEMRLHQLtqdndehlsllhvtKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKR 375
Cdd:COG1579  116 MERIEELEEELAEL--------------EAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 143-388 6.47e-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: 46.68  E-value: 6.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  143 DDIEAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVLTNDADDGTDTd 222
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  223 tptmsksitLDLLQRKVNSLLDEN-KSLKCEATQLAHQTDEVEEHER--QLMADISAQLNDANSQYDNLSLELERQREEN 299
Cdd:COG4942   99 ---------LEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRrlQYLKYLAPARREQAEELRADLAELAALRAEL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  300 RLQHEQivnLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKRSQPQ 379
Cdd:COG4942  170 EAERAE---LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246


                 ....*....
gi 24582425  380 ARSSFLGGL 388
Cdd:COG4942  247 GFAALKGKL 255
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 235-377 1.15e-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: 46.59  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    235 LQRKVNSLldENKSLKceATQLAHQTDEVEEHERQLMADisaQLNDANSQYDNLSLELER-QREENRLQ------HEQIV 307
Cdd:TIGR02168  198 LERQLKSL--ERQAEK--AERYKELKAELRELELALLVL---RLEELREELEELQEELKEaEEELEELTaelqelEEKLE 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    308 NLTARLAEAEMRLHQLTQDNDEHLSLLH-------VTKE-------NQNALALELVEFKQRYEEVLALLHSAQDQLKQQR 373
Cdd:TIGR02168  271 ELRLEVSELEEEIEELQKELYALANEISrleqqkqILRErlanlerQLEELEAQLEELESKLDELAEELAELEEKLEELK 350


                   ....
gi 24582425    374 KRSQ 377
Cdd:TIGR02168  351 EELE 354
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
143-375 1.49e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.19  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425   143 DDIEAVTRLLEEKEKDLEltvqigkELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVLtndaddgtdtd 222
Cdd:PRK02224  370 SELEEAREAVEDRREEIE-------ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL----------- 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425   223 tptmskSITLDLLQRKVN---SLLDENKSLKCE--------ATQLAHQTDEVEEHERQLmADISAQLNDANSQYDNLS-- 289
Cdd:PRK02224  432 ------EATLRTARERVEeaeALLEAGKCPECGqpvegsphVETIEEDRERVEELEAEL-EDLEEEVEEVEERLERAEdl 504

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425   290 LELERQREENRLQHEQIVNLTA----RLAEAEMRLHQLTQDNDEHLSllhvTKENQNALALELVEFKQRYEEVLALLHSA 365
Cdd:PRK02224  505 VEAEDRIERLEERREDLEELIAerreTIEEKRERAEELRERAAELEA----EAEEKREAAAEAEEEAEEAREEVAELNSK 580

                         250
                  ....*....|
gi 24582425   366 QDQLKQQRKR 375
Cdd:PRK02224  581 LAELKERIES 590
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 133-514 2.43e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  133 NRVSQMTRAYDDIEA-VTRLLEEKEkdlELTVQIgKELLTQNNALEARVADLETDLKASNDDRAQLVHELhkkNELISVL 211
Cdd:COG3883   23 KELSELQAELEAAQAeLDALQAELE---ELNEEY-NELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARAL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  212 TNDADDGTDTDTPTMSKSITlDLLQRkvnslldenkslkceatqlAHQTDEVEEHERQLMADISAQLNDANSQYDNLSLE 291
Cdd:COG3883   96 YRSGGSVSYLDVLLGSESFS-DFLDR-------------------LSALSKIADADADLLEELKADKAELEAKKAELEAK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  292 LERQREENRLQHEQIVNLTARLAEAEMRLHQLTQDNDEHLSLLhVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQ 371
Cdd:COG3883  156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL-AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  372 QRKRSQPQARSSFLGGLGTSGAGMGGSLFPPDSLHCElmESSLYSENSLDSGISGDSQRSADRISRMMMHMPSGGMSSST 451
Cdd:COG3883  235 AAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA--AGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGG 312

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582425  452 MGGSVYAGAGNVPPYKRVFDTVRCAGKSGNYMDSGNVSMTQLGAMSMSSSSGPRMASMAYPAG 514
Cdd:COG3883  313 VGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGY 375
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 235-380 3.43e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.78  E-value: 3.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    235 LQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLmadiSAQLNDANSQYDnlslELERQREE-----NRLQHEqIVNL 309
Cdd:pfam01576  375 LEKAKQALESENAELQAELRTLQQAKQDSEHKRKKL----EGQLQELQARLS----ESERQRAElaeklSKLQSE-LESV 445

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    310 TARLAEAEMRLHQLTQDNDEHLSLLHVTKE---------------------NQNALALELVEFKQRYEEVLALLHSAQDQ 368
Cdd:pfam01576  446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQEllqeetrqklnlstrlrqledERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525

                          170
                   ....*....|..
gi 24582425    369 LKQQRKRSQPQA 380
Cdd:pfam01576  526 LSDMKKKLEEDA 537
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
146-375 5.19e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425   146 EAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVADLETDLKasnddraqlvhELHKKNELISVltndaddgtdtdtpt 225
Cdd:PRK03918  189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-----------ELEELKEEIEE--------------- 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425   226 msksitldlLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLMADI--SAQLNDANSQYDNLSLELERQREENRLQH 303
Cdd:PRK03918  243 ---------LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEEYLDELREIE 313

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582425   304 EQIVNLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALAlELVEFKQRYEEVLALLhsaqDQLKQQRKR 375
Cdd:PRK03918  314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE-ELEERHELYEEAKAKK----EELERLKKR 380
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 119-325 1.05e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    119 EQTRECLNyfllcgNRVSQMTRAYDDIEavtRLLEEKEKDLELTVQIGKELLTQNNALEARVADLETDLKASNDDRAQLV 198
Cdd:TIGR04523  460 DNTRESLE------TQLKVLSRSINKIK---QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    199 HELHKKNELISVLTND-ADDGTDTDTPTMSKSItlDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEhERQlmaDISAQ 277
Cdd:TIGR04523  531 SEKKEKESKISDLEDElNKDDFELKKENLEKEI--DEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK-EKK---DLIKE 604

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 24582425    278 LndanSQYDNLSLELERQREENRLQHEQIVNLTARLAEAEMRLHQLTQ 325
Cdd:TIGR04523  605 I----EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 117-377 1.06e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    117 TKEQTRECLNYFLLCGNRVSQMTRAYDDIEAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVADLETDLKASNDDRAQ 196
Cdd:TIGR04523  164 LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    197 LVHELHKKnelisvltndaddgtdtdtptmsksitldllQRKVNSLLDENKSLKceaTQLAHQTDEVEEHERQLmADISA 276
Cdd:TIGR04523  244 KTTEISNT-------------------------------QTQLNQLKDEQNKIK---KQLSEKQKELEQNNKKI-KELEK 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    277 QLNDANSQYdnlsLELERQREEN---------RLQHEQIVNLTARLAEAEMRLHQLTQD-----------NDEHLSLLHV 336
Cdd:TIGR04523  289 QLNQLKSEI----SDLNNQKEQDwnkelkselKNQEKKLEEIQNQISQNNKIISQLNEQisqlkkeltnsESENSEKQRE 364

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 24582425    337 TKENQNALALELVEFKQRYEEVLALLHSAQD---QLKQQRKRSQ 377
Cdd:TIGR04523  365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDlesKIQNQEKLNQ 408
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
271-377 1.07e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  271 MADISAQLNDANSQYDNLSLELERQREENRLQHEQIVNLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVE 350
Cdd:COG4372   40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119

                         90       100
                 ....*....|....*....|....*..
gi 24582425  351 FKQRYEEvlalLHSAQDQLKQQRKRSQ 377
Cdd:COG4372  120 LQKERQD----LEQQRKQLEAQIAELQ 142
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 252-375 1.26e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  252 EATQLAHQtdeVEEHERQLmADISAQLNDANSQYDNLSLELERQREENRLQHEQIVNLTARLAEAEMRLHQLTqDNDEHL 331
Cdd:COG1579   18 ELDRLEHR---LKELPAEL-AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-NNKEYE 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 24582425  332 SLLH---VTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKR 375
Cdd:COG1579   93 ALQKeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
136-381 1.27e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.21  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  136 SQMTRAYDDIEAVTRLLEE-KEKDLELTVQIgKELLTQNNALEARVADLETDLKASNDDRAQLVHELH----KKNEL--- 207
Cdd:COG1340    8 SSLEELEEKIEELREEIEElKEKRDELNEEL-KELAEKRDELNAQVKELREEAQELREKRDELNEKVKelkeERDELnek 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  208 ISVLTNDADDGTDTDTPTMSKSITLDLLQRKVNSLLDEnkslkceatqlaHQTDEVE-EHERQLMADISA---------Q 277
Cdd:COG1340   87 LNELREELDELRKELAELNKAGGSIDKLRKEIERLEWR------------QQTEVLSpEEEKELVEKIKElekelekakK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  278 LNDANSQYDNLSLELERQREENRLQHEQIVNLTARLAEA--EM-----RLHQLTQDNDEhlslLHVT-KENQNALALELV 349
Cdd:COG1340  155 ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELheEMielykEADELRKEADE----LHKEiVEAQEKADELHE 230

                        250       260       270
                 ....*....|....*....|....*....|..
gi 24582425  350 EFKQRYEEvlalLHSAQDQLKQQRKRSQPQAR 381
Cdd:COG1340  231 EIIELQKE----LRELRKELKKLRKKQRALKR 258
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 137-377 1.37e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    137 QMTRAYDDIEAVTRLLEEKEKDL--EL-TVQIGK-ELLTQNNALEARVADLETDLKASNDDRAQLVHELHK-KNELISVl 211
Cdd:pfam01576  367 QAKRNKANLEKAKQALESENAELqaELrTLQQAKqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKlQSELESV- 445

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    212 tndaddgTDTDTPTMSKSITLdllQRKVNSLldenkslkceATQLaHQTDEVEEHERQLMADISAQLNDANSQYDNLSLE 291
Cdd:pfam01576  446 -------SSLLNEAEGKNIKL---SKDVSSL----------ESQL-QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQ 504

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    292 LERQREENRLQHEQIVNLTARLAEAEMRLhqltqdnDEHLSLLHVTKENQNALALELVEFKQRYEEVLAllhsAQDQLKQ 371
Cdd:pfam01576  505 LEEEEEAKRNVERQLSTLQAQLSDMKKKL-------EEDAGTLEALEEGKKRLQRELEALTQQLEEKAA----AYDKLEK 573


                   ....*.
gi 24582425    372 QRKRSQ 377
Cdd:pfam01576  574 TKNRLQ 579
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 137-365 2.01e-03

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 41.17  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    137 QMTRAYDDIEAVTRLLEEKEKDLEltvqigkELLTQNNALEARVADLETDLKASNDDRAQLVHEL---HKKNElisvltn 213
Cdd:pfam00261    9 ELDEAEERLKEAMKKLEEAEKRAE-------KAEAEVAALNRRIQLLEEELERTEERLAEALEKLeeaEKAAD------- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    214 daddgtdtDTPTMSKSItldllqrKVNSLLDENK------SLKcEATQLAHQTDE-VEEHERQLmADISAQLNDANSQYD 286
Cdd:pfam00261   75 --------ESERGRKVL-------ENRALKDEEKmeileaQLK-EAKEIAEEADRkYEEVARKL-VVVEGDLERAEERAE 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    287 ------------------NL-SLELER----QREEnrLQHEQIVNLTARLAEAEMRLHQLTQdndehlSLLHVTKENqNA 343
Cdd:pfam00261  138 laeskiveleeelkvvgnNLkSLEASEekasERED--KYEEQIRFLTEKLKEAETRAEFAER------SVQKLEKEV-DR 208

                          250       260
                   ....*....|....*....|..
gi 24582425    344 LALELVEFKQRYEEVLALLHSA 365
Cdd:pfam00261  209 LEDELEAEKEKYKAISEELDQT 230
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 133-371 2.10e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    133 NRVSQMTRaydDIEAVTRLLEEKE---KDLELT----VQIGKELLTQNNALEARVADLETDLKASNDdraqlvhelhKKN 205
Cdd:TIGR04523   33 TEEKQLEK---KLKTIKNELKNKEkelKNLDKNlnkdEEKINNSNNKIKILEQQIKDLNDKLKKNKD----------KIN 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    206 ELISvltndaddgtdtdtptmsksitlDLlqRKVNSLLD---ENKS-LKCEATQLAHQTDEVEEHERQLMADI---SAQL 278
Cdd:TIGR04523  100 KLNS-----------------------DL--SKINSEIKndkEQKNkLEVELNKLEKQKKENKKNIDKFLTEIkkkEKEL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    279 NDANSQYDNL-----SLELERQREENRLQHEQ--IVNLTARLAEAEMRLHQL---TQDNDEHLSLLHVTKENQNALALEL 348
Cdd:TIGR04523  155 EKLNNKYNDLkkqkeELENELNLLEKEKLNIQknIDKIKNKLLKLELLLSNLkkkIQKNKSLESQISELKKQNNQLKDNI 234

                          250       260
                   ....*....|....*....|...
gi 24582425    349 VEFKQRYEEVLALLHSAQDQLKQ 371
Cdd:TIGR04523  235 EKKQQEINEKTTEISNTQTQLNQ 257
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
143-375 2.29e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425   143 DDIEAVTRLLEE-KEKDLELTVQIG--KELLTQNNALEARVADLETDLKASNDDRAQLVHELHKK-----NELISVLTNd 214
Cdd:PRK03918  518 EELEKKAEEYEKlKEKLIKLKGEIKslKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesvEELEERLKE- 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425   215 addgtdtdtptmsksitLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQL------MADISAQLNDANSQYDnl 288
Cdd:PRK03918  597 -----------------LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELaetekrLEELRKELEELEKKYS-- 657

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425   289 slelerqREENRLQHEQIVNLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENqnalalelVEFKQRYEEVLALLHSAQDQ 368
Cdd:PRK03918  658 -------EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE--------LEEREKAKKELEKLEKALER 722


                  ....*..
gi 24582425   369 LKQQRKR 375
Cdd:PRK03918  723 VEELREK 729
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 149-380 2.61e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    149 TRLLEEKEKDLELTVQIGKELLTQNNalEARVADLETDLKASNDDRAQLVHELHKKNELISVLTNDADDGTDTDTPTMSK 228
Cdd:TIGR00618  653 LTLTQERVREHALSIRVLPKELLASR--QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    229 SITL----DLLQRKVNSLLDENKslkceaTQLAHQTDEVEEHERQLMADIsaQLNDansQYDNLSLELERQREenrlQHE 304
Cdd:TIGR00618  731 GSDLaareDALNQSLKELMHQAR------TVLKARTEAHFNNNEEVTAAL--QTGA---ELSHLAAEIQFFNR----LRE 795

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582425    305 QIVNLTARLaEAEMRLHQltqDNDEHLSLLHVTKENQnalalELVEFKQRYEEVLALLHSAQDQLKQQRKRSQPQA 380
Cdd:TIGR00618  796 EDTHLLKTL-EAEIGQEI---PSDEDILNLQCETLVQ-----EEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 243-329 3.17e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 40.27  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    243 LDENKSLKCEATQLahqtDEVEEHERQLMADISAQlndansqYDNLSLELERQREENRLQHEQIV----------NLTAR 312
Cdd:pfam13851   25 LELIKSLKEEIAEL----KKKEERNEKLMSEIQQE-------NKRLTEPLQKAQEEVEELRKQLEnyekdkqslkNLKAR 93

                           90
                   ....*....|....*..
gi 24582425    313 LAEAEMRLHQLTQDNDE 329
Cdd:pfam13851   94 LKVLEKELKDLKWEHEV 110
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 234-380 3.31e-03

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 40.84  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    234 LLQRKVNSLLDENKSLKceatqlaHQTDEVEEHERQLMADISAQLNDANsqydnlSLELERQREENRLQHEQIVN-LTAR 312
Cdd:pfam15294  130 LLHMEIERLKEENEKLK-------ERLKTLESQATQALDEKSKLEKALK------DLQKEQGAKKDVKSNLKEISdLEEK 196

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582425    313 LAEAEMRLHQltqdndehlsLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLkqQRKRSQPQA 380
Cdd:pfam15294  197 MAALKSDLEK----------TLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKEL--EKKFQQTAA 252
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 254-374 3.58e-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: 3.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  254 TQLAHQTDEVEEHERQLmADISAQLNDANSQYDNLSLELERQREENRLQHEQIVNLTARLAEAEMRLHQLTQDNDEHLSL 333
Cdd:COG3883   16 PQIQAKQKELSELQAEL-EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 24582425  334 LHVTKENQNALAL-----ELVEFKQRYEEVLALLHSAQDQLKQQRK 374
Cdd:COG3883   95 LYRSGGSVSYLDVllgseSFSDFLDRLSALSKIADADADLLEELKA 140
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 231-357 6.24e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 6.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425    231 TLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLMADISAQLNDANSQYDNLSLELERQREENRLQHEqivnLT 310
Cdd:TIGR00618  571 SFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK----LT 646

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 24582425    311 ARLAEAEmrlhQLTQDNDEHLSLLhvTKENQnALALELVEFKQRYEE 357
Cdd:TIGR00618  647 ALHALQL----TLTQERVREHALS--IRVLP-KELLASRQLALQKMQ 686
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 226-339 6.33e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425  226 MSKSITLDLLQRKVNSLLDENKSLKcEATQLAHQtDEVEEHERQLmADISAQLNDANSQYDN---LSLELERQREENRLQ 302
Cdd:COG0542  407 DSKPEELDELERRLEQLEIEKEALK-KEQDEASF-ERLAELRDEL-AELEEELEALKARWEAekeLIEEIQELKEELEQR 483

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 24582425  303 HEQIVNLTARLAEAEMRLHQLTQDNDEhlsllHVTKE 339
Cdd:COG0542  484 YGKIPELEKELAELEEELAELAPLLRE-----EVTEE 515
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
140-373 9.45e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 9.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425   140 RAYDDIEAVTRLLEEKEKDLE-LTVQIG----KELLTQNNALEARVADLETDLKASNDDR---------AQLVHELHK-K 204
Cdd:PRK02224  170 RASDARLGVERVLSDQRGSLDqLKAQIEekeeKDLHERLNGLESELAELDEEIERYEEQReqaretrdeADEVLEEHEeR 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425   205 NELISVLTNDADDGTDTDTPTMSKSITLD----LLQRKVNSLLDENKSLKCEA--------------TQLAHQTDEVEEH 266
Cdd:PRK02224  250 REELETLEAEIEDLRETIAETEREREELAeevrDLRERLEELEEERDDLLAEAglddadaeavearrEELEDRDEELRDR 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582425   267 ERQLMADISAQLNDANSQYDN-----------------LSLELERQREENRLQHEQIVNLTARLAEAEMRLHQLTQDNDE 329
Cdd:PRK02224  330 LEECRVAAQAHNEEAESLREDaddleeraeelreeaaeLESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGN 409

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 24582425   330 HLSLLHVTKENQNALalelvefKQRYEEVLALLHSAQDQLKQQR 373
Cdd:PRK02224  410 AEDFLEELREERDEL-------REREAELEATLRTARERVEEAE 446
 
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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