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Conserved domains on  [gi|194114924|gb|EDW36967|]
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GL25982 [Drosophila persimilis]

Protein Classification

HAP1_N and Milton domain-containing protein; trafficking kinesin-binding protein( domain architecture ID 11794712)

HAP1_N and Milton domain-containing protein; 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 super family cl25919
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 135-394 3.47e-103

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.


The actual alignment was detected with superfamily member pfam04849:

Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 327.37  E-value: 3.47e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   135 ETLEQQNEQLLMEVLCGNRVSQMTRAYDDIEAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVTDLEADLKSSNDDRS 214
Cdd:pfam04849   39 LSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEIL 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   215 QLLHELHKKNELISVLTNDADDGTDTETPTM-----------SKSITLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVE 283
Cdd:pfam04849  119 QLRHELSKKDDLLQIYSNDAEESETESSCSTplrrnesfsslHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYE 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   284 EHERQLMADIGAQLHDANSQYDNLSLECERQREENRLQHEQIVSLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNAL 363
Cdd:pfam04849  199 EKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQL 278

                          250       260       270
                   ....*....|....*....|....*....|.
gi 194114924   364 ALELVEFKQRYEEVLALLHSAQDQLKQQRKR 394
Cdd:pfam04849  279 TSELQELQDRYAECLGMLHEAQEELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 490-668 6.13e-38

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: 140.11  E-value: 6.13e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   490 RCAGKSGNYMDSGNVSmTTLGAmsmssssgPRMASMAYPAGSYYRG-GGNQSLGVKTLSNESLNSQSDDG---YPAQPsG 565
Cdd:pfam12448    3 RSLTPSPMNIPGSNQS-SSLTS--------MRSSSSSTPRSSYYGGdGSSISLDNRTNSILSETSSSQDSgydRPKKP-G 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   566 VPGAPGARELEAALKRLTPG-----------EVLARRAMLSYApiGTYNYDEPTmHGGAGasnsnlplgvrTP-DSIMST 633
Cdd:pfam12448   73 TPGTPGARDLEAALRRLSLRrqnylserrffEEERERKLLALA--GTYNYDEGE-HGGSL-----------TPnDSIMSL 138

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 194114924   634 GSSRmSASSNNMSASMTHQwRLPEKLQIIKPMEGS 668
Cdd:pfam12448  139 GSNH-SGSSSHSSGFSSRS-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 ...
 135-394 3.47e-103

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: 327.37  E-value: 3.47e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   135 ETLEQQNEQLLMEVLCGNRVSQMTRAYDDIEAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVTDLEADLKSSNDDRS 214
Cdd:pfam04849   39 LSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEIL 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   215 QLLHELHKKNELISVLTNDADDGTDTETPTM-----------SKSITLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVE 283
Cdd:pfam04849  119 QLRHELSKKDDLLQIYSNDAEESETESSCSTplrrnesfsslHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYE 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   284 EHERQLMADIGAQLHDANSQYDNLSLECERQREENRLQHEQIVSLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNAL 363
Cdd:pfam04849  199 EKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQL 278

                          250       260       270
                   ....*....|....*....|....*....|.
gi 194114924   364 ALELVEFKQRYEEVLALLHSAQDQLKQQRKR 394
Cdd:pfam04849  279 TSELQELQDRYAECLGMLHEAQEELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 490-668 6.13e-38

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: 140.11  E-value: 6.13e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   490 RCAGKSGNYMDSGNVSmTTLGAmsmssssgPRMASMAYPAGSYYRG-GGNQSLGVKTLSNESLNSQSDDG---YPAQPsG 565
Cdd:pfam12448    3 RSLTPSPMNIPGSNQS-SSLTS--------MRSSSSSTPRSSYYGGdGSSISLDNRTNSILSETSSSQDSgydRPKKP-G 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   566 VPGAPGARELEAALKRLTPG-----------EVLARRAMLSYApiGTYNYDEPTmHGGAGasnsnlplgvrTP-DSIMST 633
Cdd:pfam12448   73 TPGTPGARDLEAALRRLSLRrqnylserrffEEERERKLLALA--GTYNYDEGE-HGGSL-----------TPnDSIMSL 138

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 194114924   634 GSSRmSASSNNMSASMTHQwRLPEKLQIIKPMEGS 668
Cdd:pfam12448  139 GSNH-SGSSSHSSGFSSRS-YLPEKLQIVKPLEGS 171
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 163-393 6.19e-09

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: 60.42  E-value: 6.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   163 DIEAVTRLLEEKEKDLEltvQIGKELLTQNNALEARVT-DLEADLKSSNDDRSQLLHELHKKNELISVLTNDADD----G 237
Cdd:TIGR04523  275 ELEQNNKKIKELEKQLN---QLKSEISDLNNQKEQDWNkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQlkkeL 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   238 TDTETPTMSKSITLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVE---EHERQLMADIGAQLHDANSQYDNLSLECERQ 314
Cdd:TIGR04523  352 TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLEskiQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   315 REENRLQHEQIVSLTARLAEAEM---RLHQLTQDNDEHLSLLHVT-KENQNALALELVEFKQRYEEVLAlLHSAQDQLKQ 390
Cdd:TIGR04523  432 KETIIKNNSEIKDLTNQDSVKELiikNLDNTRESLETQLKVLSRSiNKIKQNLEQKQKELKSKEKELKK-LNEEKKELEE 510


                   ...
gi 194114924   391 QRK 393
Cdd:TIGR04523  511 KVK 513
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 163-396 3.03e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  163 DIEAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVTDLEADLKSSNDDRSQLLHELHKKNELISVLTNDADDGTDTET 242
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  243 PTMSKSITL-DLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLmADIGAQLHDANSQYDNLSLECERQREENRLQ 321
Cdd:COG1196   306 RLEERRRELeERLEELEEELAELEEELEELEEELEELEEELEEAEEEL-EEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194114924  322 HEQIVSLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKRSQ 396
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
159-336 1.01e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  159 RAYDDIEAVTRLLEEKEKDLE-LTVQIG----KELLTQNNALEARVTDLEADLKSSNDDRSQ----------LLHELHKK 223
Cdd:PRK02224  170 RASDARLGVERVLSDQRGSLDqLKAQIEekeeKDLHERLNGLESELAELDEEIERYEEQREQaretrdeadeVLEEHEER 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  224 NELISVLTNDADDGTDTETPTMSKSITLD----LLQRKVNSLLDENKSLKCEA-------TQLAHQTDEVEEHE---RQL 289
Cdd:PRK02224  250 REELETLEAEIEDLRETIAETEREREELAeevrDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDeelRDR 329

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 194114924  290 MADIGAQLHDANSQYDNLSLECERQREENRLQHEQIVSLTARLAEAE 336
Cdd:PRK02224  330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
 
Name Accession Description Interval E-value
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 135-394 3.47e-103

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: 327.37  E-value: 3.47e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   135 ETLEQQNEQLLMEVLCGNRVSQMTRAYDDIEAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVTDLEADLKSSNDDRS 214
Cdd:pfam04849   39 LSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEIL 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   215 QLLHELHKKNELISVLTNDADDGTDTETPTM-----------SKSITLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVE 283
Cdd:pfam04849  119 QLRHELSKKDDLLQIYSNDAEESETESSCSTplrrnesfsslHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYE 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   284 EHERQLMADIGAQLHDANSQYDNLSLECERQREENRLQHEQIVSLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNAL 363
Cdd:pfam04849  199 EKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQL 278

                          250       260       270
                   ....*....|....*....|....*....|.
gi 194114924   364 ALELVEFKQRYEEVLALLHSAQDQLKQQRKR 394
Cdd:pfam04849  279 TSELQELQDRYAECLGMLHEAQEELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 490-668 6.13e-38

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: 140.11  E-value: 6.13e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   490 RCAGKSGNYMDSGNVSmTTLGAmsmssssgPRMASMAYPAGSYYRG-GGNQSLGVKTLSNESLNSQSDDG---YPAQPsG 565
Cdd:pfam12448    3 RSLTPSPMNIPGSNQS-SSLTS--------MRSSSSSTPRSSYYGGdGSSISLDNRTNSILSETSSSQDSgydRPKKP-G 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   566 VPGAPGARELEAALKRLTPG-----------EVLARRAMLSYApiGTYNYDEPTmHGGAGasnsnlplgvrTP-DSIMST 633
Cdd:pfam12448   73 TPGTPGARDLEAALRRLSLRrqnylserrffEEERERKLLALA--GTYNYDEGE-HGGSL-----------TPnDSIMSL 138

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 194114924   634 GSSRmSASSNNMSASMTHQwRLPEKLQIIKPMEGS 668
Cdd:pfam12448  139 GSNH-SGSSSHSSGFSSRS-YLPEKLQIVKPLEGS 171
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 163-393 6.19e-09

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: 60.42  E-value: 6.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   163 DIEAVTRLLEEKEKDLEltvQIGKELLTQNNALEARVT-DLEADLKSSNDDRSQLLHELHKKNELISVLTNDADD----G 237
Cdd:TIGR04523  275 ELEQNNKKIKELEKQLN---QLKSEISDLNNQKEQDWNkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQlkkeL 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   238 TDTETPTMSKSITLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVE---EHERQLMADIGAQLHDANSQYDNLSLECERQ 314
Cdd:TIGR04523  352 TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLEskiQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   315 REENRLQHEQIVSLTARLAEAEM---RLHQLTQDNDEHLSLLHVT-KENQNALALELVEFKQRYEEVLAlLHSAQDQLKQ 390
Cdd:TIGR04523  432 KETIIKNNSEIKDLTNQDSVKELiikNLDNTRESLETQLKVLSRSiNKIKQNLEQKQKELKSKEKELKK-LNEEKKELEE 510


                   ...
gi 194114924   391 QRK 393
Cdd:TIGR04523  511 KVK 513
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 163-396 3.03e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  163 DIEAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVTDLEADLKSSNDDRSQLLHELHKKNELISVLTNDADDGTDTET 242
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  243 PTMSKSITL-DLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLmADIGAQLHDANSQYDNLSLECERQREENRLQ 321
Cdd:COG1196   306 RLEERRRELeERLEELEEELAELEEELEELEEELEELEEELEEAEEEL-EEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194114924  322 HEQIVSLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKRSQ 396
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 172-400 1.00e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  172 EEKEKDLELTVQIGKELLTQNNALEARVTDLEADLKSSNDDRSQLLHELHKKNELISVLTNDADDGTDTEtptMSKSITL 251
Cdd:COG1196   221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE---YELLAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  252 DLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLmadiGAQLHDANSQYDNLSLECERQREENRLQHEQIVSLTAR 331
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEEL----EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194114924  332 LAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKRSQPQAR 400
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 136-344 3.80e-05

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: 48.09  E-value: 3.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   136 TLEQQNEQLlmevlcgnrvSQMTRAYDDIEavtRLLEEKEKDLELTVQIGKELLTQNNALEARVTDLEADLKSSNDDRSQ 215
Cdd:TIGR04523  462 TRESLETQL----------KVLSRSINKIK---QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   216 LLHELHKKNELISVLTNDAD-DGTDTETPTMSKSItlDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEhERQlmaDIG 294
Cdd:TIGR04523  529 LESEKKEKESKISDLEDELNkDDFELKKENLEKEI--DEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK-EKK---DLI 602

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 194114924   295 AQLhdanSQYDNLSLECERQREENRLQHEQIVSLTARLAEAEMRLHQLTQ 344
Cdd:TIGR04523  603 KEI----EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-401 4.39e-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: 4.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  165 EAVTRLLEEKEKDLELTVQIgKELLTQNNALEARVTDLEADLKSSNDDRSQLLHELHKKNELISVLTNDADDGTDTETPT 244
Cdd:COG1196   264 ELEAELEELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  245 MSKSITLD-LLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLMADIGAQLHDAN------SQYDNLSLECERQREE 317
Cdd:COG1196   343 EEELEEAEeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleeleEAEEALLERLERLEEE 422

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  318 NRLQHEQIVSLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELvefkQRYEEVLALLHSAQDQLKQQRKRSQP 397
Cdd:COG1196   423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA----ALLEAALAELLEELAEAAARLLLLLE 498


                  ....
gi 194114924  398 QARS 401
Cdd:COG1196   499 AEAD 502
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 264-396 6.11e-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: 46.99  E-value: 6.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   264 ENKSLKCEAtqlahqtdevEEHERQLMADIGAQLHDANSQydnlsleCERQREENRLQHEQIVSLTARLAEAEMRLHQLT 343
Cdd:pfam05622  290 ENKMLRLGQ----------EGSYRERLTELQQLLEDANRR-------KNELETQNRLANQRILELQQQVEELQKALQEQG 352

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 194114924   344 QDNDEHLSLlhvtkenqnalalelvefKQRYEEVLALLHSAQDQLkqQRKRSQ 396
Cdd:pfam05622  353 SKAEDSSLL------------------KQKLEEHLEKLHEAQSEL--QKKKEQ 385
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
251-401 6.56e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 6.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  251 LDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLMADIgaqlhdANSQYDNLslecerqreeNRLQhEQIVSLTA 330
Cdd:COG4913   290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI------RGNGGDRL----------EQLE-REIERLER 352

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194114924  331 RLAEAEMRLHQLtqdnDEHLSLLHV----TKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKRSQPQARS 401
Cdd:COG4913   353 ELEERERRRARL----EALLAALGLplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-390 1.99e-04

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: 45.83  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   162 DDIEAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVTDLEADL----KSSNDDRSQLLHE-LHKKNELISVLtndadd 236
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhkleEALNDLEARLSHSrIPEIQAELSKL------ 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   237 gtDTETPTMSKSitLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHErqlmADIGAQLHDansqyDNLSLEcERQRE 316
Cdd:TIGR02169  804 --EEEVSRIEAR--LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI----KSIEKEIEN-----LNGKKE-ELEEE 869

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194114924   317 ENRLQheqivsltARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQ 390
Cdd:TIGR02169  870 LEELE--------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 135-400 2.31e-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: 45.55  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   135 ETLEQQNEQLlmevlcgnrvSQMTRAYDDIEAVTRLLEEKEKDL--EL-TVQIGK-ELLTQNNALEARVTDLEADLKSSN 210
Cdd:pfam01576  356 QALEELTEQL----------EQAKRNKANLEKAKQALESENAELqaELrTLQQAKqDSEHKRKKLEGQLQELQARLSESE 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   211 DDRSQLLHELHK-KNELISVLTNDADdgTDTETPTMSKSI---------TLDLLQ---RKVNSLLDENKSLKCEATQLAH 277
Cdd:pfam01576  426 RQRAELAEKLSKlQSELESVSSLLNE--AEGKNIKLSKDVsslesqlqdTQELLQeetRQKLNLSTRLRQLEDERNSLQE 503

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   278 QTDEVEEHERQL---MADIGAQLHDANSQYDNLSLECERQREENRLQHEQIVSLTARLAEAEMRLHQLTQDND---EHLS 351
Cdd:pfam01576  504 QLEEEEEAKRNVerqLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNrlqQELD 583

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 194114924   352 LLHVTKENQNALALELvEFKQR-YEEVLALLHSAQDQLKQQRKRSQPQAR 400
Cdd:pfam01576  584 DLLVDLDHQRQLVSNL-EKKQKkFDQMLAEEKAISARYAEERDRAEAEAR 632
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
135-391 5.98e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 5.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  135 ETLEQQNEQLLMEVLCGNRVSQMTRAYDDIEAVTRLLEEKEK---DLELTVQIGKELLTQNNALEARVTDLEADLKSSND 211
Cdd:COG4913   634 EALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEELDELKG 713

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  212 DRSQLLHELHKKNELISVLTNDADDGTDTETPTmsksitldllqrkVNSLLDEnkslkceatQLAHQTDevEEHERQLMA 291
Cdd:COG4913   714 EIGRLEKELEQAEEELDELQDRLEAAEDLARLE-------------LRALLEE---------RFAAALG--DAVERELRE 769

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  292 DIGAQLHDANSQYDNLSLECERQREE-NRLQHEQIVSLTARLAEAEM---RLHQLTQDNdehlsllhvtkenqnalaleL 367
Cdd:COG4913   770 NLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEylaLLDRLEEDG--------------------L 829

                         250       260
                  ....*....|....*....|....
gi 194114924  368 VEFKQRYEEvlaLLHSAQDQLKQQ 391
Cdd:COG4913   830 PEYEERFKE---LLNENSIEFVAD 850
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 138-399 7.40e-04

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: 43.80  E-value: 7.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   138 EQQNEQLLMEVLCGNRVSQMTRAYDDIEAVTRLLEEKEKDLELTVQIgkeLLTQNNALEARVTDLEADLKSSNddrsQLL 217
Cdd:TIGR00618  634 LQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQL---ALQKMQSEKEQLTYWKEMLAQCQ----TLL 706

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   218 HELHKKNELISVLTNDADDGTDTETPTMSKSitLDLLQRKVNSLLDENKslkceaTQLAHQTDEVEEHERQLMADI--GA 295
Cdd:TIGR00618  707 RELETHIEEYDREFNEIENASSSLGSDLAAR--EDALNQSLKELMHQAR------TVLKARTEAHFNNNEEVTAALqtGA 778

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   296 QLHDANSQYDNlsleceRQREENRLQHEqivsltARLAEAEMRLHQltqDNDEHLSLLHVTKENQnalalELVEFKQRYE 375
Cdd:TIGR00618  779 ELSHLAAEIQF------FNRLREEDTHL------LKTLEAEIGQEI---PSDEDILNLQCETLVQ-----EEEQFLSRLE 838

                          250       260
                   ....*....|....*....|....
gi 194114924   376 EVLALLHSAQDQLKQQRKRSQPQA 399
Cdd:TIGR00618  839 EKSATLGEITHQLLKYEECSKQLA 862
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
191-392 8.45e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  191 QNNALEARVTDLEADLKSSNDDRSQLLHELHKKNELISVLTNDAddgtdtetptmsKSITLDLLQRKVNSLLDENKS--- 267
Cdd:COG4717   317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE------------EELQLEELEQEIAALLAEAGVede 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  268 ----LKCEATQLAHQ-TDEVEEHERQLMADIGAQLHDANS-QYDNLSLECERQREENRLQHEQIVSLTARLAEAEMRLHQ 341
Cdd:COG4717   385 eelrAALEQAEEYQElKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 194114924  342 LTQDNDehLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQR 392
Cdd:COG4717   465 LEEDGE--LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
159-336 1.01e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  159 RAYDDIEAVTRLLEEKEKDLE-LTVQIG----KELLTQNNALEARVTDLEADLKSSNDDRSQ----------LLHELHKK 223
Cdd:PRK02224  170 RASDARLGVERVLSDQRGSLDqLKAQIEekeeKDLHERLNGLESELAELDEEIERYEEQREQaretrdeadeVLEEHEER 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  224 NELISVLTNDADDGTDTETPTMSKSITLD----LLQRKVNSLLDENKSLKCEA-------TQLAHQTDEVEEHE---RQL 289
Cdd:PRK02224  250 REELETLEAEIEDLRETIAETEREREELAeevrDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDeelRDR 329

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 194114924  290 MADIGAQLHDANSQYDNLSLECERQREENRLQHEQIVSLTARLAEAE 336
Cdd:PRK02224  330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
162-394 1.08e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  162 DDIEAVTRLLEE-KEKDLELTVQIG--KELLTQNNALEARVTDLEADLKSSNDDRSQLLHELHKKnelisvltndaddGT 238
Cdd:PRK03918  518 EELEKKAEEYEKlKEKLIKLKGEIKslKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL-------------GF 584

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  239 DTETPTMSKSITLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLmADIGAQLHDANSQYDnlSLECERQREEN 318
Cdd:PRK03918  585 ESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL-AETEKRLEELRKELE--ELEKKYSEEEY 661

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194114924  319 RLQHEQIVSLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENqnalalelVEFKQRYEEVLALLHSAQDQLKQQRKR 394
Cdd:PRK03918  662 EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE--------LEEREKAKKELEKLEKALERVEELREK 729
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 166-402 1.38e-03

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: 42.44  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  166 AVTRLLEEKEKDLELTVQIGKELLTQNNALEARVTDLEADLKSSNDDRSQLLHELHKKNELISVLTNDADDgTDTETPTM 245
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-LEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  246 SKSitLDLLQRKVNSLLDEN-KSLKCEATQLAHQTDEVEEHERQLMAdIGAQLHDANSQYDNLSLECERQREENRLQHEQ 324
Cdd:COG4942    96 RAE--LEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194114924  325 IVSLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKRSQPQARSS 402
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 165-384 1.62e-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: 41.55  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   165 EAVTRLLEEKEKdLELTVQIGKELLTQNNALEARVTDLEADLKSSNDDRSQLLHEL---HKKNElisvltnDADDGTDT- 240
Cdd:pfam00261   12 EAEERLKEAMKK-LEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLeeaEKAAD-------ESERGRKVl 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   241 ETPTMSKSITLDLLQRKVNslldenkslkcEATQLAHQTDE-VEEHERQLmADIGAQLHDANSQYDNLSLECERQREE-- 317
Cdd:pfam00261   84 ENRALKDEEKMEILEAQLK-----------EAKEIAEEADRkYEEVARKL-VVVEGDLERAEERAELAESKIVELEEElk 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   318 ---NRLQ----------------HEQIVSLTARLAEAEMRLHQLTQdndehlSLLHVTKENqNALALELVEFKQRYEEVL 378
Cdd:pfam00261  152 vvgNNLKsleaseekaseredkyEEQIRFLTEKLKEAETRAEFAER------SVQKLEKEV-DRLEDELEAEKEKYKAIS 224


                   ....*.
gi 194114924   379 ALLHSA 384
Cdd:pfam00261  225 EELDQT 230
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 247-394 1.83e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  247 KSITLDLLQRKVNSLLDENKSLKceaTQLAHQTDEVEEHERQLmADIGAQLHDANSQYDNLSLECERQREENRLQHEQIV 326
Cdd:COG1196   216 RELKEELKELEAELLLLKLRELE---AELEELEAELEELEAEL-EELEAELAELEAELEELRLELEELELELEEAQAEEY 291

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194114924  327 SLTARLAEAEM-------RLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKR 394
Cdd:COG1196   292 ELLAELARLEQdiarleeRRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
PHA03041 PHA03041
virion core protein; Provisional
 173-275 2.23e-03

virion core protein; Provisional


Pssm-ID: 222963  Cd Length: 153  Bit Score: 39.79  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  173 EKEKDLELTVQIGKELLTQNNALEARVTDLEADLKSSNDDRSQLLHE-LHKKNEL------ISVLTND-ADDGTDTETPT 244
Cdd:PHA03041    6 KYSKELETTAKNKKDEEINSNKPEISSGDVDTMLKSKEHQYQQMIIDqLEEKKMLkiknivIPAKSNKnNPQCSDVKSND 85

                          90       100       110
                  ....*....|....*....|....*....|....
gi 194114924  245 MSK---SITLDLLQRKVNSLLDENKSLKCEATQL 275
Cdd:PHA03041   86 VPKkirSISIEEIIKELESIKDETSSLQNESDSL 119
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 254-396 2.42e-03

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: 42.35  E-value: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   254 LQRKVNSLldENKSLKceATQLAHQTDEVEEHERQLMADigaQLHDANSQYDNLSLECER-QREENRLQ------HEQIV 326
Cdd:TIGR02168  198 LERQLKSL--ERQAEK--AERYKELKAELRELELALLVL---RLEELREELEELQEELKEaEEELEELTaelqelEEKLE 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   327 SLTARLAEAEMRLHQLTQDNDEHLSLLH-------VTKE-------NQNALALELVEFKQRYEEVLALLHSAQDQLKQQR 392
Cdd:TIGR02168  271 ELRLEVSELEEEIEELQKELYALANEISrleqqkqILRErlanlerQLEELEAQLEELESKLDELAEELAELEEKLEELK 350


                   ....
gi 194114924   393 KRSQ 396
Cdd:TIGR02168  351 EELE 354
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
176-360 4.42e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  176 KDLELTVQIGKELLTQNNALEARVTDLEADLKSSNDDRSQLLHELHKKNELISVLTNDADDGTDTEtptmsksiTLDLLQ 255
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA--------ELAELP 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  256 RKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLmadigAQLHDANSQYDNLSLEcERQREENRLQhEQIVSLTARLAEA 335
Cdd:COG4717   146 ERLEELEERLEELRELEEELEELEAELAELQEEL-----EELLEQLSLATEEELQ-DLAEELEELQ-QRLAELEEELEEA 218

                         170       180
                  ....*....|....*....|....*
gi 194114924  336 EMRLHQLTQDNDEHLSLLHVTKENQ 360
Cdd:COG4717   219 QEELEELEEELEQLENELEAAALEE 243
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 162-396 5.74e-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: 40.77  E-value: 5.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   162 DDIEAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVTDLEADLKSSNDDRSQLLHELHKKNELISvltndaddgtdtE 241
Cdd:TIGR04523  183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIS------------N 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   242 TptmsksitldllQRKVNSLLDENKSLKceaTQLAHQTDEVEEHERQLmADIGAQLHDANSQYDNLslecERQREEN--- 318
Cdd:TIGR04523  251 T------------QTQLNQLKDEQNKIK---KQLSEKQKELEQNNKKI-KELEKQLNQLKSEISDL----NNQKEQDwnk 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924   319 ------RLQHEQIVSLTARLAEAEMRLHQLTQD-----------NDEHLSLLHVTKENQNALALELVEFKQRYEEVLALL 381
Cdd:TIGR04523  311 elkselKNQEKKLEEIQNQISQNNKIISQLNEQisqlkkeltnsESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390

                          250
                   ....*....|....*...
gi 194114924   382 HSAQD---QLKQQRKRSQ 396
Cdd:TIGR04523  391 SQINDlesKIQNQEKLNQ 408
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
154-404 6.65e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 6.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  154 VSQMTRAYDDIEAVTRLLEEKEKDLEltvQIGKELLTQNNALEArvtdLEADLKSSNDDRSQLLHELHKKNELISVLTND 233
Cdd:COG4372    37 LFELDKLQEELEQLREELEQAREELE---QLEEELEQARSELEQ----LEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  234 ADDgtdtetptmsksitldlLQRKVNSLLDENKSLKCEATQLAHQTDEVEeherQLMADIGAQLHDANSQYDNL-----S 308
Cdd:COG4372   110 AEE-----------------LQEELEELQKERQDLEQQRKQLEAQIAELQ----SEIAEREEELKELEEQLESLqeelaA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  309 LECERQREENRLQHEQIVSLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQL 388
Cdd:COG4372   169 LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248

                         250
                  ....*....|....*.
gi 194114924  389 KQQRKRSQPQARSSFL 404
Cdd:COG4372   249 EELLEEVILKEIEELE 264
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
165-394 6.98e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  165 EAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVTDLEADLKssnddrsqllhELHKKNELISVltndaddgtdtetpt 244
Cdd:PRK03918  189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-----------ELEELKEEIEE--------------- 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194114924  245 msksitldlLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLMADIG--AQLHDANSQYDNLSLECERQREENRLQH 322
Cdd:PRK03918  243 ---------LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelKELKEKAEEYIKLSEFYEEYLDELREIE 313

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194114924  323 EQIVSLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALAlELVEFKQRYEEVLALLhsaqDQLKQQRKR 394
Cdd:PRK03918  314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE-ELEERHELYEEAKAKK----EELERLKKR 380
 
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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