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Conserved domains on  [gi|966973599|ref|XP_015007805|]
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liprin-alpha-2 isoform X16 [Macaca mulatta]

Protein Classification

liprin-alpha( domain architecture ID 13528491)

liprin-alpha belongs to the LAR (leukocyte common antigen-related) family or transmembrane protein-tyrosine phosphatase-interacting proteins and is involved in formation of the presynaptic active zone

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1073-1144 3.13e-44

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188967  Cd Length: 72  Bit Score: 154.01  E-value: 3.13e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966973599 1073 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1144
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 870-940 5.85e-44

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188961  Cd Length: 71  Bit Score: 153.49  E-value: 5.85e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966973599  870 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 940
Cdd:cd09562     1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 988-1053 1.32e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188964  Cd Length: 66  Bit Score: 152.24  E-value: 1.32e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966973599  988 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1053
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 244-564 1.63e-16

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.37  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  244 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 323
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  324 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH- 402
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAl 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  403 ---GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEKNVLIQESETF 479
Cdd:COG1196   393 raaAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELLAELLEE 471

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  480 RKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTISRTHLDTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMG 559
Cdd:COG1196   472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551


                  ....*
gi 966973599  560 VRRDE 564
Cdd:COG1196   552 VVEDD 556
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 49-402 9.84e-12

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.70  E-value: 9.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    49 LRETQESLslaqQRLQDVIYDR----DSLQRQLNSA-----------------LPQDIESLTGGLAGSKGadppEFAALT 107
Cdd:TIGR02168  181 LERTRENL----DRLEDILNELerqlKSLERQAEKAerykelkaelrelelalLVLRLEELREELEELQE----ELKEAE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   108 KELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKAl 187
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQ--------------------------KELYALANEISRLEQQKQ- 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   188 dekivalreqnvHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLsngsiDSTDETSQIVELQELLEKQNYEMAQMKERLA 267
Cdd:TIGR02168  306 ------------ILRERLANLERQLEELEAQLEELESKLDELAE-----ELAELEEKLEELKEELESLEAELEELEAELE 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   268 ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRyLSAQRESTSIHDMnDKLENELANKE 347
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE-IEELLKKLEEAEL-KELQAELEELE 446

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 966973599   348 AILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH 402
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1073-1144 3.13e-44

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188967  Cd Length: 72  Bit Score: 154.01  E-value: 3.13e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966973599 1073 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1144
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 870-940 5.85e-44

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 153.49  E-value: 5.85e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966973599  870 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 940
Cdd:cd09562     1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 988-1053 1.32e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 152.24  E-value: 1.32e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966973599  988 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1053
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 244-564 1.63e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.37  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  244 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 323
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  324 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH- 402
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAl 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  403 ---GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEKNVLIQESETF 479
Cdd:COG1196   393 raaAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELLAELLEE 471

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  480 RKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTISRTHLDTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMG 559
Cdd:COG1196   472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551


                  ....*
gi 966973599  560 VRRDE 564
Cdd:COG1196   552 VVEDD 556
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-456 9.97e-16

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: 82.80  E-value: 9.97e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   101 PEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERS---LRMTVVKRQAQSPSGVSSEVEVLKAL 177
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELEAEIEELEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   178 KSLFEHHKALDEKIVALREQnvhIQRkmASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNY 257
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQ---IEQ--LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   258 EMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMND 337
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   338 KLENELAnkeailrQMEEKNRQLQERL-ELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNI----------- 405
Cdd:TIGR02168  926 QLELRLE-------GLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVnlaaieeyeel 998

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 966973599   406 EERMRHLEGQLEEknqeLQRARQR-----EKMNEEHNKRLSDTVDRLltesNERLQ 456
Cdd:TIGR02168  999 KERYDFLTAQKED----LTEAKETleeaiEEIDREARERFKDTFDQV----NENFQ 1046
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 987-1051 7.33e-14

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 67.29  E-value: 7.33e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966973599   987 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1051
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
102-564 7.57e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 73.15  E-value: 7.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaQSPSGVSSEVEVLKALKSLF 181
Cdd:PRK02224  200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR---------EELETLEAEIEDLRETIAET 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  182 EHHK-ALDEKIVALREQNVHIQRKMASSEGSTESEHLEgmepgQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMA 260
Cdd:PRK02224  271 EREReELAEEVRDLRERLEELEEERDDLLAEAGLDDAD-----AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  261 QMKERLAALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLE 340
Cdd:PRK02224  346 SLREDADDLEERAEELREEAAELESELEEARE-------AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR 418

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  341 NELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQRIAALTKAEERHGNIEERMRHLEGQLEE 418
Cdd:PRK02224  419 EERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEE 493

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  419 KNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-EEKNVLIQESETFRKNLEESLHDKERLAE 495
Cdd:PRK02224  494 VEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEARE 572

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966973599  496 EIEKLRSELDQLKMRTGSLiePTIsRTHLDTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMGVRRDE 564
Cdd:PRK02224  573 EVAELNSKLAELKERIESL--ERI-RTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRE 638
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 49-402 9.84e-12

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: 69.70  E-value: 9.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    49 LRETQESLslaqQRLQDVIYDR----DSLQRQLNSA-----------------LPQDIESLTGGLAGSKGadppEFAALT 107
Cdd:TIGR02168  181 LERTRENL----DRLEDILNELerqlKSLERQAEKAerykelkaelrelelalLVLRLEELREELEELQE----ELKEAE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   108 KELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKAl 187
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQ--------------------------KELYALANEISRLEQQKQ- 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   188 dekivalreqnvHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLsngsiDSTDETSQIVELQELLEKQNYEMAQMKERLA 267
Cdd:TIGR02168  306 ------------ILRERLANLERQLEELEAQLEELESKLDELAE-----ELAELEEKLEELKEELESLEAELEELEAELE 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   268 ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRyLSAQRESTSIHDMnDKLENELANKE 347
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE-IEELLKKLEEAEL-KELQAELEELE 446

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 966973599   348 AILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH 402
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 240-505 1.26e-10

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 65.09  E-value: 1.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   240 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE 319
Cdd:pfam19220   45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   320 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 399
Cdd:pfam19220  125 RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   400 ERHgniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSD-------------TVDRLLTESNERLQlHLKERMAA 465
Cdd:pfam19220  205 DAT---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASlrmklealtaraaATEQLLAEARNQLR-DRDEAIRA 280

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 966973599   466 LEEKNV-LIQESETFRKNLEESLHDKERLAE---EIEKLRSELD 505
Cdd:pfam19220  281 AERRLKeASIERDTLERRLAGLEADLERRTQqfqEMQRARAELE 324
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 870-936 5.91e-09

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 53.45  E-value: 5.91e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966973599    870 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 936
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
39-432 1.11e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.31  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLnSALPQDIESLTGGLagskgadppEFAALTKELNACREQLL 118
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL-EELREELEKLEKLL---------QLLPLYQELEALEAELA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  119 EKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKIVALREQN 198
Cdd:COG4717   143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  199 VHIQRKMASSEGSTESEHLEgmepgQKVHEKRLS-------------NGSIDSTDETSQ---------IVELQELLEKQN 256
Cdd:COG4717   223 EELEEELEQLENELEAAALE-----ERLKEARLLlliaaallallglGGSLLSLILTIAgvlflvlglLALLFLLLAREK 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  257 YEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN 336
Cdd:COG4717   298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA 377

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  337 DKLENELANKEAILRQMEEKnRQLQERLELAEQKLQQ------TMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMR 410
Cdd:COG4717   378 EAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELA 456

                         410       420
                  ....*....|....*....|....
gi 966973599  411 HLEGQLE--EKNQELQRARQREKM 432
Cdd:COG4717   457 ELEAELEqlEEDGELAELLQELEE 480
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 996-1051 1.20e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.99  E-value: 1.20e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 966973599    996 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1051
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1074-1145 7.45e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 47.68  E-value: 7.45e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966973599   1074 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1145
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 43-432 1.35e-05

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 48.91  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    43 DRLLDTLRETQESLSLAQQRLQDViydRDSLQRQL--NSALPQDIESLTGGLAGSKGadppEFAALTKELNACREQLLEK 120
Cdd:pfam19220   30 SQLIEPIEAILRELPQAKSRLLEL---EALLAQERaaYGKLRRELAGLTRRLSAAEG----ELEELVARLAKLEAALREA 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   121 EEEISELKAERNNTRLLLEHLE---CLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKIVALR-- 195
Cdd:pfam19220  103 EAAKEELRIELRDKTAQAEALErqlAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQal 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   196 --EQNVHI---QRKMASSEGSTESEH--LEGMEpGQKVHEKrlsngsidstdetsqiVELQELLEKQNYEMAQMKERLAA 268
Cdd:pfam19220  183 seEQAAELaelTRRLAELETQLDATRarLRALE-GQLAAEQ----------------AERERAEAQLEEAVEAHRAERAS 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   269 LSSRVgeveqEAETARkdLIKTEEMNTkyqrdirEAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEA 348
Cdd:pfam19220  246 LRMKL-----EALTAR--AAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQ 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   349 ILRQMEEKNRQLQERLElaeqklqqTMRKAetlpeveaeLAQRIAALTKAEERHGNIEERMRHLEGQ-------LEEKNQ 421
Cdd:pfam19220  312 QFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSDRIAELTKRfeveraaLEQANR 374

                          410
                   ....*....|.
gi 966973599   422 ELQRARQREKM 432
Cdd:pfam19220  375 RLKEELQRERA 385
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 872-936 1.38e-04

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 41.10  E-value: 1.38e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966973599   872 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 936
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1074-1144 1.53e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.53e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966973599  1074 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1144
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 337-511 4.11e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.20  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  337 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 404
Cdd:cd00176    10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  405 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 474
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 966973599  475 ESETFRKNLEESLH--DKERLAEEIEKLRSELDQLKMRT 511
Cdd:cd00176   164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1073-1144 3.13e-44

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188967  Cd Length: 72  Bit Score: 154.01  E-value: 3.13e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966973599 1073 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1144
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 870-940 5.85e-44

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 153.49  E-value: 5.85e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966973599  870 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 940
Cdd:cd09562     1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 988-1053 1.32e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 152.24  E-value: 1.32e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966973599  988 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1053
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 992-1051 2.68e-31

SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188894  Cd Length: 60  Bit Score: 116.86  E-value: 2.68e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  992 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1051
Cdd:cd09495     1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 877-935 3.54e-27

SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188893  Cd Length: 58  Bit Score: 105.00  E-value: 3.54e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 966973599  877 TVVAWLELWLGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 935
Cdd:cd09494     1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 1081-1142 6.83e-25

SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188895  Cd Length: 62  Bit Score: 98.77  E-value: 6.83e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966973599 1081 RVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNN 1142
Cdd:cd09496     1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 1073-1144 1.40e-18

SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188969  Cd Length: 72  Bit Score: 80.95  E-value: 1.40e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966973599 1073 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1144
Cdd:cd09570     1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 871-935 5.07e-17

SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188963  Cd Length: 70  Bit Score: 76.72  E-value: 5.07e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966973599  871 AQWDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 935
Cdd:cd09564     2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 244-564 1.63e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.37  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  244 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 323
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  324 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH- 402
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAl 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  403 ---GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEKNVLIQESETF 479
Cdd:COG1196   393 raaAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELLAELLEE 471

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  480 RKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTISRTHLDTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMG 559
Cdd:COG1196   472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551


                  ....*
gi 966973599  560 VRRDE 564
Cdd:COG1196   552 VVEDD 556
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 987-1051 1.78e-16

SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188966  Cd Length: 65  Bit Score: 74.75  E-value: 1.78e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966973599  987 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1051
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 987-1051 1.99e-16

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188965  Cd Length: 63  Bit Score: 74.65  E-value: 1.99e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966973599  987 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1051
Cdd:cd09566     1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-456 9.97e-16

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: 82.80  E-value: 9.97e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   101 PEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERS---LRMTVVKRQAQSPSGVSSEVEVLKAL 177
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELEAEIEELEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   178 KSLFEHHKALDEKIVALREQnvhIQRkmASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNY 257
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQ---IEQ--LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   258 EMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMND 337
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   338 KLENELAnkeailrQMEEKNRQLQERL-ELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNI----------- 405
Cdd:TIGR02168  926 QLELRLE-------GLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVnlaaieeyeel 998

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 966973599   406 EERMRHLEGQLEEknqeLQRARQR-----EKMNEEHNKRLSDTVDRLltesNERLQ 456
Cdd:TIGR02168  999 KERYDFLTAQKED----LTEAKETleeaiEEIDREARERFKDTFDQV----NENFQ 1046
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 242-509 2.21e-15

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: 81.64  E-value: 2.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   242 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR 321
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   322 YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 401
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   402 hgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERL-QLHLKERMAALEEKNVLIQESE 477
Cdd:TIGR02168  871 ---LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrreLEELREKLaQLELRLEGLEVRIDNLQERLSE 947

                          250       260       270
                   ....*....|....*....|....*....|..
gi 966973599   478 TFRKNLEESLHDKERLAEEIEKLRSELDQLKM 509
Cdd:TIGR02168  948 EYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 1073-1144 2.30e-15

SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188968  Cd Length: 72  Bit Score: 71.72  E-value: 2.30e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966973599 1073 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1144
Cdd:cd09569     1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 263-516 3.16e-15

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: 81.26  E-value: 3.16e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   263 KERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENE 342
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   343 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH-------GNIEERMRHLEGQ 415
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtllneeaANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   416 LEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKER-------MAALEEKNVLIQESETFRKNLEE 485
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERasleealALLRSELEELSEELRELESKRSE 912

                          250       260       270
                   ....*....|....*....|....*....|.
gi 966973599   486 SLHDKERLAEEIEKLRSELDQLKMRTGSLIE 516
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQE 943
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 258-507 2.03e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.44  E-value: 2.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  258 EMAQMKERLAALSSRVGEVEQ-------EAETARKDLIKTEEMNtkyQRDIREAMAQKEDMEERITTLEKRYLSAQRESt 330
Cdd:COG1196   180 KLEATEENLERLEDILGELERqleplerQAEKAERYRELKEELK---ELEAELLLLKLRELEAELEELEAELEELEAEL- 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  331 sihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnIEERMR 410
Cdd:COG1196   256 ------EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE---LEEELA 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  411 HLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESL 487
Cdd:COG1196   327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeeaLLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406

                         250       260
                  ....*....|....*....|
gi 966973599  488 HDKERLAEEIEKLRSELDQL 507
Cdd:COG1196   407 EAEEALLERLERLEEELEEL 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 252-508 3.15e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 3.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  252 LEKQnyemAQMKERLAALSSRVGEVEQEA-----ETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQ 326
Cdd:COG1196   205 LERQ----AEKAERYRELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  327 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI-----------AAL 395
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELeeaeeeleeaeAEL 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  396 TKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLtesnERLQLHLKERMAALEEKNVLIQE 475
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----ERLERLEEELEELEEALAELEEE 436

                         250       260       270
                  ....*....|....*....|....*....|...
gi 966973599  476 SETFRKNLEESLHDKERLAEEIEKLRSELDQLK 508
Cdd:COG1196   437 EEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 987-1051 7.33e-14

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 67.29  E-value: 7.33e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966973599   987 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1051
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 243-516 2.59e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.97  E-value: 2.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  243 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 322
Cdd:COG1196   267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  323 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERh 402
Cdd:COG1196   347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE- 425

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  403 gnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNvliqesetfRKN 482
Cdd:COG1196   426 --LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA---------RLL 494

                         250       260       270
                  ....*....|....*....|....*....|....
gi 966973599  483 LEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 516
Cdd:COG1196   495 LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-502 5.25e-13

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: 73.94  E-value: 5.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    83 QDIESLTGGLAGSKGADPPEFAAL--TKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSrherslrmTVVKRQ 160
Cdd:TIGR02168  650 LDGDLVRPGGVITGGSAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE--------QLRKEL 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   161 AQSPSGVSSEVEVLKALKslfehhkaldEKIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRlsngsidstd 240
Cdd:TIGR02168  722 EELSRQISALRKDLARLE----------AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE---------- 781

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   241 etSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEK 320
Cdd:TIGR02168  782 --AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   321 RYLSAQREStsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEE 400
Cdd:TIGR02168  860 EIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELR----------ELESKRSELRRELEELRE 922

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   401 RHGNIEERMRHLEGQLEEKnqeLQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMAALEEKNVL-IQESETF 479
Cdd:TIGR02168  923 KLAQLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLAaIEEYEEL 998

                          410       420
                   ....*....|....*....|...
gi 966973599   480 RKNLEESLHDKERLAEEIEKLRS 502
Cdd:TIGR02168  999 KERYDFLTAQKEDLTEAKETLEE 1021
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 114-469 5.64e-13

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: 73.95  E-value: 5.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   114 REQLLEKEEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAqspsgvsseVEVLKALKSLFEHHKALDEKIVA 193
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKI---------GEIEKEIEQLEQEEEKLKERLEE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   194 LREQNVHIQRKMASSEgsTESEHLEGMEPGQ--KVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSS 271
Cdd:TIGR02169  742 LEEDLSSLEQEIENVK--SELKELEARIEELeeDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   272 RVGEVEQEAETARKdlikteEMNTKyQRDIREAMAQKEDMEERITTLEKRYLSAQRE----STSIHDMNDKLEN---ELA 344
Cdd:TIGR02169  820 KLNRLTLEKEYLEK------EIQEL-QEQRIDLKEQIKSIEKEIENLNGKKEELEEEleelEAALRDLESRLGDlkkERD 892

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   345 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA----------LTKAEERHGNIEERMRHLEG 414
Cdd:TIGR02169  893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRALEP 972

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 966973599   415 QLEEKNQELqrarqrekmnEEHNKRLSDTVDRLLTESNERLQlhLKERMAALEEK 469
Cdd:TIGR02169  973 VNMLAIQEY----------EEVLKRLDELKEKRAKLEEERKA--ILERIEEYEKK 1015
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 228-507 5.88e-13

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: 73.95  E-value: 5.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   228 EKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQ 307
Cdd:TIGR02169  701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   308 KEDMEERIttlekrylsAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAE 387
Cdd:TIGR02169  781 LNDLEARL---------SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   388 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARqrekmnEEHNKRLSDTVDRL--LTESNERLQLHLKERMAA 465
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER------DELEAQLRELERKIeeLEAQIEKKRKRLSELKAK 925

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 966973599   466 LEEKNVLIQESETFRKNLEES---LHDKERLAEEIEKLRSELDQL 507
Cdd:TIGR02169  926 LEALEEELSEIEDPKGEDEEIpeeELSLEDVQAELQRVEEEIRAL 970
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
102-564 7.57e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 73.15  E-value: 7.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaQSPSGVSSEVEVLKALKSLF 181
Cdd:PRK02224  200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR---------EELETLEAEIEDLRETIAET 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  182 EHHK-ALDEKIVALREQNVHIQRKMASSEGSTESEHLEgmepgQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMA 260
Cdd:PRK02224  271 EREReELAEEVRDLRERLEELEEERDDLLAEAGLDDAD-----AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  261 QMKERLAALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLE 340
Cdd:PRK02224  346 SLREDADDLEERAEELREEAAELESELEEARE-------AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR 418

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  341 NELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQRIAALTKAEERHGNIEERMRHLEGQLEE 418
Cdd:PRK02224  419 EERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEE 493

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  419 KNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-EEKNVLIQESETFRKNLEESLHDKERLAE 495
Cdd:PRK02224  494 VEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEARE 572

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966973599  496 EIEKLRSELDQLKMRTGSLiePTIsRTHLDTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMGVRRDE 564
Cdd:PRK02224  573 EVAELNSKLAELKERIESL--ERI-RTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRE 638
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 870-934 1.63e-12

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188962  Cd Length: 64  Bit Score: 63.40  E-value: 1.63e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966973599  870 FAQWDGPTVVAWL-ELWLGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 934
Cdd:cd09563     1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 230-514 2.92e-12

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: 71.64  E-value: 2.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   230 RLSNGSIDSTDETSQIVELQELLEKqnyemaqMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKE 309
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   310 DMEERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERLELAEQKLQQtmrkaETLPEVEAEla 389
Cdd:TIGR02169  734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIE-------ELEEDLHKLEEALNDLEARLSH-----SRIPEIQAE-- 799

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   390 qriaaLTKAEERHGNIEERMRHLEGQLEEKNQELQRArqREKMNEEHNKRlsdtvdRLLTESNERLQLHLKERMAALEEK 469
Cdd:TIGR02169  800 -----LSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQR------IDLKEQIKSIEKEIENLNGKKEEL 866

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 966973599   470 NVLIQESETFRKNLEESLHDkerLAEEIEKLRSELDQLKMRTGSL 514
Cdd:TIGR02169  867 EEELEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEEL 908
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 240-516 6.13e-12

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: 70.47  E-value: 6.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   240 DETSQIVELQELLEKQNYEMAQMKERLA-------ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 312
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   313 ERITTLEKRYLSAQRESTSihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRI 392
Cdd:TIGR02168  337 EELAELEEKLEELKEELES-------LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLE 406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   393 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRAR--QREKMNEEHNKRLSDTVDRLLTESNERLQlhLKERMAALEEKN 470
Cdd:TIGR02168  407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEE--AEQALDAAEREL 484

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 966973599   471 VLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 516
Cdd:TIGR02168  485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 49-402 9.84e-12

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: 69.70  E-value: 9.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    49 LRETQESLslaqQRLQDVIYDR----DSLQRQLNSA-----------------LPQDIESLTGGLAGSKGadppEFAALT 107
Cdd:TIGR02168  181 LERTRENL----DRLEDILNELerqlKSLERQAEKAerykelkaelrelelalLVLRLEELREELEELQE----ELKEAE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   108 KELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKAl 187
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQ--------------------------KELYALANEISRLEQQKQ- 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   188 dekivalreqnvHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLsngsiDSTDETSQIVELQELLEKQNYEMAQMKERLA 267
Cdd:TIGR02168  306 ------------ILRERLANLERQLEELEAQLEELESKLDELAE-----ELAELEEKLEELKEELESLEAELEELEAELE 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   268 ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRyLSAQRESTSIHDMnDKLENELANKE 347
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE-IEELLKKLEEAEL-KELQAELEELE 446

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 966973599   348 AILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH 402
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
39-531 9.01e-11

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 66.60  E-value: 9.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   39 LDERDRLLDTLRETQESLSLAQQRLQDVIyDRDSLQRQLNSALPQDIESLTGGLAgskgADPPEFAALTKELNACREQLL 118
Cdd:PRK02224  215 LAELDEEIERYEEQREQARETRDEADEVL-EEHEERREELETLEAEIEDLRETIA----ETEREREELAEEVRDLRERLE 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  119 EKEEEISELKAERNNTRL----LLEHLECLVSRHERSLRMTVVKRQAQSpsgvssevEVLKALKSLFEHHKALDEKIVAL 194
Cdd:PRK02224  290 ELEEERDDLLAEAGLDDAdaeaVEARREELEDRDEELRDRLEECRVAAQ--------AHNEEAESLREDADDLEERAEEL 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  195 REQNVHIQRKMASSEG--STESEHLEGMEPGQKVHEKRLSNGSIDstdetsqivelqelLEKQNYEMAQMKERLAALSSR 272
Cdd:PRK02224  362 REEAAELESELEEAREavEDRREEIEELEEEIEELRERFGDAPVD--------------LGNAEDFLEELREERDELRER 427

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  273 VGEVEQEAETARKDLIKTEEMNTKYQ-----RDIREA--MAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLEnELAN 345
Cdd:PRK02224  428 EAELEATLRTARERVEEAEALLEAGKcpecgQPVEGSphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVE 506

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  346 KEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 421
Cdd:PRK02224  507 AEDRIERLEERREDLEELIAERRETIEEKRERAEELreraAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKE 586

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  422 ELQR-ARQREKMNEEHNKRlsDTVDRL------LTESNERLQLHLKERM------------AALEEKNVLIQESETFRKN 482
Cdd:PRK02224  587 RIESlERIRTLLAAIADAE--DEIERLrekreaLAELNDERRERLAEKRerkreleaefdeARIEEAREDKERAEEYLEQ 664

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966973599  483 LEESLHDK--------------ERLAEEIEKLRSELDQLKMRTGSLIE-----PTISRTHLDTSAELR 531
Cdd:PRK02224  665 VEEKLDELreerddlqaeigavENELEELEELRERREALENRVEALEAlydeaEELESMYGDLRAELR 732
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 295-508 1.15e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  295 TKYQRDIREAMAQKEDMEERIT-------TLEKRY--LSAQRESTSIHDmndKLENELANKEAIL-----RQMEEKNRQL 360
Cdd:COG1196   168 SKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEKAERYR---ELKEELKELEAELlllklRELEAELEEL 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  361 QERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 440
Cdd:COG1196   245 EAELEELEAELEELEAELA---ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966973599  441 SDTVDRLltesNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 508
Cdd:COG1196   322 EEELAEL----EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 240-505 1.26e-10

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 65.09  E-value: 1.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   240 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE 319
Cdd:pfam19220   45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   320 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 399
Cdd:pfam19220  125 RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   400 ERHgniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSD-------------TVDRLLTESNERLQlHLKERMAA 465
Cdd:pfam19220  205 DAT---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASlrmklealtaraaATEQLLAEARNQLR-DRDEAIRA 280

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 966973599   466 LEEKNV-LIQESETFRKNLEESLHDKERLAE---EIEKLRSELD 505
Cdd:pfam19220  281 AERRLKeASIERDTLERRLAGLEADLERRTQqfqEMQRARAELE 324
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
263-514 1.30e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.86  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  263 KERLAALSSRVGEVEQEAETARKDLIKTEemntkyqRDIREAMAQKEDMEERITTLEKRYlsaqRESTSIHDMNDKLENE 342
Cdd:PRK03918  178 IERLEKFIKRTENIEELIKEKEKELEEVL-------REINEISSELPELREELEKLEKEV----KELEELKEEIEELEKE 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  343 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE--AELAQRIAAL-TKAEERHGNIEERMRHLEGQLEEK 419
Cdd:PRK03918  247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekAEEYIKLSEFyEEYLDELREIEKRLSRLEEEINGI 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  420 NQELQRARQREKMNEEHNKRLSDTVDRL--LTESNERLQ--LHLKERMAALEEKnVLIQESETFRKNLEESLHDKERLAE 495
Cdd:PRK03918  327 EERIKELEEKEERLEELKKKLKELEKRLeeLEERHELYEeaKAKKEELERLKKR-LTGLTPEKLEKELEELEKAKEEIEE 405

                         250
                  ....*....|....*....
gi 966973599  496 EIEKLRSELDQLKMRTGSL 514
Cdd:PRK03918  406 EISKITARIGELKKEIKEL 424
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-504 2.97e-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: 65.08  E-value: 2.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQdIESLTGGLAGSKGadppEFAALTKELNACREQLLE 119
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE-LESLEAELEELEA----ELEELESRLEELEEQLET 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   120 KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEV--------EVLKALKSLFEHHKALDEKI 191
Cdd:TIGR02168  384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkelqaeleELEEELEELQEELERLEEAL 463

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   192 VALREQNVHIQRKM--ASSEGSTESEHLEGMEPGQKVHEKrLSNGSIDSTDETSQIVE----LQELLE-KQNYEMAQmke 264
Cdd:TIGR02168  464 EELREELEEAEQALdaAERELAQLQARLDSLERLQENLEG-FSEGVKALLKNQSGLSGilgvLSELISvDEGYEAAI--- 539

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   265 rLAALSSRVGEVEQEAETARKDLIKT-------------------------------------------EEMNTKYQR-- 299
Cdd:TIGR02168  540 -EAALGGRLQAVVVENLNAAKKAIAFlkqnelgrvtflpldsikgteiqgndreilkniegflgvakdlVKFDPKLRKal 618

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   300 -----------DIREAMAQ--KEDMEERITTLE-----KRYLSAQRESTSIHDMNDKlENELANKEAILRQMEEKNRQLQ 361
Cdd:TIGR02168  619 syllggvlvvdDLDNALELakKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAELE 697

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   362 ERLELAEQKLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHN 437
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966973599   438 KRLSD---TVDRLLTESNERLQLhLKERMAALEEK----NVLIQESETFRKNLEESLHDKERLAEEIEKLRSEL 504
Cdd:TIGR02168  778 AEAEAeieELEAQIEQLKEELKA-LREALDELRAEltllNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 240-660 7.07e-10

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: 63.55  E-value: 7.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   240 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEemntKYQrdirEAMAQKEDMEERITTLE 319
Cdd:TIGR02169  160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE----RYQ----ALLKEKREYEGYELLKE 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   320 KRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAelaqrIAALTKAE 399
Cdd:TIGR02169  232 KEALERQKE---------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVKEKIG 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   400 ERHGNIEErmrhLEGQLEEKNQELQRA-RQREKMNEEHNKrlsdtvdrlltesnerlqlhLKERMAALEEKnvliqeset 478
Cdd:TIGR02169  298 ELEAEIAS----LERSIAEKERELEDAeERLAKLEAEIDK--------------------LLAEIEELERE--------- 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   479 frknLEESLHDKERLAEEIEKLRSELDQLKMRTGSliEPTISRTHLDTSAELRYSVGSLVDSQSDYRTTkvirRPRRGRM 558
Cdd:TIGR02169  345 ----IEEERKRRDKLTEEYAELKEELEDLRAELEE--VDKEFAETRDELKDYREKLEKLKREINELKRE----LDRLQEE 414

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   559 GVRRDEpkvkSLGDHEwnrtQQIGVLSSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAmmLQEQLDAINKE 638
Cdd:TIGR02169  415 LQRLSE----ELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD--LKEEYDRVEKE 484

                          410       420
                   ....*....|....*....|..
gi 966973599   639 IRLIQEEKESTELRAEEIENRV 660
Cdd:TIGR02169  485 LSKLQRELAEAEAQARASEERV 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 114-435 8.10e-10

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: 63.55  E-value: 8.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   114 REQLLEKEE-EISELKAERNNTRLLLEHLECLVSRHERSLRmtvvKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEkiv 192
Cdd:TIGR02169  214 QALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELE----KLTEEISELEKRLEEIEQLLEELNKKIKDLGE--- 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   193 alrEQNVHIQRKMASSEGSTES--EHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALS 270
Cdd:TIGR02169  287 ---EEQLRVKEKIGELEAEIASleRSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   271 SRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmaqKEDMEERITTLEKRYLSAQRESTSIHDMNdkleNELANKEAIL 350
Cdd:TIGR02169  364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKL---KREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKI 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   351 RQMEEKNRQLQERLELAEQKLQQTmrkaetlpeveaelaqrIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQRE 430
Cdd:TIGR02169  437 NELEEEKEDKALEIKKQEWKLEQL-----------------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499


                   ....*
gi 966973599   431 KMNEE 435
Cdd:TIGR02169  500 RASEE 504
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 259-670 8.29e-10

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 63.60  E-value: 8.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   259 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEerITTLEKRYLSAQRESTSIHDMNDK 338
Cdd:pfam15921  226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEI 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   339 LENELANKEAI-LRQMEEknrqlqerLELAEQKLQQTMRKA-----ETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 412
Cdd:pfam15921  304 IQEQARNQNSMyMRQLSD--------LESTVSQLRSELREAkrmyeDKIEELEKQLVLANSELTEARTERDQFSQESGNL 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   413 EGQLEEKNQELQRARQREKMNEEHNKRLSD-------TVDRLLTESNER-----------------LQLHLKERMAALEE 468
Cdd:pfam15921  376 DDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRnmevqrleallkamkseCQGQMERQMAAIQG 455

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   469 KNVLIQESETFRKNLEESlhdKERLAEEIEKLRSeldqlKMRTGSLIEPTISrthlDTSAELRYSVGSLVDSQSDyrTTK 548
Cdd:pfam15921  456 KNESLEKVSSLTAQLEST---KEMLRKVVEELTA-----KKMTLESSERTVS----DLTASLQEKERAIEATNAE--ITK 521

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   549 VirrprRGRMGVRRDEPK-VKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIddddRETIFSSMDLLSPSGHSDA--QTLA 625
Cdd:pfam15921  522 L-----RSRVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL----RQQIENMTQLVGQHGRTAGamQVEK 592

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 966973599   626 MMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNL 670
Cdd:pfam15921  593 AQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL 637
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 243-435 9.78e-10

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 62.15  E-value: 9.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  243 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmaqKEDMEERITTLEKRY 322
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  323 LSAQR------------ESTSIHDMNDKLEN----ELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAET-LPE 383
Cdd:COG3883    93 RALYRsggsvsyldvllGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAE 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 966973599  384 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 435
Cdd:COG3883   173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 298-513 1.28e-09

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: 61.70  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  298 QRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 377
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  378 AETLpevEAELAQRIAALTK------------------AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR 439
Cdd:COG4942    99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966973599  440 LSDTVDRLLTEsNERLQLHLKERMAALEEKNvliQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGS 513
Cdd:COG4942   176 LEALLAELEEE-RAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 38-397 1.28e-09

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: 62.78  E-value: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    38 MLDERDRLLDTLRETQESLSLAQQRLQDviydrdsLQRQLnSALPQDIESLTGGLAGSKGadppEFAALTKELNACREQL 117
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSD-------ASRKI-GEIEKEIEQLEQEEEKLKE----RLEELEEDLSSLEQEI 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   118 LEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKrqaqspsgvssevEVLKALKSLFEHHKALDEKIVAL--R 195
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP-------------EIQAELSKLEEEVSRIEARLREIeqK 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   196 EQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIdstdetsQIVELQELLEKQNYEMAQMKERLAALSSRVGE 275
Cdd:TIGR02169  821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG-------KKEELEEELEELEAALRDLESRLGDLKKERDE 893

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   276 VEQEAETARKdliKTEEMNTKYQRD---IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMnDKLENELANKEAILRQ 352
Cdd:TIGR02169  894 LEAQLRELER---KIEELEAQIEKKrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIRA 969

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 966973599   353 MEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 397
Cdd:TIGR02169  970 LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
243-514 1.89e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.00  E-value: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  243 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVE---QEAETARKDLIKTEEMNTKYQRDIR---EAMAQKEDMEERIT 316
Cdd:PRK03918  238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKkeiEELEEKVKELKELKEKAEEYIKLSEfyeEYLDELREIEKRLS 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  317 TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQME---------EKNRQLQERLELAEQKLqqtmrKAETLPEVEAE 387
Cdd:PRK03918  318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerhelyEEAKAKKEELERLKKRL-----TGLTPEKLEKE 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  388 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ---ELQRARQR-----EKMNEEHNKRLSDTVDRLLTESNERLQ-LH 458
Cdd:PRK03918  393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKaieELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEKELKeIE 472

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966973599  459 LKERMAALEEKNV---LIQESETFR--------KNLEESL--HDKERL---AEEIEKLRSELDQLKMRTGSL 514
Cdd:PRK03918  473 EKERKLRKELRELekvLKKESELIKlkelaeqlKELEEKLkkYNLEELekkAEEYEKLKEKLIKLKGEIKSL 544
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 40-510 2.14e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALpQDIESLTGGLAGSKGADppefAALTKELNACREQLLE 119
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE-ERLEELEEELAELEEEL----EELEEELEELEEELEE 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  120 KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvSSEVEVLKALKSLFEHHKALDEKIVALREQNV 199
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL----RAAAELAAQLEELEEAEEALLERLERLEEELE 424

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  200 HIQRKMASSEGS--TESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVE 277
Cdd:COG1196   425 ELEEALAELEEEeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  278 QEAETARKDLIKTE------------EMNTKYQRDIREAMA---------QKEDMEERITTLEKRYLS----------AQ 326
Cdd:COG1196   505 GFLEGVKAALLLAGlrglagavavliGVEAAYEAALEAALAaalqnivveDDEVAAAAIEYLKAAKAGratflpldkiRA 584

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  327 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE 406
Cdd:COG1196   585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  407 ERMRHLEGQLEEKNQELQRARQRE-KMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEE 485
Cdd:COG1196   665 GSRRELLAALLEAEAELEELAERLaEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744

                         490       500       510
                  ....*....|....*....|....*....|.
gi 966973599  486 SLHDKERLAEE------IEKLRSELDQLKMR 510
Cdd:COG1196   745 EELLEEEALEElpeppdLEELERELERLERE 775
PTZ00121 PTZ00121
MAEBL; Provisional
 208-489 3.04e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.70  E-value: 3.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  208 SEGSTESEHLEGMEPGQKVHEKRLSNgSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDl 287
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAE-EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE- 1595

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  288 iktEEMNTKYQRDIREAMAQKEDMEERITTLEKRylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEEKNRQ 359
Cdd:PTZ00121 1596 ---EVMKLYEEEKKMKAEEAKKAEEAKIKAEELK--KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEEAKKA 1670

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  360 LQERLELAE-QKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNK 438
Cdd:PTZ00121 1671 EEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 966973599  439 R---LSDTVDRLLTESNERLQLHLKERMAALEEKnvLIQESETFRKNLEESLHD 489
Cdd:PTZ00121 1751 KdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDKKIKD 1802
PTZ00121 PTZ00121
MAEBL; Provisional
 30-516 4.33e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.31  E-value: 4.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   30 HFEQLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDiESLTGGLAGSKGADP----PEFAA 105
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAakkkAEEAK 1342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEH--LECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEH 183
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKkkADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  184 HKALDEKIVALREQNVHIQRKMASSEGSTESEHLEGMEP-GQKVHEKRLSNGSIDSTDETSQIVELQELLE--------- 253
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEaKKKAEEAKKADEAKKKAEEAKKADEAKKKAEeakkkadea 1502

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  254 -------KQNYEMAQMKERLAALSSRVGEVEQEAETARK--------DLIKTEEMntKYQRDIREAMAQKEDMEERITTL 318
Cdd:PTZ00121 1503 kkaaeakKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeekkkadELKKAEEL--KKAEEKKKAEEAKKAEEDKNMAL 1580

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  319 EKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE---------KNRQLQERLELAEQKLQQTMRKAETLPEVEAELA 389
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  390 QRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesnERLQLHLKERMAALEEk 469
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELKKAEEENKIKAEE- 1734

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 966973599  470 nvLIQESETFRKNLEESLHD---KERLAEEIEKLRSELDQLKMRTGSLIE 516
Cdd:PTZ00121 1735 --AKKEAEEDKKKAEEAKKDeeeKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-515 5.24e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.85  E-value: 5.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  104 AALTKELNACREQL---LEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVvkrqaqspSGVSSEVEVLKALKSL 180
Cdd:PRK03918  168 GEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--------EKLEKEVKELEELKEE 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  181 FE-----------HHKALDEKIVALREQNVHIQRKmaSSEGSTESEHLEGMEPGQKVHEKrLSNGSIDSTDETSQIVELQ 249
Cdd:PRK03918  240 IEelekeleslegSKRKLEEKIRELEERIEELKKE--IEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRL 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  250 ELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRdIREAMAQKEDMEERIT-----TLEKRYLS 324
Cdd:PRK03918  317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRLTgltpeKLEKELEE 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  325 AQRESTSIHDMNDKLENELANkeaiLRQMEEKNRQLQERLELAEQKLQQTMR------KAETLPEVEAELAQRIAALTKA 398
Cdd:PRK03918  396 LEKAKEEIEEEISKITARIGE----LKKEIKELKKAIEELKKAKGKCPVCGRelteehRKELLEEYTAELKRIEKELKEI 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  399 EERHGNIEERMRHLEGQLEeKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMAALEEKnvliqeset 478
Cdd:PRK03918  472 EEKERKLRKELRELEKVLK-KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK-LKEKLIKLKGE--------- 540

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 966973599  479 fRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLI 515
Cdd:PRK03918  541 -IKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
299-510 5.46e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 60.70  E-value: 5.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  299 RDIREAMaqkEDMEERITTLE------KRYLSAQRESTSIHDMNDKLEnelankeaiLRQMEEKNRQLQERLELAEQKLQ 372
Cdd:COG4913   238 ERAHEAL---EDAREQIELLEpirelaERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  373 QTMRKAETLPEVEAELAQRIAALTKAEERHGNieERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrlLTESN 452
Cdd:COG4913   306 RLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLERELEERERRRARLEALLAALGLPLP--ASAEE 381

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 966973599  453 -ERLQLHLKERMAALEEknvliqESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 510
Cdd:COG4913   382 fAALRAEAAALLEALEE------ELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 250-531 5.46e-09

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: 60.84  E-value: 5.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   250 ELLEKQnyemAQMKERLAALSSRVGEVE-----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLS 324
Cdd:TIGR02168  203 KSLERQ----AEKAERYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   325 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALtkaeerhgn 404
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL--------- 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   405 iEERMRHLEGQLEEKNQELQRARQREKMNEEHnkrlsdtvdrLLTESNERLQLhlkermaaLEEKNVLIQESETFRKNLE 484
Cdd:TIGR02168  350 -KEELESLEAELEELEAELEELESRLEELEEQ----------LETLRSKVAQL--------ELQIASLNNEIERLEARLE 410

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 966973599   485 ESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTISRTHLDTSAELR 531
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 870-936 5.91e-09

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 53.45  E-value: 5.91e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966973599    870 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 936
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
115-510 5.95e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.46  E-value: 5.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKIVAL 194
Cdd:PRK03918  286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  195 REQnvhIQRKMASSEGstesehlegmepgqkvHEKRLSNGSIDSTDETSQIV-----ELQELLEKQNYEMAQMKERLAAL 269
Cdd:PRK03918  364 YEE---AKAKKEELER----------------LKKRLTGLTPEKLEKELEELekakeEIEEEISKITARIGELKKEIKEL 424

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  270 SSRVGEVEQE-----------AETARKDLIK--TEEMNtKYQRDIREAMAQKEDMEERITTLEKrYLSAQRESTSIHDMN 336
Cdd:PRK03918  425 KKAIEELKKAkgkcpvcgrelTEEHRKELLEeyTAELK-RIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELA 502

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  337 DKLEN-ELANKEAILRQMEEKNRQ---LQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 412
Cdd:PRK03918  503 EQLKElEEKLKKYNLEELEKKAEEyekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  413 ----EGQLEEKNQELqrarqrEKMNEEHNkRLSDTVDRL--LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEES 486
Cdd:PRK03918  583 gfesVEELEERLKEL------EPFYNEYL-ELKDAEKELerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655

                         410       420       430
                  ....*....|....*....|....*....|...
gi 966973599  487 LHDKE---------RLAEEIEKLRSELDQLKMR 510
Cdd:PRK03918  656 YSEEEyeelreeylELSRELAGLRAELEELEKR 688
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 108-507 7.13e-09

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: 60.37  E-value: 7.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   108 KELNACREQLLEKEEEISELKAERNNtrlLLEHLECLVSRHERSLRMTVVkrQAQSPSGVSSEVE-VLKALKSLFEHHKA 186
Cdd:TIGR00618  472 EQQLQTKEQIHLQETRKKAVVLARLL---ELQEEPCPLCGSCIHPNPARQ--DIDNPGPLTRRMQrGEQTYAQLETSEED 546

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   187 LDEKIVALREQNVHIQRKMASSEGSTE------SEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMA 260
Cdd:TIGR00618  547 VYHQLTSERKQRASLKEQMQEIQQSFSiltqcdNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   261 qmKERLAALSSRVGEVEQEAETArkdliKTEEMNTKYQRDIREAMAQKEDMEERitTLEKRYLSAQRESTSIHDMNDKLE 340
Cdd:TIGR00618  627 --LQDVRLHLQQCSQELALKLTA-----LHALQLTLTQERVREHALSIRVLPKE--LLASRQLALQKMQSEKEQLTYWKE 697

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   341 nELANKEAILRQMEE---KNRQLQERLELAEQKLQQTMR-KAETLPEVEAEL-AQRIAALTKAEERHGNIEER------- 408
Cdd:TIGR00618  698 -MLAQCQTLLRELEThieEYDREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKARTEAHFNNNEEvtaalqt 776

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   409 ---MRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEE 485
Cdd:TIGR00618  777 gaeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEE 856

                          410       420
                   ....*....|....*....|..
gi 966973599   486 SLHDKERLAEEIEKLRSELDQL 507
Cdd:TIGR00618  857 CSKQLAQLTQEQAKIIQLSDKL 878
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
266-514 7.36e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.08  E-value: 7.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  266 LAALSSRVGEVEQ--EAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrYLSAQREstsIHDMNDKLENEL 343
Cdd:PRK03918  127 LNAIYIRQGEIDAilESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEK-FIKRTEN---IEELIKEKEKEL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  344 ANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ---LEEKN 420
Cdd:PRK03918  203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKV 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  421 QELQRARQREKMNEEHNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLE---ESLHDKER 492
Cdd:PRK03918  283 KELKELKEKAEEYIKLSEFYEEYLDELreiekRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHE 362

                         250       260
                  ....*....|....*....|..
gi 966973599  493 LAEEIEKLRSELDQLKMRTGSL 514
Cdd:PRK03918  363 LYEEAKAKKEELERLKKRLTGL 384
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 106-515 1.13e-08

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: 59.65  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHeRSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHK 185
Cdd:TIGR04523  171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIS 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   186 ALDEKIVALREQNVHIQRKMA--SSEGSTESEHLEGMEPGQKVHEKRLSNgsIDSTDETSQIVELQELLEKQNYEMAQMK 263
Cdd:TIGR04523  250 NTQTQLNQLKDEQNKIKKQLSekQKELEQNNKKIKELEKQLNQLKSEISD--LNNQKEQDWNKELKSELKNQEKKLEEIQ 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   264 ERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREamaqKEDMEERIttlekrylsaQRESTSIHDMNDKLENEL 343
Cdd:TIGR04523  328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKL----------KKENQSYKQEIKNLESQI 393

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   344 ANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA----EERHGNIEERMRHLEGQ---- 415
Cdd:TIGR04523  394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQlkvl 473

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   416 ----------LEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLKERMAALE----EKNVLIQESETFRK 481
Cdd:TIGR04523  474 srsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEsekkEKESKISDLEDELN 548

                          410       420       430
                   ....*....|....*....|....*....|....
gi 966973599   482 NLEESLhDKERLAEEIEKLRSELDQLKMRTGSLI 515
Cdd:TIGR04523  549 KDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLK 581
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-506 1.17e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.69  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  102 EFAALTKELNACREQLLEKEEEISELKAER----------NNTRLLLEHLECLVSRHERSLRMTvVKRQAQSPSGVSSEV 171
Cdd:PRK03918  201 ELEEVLREINEISSELPELREELEKLEKEVkeleelkeeiEELEKELESLEGSKRKLEEKIREL-EERIEELKKEIEELE 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  172 EVLKALKSLFEHHKALdEKIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIdstdeTSQIVELQEL 251
Cdd:PRK03918  280 EKVKELKELKEKAEEY-IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL-----KKKLKELEKR 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  252 LEK-----QNYEMA-QMKERLAALSSRVGevEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEK---RY 322
Cdd:PRK03918  354 LEEleerhELYEEAkAKKEELERLKKRLT--GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieEL 431

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  323 LSAQ-------RESTSIHDMN--DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQ-----TMRK-AETLPEVEAE 387
Cdd:PRK03918  432 KKAKgkcpvcgRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKElAEQLKELEEK 511

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  388 LAQ-RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLsDTVDRLLTESNERLQLHLKERMAAL 466
Cdd:PRK03918  512 LKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL-DELEEELAELLKELEELGFESVEEL 590

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 966973599  467 EEKnvlIQESETFRK---NLEESLHDKERLAEEIEKLRSELDQ 506
Cdd:PRK03918  591 EER---LKELEPFYNeylELKDAEKELEREEKELKKLEEELDK 630
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-508 1.38e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.31  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  102 EFAALTKELNACREQLLE---KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALK 178
Cdd:PRK03918  315 RLSRLEEEINGIEERIKEleeKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  179 SLFEHHKALDEKIVALREQNVHIQRKMASSEGSTES-EHLEGMEPgqkvhekrLSNGSIDSTDETSQIVELQELLEKQNY 257
Cdd:PRK03918  395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElKKAKGKCP--------VCGRELTEEHRKELLEEYTAELKRIEK 466

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  258 EMAQMKERLAALSSRVGEVEQEAETARK--------DLIKT--EEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 327
Cdd:PRK03918  467 ELKEIEEKERKLRKELRELEKVLKKESEliklkelaEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  328 ESTSIHDMNDK---LENELANKEA----ILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE 400
Cdd:PRK03918  547 ELEKLEELKKKlaeLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  401 RHGNIEERMRHLEGQLEEKNQELQRARQreKMNEEHNKRLSDTVDRLltesnERLQLHLKERMAALEEknvLIQESETFR 480
Cdd:PRK03918  627 ELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLEL-----SRELAGLRAELEELEK---RREEIKKTL 696

                         410       420
                  ....*....|....*....|....*...
gi 966973599  481 KNLEESLHDKERLAEEIEKLRSELDQLK 508
Cdd:PRK03918  697 EKLKEELEEREKAKKELEKLEKALERVE 724
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 243-454 1.43e-08

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: 58.24  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  243 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 322
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  323 ----LSAQREST--------SIHDMNDkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 390
Cdd:COG4942   107 aellRALYRLGRqpplalllSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966973599  391 RIAALTKAEERHgniEERMRHLEGQLEEKNQELQRARQREkmneehnKRLSDTVDRLLTESNER 454
Cdd:COG4942   186 ERAALEALKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAA 239
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 30-514 2.67e-08

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 58.59  E-value: 2.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    30 HFEQLMVNMLDERDRLLDTLRETQESLSLAQQRlQDVIYDRDSLQRQLNSALPQDIESltgglagsKGADPPEFAALTKE 109
Cdd:pfam15921  367 QFSQESGNLDDQLQKLLADLHKREKELSLEKEQ-NKRLWDRDTGNSITIDHLRRELDD--------RNMEVQRLEALLKA 437

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   110 LNA-CREQLlekEEEISELKAERNNtrllLEHLECLVSRHERS---LRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHK 185
Cdd:pfam15921  438 MKSeCQGQM---ERQMAAIQGKNES----LEKVSSLTAQLESTkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKER 510

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   186 ALDEKIVALREQNVHIQRKMASSEG-STESEHLEGMEPGQKVHEKRLSngsidstdETSQIVE-LQELLEKQNYEMAQMK 263
Cdd:pfam15921  511 AIEATNAEITKLRSRVDLKLQELQHlKNEGDHLRNVQTECEALKLQMA--------EKDKVIEiLRQQIENMTQLVGQHG 582

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   264 ERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENEL 343
Cdd:pfam15921  583 RTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEV 662

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   344 ANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQE 422
Cdd:pfam15921  663 KTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMqLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQ 742

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   423 LQRARQREKMNEEhnkrlsdtvdrLLTESNerlqlhlKERMAALEEKNVLIQESETFRKnleeslhDKERLAEEIEKLRS 502
Cdd:pfam15921  743 IDALQSKIQFLEE-----------AMTNAN-------KEKHFLKEEKNKLSQELSTVAT-------EKNKMAGELEVLRS 797

                          490
                   ....*....|..
gi 966973599   503 ELDQLKMRTGSL 514
Cdd:pfam15921  798 QERRLKEKVANM 809
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 244-401 2.71e-08

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: 56.09  E-value: 2.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  244 QIVELQELLEkqnyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR-- 321
Cdd:COG1579     8 ALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlg 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  322 -------YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAA 394
Cdd:COG1579    84 nvrnnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEE 160


                  ....*..
gi 966973599  395 LTKAEER 401
Cdd:COG1579   161 LEAEREE 167
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 189-505 4.82e-08

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 57.65  E-value: 4.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  189 EKIVALREQNVHIQRKMASSEGSTE--SEHLEGMEPGQKVHEKRLSNGSI-DSTDETSQIVELQELLEKQNYEMAQMKER 265
Cdd:COG3096   836 AELAALRQRRSELERELAQHRAQEQqlRQQLDQLKEQLQLLNKLLPQANLlADETLADRLEELREELDAAQEAQAFIQQH 915

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  266 LAALSsrvgEVEQEAETARKDLIKTEEMNTKYQRdireAMAQKEDMEERITTLEkrYLSAQRESTSIHD----------M 335
Cdd:COG3096   916 GKALA----QLEPLVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALS--EVVQRRPHFSYEDavgllgensdL 985

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  336 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL-----TKAEERhgnIEERMR 410
Cdd:COG3096   986 NEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadAEAEER---ARIRRD 1062

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  411 HLEGQL----EEKNQ-ELQRARQREKMnEEHNKRLSDtVDRLLTESNERLQLHLKERMAALEeknvLIQESetfrkNLEE 485
Cdd:COG3096  1063 ELHEELsqnrSRRSQlEKQLTRCEAEM-DSLQKRLRK-AERDYKQEREQVVQAKAGWCAVLR----LARDN-----DVER 1131

                         330       340
                  ....*....|....*....|
gi 966973599  486 SLHDKERLAEEIEKLRSELD 505
Cdd:COG3096  1132 RLHRRELAYLSADELRSMSD 1151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 50-426 6.41e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 6.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   50 RETQESLSLAQQRLQdvIYDRDSLQRQLNSALpQDIESLTGGLAGSKGadppEFAALTKELNACREQLLEKEEEISELKA 129
Cdd:COG1196   216 RELKEELKELEAELL--LLKLRELEAELEELE-AELEELEAELEELEA----ELAELEAELEELRLELEELELELEEAQA 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  130 ERnntRLLLEHLEclvsRHERSLRMTVVKRQAQSpsgvSSEVEVLKALKSLFEHHKALDEKIVALREQNVHIQRKMASSE 209
Cdd:COG1196   289 EE---YELLAELA----RLEQDIARLEERRRELE----ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  210 G--STESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDL 287
Cdd:COG1196   358 AelAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  288 IKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELA 367
Cdd:COG1196   438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 966973599  368 EQKLQQtmRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 426
Cdd:COG1196   518 GLRGLA--GAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 353-508 7.78e-08

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: 54.55  E-value: 7.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  353 MEEKNRQLqERLELAEQKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARq 428
Cdd:COG1579     2 MPEDLRAL-LDLQELDSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  429 rEKMNEEHNKRLSDTVDR---LLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESL-HDKERLAEEIEKLRSEL 504
Cdd:COG1579    80 -EQLGNVRNNKEYEALQKeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELeEKKAELDEELAELEAEL 158


                  ....
gi 966973599  505 DQLK 508
Cdd:COG1579   159 EELE 162
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
337-503 8.94e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 8.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  337 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtLPEVEAELA---QRIAALTKAEERHGNIEERMRHLE 413
Cdd:COG4913   620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAeleAELERLDASSDDLAALEEQLEELE 698

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  414 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT-------ESNERLQLHLKERMAALEEKNVLIQESETFRKNLEES 486
Cdd:COG4913   699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDrleaaedLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778

                         170
                  ....*....|....*..
gi 966973599  487 LHDKERLAEEIEKLRSE 503
Cdd:COG4913   779 RARLNRAEEELERAMRA 795
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
243-533 9.03e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.68  E-value: 9.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  243 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 322
Cdd:COG4372    45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  323 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaetlpevEAELAQRIAALTKAEERH 402
Cdd:COG4372   125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKEANRN 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  403 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKN 482
Cdd:COG4372   196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 966973599  483 LEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTISRTHLDTSAELRYS 533
Cdd:COG4372   276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
39-432 1.11e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.31  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLnSALPQDIESLTGGLagskgadppEFAALTKELNACREQLL 118
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL-EELREELEKLEKLL---------QLLPLYQELEALEAELA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  119 EKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKIVALREQN 198
Cdd:COG4717   143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  199 VHIQRKMASSEGSTESEHLEgmepgQKVHEKRLS-------------NGSIDSTDETSQ---------IVELQELLEKQN 256
Cdd:COG4717   223 EELEEELEQLENELEAAALE-----ERLKEARLLlliaaallallglGGSLLSLILTIAgvlflvlglLALLFLLLAREK 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  257 YEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN 336
Cdd:COG4717   298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA 377

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  337 DKLENELANKEAILRQMEEKnRQLQERLELAEQKLQQ------TMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMR 410
Cdd:COG4717   378 EAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELA 456

                         410       420
                  ....*....|....*....|....
gi 966973599  411 HLEGQLE--EKNQELQRARQREKM 432
Cdd:COG4717   457 ELEAELEqlEEDGELAELLQELEE 480
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 996-1051 1.20e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.99  E-value: 1.20e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 966973599    996 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1051
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 216-507 1.24e-07

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: 56.13  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   216 HLEGMEPGQKVHEKRLSNGSIdSTDETSQIVELQELLEKQNYEMAqmkERLAALSS-RVGEVEQEAETARKDLIKTEEMN 294
Cdd:TIGR00618  100 HRKTEQPEQLYLEQKKGRGRI-LAAKKSETEEVIHDLLKLDYKTF---TRVVLLPQgEFAQFLKAKSKEKKELLMNLFPL 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   295 TKYQRDIREAMAQKEDMEERITTLEKRY----LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK 370
Cdd:TIGR00618  176 DQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ 255

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   371 ------LQQTMRKAETLPEVEAELAQRIAALTKA--EERHGNIEERMRHLEGQLEEKNQELQ-RARQREKMNEEHNKRLS 441
Cdd:TIGR00618  256 lkkqqlLKQLRARIEELRAQEAVLEETQERINRArkAAPLAAHIKAVTQIEQQAQRIHTELQsKMRSRAKLLMKRAAHVK 335

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   442 DTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLH----DKERLAEEIEKLRSELDQL 507
Cdd:TIGR00618  336 QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqQKTTLTQKLQSLCKELDIL 405
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
243-531 1.41e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.08  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  243 SQIVELQELLEKQNYEMAQMKERLAALSSRvGEVEQEAETARKDLIKTEEmntkYQRDIREAMAQKED----------ME 312
Cdd:COG4913   617 AELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVAS----AEREIAELEAELERldassddlaaLE 691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  313 ERITTLEKRYlsaqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRI 392
Cdd:COG4913   692 EQLEELEAEL--------------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERF 755

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  393 AALtKAEERHGNIEERmrhLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDRLLT--ESNERLQLHLK----ERMAA 465
Cdd:COG4913   756 AAA-LGDAVERELREN---LEERIDALRARLNRAEEElERAMRAFNREWPAETADLDAdlESLPEYLALLDrleeDGLPE 831

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966973599  466 LEEK--NVLIQESETFRKNLEESLHDKERLAEE-IEKLRSELDQLKMRTGSLIEPTISRTHLDTSAELR 531
Cdd:COG4913   832 YEERfkELLNENSIEFVADLLSKLRRAIREIKErIDPLNDSLKRIPFGPGRYLRLEARPRPDPEVREFR 900
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 195-507 1.47e-07

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: 55.95  E-value: 1.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   195 REQNVHIQRKMASSEGSTESEHLEGMEPG-QKVH-EKRLSNGSIDSTDETSQIVELQEllEKQNYEMAQMKERLAALSSR 272
Cdd:pfam01576   90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAArQKLQlEKVTTEAKIKKLEEDILLLEDQN--SKLSKERKLLEERISEFTSN 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   273 VGEVEQEAETARKDLIKTEEMNTkyqrDIREAMAQKEDMEERittLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQ 352
Cdd:pfam01576  168 LAEEEEKAKSLSKLKNKHEAMIS----DLEERLKKEEKGRQE---LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   353 MEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK------NQE 422
Cdd:pfam01576  241 KEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldttaaQQE 320

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   423 LQRARQRE--------------------KMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKNVLI--------- 473
Cdd:pfam01576  321 LRSKREQEvtelkkaleeetrsheaqlqEMRQKHTQALEELTEQL--EQAKRNKANLEKAKQALESENAELqaelrtlqq 398

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 966973599   474 --QESETFRKNLEESLHD-----------KERLAEEIEKLRSELDQL 507
Cdd:pfam01576  399 akQDSEHKRKKLEGQLQElqarlseserqRAELAEKLSKLQSELESV 445
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
325-512 2.00e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.43  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  325 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 404
Cdd:PRK02224  197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  405 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH-------------LKERMAALEE 468
Cdd:PRK02224  277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedrDEELRDRLEECrvaaqahneeaesLREDADDLEE 356

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 966973599  469 KNVLIQE-SETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTG 512
Cdd:PRK02224  357 RAEELREeAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
318-510 2.09e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.16  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  318 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 397
Cdd:COG4717    51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  398 AEERHgNIEERMRHLEGQLEE---KNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKErmaaleeknvLIQ 474
Cdd:COG4717   131 YQELE-ALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----------LAE 199

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 966973599  475 ESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 510
Cdd:COG4717   200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
259-467 3.02e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.77  E-value: 3.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  259 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREStsihdmnDK 338
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-------EK 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  339 LENELANKEAI--LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN-IEERMRHLEGQ 415
Cdd:COG4717   121 LEKLLQLLPLYqeLEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLaTEEELQDLAEE 200

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 966973599  416 LEEKNQELQRARQREKMNEEHNKRLSDTVDRLlteSNERLQLHLKERMAALE 467
Cdd:COG4717   201 LEELQQRLAELEEELEEAQEELEELEEELEQL---ENELEAAALEERLKEAR 249
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 106-499 3.80e-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: 54.64  E-value: 3.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSpsgVSSEVEVLKALKSLfEHHK 185
Cdd:TIGR04523  237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL--EKQLNQ---LKSEISDLNNQKEQ-DWNK 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   186 ALDEKIVALREQNVHIQRKMASSEGSTES--EHLEGMEpgqkvheKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMK 263
Cdd:TIGR04523  311 ELKSELKNQEKKLEEIQNQISQNNKIISQlnEQISQLK-------KELTNSESENSEKQRELEEKQNEIEKLKKENQSYK 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   264 ERLAALSSRVGEVEQEAEtarkdliKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsIHDmndkLENEL 343
Cdd:TIGR04523  384 QEIKNLESQINDLESKIQ-------NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE---IKD----LTNQD 449

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   344 ANKEAILRQMEEKNRQLQERLEL-------AEQKLQQTMR-------KAETLPEVEAELAQRIAALTKaeeRHGNIEERM 409
Cdd:TIGR04523  450 SVKELIIKNLDNTRESLETQLKVlsrsinkIKQNLEQKQKelkskekELKKLNEEKKELEEKVKDLTK---KISSLKEKI 526

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   410 RHLEGQLEEKNQEL-QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLH 488
Cdd:TIGR04523  527 EKLESEKKEKESKIsDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606

                          410
                   ....*....|.
gi 966973599   489 DKERLAEEIEK 499
Cdd:TIGR04523  607 EKEKKISSLEK 617
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
244-428 3.87e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 3.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  244 QIVELQELLEKQNyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEmnTKYQRDIREAMAQKEDMEERITTLEKRYL 323
Cdd:COG4913   250 QIELLEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLEARLDALREELD 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  324 SAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQkLQQTMRKAE-TLPEVEAELAQRI----AALTKA 398
Cdd:COG4913   327 ELEAQ---------IRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRaeaaALLEAL 396

                         170       180       190
                  ....*....|....*....|....*....|
gi 966973599  399 EERHGNIEERMRHLEGQLEEKNQELQRARQ 428
Cdd:COG4913   397 EEELEALEEALAEAEAALRDLRRELRELEA 426
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
102-530 4.47e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.39  E-value: 4.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQaqspsgVSSEVEVLKALKSLF 181
Cdd:COG4717    82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE------LAELPERLEELEERL 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  182 EHHKALDEKIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLsngsidstdetSQIVELQELLEKQNYEMAQ 261
Cdd:COG4717   156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ-----------QRLAELEEELEEAQEELEE 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  262 MKERLAALSSRVGEVEQEAETARKD-----------------------------------LIKTEEMNTKYQRDIREAMA 306
Cdd:COG4717   225 LEEELEQLENELEAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlgLLALLFLLLAREKASLGKEA 304

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  307 QKEDMEERITTLEKRYLSAQRESTSI-HDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE 385
Cdd:COG4717   305 EELQALPALEELEEEELEELLAALGLpPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  386 AELAQRIAALTKAEErhgnIEERMRHLEGQLEEKNQELQRARQREKmNEEHNKRLSDTVDRLLTESNERLQLHlkERMAA 465
Cdd:COG4717   385 EELRAALEQAEEYQE----LKEELEELEEQLEELLGELEELLEALD-EEELEEELEELEEELEELEEELEELR--EELAE 457

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966973599  466 LEEKNVLIQESETfrknLEESLHDKERLAEEIEKLRSELDQLKMrTGSLIEPTISRTHLDTSAEL 530
Cdd:COG4717   458 LEAELEQLEEDGE----LAELLQELEELKAELRELAEEWAALKL-ALELLEEAREEYREERLPPV 517
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 169-508 5.46e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 53.97  E-value: 5.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   169 SEVEVLKALKSLFEHHKALDEKIVALREQNVHIQR-KMASSEGSTESEHLEGMEPGQKVHEKRLS-NGSIDSTDETSQIV 246
Cdd:pfam17380  266 TENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERlRQEKEEKAREVERRRKLEEAEKARQAEMDrQAAIYAEQERMAME 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   247 ELQEL----LEKQNYEMAQMK-ERLAALSSRVGEVEQ-EAETARKdlikteemNTKYQRDIREAMAQKEDMEERittlEK 320
Cdd:pfam17380  346 RERELerirQEERKRELERIRqEEIAMEISRMRELERlQMERQQK--------NERVRQELEAARKVKILEEER----QR 413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   321 RYLSAQRESTSIhdmndKLENELANKEAILRQMEEKNRQLqERLELAEQKLQQTMrkaETLPEVEAELAQRIAALTKAEE 400
Cdd:pfam17380  414 KIQQQKVEMEQI-----RAEQEEARQREVRRLEEERAREM-ERVRLEEQERQQQV---ERLRQQEEERKRKKLELEKEKR 484

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   401 RHGNIEERMRH-LEGQLEEKnqelqrarqREKMNEEHNKRlsdtvdrlltesnERLQLHLKERMAALEEKNVLIQESETF 479
Cdd:pfam17380  485 DRKRAEEQRRKiLEKELEER---------KQAMIEEERKR-------------KLLEKEMEERQKAIYEEERRREAEEER 542

                          330       340
                   ....*....|....*....|....*....
gi 966973599   480 RKNLEesLHDKERLAEEIEKLRSELDQLK 508
Cdd:pfam17380  543 RKQQE--MEERRRIQEQMRKATEERSRLE 569
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
219-508 5.55e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.37  E-value: 5.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  219 GMEPGQKVHEKRLSNGSIdSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ 298
Cdd:COG4372     1 GDRLGEKVGKARLSLFGL-RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  299 RDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 378
Cdd:COG4372    80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  379 ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH 458
Cdd:COG4372   160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 966973599  459 LKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 508
Cdd:COG4372   240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1074-1145 7.45e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 47.68  E-value: 7.45e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966973599   1074 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1145
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
PRK12704 PRK12704
phosphodiesterase; Provisional
 342-499 1.09e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.86  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  342 ELANKEAIlRQMEEKNRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 421
Cdd:PRK12704   34 KEAEEEAK-RILEEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  422 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEtfrknlEESLHDKERLAEEIE 498
Cdd:PRK12704  111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179


                  .
gi 966973599  499 K 499
Cdd:PRK12704  180 E 180
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 39-446 1.38e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIESLTGGLAGSKgadppEFAALTKELNACREQLL 118
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-----ALEEAAEEEAELEEEEE 459

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  119 EKEEEISELKAERNNTRLLLEHLecLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKI------- 191
Cdd:COG1196   460 ALLELLAELLEEAALLEAALAEL--LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveaaye 537

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  192 ----VALREQNVHIQR---------------------------KMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTD 240
Cdd:COG1196   538 aaleAALAAALQNIVVeddevaaaaieylkaakagratflpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  241 ETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEK 320
Cdd:COG1196   618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  321 RYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE 400
Cdd:COG1196   698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966973599  401 RHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDR 446
Cdd:COG1196   778 ALGPVnllaieeyeelEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
PTZ00121 PTZ00121
MAEBL; Provisional
 215-499 1.47e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  215 EHLEGMEPGQKVHEKRLSNGSIDSTDET-----SQIVELQELL-EKQNYEMAQMKErlaalsSRVGEVEQEAETARKDLI 288
Cdd:PTZ00121 1031 ELTEYGNNDDVLKEKDIIDEDIDGNHEGkaeakAHVGQDEGLKpSYKDFDFDAKED------NRADEATEEAFGKAEEAK 1104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  289 KTEEMNTKYQRDIREAMAQKEDMeerittlekRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKnRQLQERLELAE 368
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDA---------RKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA-RKAEEARKAED 1174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  369 QKLQQTMRKAETLPEVE----AELAQRIAALTKAEERHgNIEERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTV 444
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEelrkAEDARKAEAARKAEEER-KAEEARKAED---AKKAEAVKKAEEAKKDAEEAKKAEEERN 1250

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 966973599  445 DRLLTESNERLQLHLKERMAAL--EEKnvliQESETFRKNLEESLHDKERLAEEIEK 499
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIkaEEA----RKADELKKAEEKKKADEAKKAEEKKK 1303
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 44-469 1.76e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 52.42  E-value: 1.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    44 RLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSA------LPQDIESLTGGLAGSKGADPPEFAALTKELNACREQL 117
Cdd:pfam05483  307 RSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAkaahsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMEL 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   118 LEKEEEISELKAERNNTRLLLEHLECLVSRHERSL-RMTVVKRQAQSPSGvsSEVEVLKALKSLFEHHKALDEKIVALRE 196
Cdd:pfam05483  387 QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLdEKKQFEKIAEELKG--KEQELIFLLQAREKEIHDLEIQLTAIKT 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   197 QNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSI--DSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVG 274
Cdd:pfam05483  465 SEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELtqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM 544

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   275 EVEQEAETARKDLI-----------KTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN------- 336
Cdd:pfam05483  545 NLRDELESVREEFIqkgdevkckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkg 624

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   337 --------------DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL--------PEVEAELAQRIAA 394
Cdd:pfam05483  625 saenkqlnayeikvNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIadeavklqKEIDKRCQHKIAE 704

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   395 LTKAEERHGN-----IEERMRHLeGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT---ESNERLQLHLKERMAAL 466
Cdd:pfam05483  705 MVALMEKHKHqydkiIEERDSEL-GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKENTAIL 783


                   ...
gi 966973599   467 EEK 469
Cdd:pfam05483  784 KDK 786
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 102-579 1.78e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 52.53  E-value: 1.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   102 EFAALTKELNacrEQLLEKEEEISELKAERNNTRLLL--------EHLECLVSRHERSLRMTVVKR---QAQSPSgVSSE 170
Cdd:pfam12128  280 ERQETSAELN---QLLRTLDDQWKEKRDELNGELSAAdaavakdrSELEALEDQHGAFLDADIETAaadQEQLPS-WQSE 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   171 VEVL-KALKSLFEHHKALDEKIVALR----EQNVHI----------QRKMASSEGSTESEHLEGME-PGQKVHEKRLSNG 234
Cdd:pfam12128  356 LENLeERLKALTGKHQDVTAKYNRRRskikEQNNRDiagikdklakIREARDRQLAVAEDDLQALEsELREQLEAGKLEF 435

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   235 SIDSTDETSQIVELQELLEKQNYEmAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEER 314
Cdd:pfam12128  436 NEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAANAEV-------ERLQSELRQARKRRDQASEA 507

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   315 ITTLEKRYLSAQRESTSIHDMND----KLENELANKEAILRQMEEK--NRQLQERLELAEQKLQQTMRKAETL------- 381
Cdd:pfam12128  508 LRQASRRLEERQSALDELELQLFpqagTLLHFLRKEAPDWEQSIGKviSPELLHRTDLDPEVWDGSVGGELNLygvkldl 587

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   382 ------------PEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL-- 447
Cdd:pfam12128  588 kridvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEkd 667

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   448 -LTESNERLQLHLKERMAALE-EKNVLIQESETF-----RKNLEESLHDKERLAEEIEKLRSELDQLKmrTGSLIEPTIS 520
Cdd:pfam12128  668 kKNKALAERKDSANERLNSLEaQLKQLDKKHQAWleeqkEQKREARTEKQAYWQVVEGALDAQLALLK--AAIAARRSGA 745

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966973599   521 RTHLDTSAELRY-SVGSL-VDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLgdHEWNRTQ 579
Cdd:pfam12128  746 KAELKALETWYKrDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY--FDWYQET 804
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 39-508 2.05e-06

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: 52.28  E-value: 2.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIE--SLTGGLAGSKGADPPEFAALTKELNACREQ 116
Cdd:TIGR00618  371 SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrDLQGQLAHAKKQQELQQRYAELCAAAITCT 450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   117 LLEKEEEISELKAERNNTRLLLEHLECLVSRHERslrmtvVKRQAQspsgvssevEVLKALKSLFEHHKALDEKivaLRE 196
Cdd:TIGR00618  451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ------ETRKKA---------VVLARLLELQEEPCPLCGS---CIH 512

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   197 QNVHIQrkmASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQEllekqnyEMAQMKERLAALSSRVGEV 276
Cdd:TIGR00618  513 PNPARQ---DIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE-------QMQEIQQSFSILTQCDNRS 582

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   277 EQEAETARK---DLIKTEEMNTKYQRDIREAM-AQKEDMEERITTLEKRYLS---AQRESTSIHDMNDKLENELANKEAI 349
Cdd:TIGR00618  583 KEDIPNLQNitvRLQDLTEKLSEAEDMLACEQhALLRKLQPEQDLQDVRLHLqqcSQELALKLTALHALQLTLTQERVRE 662

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   350 -LRQMEEKNRQLQERLELAEQKLQQtmrKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRarQ 428
Cdd:TIGR00618  663 hALSIRVLPKELLASRQLALQKMQS---EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA--R 737

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   429 REKMNEEHNK--RLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 506
Cdd:TIGR00618  738 EDALNQSLKElmHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817


                   ..
gi 966973599   507 LK 508
Cdd:TIGR00618  818 IL 819
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
224-410 2.65e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.94  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  224 QKVHEKRLSNGSIDSTDET----SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDlikteEMNTKYQR 299
Cdd:COG3206   196 AALEEFRQKNGLVDLSEEAklllQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRA 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  300 DIREAMAQKEDMEERITTLEKRYLSAQREstsIHDMNDKLENELankEAILRQMEEKNRQLQERLELAEQKLQQTMRKAE 379
Cdd:COG3206   271 QLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEA---QRILASLEAELEALQAREASLQAQLAQLEARLA 344

                         170       180       190
                  ....*....|....*....|....*....|.
gi 966973599  380 TLPEVEAELAQRIAALTKAEERHGNIEERMR 410
Cdd:COG3206   345 ELPELEAELRRLEREVEVARELYESLLQRLE 375
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 242-527 3.30e-06

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 51.59  E-value: 3.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   242 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKr 321
Cdd:TIGR00606  842 VSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK- 920

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   322 ylSAQRESTSIHDMNDklENELANKEaiLRQMEEKNRQLQERLELAEQKLQQTmrKAETLPEVEAELAQRIAALTKAEER 401
Cdd:TIGR00606  921 --DQQEKEELISSKET--SNKKAQDK--VNDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVNAQLEECEKH 992

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   402 HGNIEERMRHLEGQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESET 478
Cdd:TIGR00606  993 QEKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHV 1071

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 966973599   479 F-----RKNLEESLHDKERLAEEI-----EKLRSELDQLKMRTGSLIEPTISRTHLDTS 527
Cdd:TIGR00606 1072 LalgrqKGYEKEIKHFKKELREPQfrdaeEKYREMMIVMRTTELVNKDLDIYYKTLDQA 1130
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 301-468 4.04e-06

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: 49.54  E-value: 4.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  301 IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAeqklqQTMRKAET 380
Cdd:COG1579    19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----RNNKEYEA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  381 LpevEAELAQriaaltkAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLK 460
Cdd:COG1579    94 L---QKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163


                  ....*...
gi 966973599  461 ERMAALEE 468
Cdd:COG1579   164 EREELAAK 171
mukB PRK04863
chromosome partition protein MukB;
226-514 4.09e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 51.50  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  226 VHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDL------IKTEEMNTKYQR 299
Cdd:PRK04863  276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQA 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  300 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELA----------------------------------- 344
Cdd:PRK04863  356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqaldvqqtraiqyqqavqalerakqlcglpdl 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  345 ---NKEAILRQMEEKNRQLQERLELAEQKLQQTmRKAETLPEVEAELAQRIAALTKAEERHgnieERMRHLEGQLEEKNQ 421
Cdd:PRK04863  436 tadNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRKIAGEVSRSEAW----DVARELLRRLREQRH 510

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  422 ELQRARQ-REKMNE-EHNKRLSDTVDRLLTESNERLQLHLkERMAALEEknvLIQESETFRKNLEESlhdKERLAEEIEK 499
Cdd:PRK04863  511 LAEQLQQlRMRLSElEQRLRQQQRAERLLAEFCKRLGKNL-DDEDELEQ---LQEELEARLESLSES---VSEARERRMA 583

                         330
                  ....*....|....*
gi 966973599  500 LRSELDQLKMRTGSL 514
Cdd:PRK04863  584 LRQQLEQLQARIQRL 598
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 300-477 4.63e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.60  E-value: 4.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  300 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA- 378
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALy 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  379 ---ETLPEVEA--------ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL 447
Cdd:COG3883    97 rsgGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176

                         170       180       190
                  ....*....|....*....|....*....|
gi 966973599  448 LTESNERLQLHLKERMAALEEKNVLIQESE 477
Cdd:COG3883   177 QAEQEALLAQLSAEEAAAEAQLAELEAELA 206
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 102-513 4.80e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 50.98  E-value: 4.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   102 EFAALTKELNACREQLLEKEEEISELKAERNNtrlLLEHLEclvsrhERSLRMTVVKRQAQSPSGVSSEVEVlkALKSLF 181
Cdd:pfam10174  374 EKSTLAGEIRDLKDMLDVKERKINVLQKKIEN---LQEQLR------DKDKQLAGLKERVKSLQTDSSNTDT--ALTTLE 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   182 EhhkALDEK---IVALREQNvhiqrkmaSSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYE 258
Cdd:pfam10174  443 E---ALSEKeriIERLKEQR--------EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASS 511

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   259 MAQMKERLAALssrvgevEQEAETARKDLIKTEEMNTKYQrDIREAMAQKEDMEERITTLEKRYLSAQRESTsihdmndK 338
Cdd:pfam10174  512 GLKKDSKLKSL-------EIAVEQKKEECSKLENQLKKAH-NAEEAVRTNPEINDRIRLLEQEVARYKEESG-------K 576

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   339 LENELANKEAILRQME----EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTkaEERHGNIEERMR-HLE 413
Cdd:pfam10174  577 AQAEVERLLGILREVEneknDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLL--EEARRREDNLADnSQQ 654

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   414 GQLEEKNQELQRARQREkmnEEHNKRLSDTV------DRLLTESNERLQLHLKERM--------AALEEKNVLIQEsetf 479
Cdd:pfam10174  655 LQLEELMGALEKTRQEL---DATKARLSSTQqslaekDGHLTNLRAERRKQLEEILemkqeallAAISEKDANIAL---- 727

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 966973599   480 rknLEESLHDKERLAEEIEKLRSELD----QLKMRTGS 513
Cdd:pfam10174  728 ---LELSSSKKKKTQEEVMALKREKDrlvhQLKQQTQN 762
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 239-507 4.96e-06

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: 50.79  E-value: 4.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   239 TDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT-----------EEMNTKYQRDIReamaQ 307
Cdd:TIGR04523   92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFlteikkkekelEKLNNKYNDLKK----Q 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   308 KEDMEERITTLEKrylsaqrESTSIHDMNDKLENELANKE---AILRQMEEKNRQLQ-ERLELAEQKLQQTmrkaETLPE 383
Cdd:TIGR04523  168 KEELENELNLLEK-------EKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLEsQISELKKQNNQLK----DNIEK 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   384 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRArqrEKMNEEHNKRLSDTVDRLLTESNERLQLHLKERM 463
Cdd:TIGR04523  237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK 313

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 966973599   464 AALEEKNVLIQESETFRKNLEESLhdkERLAEEIEKLRSELDQL 507
Cdd:TIGR04523  314 SELKNQEKKLEEIQNQISQNNKII---SQLNEQISQLKKELTNS 354
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 240-504 6.35e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 50.74  E-value: 6.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   240 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVE----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 315
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlqelKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   316 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA- 394
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKe 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   395 ----LTKAEERHGNIEERMRHLEGQLEEKN---QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 467
Cdd:pfam02463  319 sekeKKKAEKELKKEKEEIEELEKELKELEikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 966973599   468 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSEL 504
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 41-358 6.45e-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: 50.84  E-value: 6.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    41 ERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIESLTGG------LAGSKGADPPEFAALTKELNACR 114
Cdd:TIGR02169  171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegyeLLKEKEALERQKEAIERQLASLE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSLFEHHKALDEKIVA 193
Cdd:TIGR02169  251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEKERELEDAEERLAK 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   194 LREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKR----LSNGSIDSTDETSQI-----VELQELLEKQNYEMAQMK- 263
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeleDLRAELEEVDKEFAEtrdelKDYREKLEKLKREINELKr 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   264 ------ERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMND 337
Cdd:TIGR02169  407 eldrlqEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486

                          330       340
                   ....*....|....*....|.
gi 966973599   338 KLENELANKEAILRQMEEKNR 358
Cdd:TIGR02169  487 KLQRELAEAEAQARASEERVR 507
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 996-1047 8.74e-06

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 44.15  E-value: 8.74e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 966973599  996 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1047
Cdd:cd09487     4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
327-496 9.65e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 9.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  327 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtLPEVEAELAQRIAALTKAEERHGNIE 406
Cdd:COG4717    81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEELEERLEELR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  407 E---RMRHLEGQLEEKNQELQRARQRekMNEEHNKRLSDTVDRlLTESNERLQlHLKERMAALEEKNVLIQESETFRKNL 483
Cdd:COG4717   160 EleeELEELEAELAELQEELEELLEQ--LSLATEEELQDLAEE-LEELQQRLA-ELEEELEEAQEELEELEEELEQLENE 235

                         170
                  ....*....|...
gi 966973599  484 EESLHDKERLAEE 496
Cdd:COG4717   236 LEAAALEERLKEA 248
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 260-508 1.03e-05

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 49.74  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   260 AQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRylsaqrestsihdmndkl 339
Cdd:pfam05557    2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKR------------------ 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   340 eneLANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgnieermrhlEGQLEEK 419
Cdd:pfam05557   64 ---EAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA----------ELELQST 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   420 NQELQRARQRekmNEEHNKRLSDtvdrlLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAeEIEK 499
Cdd:pfam05557  131 NSELEELQER---LDLLKAKASE-----AEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELA-RIPE 201


                   ....*....
gi 966973599   500 LRSELDQLK 508
Cdd:pfam05557  202 LEKELERLR 210
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 244-516 1.17e-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: 49.63  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   244 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK----------EDMEE 313
Cdd:TIGR04523  132 QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsnlKKKIQ 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   314 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAI-------LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 386
Cdd:TIGR04523  212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEisntqtqLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   387 ELAQRIAALTKAEERH---------GNIEERMRHLEGQLEEKNQELQRARQ------REKMNEEHNKRlsdTVDRLLTES 451
Cdd:TIGR04523  292 QLKSEISDLNNQKEQDwnkelkselKNQEKKLEEIQNQISQNNKIISQLNEqisqlkKELTNSESENS---EKQRELEEK 368

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966973599   452 NERLQLHLKERMAALEEKNVL----------IQESETFRKNLEESLH----DKERLAEEIEKLRSELDQLKMRTGSLIE 516
Cdd:TIGR04523  369 QNEIEKLKKENQSYKQEIKNLesqindleskIQNQEKLNQQKDEQIKklqqEKELLEKEIERLKETIIKNNSEIKDLTN 447
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 43-432 1.35e-05

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 48.91  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    43 DRLLDTLRETQESLSLAQQRLQDViydRDSLQRQL--NSALPQDIESLTGGLAGSKGadppEFAALTKELNACREQLLEK 120
Cdd:pfam19220   30 SQLIEPIEAILRELPQAKSRLLEL---EALLAQERaaYGKLRRELAGLTRRLSAAEG----ELEELVARLAKLEAALREA 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   121 EEEISELKAERNNTRLLLEHLE---CLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKIVALR-- 195
Cdd:pfam19220  103 EAAKEELRIELRDKTAQAEALErqlAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQal 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   196 --EQNVHI---QRKMASSEGSTESEH--LEGMEpGQKVHEKrlsngsidstdetsqiVELQELLEKQNYEMAQMKERLAA 268
Cdd:pfam19220  183 seEQAAELaelTRRLAELETQLDATRarLRALE-GQLAAEQ----------------AERERAEAQLEEAVEAHRAERAS 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   269 LSSRVgeveqEAETARkdLIKTEEMNTkyqrdirEAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEA 348
Cdd:pfam19220  246 LRMKL-----EALTAR--AAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQ 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   349 ILRQMEEKNRQLQERLElaeqklqqTMRKAetlpeveaeLAQRIAALTKAEERHGNIEERMRHLEGQ-------LEEKNQ 421
Cdd:pfam19220  312 QFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSDRIAELTKRfeveraaLEQANR 374

                          410
                   ....*....|.
gi 966973599   422 ELQRARQREKM 432
Cdd:pfam19220  375 RLKEELQRERA 385
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 340-508 1.38e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.06  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  340 ENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK 419
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN---ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  420 NQELQRARQREKMNEE--HNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKnvliqesetfRKNLEESLHDKER 492
Cdd:COG3883    92 ARALYRSGGSVSYLDVllGSESFSDFLDRLsalskIADADADLLEELKADKAELEAK----------KAELEAKLAELEA 161

                         170
                  ....*....|....*.
gi 966973599  493 LAEEIEKLRSELDQLK 508
Cdd:COG3883   162 LKAELEAAKAELEAQQ 177
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 38-505 2.15e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.96  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    38 MLDERDRLLDTLRETQESLSLAQQRLQDVIYDRD---SLQRQLNSALPQDIESLTGGLAGSKGAdppefaaltkeLNACR 114
Cdd:pfam15921  122 MQMERDAMADIRRRESQSQEDLRNQLQNTVHELEaakCLKEDMLEDSNTQIEQLRKMMLSHEGV-----------LQEIR 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   115 EQLLEKEEEISELKAERNN-TRLLLEHLECLVSRHERSLRMTVVKRQAQSPSgVSSEVEVLKA-----LKSLFEHHKALD 188
Cdd:pfam15921  191 SILVDFEEASGKKIYEHDSmSTMHFRSLGSAISKILRELDTEISYLKGRIFP-VEDQLEALKSesqnkIELLLQQHQDRI 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   189 EKIVAlrEQNVHIQrkmasseGSTEsehlegmepgqKVHEKRLSNGSIDstdetSQIVELQELLEKQNyemAQMKERLAA 268
Cdd:pfam15921  270 EQLIS--EHEVEIT-------GLTE-----------KASSARSQANSIQ-----SQLEIIQEQARNQN---SMYMRQLSD 321

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   269 LSSRVGEVEQEAETARKdlikteemntKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEA 348
Cdd:pfam15921  322 LESTVSQLRSELREAKR----------MYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREK 391

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   349 ILRQMEEKNRQLQERlelaeqklqqTMRKAETLPEVEAEL------AQRIAALTKA--EERHGNIEERMRHLEGqleeKN 420
Cdd:pfam15921  392 ELSLEKEQNKRLWDR----------DTGNSITIDHLRRELddrnmeVQRLEALLKAmkSECQGQMERQMAAIQG----KN 457

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   421 QELQRARQrekmneehnkrlsdtvdrlLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAE----E 496
Cdd:pfam15921  458 ESLEKVSS-------------------LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEatnaE 518


                   ....*....
gi 966973599   497 IEKLRSELD 505
Cdd:pfam15921  519 ITKLRSRVD 527
PRK01156 PRK01156
chromosome segregation protein; Provisional
 35-456 2.22e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 48.74  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   35 MVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSA-------------LPQDIESLTGGLAGSKGADPP 101
Cdd:PRK01156  244 LSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPvyknrnyindyfkYKNDIENKKQILSNIDAEINK 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  102 EFAALTK--ELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHErSLRM-----------------TVVKRQAQ 162
Cdd:PRK01156  324 YHAIIKKlsVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE-SLKKkieeyskniermsafisEILKIQEI 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  163 SPSGVSSEV-EVLKALKSLFEHHKALDEKIVALREQNVHIQRKMASSEGSTESEhLEGMEPGQKVHEKRLSNGSIDSTDE 241
Cdd:PRK01156  403 DPDAIKKELnEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCP-VCGTTLGEEKSNHIINHYNEKKSRL 481

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  242 TSQIVELQELLEKQNYEMAQMKERLAALSSrvGEVEQ------EAETARKDL--IKTEEMNTKYQRDIREAMAQK----- 308
Cdd:PRK01156  482 EEKIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKsineynKIESARADLedIKIKINELKDKHDKYEEIKNRykslk 559

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  309 -EDMEERITTLEKryLSAQRESTSIhDMNDKLENELANK----------------------EAILRQMEEKNRQLQERLE 365
Cdd:PRK01156  560 lEDLDSKRTSWLN--ALAVISLIDI-ETNRSRSNEIKKQlndlesrlqeieigfpddksyiDKSIREIENEANNLNNKYN 636

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  366 LAEQK--LQQTMR-KAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSD 442
Cdd:PRK01156  637 EIQENkiLIEKLRgKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSD 716

                         490
                  ....*....|....
gi 966973599  443 TVdrllTESNERLQ 456
Cdd:PRK01156  717 RI----NDINETLE 726
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 330-440 2.64e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 48.67  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  330 TSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGN 404
Cdd:PRK00409  509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 966973599  405 IEERMRHLE--GQLEEKNQELQRARQR-EKMNEEHNKRL 440
Cdd:PRK00409  589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 171-513 2.89e-05

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 48.42  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  171 VEVLKALKSLFEHHKALDEKIVALREQNVHIQRKMASSEGSTESEhLEGMEPGQKVHEKRLSNGS--IDSTDETSQIVEL 248
Cdd:COG5185   183 GLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKE-IINIEEALKGFQDPESELEdlAQTSDKLEKLVEQ 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  249 -QELLEKQNYEMAQMKERLAALSS-----------RVGEVEQEAETAR-----KDLIKTEEMNTKYQRDIREA----MAQ 307
Cdd:COG5185   262 nTDLRLEKLGENAESSKRLNENANnlikqfentkeKIAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETetgiQNL 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  308 KEDMEERITTLEKRYLSAQRESTSIHDMND------KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL 381
Cdd:COG5185   342 TAEIEQGQESLTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQ 421

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  382 PE--------VEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQRE--KMNEEHNKRLSDTVDRLLT-- 449
Cdd:COG5185   422 IEelqrqieqATSSNEEVSKLLNELISE---LNKVMREADEESQSRLEEAYDEINRSvrSKKEDLNEELTQIESRVSTlk 498

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966973599  450 ESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERlaEEIEKLRSELDQLKMRTGS 513
Cdd:COG5185   499 ATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL--ENLIPASELIQASNAKTDG 560
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
104-546 3.33e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  104 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMtvvkrqaqspsgvssevevlkalkslfeh 183
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV----------------------------- 663

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  184 hKALDEKIVALREQnvhiqrkmassegstesehLEgmepgqkvhekRLSNGSIDstdetsqIVELQELLEKQNYEMAQMK 263
Cdd:COG4913   664 -ASAEREIAELEAE-------------------LE-----------RLDASSDD-------LAALEEQLEELEAELEELE 705

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  264 ERLAALSSRVGEVEQEAETArkdlikteemntkyQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIhdmnDKLENEL 343
Cdd:COG4913   706 EELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLEERFAAALG----DAVEREL 767

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  344 AnkeailRQMEEKNRQLQERLELAEQKLQQTMRKA-ETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegQLEEKNQE 422
Cdd:COG4913   768 R------ENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLPEYLALLDRLEED------GLPEYEER 835

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  423 LQRARQR----------EKMNEEHN---KRLsDTVDRLLTESN----ERLQLHLKERmaALEEKNVLIQE-----SETFR 480
Cdd:COG4913   836 FKELLNEnsiefvadllSKLRRAIReikERI-DPLNDSLKRIPfgpgRYLRLEARPR--PDPEVREFRQElravtSGASL 912

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966973599  481 KNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIepTISRTHLDTSAELRYSV-GSLVDSQSDYRT 546
Cdd:COG4913   913 FDEELSEARFAALKRLIERLRSEEEESDRRWRARV--LDVRNHLEFDAEEIDREdGEEVETYSSSGG 977
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 237-509 3.42e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 48.28  E-value: 3.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   237 DSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT-EEMNTKYQrdIREAMAQKEDMEERI 315
Cdd:pfam10174  158 ESIKKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLrEELHRRNQ--LQPDPAKTKALQTVI 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   316 TTLEKRYLSAQRestSIHDMNDKLENELAN-------KEAILRQME----------EKNRQLQERLELAEQKLQQTMRKA 378
Cdd:pfam10174  236 EMKDTKISSLER---NIRDLEDEVQMLKTNgllhtedREEEIKQMEvykshskfmkNKIDQLKQELSKKESELLALQTKL 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   379 ETLPEVEAELAQRI----AALTKAEERHGNIEERMRHLEGQLEEKNQEL-QRARQREKMNEE---------HNKRLSDTV 444
Cdd:pfam10174  313 ETLTNQNSDCKQHIevlkESLTAKEQRAAILQTEVDALRLRLEEKESFLnKKTKQLQDLTEEkstlageirDLKDMLDVK 392

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966973599   445 DR---LLTESNERLQLHLKERMAALEEKNVLIQESETFRKN-------LEESLHDKERLAEEIEKLRSELDQLKM 509
Cdd:pfam10174  393 ERkinVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalttLEEALSEKERIIERLKEQREREDRERL 467
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 224-377 3.58e-05

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 46.05  E-value: 3.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   224 QKVHEKRLSNgsIDSTDEtsqivELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRE 303
Cdd:pfam15619   41 QKRQEKALGK--YEGTES-----ELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSED 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   304 A-MAQKEDMEERITTLEKRYLSAQREstsIHDMNDKLEN-------ELANKEAILRQMEEKNRQLQERLELAEQKLQQTM 375
Cdd:pfam15619  114 KnLAEREELQKKLEQLEAKLEDKDEK---IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKE 190


                   ..
gi 966973599   376 RK 377
Cdd:pfam15619  191 RE 192
PRK12705 PRK12705
hypothetical protein; Provisional
 358-555 4.13e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.78  E-value: 4.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  358 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegqlEEKNQELQRARQREKMNEEHN 437
Cdd:PRK12705   26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  438 KRLSDTVDRLLTESN----ERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHD--KERLAEEIEKLRSELD-QLKMR 510
Cdd:PRK12705   98 EKLDNLENQLEEREKalsaRELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAelEEEKAQRVKKIEEEADlEAERK 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 966973599  511 TGSLIEPTISRTHLDTSAELRYSVgslVDSQSDYRTTKVIRRPRR 555
Cdd:PRK12705  178 AQNILAQAMQRIASETASDLSVSV---VPIPSDAMKGRIIGREGR 219
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 45-507 4.85e-05

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: 47.86  E-value: 4.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    45 LLDTLRETQESLSLAQQRLQDVIYDRDSLQRQL------NSALPQDIESLTGGLAGSKGAD---PPEFAALTKEL----- 110
Cdd:pfam01576  234 LRAQLAKKEEELQAALARLEEETAQKNNALKKIreleaqISELQEDLESERAARNKAEKQRrdlGEELEALKTELedtld 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   111 --NACREQLLEKEEEISELKaernntrlllEHLECLVSRHERSLRmTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKAld 188
Cdd:pfam01576  314 ttAAQQELRSKREQEVTELK----------KALEEETRSHEAQLQ-EMRQKHTQALEELTEQLEQAKRNKANLEKAKQ-- 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   189 ekivALREQNVHIQRKMAS-SEGSTESEHlegmepGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEmaqmkerLA 267
Cdd:pfam01576  381 ----ALESENAELQAELRTlQQAKQDSEH------KRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE-------LE 443

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   268 ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrylsaqrESTSIHDMndkLENELANKE 347
Cdd:pfam01576  444 SVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLED-------ERNSLQEQ---LEEEEEAKR 513

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   348 AILRQMEEKNRQLQErlelAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERM----RHLEGQLEEKNQEL 423
Cdd:pfam01576  514 NVERQLSTLQAQLSD----MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLektkNRLQQELDDLLVDL 589

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   424 QRARQREKMNEEHNKRLsdtvDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSE 503
Cdd:pfam01576  590 DHQRQLVSNLEKKQKKF----DQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAE 665


                   ....
gi 966973599   504 LDQL 507
Cdd:pfam01576  666 MEDL 669
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 248-510 6.47e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.20  E-value: 6.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   248 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 327
Cdd:pfam07888   32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   328 ESTSIHdmndklenelANKEAILRQMEEKNRQLQErLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE-RHGNIE 406
Cdd:pfam07888  109 SSEELS----------EEKDALLAQRAAHEARIRE-LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEaERKQLQ 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   407 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH--LKERMAALEEK-NVLIQESETFR 480
Cdd:pfam07888  178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkLTTAHRKEAENeaLLEELRSLQERlNASERKVEGLG 257

                          250       260       270
                   ....*....|....*....|....*....|
gi 966973599   481 KNLEESLHDKERLAEEIEKLRSELDQLKMR 510
Cdd:pfam07888  258 EELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 83-509 7.40e-05

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: 47.09  E-value: 7.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    83 QDIESLTGGLAGSKGADPPEFAALTKELNACREQLLEKEEEIS-------ELKAERNNTRLLLEHLECLVSRHERSLRMT 155
Cdd:pfam01576  204 QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQaalarleEETAQKNNALKKIRELEAQISELQEDLESE 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   156 VVKRqAQSPSGVSSEVEVLKALKSLFEH---HKALDEKIVALREQNVHIQRKMASSEGstesehlegmepgqKVHEKRLS 232
Cdd:pfam01576  284 RAAR-NKAEKQRRDLGEELEALKTELEDtldTTAAQQELRSKREQEVTELKKALEEET--------------RSHEAQLQ 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   233 NGSIDstdETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETarkdlIKTEEMNTKYQRDIREAMAQKedme 312
Cdd:pfam01576  349 EMRQK---HTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRT-----LQQAKQDSEHKRKKLEGQLQE---- 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   313 erittLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaETLPEveaELAQRI 392
Cdd:pfam01576  417 -----LQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ---ELLQE---ETRQKL 485

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   393 AALTKAEErhgnIEERMRHLEGQLEEknqELQRARQREKMNEEHNKRLSDTVDRLLTESnerlqlhlkERMAALEE-KNV 471
Cdd:pfam01576  486 NLSTRLRQ----LEDERNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDA---------GTLEALEEgKKR 549

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 966973599   472 LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKM 509
Cdd:pfam01576  550 LQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLV 587
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
247-429 7.67e-05

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 46.99  E-value: 7.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  247 ELQELLEKQNyEMAQMKERL-------AALSSRVGEVEQ-EAEtaRKDLIKTEEMNTKYQRdIREAMAQKED-MEERITT 317
Cdd:COG0497   173 ELEELRADEA-ERARELDLLrfqleelEAAALQPGEEEElEEE--RRRLSNAEKLREALQE-ALEALSGGEGgALDLLGQ 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  318 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQKLQ---QTMRK----AETLPEVEAE 387
Cdd:COG0497   249 ALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdpERLEEVEERLAllrRLARKygvtVEELLAYAEE 328

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 966973599  388 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 429
Cdd:COG0497   329 LRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
393-516 9.19e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.77  E-value: 9.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  393 AALTKAEERHGNIEErmrhlegqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTEsNERLQLHLKERMAALEEknvL 472
Cdd:COG2433   380 EALEELIEKELPEEE---------PEAEREKEHEERELTEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---L 446

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 966973599  473 IQESETFRKNLEESLH-DKE--RLAEEIEKLRSELDQLKMRTGSLIE 516
Cdd:COG2433   447 ERELSEARSEERREIRkDREisRLDREIERLERELEEERERIEELKR 493
PRK11281 PRK11281
mechanosensitive channel MscK;
308-507 1.07e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.83  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  308 KEDMEERITTLEKRYLSAQRESTSIHDmndkLENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA- 386
Cdd:PRK11281   38 EADVQAQLDALNKQKLLEAEDKLVQQD----LEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  387 ELAQRIAALTkaeerhgnieerMRHLEGQLEEKNQELQRARqrekmneehnKRLSDTVDRLLTESN--ERLQlhlkermA 464
Cdd:PRK11281  113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQ-------A 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 966973599  465 ALEEKNVLIQESETFRKNLEESlhDKERLAEEIEKLRSELDQL 507
Cdd:PRK11281  164 ALYANSQRLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQALL 204
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 247-502 1.11e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.87  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  247 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEERITTLEKrylsaQ 326
Cdd:COG3096   358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL-------ADYQQALDVQQTRAIQYQQAVQALEK-----A 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  327 RESTSIHDMN-DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PEVEAELA-QRIAALTKAEE 400
Cdd:COG3096   426 RALCGLPDLTpENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVckiaGEVERSQAwQTARELLRRYR 505

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  401 RHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKERMAALEEknvLIQESETFR 480
Cdd:COG3096   506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----AAEELEELLAELEAQLEE---LEEQAAEAV 577

                         250       260
                  ....*....|....*....|..
gi 966973599  481 KNLEESLHDKERLAEEIEKLRS 502
Cdd:COG3096   578 EQRSELRQQLEQLRARIKELAA 599
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
301-508 1.21e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  301 IREAMAQKEDMEERITTLEKRYlsaqresTSIHDMNDKLEnELANKEAILRQMEEKNRQLQE-RLELAEQKLQQTMRKAE 379
Cdd:COG4913   213 VREYMLEEPDTFEAADALVEHF-------DDLERAHEALE-DAREQIELLEPIRELAERYAAaRERLAELEYLRAALRLW 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  380 TLPEVEAELAQRIAALtkaEERHGNIEERMRHLEGQLEEKNQELQRARQRekmneehnkRLSDTVDRL--LTESNERLQL 457
Cdd:COG4913   285 FAQRRLELLEAELEEL---RAELARLEAELERLEARLDALREELDELEAQ---------IRGNGGDRLeqLEREIERLER 352

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 966973599  458 HLKERMAALEEKNVLIQ--------ESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 508
Cdd:COG4913   353 ELEERERRRARLEALLAalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 247-510 1.37e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.68  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   247 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRE--AMAQKEDMEERITTLE--KRY 322
Cdd:pfam13868   56 ALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEedQAEAEEKLEKQRQLREeiDEF 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   323 LSAQRESTSIHDMNDKLENElANKEAILRQMEEKNRQLQERLELAEQK----------LQQTMRKAETLPEVEAELAQ-- 390
Cdd:pfam13868  136 NEEQAEWKELEKEEEREEDE-RILEYLKEKAEREEEREAEREEIEEEKereiarlraqQEKAQDEKAERDELRAKLYQee 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   391 -----RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAA 465
Cdd:pfam13868  215 qerkeRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRE 294

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 966973599   466 LEEknvLIQESE-TFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 510
Cdd:pfam13868  295 LEK---QIEEREeQRAAEREEELEEGERLREEEAERRERIEEERQK 337
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 872-936 1.38e-04

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 41.10  E-value: 1.38e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966973599   872 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 936
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1074-1144 1.53e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.53e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966973599  1074 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1144
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 172-508 1.55e-04

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 46.00  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   172 EVLKALKSLFEHHKALDEKIVALREQNVHIQRKMASSEGStesehlegMEPGQKVHEKRLSNgsIDStdetsQIVELQEL 251
Cdd:pfam06160  104 QILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFS--------YGPAIDELEKQLAE--IEE-----EFSQFEEL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   252 LEKQNYEMA-----QMKERLAALSSRVGEVEQEAETARKDLikTEEMNtkyqrDIREAMAQkedMEERITTLEkrYLSAQ 326
Cdd:pfam06160  169 TESGDYLEArevleKLEEETDALEELMEDIPPLYEELKTEL--PDQLE-----ELKEGYRE---MEEEGYALE--HLNVD 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   327 RESTSIHDMNDKLENELANKEaiLRQMEEKNRQLQERLElaeqKLQQTMRKaetlpEVEAELaqriaaltKAEERHGNIE 406
Cdd:pfam06160  237 KEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERID----QLYDLLEK-----EVDAKK--------YVEKNLPEIE 297

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   407 ERMRHLEGQLEEKNQELQRARQREKMNEEH-------NKRLsDTVDRLLTESNERLQLH------LKERMAALEEKNVLI 473
Cdd:pfam06160  298 DYLEHAEEQNKELKEELERVQQSYTLNENElervrglEKQL-EELEKRYDEIVERLEEKevayseLQEELEEILEQLEEI 376

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 966973599   474 QES-ETFRKNLeESLHDKERLA-EEIEKLRSELDQLK 508
Cdd:pfam06160  377 EEEqEEFKESL-QSLRKDELEArEKLDEFKLELREIK 412
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 247-475 1.74e-04

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 44.71  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   247 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKryLSAQ 326
Cdd:pfam06008   27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKE--INEK 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   327 RESTSIHDM---NDKLENELANKEAILRQMeeKNRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRIAALTKAeerhg 403
Cdd:pfam06008  105 VATLGENDFalpSSDLSRMLAEAQRMLGEI--RSRDFGTQLQNAEAEL----KAAQDLLSRIQTWFQSPQEENKA----- 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   404 nIEERMRHLEGQLEEKNQELQ--------RARQREKMNEEHNKRLSDTVDRLLT--ESNERLQLHLKERMAALEEKNVLI 473
Cdd:pfam06008  174 -LANALRDSLAEYEAKLSDLRellreaaaKTRDANRLNLANQANLREFQRKKEEvsEQKNQLEETLKTARDSLDAANLLL 252


                   ..
gi 966973599   474 QE 475
Cdd:pfam06008  253 QE 254
mukB PRK04863
chromosome partition protein MukB;
350-500 1.79e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.10  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  350 LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQr 429
Cdd:PRK04863  525 LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAP- 603

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966973599  430 ekmnEEHNkrLSDTVDRLLTESNERLqlhlkERMAALEE--KNVLIQESETfRKNLEESLHDKERLAEEIEKL 500
Cdd:PRK04863  604 ----AWLA--AQDALARLREQSGEEF-----EDSQDVTEymQQLLEREREL-TVERDELAARKQALDEEIERL 664
PRK01156 PRK01156
chromosome segregation protein; Provisional
 41-543 1.88e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 45.66  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   41 ERDRLLDTLRETqESLSLAQQRLQDVI-----------YDRDSLQRQLNsalpqDIESLTGGLAgskgADPPEFAALTKE 109
Cdd:PRK01156  150 QRKKILDEILEI-NSLERNYDKLKDVIdmlraeisnidYLEEKLKSSNL-----ELENIKKQIA----DDEKSHSITLKE 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  110 LNACREQLLEKEEEISELKAERNNtrllLEHLECLVSRHERSLRmtvvkrqaQSPSGVSSEVEVLKALKSLFEHHKAL-D 188
Cdd:PRK01156  220 IERLSIEYNNAMDDYNNLKSALNE----LSSLEDMKNRYESEIK--------TAESDLSMELEKNNYYKELEERHMKIiN 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  189 EKIVALREQ---------NVHIQRKMAS---SEGSTESEHLEGMEPGQKVHEKRLSNGSiDSTDETSQIVELQELLEK-- 254
Cdd:PRK01156  288 DPVYKNRNYindyfkyknDIENKKQILSnidAEINKYHAIIKKLSVLQKDYNDYIKKKS-RYDDLNNQILELEGYEMDyn 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  255 ---QNYEMAQMK--------ERLAALSSRV--------GEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 315
Cdd:PRK01156  367 sylKSIESLKKKieeyskniERMSAFISEIlkiqeidpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNM 446

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  316 TTLEKR--------YLSAQRESTSIHDMNDK---LENELANKEAILRQMEEKNRQLQERLE-LAEQKLQQTMRKAETLPE 383
Cdd:PRK01156  447 EMLNGQsvcpvcgtTLGEEKSNHIINHYNEKksrLEEKIREIEIEVKDIDEKIVDLKKRKEyLESEEINKSINEYNKIES 526

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  384 VEAELAQ---RIAALTKAEERHGNIEERMRHLE-GQLEEKNQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNERLQlh 458
Cdd:PRK01156  527 ARADLEDikiKINELKDKHDKYEEIKNRYKSLKlEDLDSKRTSWLNAlAVISLIDIETNRSRSNEIKKQLNDLESRLQ-- 604

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  459 lkERMAALEEKNVLIQESETFRKNLEESLHDKERLAEE----IEKLRSELDQLKMRTGSL--IEP---TISRTHLDTSAE 529
Cdd:PRK01156  605 --EIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQEnkilIEKLRGKIDNYKKQIAEIdsIIPdlkEITSRINDIEDN 682

                         570
                  ....*....|....
gi 966973599  530 LRYSVGSLVDSQSD 543
Cdd:PRK01156  683 LKKSRKALDDAKAN 696
pepcterm_ChnLen TIGR03007
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ...
 235-390 2.04e-04

polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this protein family belong to the family of polysaccharide chain length determinant proteins (pfam02706). All are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria, and are found near the epsH homolog that is the putative exosortase gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274386 [Multi-domain]  Cd Length: 498  Bit Score: 45.43  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   235 SIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLI-----KTEEMNTKYQR---------- 299
Cdd:TIGR03007  196 PDQEGDYYSEISEAQEELEAARLELNEAIAQRDALKRQLGGEEPVLLAGSSVANseldgRIEALEKQLDAlrlrytdkhp 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   300 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqQTMRKAE 379
Cdd:TIGR03007  276 DVIATKREIAQLEEQKEEEGSAKNGGPERGEIANPVYQQLQIELAEAEAEIASLEARVAELTARIE-------RLESLLR 348

                          170
                   ....*....|.
gi 966973599   380 TLPEVEAELAQ 390
Cdd:TIGR03007  349 TIPEVEAELTQ 359
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 40-421 2.32e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 45.71  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   40 DERDRLLDTLRETQEsLSLAQQRL-QDVIYDRDSLQRQLNsALPQ---------DIESLTGGLAGSKGAdppeFAALTKE 109
Cdd:COG3096   303 EEQYRLVEMARELEE-LSARESDLeQDYQAASDHLNLVQT-ALRQqekieryqeDLEELTERLEEQEEV----VEEAAEQ 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  110 LNACREQLLEKEEEISELKAErnntrlLLEHLECLVSRHERSLRMtvvkRQAQSPSGVSSEVEVLKAL--KSLFEHHKAL 187
Cdd:COG3096   377 LAEAEARLEAAEEEVDSLKSQ------LADYQQALDVQQTRAIQY----QQAVQALEKARALCGLPDLtpENAEDYLAAF 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  188 DEKIVALREQNVHIQRKMASSEgSTESEHLEGMEPGQKVhekrlsNGSIDSTDETSQIvelQELLEKQNYEMAQMkERLA 267
Cdd:COG3096   447 RAKEQQATEEVLELEQKLSVAD-AARRQFEKAYELVCKI------AGEVERSQAWQTA---RELLRRYRSQQALA-QRLQ 515

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  268 ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAM---AQKEDMEERITTLEKRYLSAQRESTSIHdmndKLENELA 344
Cdd:COG3096   516 QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEeleELLAELEAQLEELEEQAAEAVEQRSELR----QQLEQLR 591

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966973599  345 NKEAILRQMEEKNRQLQERLE-LAEQKLQQTmrkaETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 421
Cdd:COG3096   592 ARIKELAARAPAWLAAQDALErLREQSGEAL----ADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 266-501 3.66e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.83  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  266 LAALSSRVGEVEQEAET-----ARKDLIKTEEMNTKYQRD---IREAMA----QKEDMEERITTLEKRYLSAQRE----S 329
Cdd:PRK04778   81 LPDIEEQLFEAEELNDKfrfrkAKHEINEIESLLDLIEEDieqILEELQelleSEEKNREEVEQLKDLYRELRKSllanR 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  330 TSIHDMNDKLENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI-AALTKAEE--- 400
Cdd:PRK04778  161 FSFGPALDELEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKAgyr 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  401 ---------RHGNIEERMRHLEGQLEEKNQELQR---ARQREKmNEEHNKRLSDTVDRLLTEsnerlqlhlkerMAAlee 468
Cdd:PRK04778  241 elveegyhlDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEK-NEEIQERIDQLYDILERE------------VKA--- 304

                         250       260       270
                  ....*....|....*....|....*....|...
gi 966973599  469 KNVLIQESETFRKNLEESLHDKERLAEEIEKLR 501
Cdd:PRK04778  305 RKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVK 337
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
354-507 3.68e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  354 EEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK-------------AEERHGNIEERMRHLE---GQLE 417
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvasAEREIAELEAELERLDassDDLA 688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  418 EKNQELQRARQREKMNEEHNKRLSDTVDRLLTE--SNERLQLHLKERMAALEEKNVLIQES---ETFRKNLEESLHDK-- 490
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIGRLEKEleQAEEELDELQDRLEAAEDLARLELRAlleERFAAALGDAVERElr 768

                         170
                  ....*....|....*..
gi 966973599  491 ERLAEEIEKLRSELDQL 507
Cdd:COG4913   769 ENLEERIDALRARLNRA 785
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 242-527 3.94e-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: 44.96  E-value: 3.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   242 TSQIVELQELLEKQNYemAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEkr 321
Cdd:TIGR00618  273 RAQEAVLEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ-- 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   322 ylSAQRESTSIHDMNDKlenELANKEAILRQMEEKN--RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAaltkae 399
Cdd:TIGR00618  349 --TLHSQEIHIRDAHEV---ATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTS------ 417

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   400 erhgnieeRMRHLEGQLeeknqelQRARQREKMNEEHNkrlsdtvdrlltesnERLQLHLKERMAALEEKNVLIQESETF 479
Cdd:TIGR00618  418 --------AFRDLQGQL-------AHAKKQQELQQRYA---------------ELCAAAITCTAQCEKLEKIHLQESAQS 467

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 966973599   480 RKNLEESLHDKERLAEEIEKLRSELDQLKMR--------TGSLIEPTISRTHLDTS 527
Cdd:TIGR00618  468 LKEREQQLQTKEQIHLQETRKKAVVLARLLElqeepcplCGSCIHPNPARQDIDNP 523
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 337-511 4.11e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.20  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  337 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 404
Cdd:cd00176    10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  405 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 474
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 966973599  475 ESETFRKNLEESLH--DKERLAEEIEKLRSELDQLKMRT 511
Cdd:cd00176   164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
255-485 4.38e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 4.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  255 QNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQR--DIREAMAQKEDMEERITTLEKRYLSAQREstsi 332
Cdd:COG3206   159 EAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAE---- 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  333 hdmndklenelankeaiLRQMEEKNRQLQERLELAEQKLQQTMRkAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 412
Cdd:COG3206   235 -----------------LAEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966973599  413 EGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEE 485
Cdd:COG3206   297 RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 152-666 4.84e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.65  E-value: 4.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   152 LRMTVVKRQAQSPSG------VSSEVEVLKALKSLFEHHKA----LDEKIVALREQNVHIQRKMASSEGSTESEHLEGME 221
Cdd:TIGR00606  222 IRDQITSKEAQLESSreivksYENELDPLKNRLKEIEHNLSkimkLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   222 PGQKVHEKRLSNGSidstDETSQIVELQELLEKQNYEMAQMKERLAALSSRVG------EVEQEAETARKDLIKTEEMNT 295
Cdd:TIGR00606  302 QLNDLYHNHQRTVR----EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrlqlqaDRHQEHIRARDSLIQSLATRL 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   296 KY---------QRDIREAMA-QKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLE 365
Cdd:TIGR00606  378 ELdgfergpfsERQIKNFHTlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK 457

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   366 LAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNkRLSDTVD 445
Cdd:TIGR00606  458 FVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLN-HHTTTRT 535

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   446 RLLTESNERLQLHLKERMAALEEKNVLIQESETF--RKNLEESLH----DKERLAEEIEKLRSELDQLKMRTGSLIEPTI 519
Cdd:TIGR00606  536 QMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWLHskskEINQTRDRLAKLNKELASLEQNKNHINNELE 615

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   520 SRTHLDTSAELR-YSVGSLVDSQSDY-RTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLSSHPFESDTEMSD 597
Cdd:TIGR00606  616 SKEEQLSSYEDKlFDVCGSQDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQE 695

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966973599   598 IDDDdretiFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLE 666
Cdd:TIGR00606  696 FISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRD 759
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 45-513 4.97e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.43  E-value: 4.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599    45 LLDTLRETQES---LSLAQQRLQDVIydrdSLQRQLNSALPQDIESlTGGLAGSKGADPP-----------EFAALTKEL 110
Cdd:pfam10174   58 LKEQYRVTQEEnqhLQLTIQALQDEL----RAQRDLNQLLQQDFTT-SPVDGEDKFSTPElteenfrrlqsEHERQAKEL 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   111 NACREQLLEKEEEISE----LKAERNNTRLLLEHLEC-------LVSRHERSLRMTVVKRQAQSPSG------------- 166
Cdd:pfam10174  133 FLLRKTLEEMELRIETqkqtLGARDESIKKLLEMLQSkglpkksGEEDWERTRRIAEAEMQLGHLEVlldqkekenihlr 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   167 --------VSSEVEVLKALKSLFEhhkALDEKIVAL----REQNVHIQRKMASSEGSTE--SEHLEGMEPgQKVHEKRLS 232
Cdd:pfam10174  213 eelhrrnqLQPDPAKTKALQTVIE---MKDTKISSLerniRDLEDEVQMLKTNGLLHTEdrEEEIKQMEV-YKSHSKFMK 288

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   233 NgSIDSTDE-----TSQIVELQ---ELLEKQNYEMAQ----MKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ-- 298
Cdd:pfam10174  289 N-KIDQLKQelskkESELLALQtklETLTNQNSDCKQhievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTkq 367

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   299 ---------------RDIREAMAQKE------------------DMEERITTLEKRYLSAQRESTSIHDMNDKLENELAN 345
Cdd:pfam10174  368 lqdlteekstlageiRDLKDMLDVKErkinvlqkkienlqeqlrDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSE 447

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   346 KEAIL-RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN-------IEERMRHLEGQLE 417
Cdd:pfam10174  448 KERIIeRLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlassglkKDSKLKSLEIAVE 527

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   418 EKNQE-------LQRARQRE---KMNEEHNKRLS---DTVDRLLTESN------ERLQLHLKE----------RMAALEE 468
Cdd:pfam10174  528 QKKEEcsklenqLKKAHNAEeavRTNPEINDRIRlleQEVARYKEESGkaqaevERLLGILREvenekndkdkKIAELES 607

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966973599   469 -------------KNVLIQESETFRKN---LEESLHDK------------ERLAEEIEKLRSELDQLKMRTGS 513
Cdd:pfam10174  608 ltlrqmkeqnkkvANIKHGQQEMKKKGaqlLEEARRREdnladnsqqlqlEELMGALEKTRQELDATKARLSS 680
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 242-507 5.02e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.06  E-value: 5.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  242 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE-- 319
Cdd:PRK04778  111 ESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVELTes 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  320 ------KRYLSAQRESTS------------IHDMNDKLENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMR 376
Cdd:PRK04778  191 gdyveaREILDQLEEELAaleqimeeipelLKELQTELPDQLQELKAGYRELVEEGyhldhLDIEKEIQDLKEQIDENLA 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  377 KAETLpeveaelaqriaALTKAEERHGNIEERMRHLEGQLE---------EKNQElqRARQREKMNEEHNKRLSDTVDRL 447
Cdd:PRK04778  271 LLEEL------------DLDEAEEKNEEIQERIDQLYDILErevkarkyvEKNSD--TLPDFLEHAKEQNKELKEEIDRV 336

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966973599  448 -----LTESNERLQLHLKERMAALEEKNVLIQE---------SETfRKNLEESLHDKERLAEEIEKLRSELDQL 507
Cdd:PRK04778  337 kqsytLNESELESVRQLEKQLESLEKQYDEITEriaeqeiaySEL-QEELEEILKQLEEIEKEQEKLSEMLQGL 409
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 873-931 5.13e-04

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.


Pssm-ID: 188903  Cd Length: 74  Bit Score: 39.62  E-value: 5.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966973599  873 WDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 931
Cdd:cd09504     5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 347-512 5.84e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.17  E-value: 5.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  347 EAILRQMEEKNRQLQERLELAE---QKLQQTMRKAETLPEVEAELAQRIAALtkaEERHGNIEERMRHLEGQLEEKNQEL 423
Cdd:COG3096   518 RAQLAELEQRLRQQQNAERLLEefcQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARI 594

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  424 QRARQREKMNEEHNKRLSdtvdRLLTESNERLQlHLKERMAALEekNVLIQESETFRKNlEESLHDKERLAEEIEKLR-- 501
Cdd:COG3096   595 KELAARAPAWLAAQDALE----RLREQSGEALA-DSQEVTAAMQ--QLLEREREATVER-DELAARKQALESQIERLSqp 666

                         170
                  ....*....|....*.
gi 966973599  502 -----SELDQLKMRTG 512
Cdd:COG3096   667 ggaedPRLLALAERLG 682
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 221-406 6.34e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  221 EPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEE-------- 292
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREelgerara 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  293 -----------------------------MNTKYQRD---IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLE 340
Cdd:COG3883    95 lyrsggsvsyldvllgsesfsdfldrlsaLSKIADADadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966973599  341 NELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE 406
Cdd:COG3883   175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
293-508 6.62e-04

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.91  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  293 MNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsihdmndkLENELANKEAILRQMEEKNRQLQErleLAEQKLQ 372
Cdd:COG0497   138 LDPDAQRELLDAFAGLEELLEEYREAYRAWRALKKE----------LEELRADEAERARELDLLRFQLEE---LEAAALQ 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  373 qtmrkaetlPEVEAELAQRIAALTKAEERHGNIEERMRHLEGqlEEKN--QELQRARQR-EKMnEEHNKRLSDTVDRL-- 447
Cdd:COG0497   205 ---------PGEEEELEEERRRLSNAEKLREALQEALEALSG--GEGGalDLLGQALRAlERL-AEYDPSLAELAERLes 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  448 ----LTESNERLQLHLK------ERMAALEEK-----------NVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 506
Cdd:COG0497   273 alieLEEAASELRRYLDslefdpERLEEVEERlallrrlarkyGVTVEELLAYAEELRAELAELENSDERLEELEAELAE 352


                  ..
gi 966973599  507 LK 508
Cdd:COG0497   353 AE 354
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
361-532 6.77e-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: 6.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  361 QERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHGNIEERmRHLEGQLEEKNQELQRARQREKMNEEHNKRL 440
Cdd:COG4913   609 RAKLAALEAELA----------ELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAEREIAELEAEL 677

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  441 SDtvdrlLTESNERLQlHLKERMAALEEknvliqESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEptIS 520
Cdd:COG4913   678 ER-----LDASSDDLA-ALEEQLEELEA------ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED--LA 743

                         170
                  ....*....|..
gi 966973599  521 RTHLDTSAELRY 532
Cdd:COG4913   744 RLELRALLEERF 755
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 361-499 6.94e-04

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 41.14  E-value: 6.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   361 QERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 440
Cdd:pfam12718   13 QERAEELEEKVKE-------LEQENLEKEQEIKSLTH---KNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTRKI 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 966973599   441 sdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEK 499
Cdd:pfam12718   83 -----QLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEE 136
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 243-395 7.09e-04

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: 42.20  E-value: 7.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   243 SQIVELQELLEKQNYEMA-------QMKERLAALSSRVGEVEQEAETARKD---LIKTEEMNTKYQRDIREAMAQKEDME 312
Cdd:pfam13851   33 EEIAELKKKEERNEKLMSeiqqenkRLTEPLQKAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEHEVLE 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   313 ERITTLEKRY--LSAQREStSIHDMNDKLENE---LANK-EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 386
Cdd:pfam13851  113 QRFEKVERERdeLYDKFEA-AIQDVQQKTGLKnllLEKKlQALGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLE 191


                   ....*....
gi 966973599   387 ELAQRIAAL 395
Cdd:pfam13851  192 SKNQLIKDL 200
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
174-531 7.93e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 7.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  174 LKALKSLFEHHKALDEKIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHEKRLSNGSIDStdETSQIVELQELLE 253
Cdd:COG4717    80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELR-----EELEKLEKLLQLLPLYQELEALEA--ELAELPERLEELE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  254 KQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsih 333
Cdd:COG4717   153 ERLEELRELEEELEELEAELAELQEELEELLEQL------SLATEEELQDLAEELEELQQRLAELEEELEEAQEE----- 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  334 dmNDKLENELANKEAILRQMEEKNRQLQERLELA--------EQKLQQTMRKAETLPEVEAELAQRIAA----LTKAEER 401
Cdd:COG4717   222 --LEELEEELEQLENELEAAALEERLKEARLLLLiaaallalLGLGGSLLSLILTIAGVLFLVLGLLALlfllLAREKAS 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  402 HGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrLSDTVDRLLTESNERLQLHLKERMAALEEknVLIQESETFRK 481
Cdd:COG4717   300 LGKEAEELQALPALEELEEEELEELLAALGLPPD----LSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEIA 373

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 966973599  482 NL--------EESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTISRTHLDTSAELR 531
Cdd:COG4717   374 ALlaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE 431
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 295-508 8.44e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.81  E-value: 8.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   295 TKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIhDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK---- 370
Cdd:pfam02463  165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL-KEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIdllq 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   371 -----LQQTMRKAETLPEVEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRlsdtVD 445
Cdd:pfam02463  244 ellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEK---EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE----KL 316

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966973599   446 RLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 508
Cdd:pfam02463  317 KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 275-508 8.76e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.56  E-value: 8.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   275 EVEQEAETARKdlikteEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAILRQME 354
Cdd:pfam05483  201 ELRVQAENARL------EMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQIT-------EKENKMKDLTFLLEESR 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   355 EKNRQLQERLELAEQKLQQTMRK----AETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQRE 430
Cdd:pfam05483  268 DKANQLEEKTKLQDENLKELIEKkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAH 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   431 KMNEEHNKRLSDTVDRLLTESNERLQLH---LKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 507
Cdd:pfam05483  348 SFVVTEFEATTCSLEELLRTEQQRLEKNedqLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF 427


                   .
gi 966973599   508 K 508
Cdd:pfam05483  428 E 428
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 461-519 1.09e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 42.90  E-value: 1.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  461 ERMAALEEKNV-LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKmrTGSLIEPTI 519
Cdd:PRK03992    1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELEKLK--SPPLIVATV 58
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
331-508 1.23e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 41.73  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  331 SIHDMND---KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK---------AETLPEVEAELAQRIAALTKA 398
Cdd:COG1842    31 AIRDMEEdlvEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlareaLERKAELEAQAEALEAQLAQL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  399 EERHGNIEERMRHLEGQLEEKNQELQRARQREKMNeEHNKRLSDTVDRLLTESNErlqlhlkERMAALEEKnvliQESET 478
Cdd:COG1842   111 EEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDAT-------SALERMEEK----IEEME 178

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 966973599  479 FRKNLEESLHDKERLAEEIEKLRS------ELDQLK 508
Cdd:COG1842   179 ARAEAAAELAAGDSLDDELAELEAdsevedELAALK 214
COG5022 COG5022
Myosin heavy chain [General function prediction only];
284-507 1.80e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 42.76  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  284 RKDLIKTEEMNTKYQRDIREAMAQKEdMEERITTLEkrylsaqreSTSIHdmNDKLENELANKEAILRQMEEKNRQLQER 363
Cdd:COG5022   809 RKEYRSYLACIIKLQKTIKREKKLRE-TEEVEFSLK---------AEVLI--QKFGRSLKAKKRFSLLKKETIYLQSAQR 876

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  364 LELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE-----ERMRHLEGQLEEKNQELQRARQREKmNEE 435
Cdd:COG5022   877 VELAERQlqeLKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENlefktELIARLKKLLNNIDLEEGPSIEYVK-LPE 955

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966973599  436 HNKRLsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 507
Cdd:COG5022   956 LNKLH--EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV 1025
PTZ00121 PTZ00121
MAEBL; Provisional
 209-504 1.99e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  209 EGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK--D 286
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeE 1288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  287 LIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIhdmndKLENELANKEAILRQMEEKNRQlqERLEL 366
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAA-----KKKAEEAKKAAEAAKAEAEAAA--DEAEA 1361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  367 AEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEgQLEEKNQELQRARQREKMNEEhnKRLSDTVDR 446
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKKADEAKKKAEE--KKKADEAKK 1438

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966973599  447 LLTESN--ERLQLHLKERMAA--LEEKNVLIQESETFRKNLEESLHDKE--RLAEEIEKLRSEL 504
Cdd:PTZ00121 1439 KAEEAKkaDEAKKKAEEAKKAeeAKKKAEEAKKADEAKKKAEEAKKADEakKKAEEAKKKADEA 1502
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
 223-595 2.25e-03

GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 42.42  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  223 GQKVHEK--RLSNGSID----STDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEvEQEAETARKDLIKTEEMNTk 296
Cdd:COG5192   415 GKAIAEEtsREDELSFDdsdvSTSDENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFD-ESEGNLRWKEGLASKLAYS- 492

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  297 yQRDIREAMAQKEDMEERITTlEKRYLSAQRESTSIHDMNDKLENElanKEAILRQMEEKNRQLQERLE-LAEQKLQQTM 375
Cdd:COG5192   493 -QSGKRGRNIQKIFYDESLSP-EECIEEYKGESAKSSESDLVVQDE---PEDFFDVSKVANESISSNHEkLMESEFEELK 567

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  376 RKAETLPEVEAELAQriAALTKAEERHgniEErmrhLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERL 455
Cdd:COG5192   568 KKWSSLAQLKSRFQK--DATLDSIEGE---EE----LIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVD 638

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  456 QLHLKERMAALEEK---NVLIQESETFRKN-LEESLHDKERLAEEIEKLRSELDQL---------KMRTGSLIEPTISRT 522
Cdd:COG5192   639 YETEREENARKKEElrgNFELEERGDPEKKdVDWYTEEKRKIEEQLKINRSEFETMvpesrvvieGYRAGRYVRIVLSHV 718

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966973599  523 HLDTSAELRYS----VGSLVDSQSDYRTTKV-IRRPRRGRMGVRRDEPKVKSLGdheWNRTQQIGVLSSHPFESDTEM 595
Cdd:COG5192   719 PLEFVDEFNSRypivLGGLLPAEKEMGIVQGrIKRHRWHKKILKTNDPLIFSVG---WRRFQSIPVYSMKDSRTRNRM 793
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 337-504 2.29e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 40.82  E-value: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   337 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 405
Cdd:pfam04012   39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   406 EERMRHLEGQLEEKNQE-------LQRARQREKMNEehnkrlsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEt 478
Cdd:pfam04012  117 RKQLAALETKIQQLKAKknllkarLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELA- 187

                          170       180
                   ....*....|....*....|....*.
gi 966973599   479 FRKNLEESLHDKERLAEEIEKLRSEL 504
Cdd:pfam04012  188 SAVDLDAKLEQAGIQMEVSEDVLARL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 249-427 2.30e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.89  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  249 QELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteEMNTKYQRDIREAmaqkEDMEERITTLEKRYLSaqre 328
Cdd:cd00176    64 EQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRL----EEALDLQQFFRDA----DDLEQWLEEKEAALAS---- 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  329 stsihdmnDKLENELANKEAILRQMEEknrqLQERLELAEQKLQQTMRKAETLPEveaelAQRIAALTKAEERHGNIEER 408
Cdd:cd00176   132 --------EDLGKDLESVEELLKKHKE----LEEELEAHEPRLKSLNELAEELLE-----EGHPDADEEIEEKLEELNER 194

                         170
                  ....*....|....*....
gi 966973599  409 MRHLEGQLEEKNQELQRAR 427
Cdd:cd00176   195 WEELLELAEERQKKLEEAL 213
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 234-417 2.48e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.59  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  234 GSIDSTDETSQIVELQELLEKQNYEMAQM---------KERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIrea 304
Cdd:cd22656    82 AQNAGGTIDSYYAEILELIDDLADATDDEeleeakktiKALLDDLLKEAKKYQDKAAKVVDKL-------TDFENQT--- 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  305 MAQKEDMEERITTLEKRYlsaQRESTSIHDMN-DKLENELAN-KEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 382
Cdd:cd22656   152 EKDQTALETLEKALKDLL---TDEGGAIARKEiKDLQKELEKlNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 966973599  383 EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 417
Cdd:cd22656   229 AADTDLDNLLALIGPAIPALEKLQGAWQAIATDLD 263
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 95-374 2.49e-03

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.87  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   95 SKGADPPEFAALTKELNACREQLLEKEEEISELKAERNNTRL-----LLEHLECLVSRHERSLRMTvvKRQAQSPSGVSS 169
Cdd:COG5185   236 KGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSkrlneNANNLIKQFENTKEKIAEY--TKSIDIKKATES 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  170 EVEVLKALKSLFEHHKALDEKIVALREQNVHIQRKMASSEGSTEsEHLEGMEpgQKVHEKRLSNGSIDSTDETSQIVEL- 248
Cdd:COG5185   314 LEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLE-AIKEEIE--NIVGEVELSKSSEELDSFKDTIESTk 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  249 QELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKED-MEERITTLEKRYLSAQR 327
Cdd:COG5185   391 ESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKvMREADEESQSRLEEAYD 470

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 966973599  328 E-STSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQT 374
Cdd:COG5185   471 EiNRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSK 518
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
996-1051 2.83e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 37.25  E-value: 2.83e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 966973599   996 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1051
Cdd:pfam07647   11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 350-463 3.09e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.99  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  350 LRQMEEKNRQLQ-ERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 428
Cdd:COG0542   413 LDELERRLEQLEiEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 966973599  429 R----EKMNEEHNKRLSDTVD-----------------RLLTESNERLqLHLKERM 463
Cdd:COG0542   493 ElaelEEELAELAPLLREEVTeediaevvsrwtgipvgKLLEGEREKL-LNLEEEL 547
PRK12704 PRK12704
phosphodiesterase; Provisional
 278-435 3.38e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  278 QEAETARKDLIKTEEmntkyqrdiREAMAQKEDMEerittlekryLSAQREstsIHDMNDKLENELANKEAILRQMEEKN 357
Cdd:PRK12704   34 KEAEEEAKRILEEAK---------KEAEAIKKEAL----------LEAKEE---IHKLRNEFEKELRERRNELQKLEKRL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  358 RQLQERLElaeqklqqtmRKAETLPEVEAELAQRIAALTKAEErhgNIEERmrhlEGQLEEK----NQELQR-------- 425
Cdd:PRK12704   92 LQKEENLD----------RKLELLEKREEELEKKEKELEQKQQ---ELEKK----EEELEELieeqLQELERisgltaee 154

                         170
                  ....*....|..
gi 966973599  426 ARQR--EKMNEE 435
Cdd:PRK12704  155 AKEIllEKVEEE 166
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 244-455 3.85e-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: 41.70  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   244 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTlekryl 323
Cdd:pfam01576  890 RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKS------ 963

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   324 saqrestsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK-AETLPEVEAElaQRIAALTKAEERH 402
Cdd:pfam01576  964 --------------KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKlKEVLLQVEDE--RRHADQYKDQAEK 1027

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 966973599   403 GNIeeRMRHLEGQLEEKNQELQRAR-QREKMNEEhnkrLSDTvdrllTESNERL 455
Cdd:pfam01576 1028 GNS--RMKQLKRQLEEAEEEASRANaARRKLQRE----LDDA-----TESNESM 1070
BAR_SNX7 cd07666
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ...
 252-443 3.90e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX7 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153350  Cd Length: 243  Bit Score: 40.27  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  252 LEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQrDIREAMAQK----EDMEERITTLEKRYLSAQR 327
Cdd:cd07666    14 LTAQAWELSSHKKQGPGLLSRMGQTVKAVASSVRGVKNRPEEFTEMN-EYVEAFSQKinvlDKISQRIYKEQREYFEELK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  328 ESTSIHDMNDKLENELANK--------EAILRQMEEKNRQLQERLE-------LAEQKLQQTMRKAEtlpEVEAELAQRI 392
Cdd:cd07666    93 EYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpviheyvLYSETLMGVIKRRD---QIQAELDSKV 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 966973599  393 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 443
Cdd:cd07666   170 EALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFT 220
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 247-499 4.27e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.79  E-value: 4.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   247 ELQELLEKQNYEMAQMKERLAALSSRvgEVEQEAETARKDLIKTEEmntKYQRDIRE-AMAQKEDMEERITTLEKRYLSA 325
Cdd:pfam15558   35 EELRRRDQKRQETLERERRLLLQQSQ--EQWQAEKEQRKARLGREE---RRRADRREkQVIEKESRWREQAEDQENQRQE 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   326 QRESTSIHDMNDKLENE--LANKEAILRQMEEKNR-QLQERLELAEQKLQQ--------------------TMRKAETLP 382
Cdd:pfam15558  110 KLERARQEAEQRKQCQEqrLKEKEEELQALREQNSlQLQERLEEACHKRQLkereeqkkvqennlsellnhQARKVLVDC 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   383 EVEAELAQRIAAL----TKAEERH-GNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTV---DRLLTESNE 453
Cdd:pfam15558  190 QAKAEELLRRLSLeqslQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHKEALAelaDRKIQQARQ 269

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 966973599   454 RLQLHLKERMAALEEKNVLIQ------------ESETFRKNLEESLHDKERLAEEIEK 499
Cdd:pfam15558  270 VAHKTVQDKAQRARELNLEREknhhilklkvekEEKCHREGIKEAIKKKEQRSEQISR 327
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 172-500 4.32e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 41.36  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  172 EVLKALKSLFEHHKALDEKIVALREQNVHIQRKMASSE---GSTES---EHLEGMEPGQKVHEKRLSNGsidstdetsQI 245
Cdd:PRK04778  123 QILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRfsfGPALDeleKQLENLEEEFSQFVELTESG---------DY 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  246 VELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT-EEM--------NTKYQRDIREAMAQKEDMEERIT 316
Cdd:PRK04778  194 VEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGyRELveegyhldHLDIEKEIQDLKEQIDENLALLE 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  317 TLEKRYLSAQRE--STSIHDMNDKLENELANK----------EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEV 384
Cdd:PRK04778  274 ELDLDEAEEKNEeiQERIDQLYDILEREVKARkyveknsdtlPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQL 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  385 EAELAQRIAALTKAEERHGN-------IEERMRHLEGQLE--EKNQE-----LQRARQ-----REKMnEEHNKRLSdTVD 445
Cdd:PRK04778  354 EKQLESLEKQYDEITERIAEqeiayseLQEELEEILKQLEeiEKEQEklsemLQGLRKdeleaREKL-ERYRNKLH-EIK 431

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966973599  446 RLLTESN------------ERLQLHLKERMAALEEKNVLIqesETFRKNLEESLHDKERLAEEIEKL 500
Cdd:PRK04778  432 RYLEKSNlpglpedylemfFEVSDEIEALAEELEEKPINM---EAVNRLLEEATEDVETLEEETEEL 495
mukB PRK04863
chromosome partition protein MukB;
104-440 4.35e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.48  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  104 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHerslrmtvvkrqaqspSGVSSEVEVLKALKslfeh 183
Cdd:PRK04863  782 AAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSH----------------LAVAFEADPEAELR----- 840

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  184 hkaldekivALREQNVHIQRKMASSEGSTE--SEHLEGMEPGQKVHEKRLsnGSIDSTDETSQIVELQELLEkQNYEMAQ 261
Cdd:PRK04863  841 ---------QLNRRRVELERALADHESQEQqqRSQLEQAKEGLSALNRLL--PRLNLLADETLADRVEEIRE-QLDEAEE 908

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  262 MKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMAQKEDMEERITTL----EKR----YLSAQRESTSIH 333
Cdd:PRK04863  909 AKRFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQDYQQAQQTQRDAKQQAFALtevvQRRahfsYEDAAEMLAKNS 984

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  334 DMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALT---------KAEERHGN 404
Cdd:PRK04863  985 DLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvpadsgaeeRARARRDE 1064

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 966973599  405 IEERMRHLEGQleeKNQ-ELQRARQREKMNEEhNKRL 440
Cdd:PRK04863 1065 LHARLSANRSR---RNQlEKQLTFCEAEMDNL-TKKL 1097
RNase_Y_N pfam12072
RNase Y N-terminal region;
358-498 4.62e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.87  E-value: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   358 RQLQERLELAEQKLQQTMRKAETLP----------------EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 421
Cdd:pfam12072   27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   422 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEtfrknlEESLHDKERLAEEIE 498
Cdd:pfam12072  107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 878-935 6.24e-03

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 36.06  E-value: 6.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 966973599  878 VVAWLElWLGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 935
Cdd:cd09487     2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
Kre28 pfam17097
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ...
 297-528 6.44e-03

Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore microtubule binding complex, which bridges between centromeric heterochromatin and kinetochore MAPs (microtubule associated protein, such as Bim1, Bik1 and SIk19) and motors (Cin8, Kar3). It may be regulated by sumoylation.


Pssm-ID: 407241 [Multi-domain]  Cd Length: 360  Bit Score: 40.17  E-value: 6.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   297 YQRDIREAMAQKEDM-EERITTLEKRYLSAQREST-SIHDMND-----KLENELANKEAILRQMEEKNRQLQERLELaeq 369
Cdd:pfam17097    9 YEAQLRELEEQTAHSsEQVLTEQDKRLLGALRELTqSVIQLIEenslvTVSGDAANLLIDPSGIEVKIRQLDQLVEL--- 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   370 kLQQTMRKAETLPEVEAELAQRIAAL---TKAEERHGNIEERMRHLE-GQLEEKNQELQRAR------------QREKMN 433
Cdd:pfam17097   86 -LKVTHLEQETLDNFLRYTISSTDLLqleSVSDPKYASLEDEVSQLEdDTLTVLNQEIDQIKgdilqvaqeiadKQDQVN 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   434 EE--HNKRLSDTVDRLLTESNE-RLQLHLKERMAALEEKNVLIQESETFR--KNLEESLHDKERLAEEIEKLRSELDQLK 508
Cdd:pfam17097  165 ELclETSNELDECWELLNELERlRDQRITVEEQTSNEKDTELDPVEETYEewKSLQESLQQLEHLKEELDQLQKQKDSLE 244

                          250       260
                   ....*....|....*....|
gi 966973599   509 MRTGSliepTISRTHLDTSA 528
Cdd:pfam17097  245 KVDKS----SINRTQNDEES 260
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
347-516 7.06e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  347 EAILRQMEEKNRQLQERLELAEQKlqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 426
Cdd:PRK03918  138 DAILESDESREKVVRQILGLDDYE-----NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  427 RQREKmneehnkRLSDTVDRLltesnERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKErlaEEIEKLRSELDQ 506
Cdd:PRK03918  213 SSELP-------ELREELEKL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE---ERIEELKKEIEE 277

                         170
                  ....*....|
gi 966973599  507 LKMRTGSLIE 516
Cdd:PRK03918  278 LEEKVKELKE 287
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 367-508 7.17e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 39.96  E-value: 7.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   367 AEQKLQQTMRKAETlpeVEAELAQRIAALTKAE----ERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSD 442
Cdd:pfam02841  174 AEEVLQEFLQSKEA---VEEAILQTDQALTAKEkaieAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIE 250

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966973599   443 TVdrlltESNERLQLHLKERMAALEEknvliQESETFRKnleeslhdkERLAEEIEKLRSELDQLK 508
Cdd:pfam02841  251 KM-----EAEREQLLAEQERMLEHKL-----QEQEELLK---------EGFKTEAESLQKEIQDLK 297
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 249-654 7.26e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.49  E-value: 7.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   249 QELLEKQNYE-MAQMKERLAALSSRVGEVEqEAETARKDLIktEEMNTKYQRDIREAMAQKEDMEeRITTLEKrylsaqr 327
Cdd:pfam17380  290 QEKFEKMEQErLRQEKEEKAREVERRRKLE-EAEKARQAEM--DRQAAIYAEQERMAMERERELE-RIRQEER------- 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   328 estsihdmndKLENELANKEAILRQMEeKNRQLqERLELAEQKLQQTMRKaetlpEVEAELAQRIaaltKAEERHGNIEE 407
Cdd:pfam17380  359 ----------KRELERIRQEEIAMEIS-RMREL-ERLQMERQQKNERVRQ-----ELEAARKVKI----LEEERQRKIQQ 417

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   408 RMRHLEGQLEEknQELQRARQREKMNEEHNKRLsdtvdrlltesnERLQLHLKERMAALEEknVLIQESETFRKNLEesL 487
Cdd:pfam17380  418 QKVEMEQIRAE--QEEARQREVRRLEEERAREM------------ERVRLEEQERQQQVER--LRQQEEERKRKKLE--L 479

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   488 HDKERLAEEIEKLRSEL--DQLKMRTGSLIEPTISRthldtsaelrysvgSLVDSQSDYRTTKVIRRPRRgrmgvRRDEp 565
Cdd:pfam17380  480 EKEKRDRKRAEEQRRKIleKELEERKQAMIEEERKR--------------KLLEKEMEERQKAIYEEERR-----REAE- 539

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   566 kvkslgdhEWNRTQQigvlsshpfesdtEMsdiddDDRETIFSSMDLLSPSghsdaqtlammlQEQLDAINKEIRLIQEE 645
Cdd:pfam17380  540 --------EERRKQQ-------------EM-----EERRRIQEQMRKATEE------------RSRLEAMEREREMMRQI 581


                   ....*....
gi 966973599   646 KESTELRAE 654
Cdd:pfam17380  582 VESEKARAE 590
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 996-1040 8.14e-03

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 36.13  E-value: 8.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 966973599  996 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 1040
Cdd:cd09501    11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
332-522 8.91e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 8.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  332 IHDMndkLENELANK-EAILRQMEEKNRQLQERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKAEERHGNIEERMR 410
Cdd:COG4717    43 IRAM---LLERLEKEaDELFKPQGRKPELNLKELKELEEELKE-------AEEKEEEYAELQEELEELEEELEELEAELE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  411 HLEGQLEEKNQELQRARQREKMnEEHNKRLSDtvdrlltesnerlqlhLKERMAALEEKnvliqesetfRKNLEESLHDK 490
Cdd:COG4717   113 ELREELEKLEKLLQLLPLYQEL-EALEAELAE----------------LPERLEELEER----------LEELRELEEEL 165

                         170       180       190
                  ....*....|....*....|....*....|..
gi 966973599  491 ERLAEEIEKLRSELDQLKMRTGSLIEPTISRT 522
Cdd:COG4717   166 EELEAELAELQEELEELLEQLSLATEEELQDL 197
PRK09039 PRK09039
peptidoglycan -binding protein;
306-427 9.03e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 9.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  306 AQKEDMEERITTLEKRYLSAQREstsihdmNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE 385
Cdd:PRK09039   74 QGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 966973599  386 AELAQRIAAL--------TKAEERHGNIEERMRHLEGQLEEKNQELQRAR 427
Cdd:PRK09039  147 AALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 247-390 9.53e-03

PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.


Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 38.51  E-value: 9.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   247 ELQELLEKQNYEMAQMKER-LAALSSRVGEVEQEAETARKDLIKteEMNTKYQRDIREAMAQKEDmeERITTLEKRYLSA 325
Cdd:pfam08703   13 ELLELREEQYEQEKKRKEQhLTEQIQKLKELAREKQAAELKALK--ESSESEKKEMKKKLERKRL--ESIQEAKKRTSDK 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966973599   326 QRESTSIHDMNDKLENELANkeaILRQMEEKNRQLQERLELAEQKLQQTMRkaETLPEVEAELAQ 390
Cdd:pfam08703   89 AAQERLKKEINNSHIQEVVQ---SIKQLEEKQKRRQEKLEEKQAECLQQIK--EEEPQLQAELNA 148
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 397-663 9.54e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 9.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   397 KAEERHGNIEERMRHLEGQLEEKNQELQR-ARQREKMNEehnkrlsdtVDRLLTESNE-RLQLHLKERMAALEEKNVLIQ 474
Cdd:TIGR02169  174 KALEELEEVEENIERLDLIIDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLKEKEALERQKEAIER 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   475 ESETFRKNLEESLHDKERLAEEIEKLRSELDQLK---MRTGSLIEPTISRTHLDTSAELRysvgSLVDSQSDYRTTKVIR 551
Cdd:TIGR02169  245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkiKDLGEEEQLRVKEKIGELEAEIA----SLERSIAEKERELEDA 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599   552 RPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVlsshpfESDTEMSDIDDDDRETIFSSMDLLSPSG------HSDAQTLA 625
Cdd:TIGR02169  321 EERLAKLEAEIDKLLAEIEELEREIEEERKRR------DKLTEEYAELKEELEDLRAELEEVDKEFaetrdeLKDYREKL 394

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 966973599   626 MMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASV 663
Cdd:TIGR02169  395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
46 PHA02562
endonuclease subunit; Provisional
 269-508 9.97e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.00  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  269 LSSRVGEVEQEAET--ARKDLIKTE-EMNTKYQRDIREAMAQkedmeeRITTLEKRYLSAQRESTSIHDMNDKLENELAN 345
Cdd:PHA02562  172 NKDKIRELNQQIQTldMKIDHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLN 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  346 keaILRQMEEKNRQLQE-RLELAEQKLQ-QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQEL 423
Cdd:PHA02562  246 ---LVMDIEDPSAALNKlNTAAAKIKSKiEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966973599  424 QRARQREKMNEEHNKRLSDTvdrlltesneRLQLHLKERMAALEEKNVLIQESETfrKNLEESLHDKErlaEEIEKLRSE 503
Cdd:PHA02562  323 DELEEIMDEFNEQSKKLLEL----------KNKISTNKQSLITLVDKAKKVKAAI--EELQAEFVDNA---EELAKLQDE 387


                  ....*
gi 966973599  504 LDQLK 508
Cdd:PHA02562  388 LDKIV 392
 
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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