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Conserved domains on  [gi|1474844183|ref|XP_026253031|]
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liprin-alpha-4 isoform X1 [Urocitellus parryii]

Protein Classification

liprin-alpha( domain architecture ID 13527058)

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_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 976-1041 1.34e-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: 1.34e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1474844183  976 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1041
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
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 ...
 848-918 2.53e-42

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: 148.87  E-value: 2.53e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1474844183  848 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 918
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
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 ...
 1061-1132 3.68e-41

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: 145.54  E-value: 3.68e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474844183 1061 DVLVWTNDQVVHWVQSIGLRDYAGNLQESGVHGALLALDENFDHNTLALVLQIPTQNTQARQVMEREFNNLL 1132
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-493 6.37e-17

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: 86.65  E-value: 6.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  170 ERLRAALERVT----TLEEQLAGAHQQVSALQQGAVVRdgvaEEEGTVELgpkRLWkddTGRVEELQELLEKQNFELSQA 245
Cdd:TIGR02168  182 ERTRENLDRLEdilnELERQLKSLERQAEKAERYKELK----AELRELEL---ALL---VLRLEELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  246 RERLVTLTATVTELEEDLgtarrdliksEELSSKHQRdlrealaqkedMEERITTLEKRYLAAQREatsIHDL------- 318
Cdd:TIGR02168  252 EEELEELTAELQELEEKL----------EELRLEVSE-----------LEEEIEELQKELYALANE---ISRLeqqkqil 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  319 NDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ 398
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  399 LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQ----LHLKERMAALEEKNTLIQELESSQRQIEEQhhhKG 474
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkleeAELKELQAELEELEEELEELQEELERLEEA---LE 464

                          330
                   ....*....|....*....
gi 1474844183  475 RLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02168  465 ELREELEEAEQALDAAERE 483
PRK02224 super family cl32023
DNA double-strand break repair Rad50 ATPase;
31-305 7.40e-04

DNA double-strand break repair Rad50 ATPase;


The actual alignment was detected with superfamily member PRK02224:

Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 7.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   31 VNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRhlnsalpqefatLTRELSMCREQLLEREEEISELKAERNN 110
Cdd:PRK02224   467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE------------AEDRIERLEERREDLEELIAERRETIEE 534

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  111 TRLLLEHLECLVSRHERSLRmtvVKRQAQSPSGVSSEvEVLKALKSLFEHHKALDEKvrerlRAALERVTTLEEQLAGAH 190
Cdd:PRK02224   535 KRERAEELRERAAELEAEAE---EKREAAAEAEEEAE-EAREEVAELNSKLAELKER-----IESLERIRTLLAAIADAE 605

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  191 QQVSALQQGavvRDGVAE--EEGTVELGPKRLWKD------DTGRVEELQEllEKQNFE--LSQARERLVTLTATVTELE 260
Cdd:PRK02224   606 DEIERLREK---REALAElnDERRERLAEKRERKReleaefDEARIEEARE--DKERAEeyLEQVEEKLDELREERDDLQ 680

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1474844183  261 EDLGTARRDLIKSEELsskhqRDLREALAQK----EDMEERITTLEKRY 305
Cdd:PRK02224   681 AEIGAVENELEELEEL-----RERREALENRvealEALYDEAEELESMY 724
 
Name Accession Description Interval E-value
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 ...
 976-1041 1.34e-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: 1.34e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1474844183  976 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1041
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
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 ...
 848-918 2.53e-42

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: 148.87  E-value: 2.53e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1474844183  848 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 918
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
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 ...
 1061-1132 3.68e-41

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: 145.54  E-value: 3.68e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474844183 1061 DVLVWTNDQVVHWVQSIGLRDYAGNLQESGVHGALLALDENFDHNTLALVLQIPTQNTQARQVMEREFNNLL 1132
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-493 6.37e-17

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: 86.65  E-value: 6.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  170 ERLRAALERVT----TLEEQLAGAHQQVSALQQGAVVRdgvaEEEGTVELgpkRLWkddTGRVEELQELLEKQNFELSQA 245
Cdd:TIGR02168  182 ERTRENLDRLEdilnELERQLKSLERQAEKAERYKELK----AELRELEL---ALL---VLRLEELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  246 RERLVTLTATVTELEEDLgtarrdliksEELSSKHQRdlrealaqkedMEERITTLEKRYLAAQREatsIHDL------- 318
Cdd:TIGR02168  252 EEELEELTAELQELEEKL----------EELRLEVSE-----------LEEEIEELQKELYALANE---ISRLeqqkqil 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  319 NDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ 398
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  399 LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQ----LHLKERMAALEEKNTLIQELESSQRQIEEQhhhKG 474
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkleeAELKELQAELEELEEELEELQEELERLEEA---LE 464

                          330
                   ....*....|....*....
gi 1474844183  475 RLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02168  465 ELREELEEAEQALDAAERE 483
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 227-495 1.21e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.76  E-value: 1.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  227 RVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDME-------ERIT 299
Cdd:COG1196    233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiarleERRR 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  300 TLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALT 379
Cdd:COG1196    313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  380 KAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQEL 459
Cdd:COG1196    393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1474844183  460 ESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGRGG 495
Cdd:COG1196    473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 975-1039 5.54e-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: 67.68  E-value: 5.54e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474844183  975 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1039
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
38-493 8.34e-14

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 76.23  E-value: 8.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   38 EKLLESLRESQETLAATQSRLQDA-LHERdqlqrhLNsALPQEFATLTRElsmcreqllereeeISELKAERNNTRLLLE 116
Cdd:PRK02224   179 ERVLSDQRGSLDQLKAQIEEKEEKdLHER------LN-GLESELAELDEE--------------IERYEEQREQARETRD 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  117 HLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalERVTTLEEQLAGAHQQVSAL 196
Cdd:PRK02224   238 EADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDDL 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  197 QQGAVVRDGVAEeegTVELGPKRLWKDDtgrvEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEEL 276
Cdd:PRK02224   299 LAEAGLDDADAE---AVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  277 SSKHQRDLREALAQKEDMEERITTLEKRYLAAqreATSIHDLNDKLENELANKESLHRQCEEkarhlqelLEVAEQKLQQ 356
Cdd:PRK02224   372 LEEAREAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELREREAE--------LEATLRTARE 440

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  357 TMRKAETL------PEVEAEL--AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMnEDHNKRLSD--- 425
Cdd:PRK02224   441 RVEEAEALleagkcPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEErre 519

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474844183  426 TVDRLLSESNERLQlhlkERMAALEEKNTLIQELESSQrqiEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PRK02224   520 DLEELIAERRETIE----EKRERAEELRERAAELEAEA---EEKREAAAEAEEEAEEAREEVAELNSK 580
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 31-491 1.41e-10

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: 65.90  E-value: 1.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   31 VNMLDEREKLL-ESLRESQETLAATQSRLQD-------------ALHERDQLQRHLNSALPQEFATLTRELSmcrEQLLE 96
Cdd:pfam05483  270 ANQLEEKTKLQdENLKELIEKKDHLTKELEDikmslqrsmstqkALEEDLQIATKTICQLTEEKEAQMEELN---KAKAA 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   97 REEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEHHKALDEKvrER 171
Cdd:pfam05483  347 HSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  172 LRAALERVTTLEEQLAGAHQQVSALQQGAVVRDGVAEEEGTVELGPKRLWkddTGRVEELQELLEKQ---NFELSQARER 248
Cdd:pfam05483  420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY---LKEVEDLKTELEKEklkNIELTAHCDK 496

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  249 LVTLTATVTELEEDLgtarrdlikSEELSsKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD----LNDKLEN 324
Cdd:pfam05483  497 LLLENKELTQEASDM---------TLELK-KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqKGDEVKC 566

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  325 ELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTK---AEERHGNIEE-HLRQLEGQLE 400
Cdd:pfam05483  567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKkgsAENKQLNAYEiKVNKLELELA 646

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  401 EKNQ---ELARVRQRE----KMNEDH-------NKRLSDTVDRLLSESNERLQLHLKErMAALEEK-----NTLIQELES 461
Cdd:pfam05483  647 SAKQkfeEIIDNYQKEiedkKISEEKlleevekAKAIADEAVKLQKEIDKRCQHKIAE-MVALMEKhkhqyDKIIEERDS 725

                          490       500       510
                   ....*....|....*....|....*....|....
gi 1474844183  462 S----QRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam05483  726 ElglyKNKEQEQSSAKAALEIELSNIKAELLSLK 759
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 848-914 4.81e-08

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: 51.14  E-value: 4.81e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474844183   848 FAQWDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 914
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 984-1039 9.45e-08

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: 9.45e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1474844183   984 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1039
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1062-1132 3.20e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 45.72  E-value: 3.20e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1474844183 1062 VLVWTNDQVVHWVQSIGLRDYAGNLQESGVHGALLALdeNFDHNTLAlvlQIPTQNTQARQVMEREFNNLL 1132
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1062-1133 8.01e-06

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: 44.59  E-value: 8.01e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474844183  1062 VLVWTNDQVVHWVQSIGLRDYAGNLQESGVHGALLALDENFDHntlalVLQIPTQNTQARQVMEREFNNLLA 1133
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEED-----LKELGITKLGHRKKILKAIQKLKE 67
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 338-493 3.13e-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: 43.59  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  338 EKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNE 417
Cdd:cd00176     40 KKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEELNQRWEELRELAEERRQRLEEALDLQQFFR 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  418 DH---NKRLSDTVDRLLSESN-------ERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGR--LSEEIEKLRQ 485
Cdd:cd00176    114 DAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeeIEEKLEELNE 193


                   ....*...
gi 1474844183  486 EVDQLKGR 493
Cdd:cd00176    194 RWEELLEL 201
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
31-305 7.40e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 7.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   31 VNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRhlnsalpqefatLTRELSMCREQLLEREEEISELKAERNN 110
Cdd:PRK02224   467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE------------AEDRIERLEERREDLEELIAERRETIEE 534

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  111 TRLLLEHLECLVSRHERSLRmtvVKRQAQSPSGVSSEvEVLKALKSLFEHHKALDEKvrerlRAALERVTTLEEQLAGAH 190
Cdd:PRK02224   535 KRERAEELRERAAELEAEAE---EKREAAAEAEEEAE-EAREEVAELNSKLAELKER-----IESLERIRTLLAAIADAE 605

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  191 QQVSALQQGavvRDGVAE--EEGTVELGPKRLWKD------DTGRVEELQEllEKQNFE--LSQARERLVTLTATVTELE 260
Cdd:PRK02224   606 DEIERLREK---REALAElnDERRERLAEKRERKReleaefDEARIEEARE--DKERAEeyLEQVEEKLDELREERDDLQ 680

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1474844183  261 EDLGTARRDLIKSEELsskhqRDLREALAQK----EDMEERITTLEKRY 305
Cdd:PRK02224   681 AEIGAVENELEELEEL-----RERREALENRvealEALYDEAEELESMY 724
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 850-914 1.70e-03

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: 38.02  E-value: 1.70e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474844183  850 QWDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 914
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-303 7.17e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 7.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   27 EQLMVNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLnSALPQEFATLTRELSMCREQLLEREEEISELKA 106
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI-AATERRLEDLEEQIEELSEDIESLAAEIEELEE 866

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  107 ERNNTRLLLEHLECLVSRHERSLRmtvvkrqaqspsgvssevEVLKALKSLFEHHKALDEKVRE---RLRAALERVTTLE 183
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALA------------------LLRSELEELSEELRELESKRSElrrELEELREKLAQLE 928

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  184 EQLAGAHQQVSALQQgavvrdgVAEEEGTVELgpkrlwkddtgrvEELQELLEKQNFELSQARERLVTLTATVTELeedl 263
Cdd:TIGR02168  929 LRLEGLEVRIDNLQE-------RLSEEYSLTL-------------EEAEALENKIEDDEEEARRRLKRLENKIKEL---- 984

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1474844183  264 gtARRDLIKSEELSSKHQRdLREALAQKEDMEERITTLEK 303
Cdd:TIGR02168  985 --GPVNLAAIEEYEELKER-YDFLTAQKEDLTEAKETLEE 1021
 
Name Accession Description Interval E-value
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 ...
 976-1041 1.34e-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: 1.34e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1474844183  976 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1041
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
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 ...
 848-918 2.53e-42

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: 148.87  E-value: 2.53e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1474844183  848 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 918
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
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 ...
 1061-1132 3.68e-41

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: 145.54  E-value: 3.68e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474844183 1061 DVLVWTNDQVVHWVQSIGLRDYAGNLQESGVHGALLALDENFDHNTLALVLQIPTQNTQARQVMEREFNNLL 1132
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 980-1039 1.33e-30

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: 114.94  E-value: 1.33e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  980 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1039
Cdd:cd09495      1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 1069-1130 3.51e-27

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: 105.31  E-value: 3.51e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474844183 1069 QVVHWVQSIGLRDYAGNLQESGVHGALLALDENFDHNTLALVLQIPTQNTQARQVMEREFNN 1130
Cdd:cd09496      1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 855-913 3.67e-25

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: 99.22  E-value: 3.67e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1474844183  855 TVVSWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 913
Cdd:cd09494      1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 1061-1132 5.25e-20

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: 85.19  E-value: 5.25e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474844183 1061 DVLVWTNDQVVHWVQSIGLRDYAGNLQESGVHGALLALDENFDHNTLALVLQIPTQNTQARQVMEREFNNLL 1132
Cdd:cd09570      1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-493 6.37e-17

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: 86.65  E-value: 6.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  170 ERLRAALERVT----TLEEQLAGAHQQVSALQQGAVVRdgvaEEEGTVELgpkRLWkddTGRVEELQELLEKQNFELSQA 245
Cdd:TIGR02168  182 ERTRENLDRLEdilnELERQLKSLERQAEKAERYKELK----AELRELEL---ALL---VLRLEELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  246 RERLVTLTATVTELEEDLgtarrdliksEELSSKHQRdlrealaqkedMEERITTLEKRYLAAQREatsIHDL------- 318
Cdd:TIGR02168  252 EEELEELTAELQELEEKL----------EELRLEVSE-----------LEEEIEELQKELYALANE---ISRLeqqkqil 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  319 NDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ 398
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  399 LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQ----LHLKERMAALEEKNTLIQELESSQRQIEEQhhhKG 474
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkleeAELKELQAELEELEEELEELQEELERLEEA---LE 464

                          330
                   ....*....|....*....
gi 1474844183  475 RLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02168  465 ELREELEEAEQALDAAERE 483
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 227-495 1.21e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.76  E-value: 1.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  227 RVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDME-------ERIT 299
Cdd:COG1196    233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiarleERRR 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  300 TLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALT 379
Cdd:COG1196    313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  380 KAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQEL 459
Cdd:COG1196    393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1474844183  460 ESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGRGG 495
Cdd:COG1196    473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 1061-1132 3.87e-16

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: 74.03  E-value: 3.87e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474844183 1061 DVLVWTNDQVVHWVQSIGLRDYAGNLQESGVHGALLALDENFDHNTLALVLQIPTQNTQARQVMEREFNNLL 1132
Cdd:cd09569      1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 975-1039 3.97e-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: 73.98  E-value: 3.97e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474844183  975 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1039
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 ...
 975-1039 4.71e-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: 73.50  E-value: 4.71e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474844183  975 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1039
Cdd:cd09566      1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 849-913 1.08e-15

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: 72.87  E-value: 1.08e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474844183  849 AQWDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 913
Cdd:cd09564      2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 975-1039 5.54e-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: 67.68  E-value: 5.54e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474844183  975 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1039
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
38-493 8.34e-14

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 76.23  E-value: 8.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   38 EKLLESLRESQETLAATQSRLQDA-LHERdqlqrhLNsALPQEFATLTRElsmcreqllereeeISELKAERNNTRLLLE 116
Cdd:PRK02224   179 ERVLSDQRGSLDQLKAQIEEKEEKdLHER------LN-GLESELAELDEE--------------IERYEEQREQARETRD 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  117 HLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalERVTTLEEQLAGAHQQVSAL 196
Cdd:PRK02224   238 EADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDDL 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  197 QQGAVVRDGVAEeegTVELGPKRLWKDDtgrvEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEEL 276
Cdd:PRK02224   299 LAEAGLDDADAE---AVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  277 SSKHQRDLREALAQKEDMEERITTLEKRYLAAqreATSIHDLNDKLENELANKESLHRQCEEkarhlqelLEVAEQKLQQ 356
Cdd:PRK02224   372 LEEAREAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELREREAE--------LEATLRTARE 440

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  357 TMRKAETL------PEVEAEL--AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMnEDHNKRLSD--- 425
Cdd:PRK02224   441 RVEEAEALleagkcPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEErre 519

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474844183  426 TVDRLLSESNERLQlhlkERMAALEEKNTLIQELESSQrqiEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PRK02224   520 DLEELIAERRETIE----EKRERAEELRERAAELEAEA---EEKREAAAEAEEEAEEAREEVAELNSK 580
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 36-439 1.61e-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: 75.48  E-value: 1.61e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   36 EREKLLESLR----ESQETLAATQSRLQDALHERDQLQrhlnsalpQEFATLTRELSMCREQLLEREEEISELKAERNNT 111
Cdd:TIGR02168  674 ERRREIEELEekieELEEKIAELEKALAELRKELEELE--------EELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  112 RLLLEHLECLVSRHErslrmtvvkrqaqspsgvSSEVEVLKALKSLFEHHKALDEK---VRERLRAALERVTTLEEQLAG 188
Cdd:TIGR02168  746 EERIAQLSKELTELE------------------AEIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDE 807

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  189 AHQQVSALQQGAvvrdgvaeeeGTVELGPKRLwkddTGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARR 268
Cdd:TIGR02168  808 LRAELTLLNEEA----------ANLRERLESL----ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  269 DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREAtsiHDLNDKLENELANKESLhrqcEEKARHLQE-LL 347
Cdd:TIGR02168  874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL---EELREKLAQLELRLEGL----EVRIDNLQErLS 946

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  348 EVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNI----EEHLRQLEGQLEEKNQE---LARVRQR-----EKM 415
Cdd:TIGR02168  947 EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVnlaaIEEYEELKERYDFLTAQkedLTEAKETleeaiEEI 1026

                          410       420
                   ....*....|....*....|....
gi 1474844183  416 NEDHNKRLSDTVDRLlsesNERLQ 439
Cdd:TIGR02168 1027 DREARERFKDTFDQV----NENFQ 1046
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-490 1.70e-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: 75.48  E-value: 1.70e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  147 EVEVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQ-QGAVVRDGVAEEEGTVelgpkrlwKDDT 225
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKELTELEaEIEELEERLEEAEEEL--------AEAE 781

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  226 GRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRY 305
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  306 LAAQREATSIHDLNDKLENELANkeslhrqceekarhLQELLEVAEQKLQQTMrkaETLPEVEAELAQRIAALTKAEERH 385
Cdd:TIGR02168  862 EELEELIEELESELEALLNERAS--------------LEEALALLRSELEELS---EELRELESKRSELRRELEELREKL 924

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  386 GNIEEHLRQLEGQLEEKNQelaRVRQREKMNEDHNKRLSDTVDRLLSESNERLQLhLKERMAALEEKN-TLIQELESSQR 464
Cdd:TIGR02168  925 AQLELRLEGLEVRIDNLQE---RLSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNlAAIEEYEELKE 1000

                          330       340
                   ....*....|....*....|....*.
gi 1474844183  465 QIEEQHHHKGRLSEEIEKLRQEVDQL 490
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEAIEEI 1026
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 218-491 1.17e-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: 72.79  E-value: 1.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  218 KRLWKDDTGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEE----LSSKHQRDLREALAQKED 293
Cdd:TIGR02169  155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEA 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHL--QELLEVAEQ--KLQQTMRKAE-TLPEVE 368
Cdd:TIGR02169  235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKigELEAEIASLErSIAEKE 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  369 AELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDhnkRLSDTVDRLLSESnerlqlhlKERMAA 448
Cdd:TIGR02169  315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE---ELEDLRAELEEVD--------KEFAET 383

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1474844183  449 LEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR02169  384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 37-409 1.54e-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: 72.40  E-value: 1.54e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   37 REKLLESLRESQETLAatqsRLQDALHERD-QLQR-HLNSALPQEFATLTRELSmcREQLLEREEEISELKAERNNTRLL 114
Cdd:TIGR02168  174 RKETERKLERTRENLD----RLEDILNELErQLKSlERQAEKAERYKELKAELR--ELELALLVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  115 LEHLECLVSRHERSLRMTvvkrqaqspsgvSSEVEVLKALKSlfEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:TIGR02168  248 LKEAEEELEELTAELQEL------------EEKLEELRLEVS--ELEEEIEE-LQKELYALANEISRLEQQKQILRERLA 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  195 ALQQGAVVRDGVAEEEGTVELGPKRLWKDDTGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSE 274
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  275 ELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATS-----IHDLNDKLENELANKESLHRQCEEKARHLQELLEV 349
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEELEEELEELQEELERLEEALEELREELEE 472

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  350 AEQKLQQTMRKaetlpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARV 409
Cdd:TIGR02168  473 AEQALDAAERE-------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 36-493 3.12e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.12  E-value: 3.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   36 EREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLL 115
Cdd:COG1196    324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE-EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  116 EHLECLVSRHERSLRMTVVKRQAQspsgvssEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSA 195
Cdd:COG1196    403 EELEEAEEALLERLERLEEELEEL-------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  196 LQQGAVVRDGVAEEEGTVELGPKRLWKDDTGRVEELQELLEKQNFELSQA-RERLVTLTATVTELEEDLGTARRDLIKSE 274
Cdd:COG1196    476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvAVLIGVEAAYEAALEAALAAALQNIVVED 555

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  275 ElsskhQRDLREALAQKEDMEERITTLEKRyLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKL 354
Cdd:COG1196    556 D-----EVAAAAIEYLKAAKAGRATFLPLD-KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  355 QQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSES 434
Cdd:COG1196    630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1474844183  435 NERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEE-------IEKLRQEVDQLKGR 493
Cdd:COG1196    710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEelpeppdLEELERELERLERE 775
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 267-491 1.58e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 1.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  267 RRDLIksEELS--SKHQRDLREALAQKEDMEERIT-------TLEKRY--LAAQRE-ATSIHDLNDKLEnELANKESLHR 334
Cdd:COG1196    157 RRAII--EEAAgiSKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEkAERYRELKEELK-ELEAELLLLK 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  335 qceekARHLQELLEVAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREK 414
Cdd:COG1196    234 -----LRELEAELEELEAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  415 MNEDHNKRLSDTVDRL---LSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG1196    306 RLEERRRELEERLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 20-483 1.62e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 1.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   20 ADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREE 99
Cdd:COG1196    329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-EELLEALRAAAELAAQLEELEE 407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  100 EISELKAERNNTRLLLEHLEclvSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG1196    408 AEEALLERLERLEEELEELE---EALAELEEEEEEEEEALE-----EAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  180 TTLEEQLAGAHQQVSALQQGAVVRDGvaEEEGTVELGPKRLWKDDTGRVEELQELLEKqnFELSQARERLVTLTATVTEL 259
Cdd:COG1196    480 AELLEELAEAAARLLLLLEAEADYEG--FLEGVKAALLLAGLRGLAGAVAVLIGVEAA--YEAALEAALAAALQNIVVED 555

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  260 EEDLGTARRDLIKSEE-------LSSKHQRDLREALAQKEDMEERITTL--EKRYLAAQREATSIHDLNDKLENE-LANK 329
Cdd:COG1196    556 DEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVasDLREADARYYVLGDTLLGRTLVAArLEAA 635

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  330 ESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgniEEHLRQLEGQLEEKNQELARV 409
Cdd:COG1196    636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE---ELELEEALLAEEEEERELAEA 712

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474844183  410 RQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEeqhhhkgRLSEEIEKL 483
Cdd:COG1196    713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE-------RLEREIEAL 779
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
26-486 2.77e-11

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 68.40  E-value: 2.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   26 FEQLMVNMLDER-EKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSALPQEFATLTRElsmcreqllereeeISEL 104
Cdd:COG4913    285 FAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLERE--------------IERL 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  105 KAERNNTRLLLEHLECLVsrheRSLRMTVvkrqaqsPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEE 184
Cdd:COG4913    351 ERELEERERRRARLEALL----AALGLPL-------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  185 QLAGAHQQVSALQQGAV--------VRD------GVAEEE------------------GTVE--LGPKRL---------- 220
Cdd:COG4913    420 ELRELEAEIASLERRKSniparllaLRDalaealGLDEAElpfvgelievrpeeerwrGAIErvLGGFALtllvppehya 499

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  221 ----WKD--------DTGRVEELQE-----------LLEKQNFELSQARERLVTLTATVTEL-----EEDLGTARRD--- 269
Cdd:COG4913    500 aalrWVNrlhlrgrlVYERVRTGLPdperprldpdsLAGKLDFKPHPFRAWLEAELGRRFDYvcvdsPEELRRHPRAitr 579

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  270 --LIKSEelSSKHQRDLREALAQK----EDMEERITTLEKRYLAAQREAtsihdlnDKLENELANKESLHRQCEEKARHL 343
Cdd:COG4913    580 agQVKGN--GTRHEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEEL-------AEAEERLEALEAELDALQERREAL 650

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  344 QELLEVAEQKLQqTMRKAETLPEVEAELAQRIAA---LTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHN 420
Cdd:COG4913    651 QRLAEYSWDEID-VASAEREIAELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1474844183  421 KRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQE 486
Cdd:COG4913    730 DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
278-494 3.89e-11

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 67.63  E-value: 3.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  278 SKHQRDLREALAQKEDMEERITTLE------KRYLAAQREATSIHDLNDKLENELAnkeslhrqcEEKARHLQELLEVAE 351
Cdd:COG4913    231 VEHFDDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFA---------QRRLELLEAELEELR 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  352 QKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEehLRQLEGQLEEKNQELARVRQREKmnedhnkRLSDTVDRL- 430
Cdd:COG4913    302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDR--LEQLEREIERLERELEERERRRA-------RLEALLAALg 372

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1474844183  431 --LSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHhkgRLSEEIEKLRQEVDQLKGRG 494
Cdd:COG4913    373 lpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR---DLRRELRELEAEIASLERRK 435
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
35-490 6.41e-11

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 66.99  E-value: 6.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   35 DEREKLLESLRESQETLAA---TQSRLQDALHERDQLQRHLnSALPQEFATLTRELSMCREQLLEREEEISELKAERNNT 111
Cdd:PRK02224   227 EQREQARETRDEADEVLEEheeRREELETLEAEIEDLRETI-AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  112 RL----LLEHLECLVSRHERSLRMTVVKRQAQSpsgvssevEVLKALKSLFEHHKALDEKVRErlraALERVTTLEEQLA 187
Cdd:PRK02224   306 DAdaeaVEARREELEDRDEELRDRLEECRVAAQ--------AHNEEAESLREDADDLEERAEE----LREEAAELESELE 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  188 GAHQQVSALQ-QGAVVRDGVAEEEGTVELGPkrlwkDDTGRVEELQELLEKqnfELSQARERLVTLTATVTELEEDLGTA 266
Cdd:PRK02224   374 EAREAVEDRReEIEELEEEIEELRERFGDAP-----VDLGNAEDFLEELRE---ERDELREREAELEATLRTARERVEEA 445

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  267 RRDLI--KSEEL-----SSKHQRDLREALAQKEDMEERITTLEkrylaaqreaTSIHDLNDKLE--NELANKESLHRQCE 337
Cdd:PRK02224   446 EALLEagKCPECgqpveGSPHVETIEEDRERVEELEAELEDLE----------EEVEEVEERLEraEDLVEAEDRIERLE 515

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  338 EKARHLQELLEVAEQKLQQTMRKAETL----PEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ-R 412
Cdd:PRK02224   516 ERREDLEELIAERRETIEEKRERAEELreraAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERiR 595

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  413 EKMNEDHNKRlsDTVDRlLSESNERLQLHLKERMAALEEKNTLIQELESS--QRQIEEQHHHKGRLSEEIEKLRQEVDQL 490
Cdd:PRK02224   596 TLLAAIADAE--DEIER-LREKREALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDEL 672
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 229-407 9.99e-11

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: 63.41  E-value: 9.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  229 EELQELLEKQNF--ELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRyl 306
Cdd:COG1579      4 EDLRALLDLQELdsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  307 aaQREATSIHDLNDkLENELANKESLHRQCEEKARHLQELLEVAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHG 386
Cdd:COG1579     82 --LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEKKAELD 148

                          170       180
                   ....*....|....*....|.
gi 1474844183  387 NIEEHLRQLEGQLEEKNQELA 407
Cdd:COG1579    149 EELAELEAELEELEAEREELA 169
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 20-491 1.08e-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: 66.23  E-value: 1.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   20 ADADANFEQLmVNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSAL-PQEFATLTRELS----MCREQL 94
Cdd:TIGR02168  375 EELEEQLETL-RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEeleeELEELQ 453

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   95 LEREEEISELKAERNNTRLLLEHLECLVSRHER-SLRMTVVKRQAQSPSGVSSEV-EVLKALKSLFEHHKALDE--KVRE 170
Cdd:TIGR02168  454 EELERLEEALEELREELEEAEQALDAAERELAQlQARLDSLERLQENLEGFSEGVkALLKNQSGLSGILGVLSEliSVDE 533

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  171 RLRAALErvTTLEEQL--------AGAHQQVSALQQGAVVR------DGVAEEEGTVELGPKRLWKDDTGR--------- 227
Cdd:TIGR02168  534 GYEAAIE--AALGGRLqavvvenlNAAKKAIAFLKQNELGRvtflplDSIKGTEIQGNDREILKNIEGFLGvakdlvkfd 611

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  228 ----------------VEELQELLEKQNfeLSQARERLVTLTATVT---------ELEEDLGTARRDlIKSEELSSK--- 279
Cdd:TIGR02168  612 pklrkalsyllggvlvVDDLDNALELAK--KLRPGYRIVTLDGDLVrpggvitggSAKTNSSILERR-REIEELEEKiee 688

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  280 HQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQ-ELLEVAEQKLQQTM 358
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSkELTELEAEIEELEE 768

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  359 RKAE---TLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesn 435
Cdd:TIGR02168  769 RLEEaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL----- 843

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1474844183  436 erlqlhlKERMAALEEkntliqELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR02168  844 -------EEQIEELSE------DIESLAAEIEELEELIEELESELEALLNERASLE 886
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 36-439 1.13e-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: 1.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   36 EREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLL 115
Cdd:COG1196    397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  116 EHL-ECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDE--KVRERLRAALE---------RVTTLE 183
Cdd:COG1196    477 AALaELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVliGVEAAYEAALEaalaaalqnIVVEDD 556

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  184 EQLAGAHQQVSALQQGAVVRDGVAEEEGTVELGPKRLWKDDTGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDL 263
Cdd:COG1196    557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  264 GTAR----RDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEK 339
Cdd:COG1196    637 RRAVtlagRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  340 ARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEK---N----QELARVRQR 412
Cdd:COG1196    717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvNllaiEEYEELEER 796

                          410       420       430
                   ....*....|....*....|....*....|....
gi 1474844183  413 -EKMNEDHN------KRLSDTVDRLLSESNERLQ 439
Cdd:COG1196    797 yDFLSEQREdleearETLEEAIEEIDRETRERFL 830
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 848-912 1.21e-10

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: 58.01  E-value: 1.21e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1474844183  848 FAQWDGPTVVSWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQ 912
Cdd:cd09563      1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 31-491 1.41e-10

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: 65.90  E-value: 1.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   31 VNMLDEREKLL-ESLRESQETLAATQSRLQD-------------ALHERDQLQRHLNSALPQEFATLTRELSmcrEQLLE 96
Cdd:pfam05483  270 ANQLEEKTKLQdENLKELIEKKDHLTKELEDikmslqrsmstqkALEEDLQIATKTICQLTEEKEAQMEELN---KAKAA 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   97 REEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEHHKALDEKvrER 171
Cdd:pfam05483  347 HSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  172 LRAALERVTTLEEQLAGAHQQVSALQQGAVVRDGVAEEEGTVELGPKRLWkddTGRVEELQELLEKQ---NFELSQARER 248
Cdd:pfam05483  420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY---LKEVEDLKTELEKEklkNIELTAHCDK 496

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  249 LVTLTATVTELEEDLgtarrdlikSEELSsKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD----LNDKLEN 324
Cdd:pfam05483  497 LLLENKELTQEASDM---------TLELK-KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqKGDEVKC 566

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  325 ELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTK---AEERHGNIEE-HLRQLEGQLE 400
Cdd:pfam05483  567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKkgsAENKQLNAYEiKVNKLELELA 646

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  401 EKNQ---ELARVRQRE----KMNEDH-------NKRLSDTVDRLLSESNERLQLHLKErMAALEEK-----NTLIQELES 461
Cdd:pfam05483  647 SAKQkfeEIIDNYQKEiedkKISEEKlleevekAKAIADEAVKLQKEIDKRCQHKIAE-MVALMEKhkhqyDKIIEERDS 725

                          490       500       510
                   ....*....|....*....|....*....|....
gi 1474844183  462 S----QRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam05483  726 ElglyKNKEQEQSSAKAALEIELSNIKAELLSLK 759
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 21-491 1.80e-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: 65.52  E-value: 1.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   21 DADANFEQLMVNMLDErEKLLESLREsqeTLAATQSRLQDALHERDQLQ----RHLNSALPQEFATLTRELSMCREQLLE 96
Cdd:pfam15921  167 DSNTQIEQLRKMMLSH-EGVLQEIRS---ILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   97 REEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-----RMTVVKRQAQSpsgVSSEVEV------------LKAL 154
Cdd:pfam15921  243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQL 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  155 KSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHqqvSALQQGAVVRDGVAEEEGTV----------------ELG-- 216
Cdd:pfam15921  320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN---SELTEARTERDQFSQESGNLddqlqklladlhkrekELSle 396

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  217 ---PKRLWKDDTGR---VEELQELLEKQNFEL----------------------------SQARERLVTLTATVTELEED 262
Cdd:pfam15921  397 keqNKRLWDRDTGNsitIDHLRRELDDRNMEVqrleallkamksecqgqmerqmaaiqgkNESLEKVSSLTAQLESTKEM 476

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  263 LGTARRDLIKSE---ELSSKHQRDLREALAQKEDMEE----RITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQ 335
Cdd:pfam15921  477 LRKVVEELTAKKmtlESSERTVSDLTASLQEKERAIEatnaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 556

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  336 CEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQriaaLTKA-EERHGNIEEhLRQLEGQLEEKNQEL-ARVRQRE 413
Cdd:pfam15921  557 MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ----LEKEiNDRRLELQE-FKILKDKKDAKIRELeARVSDLE 631

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  414 ----KMNEDHNKRLSDTVDRllseSNERLQLhLKERMAALEEKNTLIQELESSQRQI----EEQHHHKGRLSEEIEKLRQ 485
Cdd:pfam15921  632 lekvKLVNAGSERLRAVKDI----KQERDQL-LNEVKTSRNELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQS 706


                   ....*.
gi 1474844183  486 EVDQLK 491
Cdd:pfam15921  707 ELEQTR 712
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-493 2.20e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.09  E-value: 2.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  102 SELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVR--ERLRAALER 178
Cdd:PRK03918   296 IKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHElyEEAKAKKEE 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  179 VTTLEEQLAGahqqvsalqqgavvrdgvaEEEGTVELGPKRLWKddtgRVEELQELLEKQNFELSQARERLVTLTATVTE 258
Cdd:PRK03918   374 LERLKKRLTG-------------------LTPEKLEKELEELEK----AKEEIEEEISKITARIGELKKEIKELKKAIEE 430

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  259 LEEDLG---TARRDLIKSE--ELSSKHQRDLREALAQKEDMEERITTLEKR------YLAAQREATSIHDLNDKLEN--- 324
Cdd:PRK03918   431 LKKAKGkcpVCGRELTEEHrkELLEEYTAELKRIEKELKEIEEKERKLRKElrelekVLKKESELIKLKELAEQLKElee 510

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  325 --ELANKESLHRQCEEkARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQL----EGQ 398
Cdd:PRK03918   511 klKKYNLEELEKKAEE-YEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEE 589

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  399 LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQL--HLKERMAALEEKNTLIQELES--SQRQIEEQHHHKG 474
Cdd:PRK03918   590 LEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAfeELAETEKRLEELRKELEELEKkySEEEYEELREEYL 669

                          410
                   ....*....|....*....
gi 1474844183  475 RLSEEIEKLRQEVDQLKGR 493
Cdd:PRK03918   670 ELSRELAGLRAELEELEKR 688
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
34-491 2.44e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.09  E-value: 2.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   34 LDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLnSALPQEFATLTRELSmcreQLLEREEEISELKAERNNTRL 113
Cdd:PRK03918   278 LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL-SRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEK 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  114 LLEHLEclvSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKAlDEKVRERLRAALERVTTLEEQLAGAHQQV 193
Cdd:PRK03918   353 RLEELE---ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA-KEEIEEEISKITARIGELKKEIKELKKAI 428

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  194 SALQqGAVVRDGVAEEEGTvELGPKRLWKDDTGRVEELQELLEKQNFELSQARERLVTLTaTVTELEEDLGTARR--DLI 271
Cdd:PRK03918   429 EELK-KAKGKCPVCGRELT-EEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELE-KVLKKESELIKLKElaEQL 505

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  272 KS--EELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK---LENELANKES----LHRQCEEKARH 342
Cdd:PRK03918   506 KEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEelaeLLKELEELGFE 585

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  343 LQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELarvrqrekmnEDHNKR 422
Cdd:PRK03918   586 SVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL----------EELEKK 655

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474844183  423 LSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:PRK03918   656 YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 169-490 6.17e-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: 63.93  E-value: 6.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  169 RERLRAALERVTTLEEQLAGAHQQVSALQQgavvrdgvAEEEGTVELgpkrlwKDDTGRVEELQELLEKQNFELSQARER 248
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIEN--------RLDELSQEL------SDASRKIGEIEKEIEQLEQEEEKLKER 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  249 LVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERIttlekrylaAQREATSIHDLNDKLENELAN 328
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL---------SHSRIPEIQAELSKLEEEVSR 809

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  329 KESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL-TKAEERHGNIEEH---LRQLEGQLEEKNQ 404
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLnGKKEELEEELEELeaaLRDLESRLGDLKK 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  405 ElaRVRQREKMNEDHNKRlsdtvdRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHK---GRLSEEIE 481
Cdd:TIGR02169  890 E--RDELEAQLRELERKI------EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDVQAELQ 961


                   ....*....
gi 1474844183  482 KLRQEVDQL 490
Cdd:TIGR02169  962 RVEEEIRAL 970
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
142-492 6.53e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.54  E-value: 6.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  142 SGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALqqgavvRDGVAEEEgtvELGPKRLw 221
Cdd:PRK03918   224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL------EEKVKELK---ELKEKAE- 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  222 kddtgRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLgtarrdliksEELSSKHQRdLREALAQKEDMEERITTL 301
Cdd:PRK03918   294 -----EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----------KELEEKEER-LEELKKKLKELEKRLEEL 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  302 EKRYLAAQrEATSIHDLNDKLENELANKESlhrqceEKarhLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKA 381
Cdd:PRK03918   358 EERHELYE-EAKAKKEELERLKKRLTGLTP------EK---LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  382 EER-----------HGNIEEHLRqlEGQLEEKNQELARVRQREKMNEDHNKRLSD---TVDRLLSESNERLQLH-LKERM 446
Cdd:PRK03918   428 IEElkkakgkcpvcGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKelrELEKVLKKESELIKLKeLAEQL 505

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1474844183  447 AALEEK--NTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKG 492
Cdd:PRK03918   506 KELEEKlkKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
261-495 6.81e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.54  E-value: 6.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  261 EDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKA 340
Cdd:PRK03918   158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  341 RHLQEL----------LEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER----------HGNIEEHLRQLEGQLE 400
Cdd:PRK03918   238 EEIEELekeleslegsKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKaeeyiklsefYEEYLDELREIEKRLS 317

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  401 EKNQELARVRQREKMNEDHNKRLSDTVDRL------LSESNERLQLH-----LKERMAALEEKNTlIQELESSQRQIEEQ 469
Cdd:PRK03918   318 RLEEEINGIEERIKELEEKEERLEELKKKLkelekrLEELEERHELYeeakaKKEELERLKKRLT-GLTPEKLEKELEEL 396

                          250       260
                   ....*....|....*....|....*.
gi 1474844183  470 HHHKGRLSEEIEKLRQEVDQLKGRGG 495
Cdd:PRK03918   397 EKAKEEIEEEISKITARIGELKKEIK 422
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 183-480 8.08e-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: 8.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  183 EEQLAGAHQQVSALQQGAVVRDGVAEEEGTV-----ELGPKRLWKDDTGRVEELQELLEKQNFELSQARERLVTLTATVT 257
Cdd:pfam15921  162 EDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIF 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  258 ELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEerITTLEKRYLAAQREATSIHDLNDKLENELANKESLHrqce 337
Cdd:pfam15921  242 PVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMY---- 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  338 ekARHLQELLEVAEQkLQQTMRKA-----ETLPEVEAELAQRIAALTKAE-------ERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:pfam15921  316 --MRQLSDLESTVSQ-LRSELREAkrmyeDKIEELEKQLVLANSELTEARterdqfsQESGNLDDQLQKLLADLHKREKE 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  406 LARVRQREKMNEDHNKRLSDTVDRLLSESNER-----------------LQLHLKERMAALEEKNTLIQELESSQRQIEE 468
Cdd:pfam15921  393 LSLEKEQNKRLWDRDTGNSITIDHLRRELDDRnmevqrleallkamkseCQGQMERQMAAIQGKNESLEKVSSLTAQLES 472

                          330
                   ....*....|..
gi 1474844183  469 QHHHKGRLSEEI 480
Cdd:pfam15921  473 TKEMLRKVVEEL 484
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
34-470 1.11e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 62.48  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   34 LDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSA---------------LPQEFATLTRELSMCREQLLERE 98
Cdd:COG4717     73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeleklekllqllpLYQELEALEAELAELPERLEELE 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   99 EEISELKAERNNTRLLLEHLEclvsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALER 178
Cdd:COG4717    153 ERLEELRELEEELEELEAELA----ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  179 VTTLEEQLAGAH--QQVSALQQGAVVRDGVAEEEGTVELGPKRLWKDD------TGRVEELQELLEKQNFELSQARERLV 250
Cdd:COG4717    229 LEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvLGLLALLFLLLAREKASLGKEAEELQ 308

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  251 TLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLND---KLENELA 327
Cdd:COG4717    309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEagvEDEEELR 388

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  328 NKESLHRQCEEkarhLQELLEVAEQKLqqtmrkAETLPEVEAELAQriAALTKAEERHGNIEEHLRQLEGQLEEKNQELA 407
Cdd:COG4717    389 AALEQAEEYQE----LKEELEELEEQL------EELLGELEELLEA--LDEEELEEELEELEEELEELEEELEELREELA 456

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474844183  408 RVRQREKMNEDhnkrlSDTVDRLLSEsnerlQLHLKERMAALEEK----NTLIQELESSQRQIEEQH 470
Cdd:COG4717    457 ELEAELEQLEE-----DGELAELLQE-----LEELKAELRELAEEwaalKLALELLEEAREEYREER 513
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
164-412 2.20e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.85  E-value: 2.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  164 LDEK-VRERLRAALERVTTL---EEQLAGAHQQVSALQQgaVVRDGVAeeegtvelgpkrlWKDDTGRVEELQELLEKqn 239
Cdd:COG4913    218 LEEPdTFEAADALVEHFDDLeraHEALEDAREQIELLEP--IRELAER-------------YAAARERLAELEYLRAA-- 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  240 FELSQARERLVTLTATVTELEEDLgtarrdlikseelsSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATsihdln 319
Cdd:COG4913    281 LRLWFAQRRLELLEAELEELRAEL--------------ARLEAELERLEARLDALREELDELEAQIRGNGGDRL------ 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  320 DKLENELANKESLHRQCEEKARHLQELLEVAEqklqqtmrkaETLPEVEAELAQRI----AALTKAEERHGNIEEH---- 391
Cdd:COG4913    341 EQLEREIERLERELEERERRRARLEALLAALG----------LPLPASAEEFAALRaeaaALLEALEEELEALEEAlaea 410

                          250       260
                   ....*....|....*....|....
gi 1474844183  392 ---LRQLEGQLEEKNQELARVRQR 412
Cdd:COG4913    411 eaaLRDLRRELRELEAEIASLERR 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 58-418 2.44e-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: 2.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   58 LQDALHERDQLQRHLnsalpqEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrq 137
Cdd:COG1196    218 LKEELKELEAELLLL------KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-------- 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  138 aqspsgvssevevlkalkslfehhkaldEKVRERLRAALERVTTLEEQLAGAHQQVSALQQgavvrdgvaeeegtvelgp 217
Cdd:COG1196    284 ----------------------------EEAQAEEYELLAELARLEQDIARLEERRRELEE------------------- 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  218 krlwkddtgRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELsskhqrdLREALAQKEDMEER 297
Cdd:COG1196    317 ---------RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-------LLEAEAELAEAEEE 380

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  298 ITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlpEVEAELAQRIAA 377
Cdd:COG1196    381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---EAAEEEAELEEE 457

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1474844183  378 LTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNED 418
Cdd:COG1196    458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 35-490 3.09e-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: 61.61  E-value: 3.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   35 DEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNS------ALPQEFATLTRELSMCREQLLEREEEISELKAER 108
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeeleSLEAELEELEAELEELESRLEELEEQLETLRSKV 388

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  109 NNTRL-----------LLEHLECLVSRHER------SLRMTVVKRQAQSPSGVSSEVE-VLKALKSLFEHHKALDEKVRE 170
Cdd:TIGR02168  389 AQLELqiaslnneierLEARLERLEDRRERlqqeieELLKKLEEAELKELQAELEELEeELEELQEELERLEEALEELRE 468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  171 RLRAALERVTTLEEQLAGAHQQVSALQQGAVVRDGVAEEEGTVELGPKRLwKDDTGRVEEL------------------- 231
Cdd:TIGR02168  469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL-SGILGVLSELisvdegyeaaieaalggrl 547

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  232 --------------QELLEKQN------FELSQARERL--VTLTATVTELEEDLGTARrDLIKSEELSSK-------HQR 282
Cdd:TIGR02168  548 qavvvenlnaakkaIAFLKQNElgrvtfLPLDSIKGTEiqGNDREILKNIEGFLGVAK-DLVKFDPKLRKalsyllgGVL 626

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  283 ---DLREALAQ--KEDMEERITTLE-----KRYLAAQREATSIHDLNDKlENELANKESLHRQCEEKARHLQELLEVAEQ 352
Cdd:TIGR02168  627 vvdDLDNALELakKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAELEKALAELRK 705

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  353 KLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVD 428
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474844183  429 RL-----------------LSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQL 490
Cdd:TIGR02168  786 ELeaqieqlkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 163-414 3.48e-09

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: 61.51  E-value: 3.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  163 ALDEKVRERLRAALERVTTLEEQLAgahQQVSALQQGAVVRDGVAEEEGTVE--LGPKRLWKDDT--GRVEELQELLEkq 238
Cdd:COG3096    829 AFAPDPEAELAALRQRRSELERELA---QHRAQEQQLRQQLDQLKEQLQLLNklLPQANLLADETlaDRLEELREELD-- 903

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  239 nfELSQARERLVTLTATVTELEEDLGTARRDLIKSEELsskhQRDLREALAQKEDMEERITTLEkrYLAAQREATSIHD- 317
Cdd:COG3096    904 --AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQL----QADYLQAKEQQRRLKQQIFALS--EVVQRRPHFSYEDa 975

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  318 ---------LNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL-----TKAEE 383
Cdd:COG3096    976 vgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadAEAEE 1055

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1474844183  384 RhgnIEEHLRQLEGQLeekNQELARVRQREK 414
Cdd:COG3096   1056 R---ARIRRDELHEEL---SQNRSRRSQLEK 1080
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 342-493 5.15e-09

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: 58.01  E-value: 5.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  342 HLQELLEVAE--QKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRqrEKM 415
Cdd:COG1579      5 DLRALLDLQEldSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE--EQL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  416 NEDHNKRLSDTVDR---LLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHH-KGRLSEEIEKLRQEVDQLK 491
Cdd:COG1579     83 GNVRNNKEYEALQKeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEkKAELDEELAELEAELEELE 162


                   ..
gi 1474844183  492 GR 493
Cdd:COG1579    163 AE 164
PTZ00121 PTZ00121
MAEBL; Provisional
 159-451 6.01e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.93  E-value: 6.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAVVRDgvAEEEGTVElgPKRLWKDDTG----RVEELQEL 234
Cdd:PTZ00121  1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK--AEEKKKAE--EAKKAEEDKNmalrKAEEAKKA 1589

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  235 LEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATs 314
Cdd:PTZ00121  1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK- 1668

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  315 ihdlndKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQ 394
Cdd:PTZ00121  1669 ------KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1474844183  395 lEGQLEEKNQELARVRQREKmnedhnkrlsDTVDRLLSESNERLQLHLKERMAALEE 451
Cdd:PTZ00121  1738 -EAEEDKKKAEEAKKDEEEK----------KKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 34-487 6.67e-09

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: 60.62  E-value: 6.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   34 LDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSmcrEQLLEREEEISELKAERNNTRl 113
Cdd:pfam12128  246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWK---EKRDELNGELSAADAAVAKDR- 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  114 llEHLECLVSRHERSLRMTVVKR---QAQSPSgVSSEVEVL-KALKSLFEHHK-------ALDEKVRERLRAALERVT-- 180
Cdd:pfam12128  322 --SELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQdvtakynRRRSKIKEQNNRDIAGIKdk 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  181 ------TLEEQLAGAHQQVSALQQ-------GAVVRDGVAEEEGTVELGPKRLWKDDTGRVEELQELLEKQNFELSQARE 247
Cdd:pfam12128  399 lakireARDRQLAVAEDDLQALESelreqleAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERARE 478

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  248 RLVTLTATVTELEEDLGTARRdliKSEELSSKHQRDLREALAQKEDMEERITTLEKRylaaqrEATSIHDLNDKLEN--- 324
Cdd:pfam12128  479 EQEAANAEVERLQSELRQARK---RRDQASEALRQASRRLEERQSALDELELQLFPQ------AGTLLHFLRKEAPDweq 549

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  325 ---ELANKESLHR---QCEEKARHLQELLEVAEQKLQ----QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQ 394
Cdd:pfam12128  550 sigKVISPELLHRtdlDPEVWDGSVGGELNLYGVKLDlkriDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQ 629

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  395 LEGQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllSESNERLQLHlKERMAALEEKNTLIQELESSQRQIEEQH---- 470
Cdd:pfam12128  630 ANGELEKASREETFARTALKNARLDLRRLFD------EKQSEKDKKN-KALAERKDSANERLNSLEAQLKQLDKKHqawl 702

                          490       500
                   ....*....|....*....|.
gi 1474844183  471 -HHKGRLSE---EIEKLRQEV 487
Cdd:pfam12128  703 eEQKEQKREartEKQAYWQVV 723
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
42-485 8.35e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 60.05  E-value: 8.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   42 ESLRESQETLAATQSRLQDALHE-RDQLQRHLNSA----------------LPQEFATLTRELSMCREQLLEREEEISEL 104
Cdd:PRK02224   310 EAVEARREELEDRDEELRDRLEEcRVAAQAHNEEAeslredaddleeraeeLREEAAELESELEEAREAVEDRREEIEEL 389

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  105 KAERNNTRL-----------LLEHLECLVSRHERslrmtVVKRQAQSPSGVSSEVEVLKALKSLFEHHKA-------LDE 166
Cdd:PRK02224   390 EEEIEELRErfgdapvdlgnAEDFLEELREERDE-----LREREAELEATLRTARERVEEAEALLEAGKCpecgqpvEGS 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  167 KVRERLRAALERVTTLEEQLAGAHQQVSALQQgavvRDGVAEEEGTVELGPKRLWKddtgRVEELQELLEKQNFELSQAR 246
Cdd:PRK02224   465 PHVETIEEDRERVEELEAELEDLEEEVEEVEE----RLERAEDLVEAEDRIERLEE----RREDLEELIAERRETIEEKR 536

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  247 ERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKrylaaqreatsIHDLNDKLENEL 326
Cdd:PRK02224   537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-----------IRTLLAAIADAE 605

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  327 ANKESLhrqcEEKARHLQELLEVAEQKLQQtmrKAETLPEVEAELAQriAALTKAEERHGNIEEHLRQLEGQLEEKNQEL 406
Cdd:PRK02224   606 DEIERL----REKREALAELNDERRERLAE---KRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREER 676

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474844183  407 ARVRQREKMNEDHNKRLSDtvdrllsesnerlqlhLKERMAALEEKntlIQELESSQRQIEEQHHHKGRLSEEiekLRQ 485
Cdd:PRK02224   677 DDLQAEIGAVENELEELEE----------------LRERREALENR---VEALEALYDEAEELESMYGDLRAE---LRQ 733
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 32-484 1.39e-08

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: 59.21  E-value: 1.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   32 NMLDEREKLLESLRESQETLAATQsRLQDALHERDQLQRHLNSALPQEfATLTRELSmcreqllereeEISELKAERNNT 111
Cdd:TIGR00618  223 VLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARI-EELRAQEA-----------VLEETQERINRA 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  112 RllleHLECLVsrhERSLRMTVVKRQAQspsgvssevevlkalkslfEHHKALDEKVRERLRAALERVTTLEEQLAGAHQ 191
Cdd:TIGR00618  290 R----KAAPLA---AHIKAVTQIEQQAQ-------------------RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  192 QVSALQQGAvvrdgvAEEEGTVELGPKRLWKDDTGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGT------ 265
Cdd:TIGR00618  344 RRLLQTLHS------QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATidtrts 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  266 ARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHdlnDKLENELANKESLHRQCEE-KARHLQ 344
Cdd:TIGR00618  418 AFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL---KEREQQLQTKEQIHLQETRkKAVVLA 494

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  345 ELLEVAEQklQQTMRKAETLPEVEAELAQRIAALT----KAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHN 420
Cdd:TIGR00618  495 RLLELQEE--PCPLCGSCIHPNPARQDIDNPGPLTrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474844183  421 KRLSDTVDRLLSESNERLQLhlkermaaLEEKNTLIQELESSQRQI-EEQHHHKGRLSEEIEKLR 484
Cdd:TIGR00618  573 SILTQCDNRSKEDIPNLQNI--------TVRLQDLTEKLSEAEDMLaCEQHALLRKLQPEQDLQD 629
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 246-493 1.40e-08

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: 59.31  E-value: 1.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  246 RERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENE 325
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  326 LANKESLHR-------QCEEKARHLQELLE-----VAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnieehLR 393
Cdd:TIGR02169  753 IENVKSELKelearieELEEDLHKLEEALNdlearLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-------LT 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  394 QLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERlqlhLKERMAALEEkntLIQELESSQRQIEEQHHHK 473
Cdd:TIGR02169  826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRD---LESRLGDLKKERDELEAQL 898

                          250       260
                   ....*....|....*....|
gi 1474844183  474 GRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02169  899 RELERKIEELEAQIEKKRKR 918
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 47-492 1.42e-08

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: 59.21  E-value: 1.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   47 SQETLAATQSRLQDALHERDQLQRHLnsalpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVsrhE 126
Cdd:TIGR00618  436 QQRYAELCAAAITCTAQCEKLEKIHL-----QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL---C 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  127 RSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKALdEKVRERLRAALERVTTLEEQLAGAHQQVSALQQ-----GAV 201
Cdd:TIGR00618  508 GSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSE-EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQcdnrsKED 585

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  202 VRDGVAEEEGTVELGPKRLWKDDTGRVEELQELLEKQ-------------NFELSQARErLVTLTATVTEL--EEDLGTA 266
Cdd:TIGR00618  586 IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQpeqdlqdvrlhlqQCSQELALK-LTALHALQLTLtqERVREHA 664

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  267 RRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDlNDKLENELANKESLHRQceekarHLQEL 346
Cdd:TIGR00618  665 LSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE-YDREFNEIENASSSLGS------DLAAR 737

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  347 LEVAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ---LEEKNQELArvrqrEKMNEDHNKR 422
Cdd:TIGR00618  738 EDALNQSLKELMHQARTvLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFnrlREEDTHLLK-----TLEAEIGQEI 812

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  423 LSDTVDRLLSEsnERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKG 492
Cdd:TIGR00618  813 PSDEDILNLQC--ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
mukB PRK04863
chromosome partition protein MukB;
169-485 1.50e-08

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 59.59  E-value: 1.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  169 RERLRAALERVTTLEEQLAGAHQQVSALQQ--GAVVR--DGVAEEEGTVE----LGPKRLWKDDTGR------------V 228
Cdd:PRK04863   278 ANERRVHLEEALELRRELYTSRRQLAAEQYrlVEMARelAELNEAESDLEqdyqAASDHLNLVQTALrqqekieryqadL 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  229 EELQELLEKQNFELSQARERLVTLTATVTELEEDlgtarrdlikseelsskhQRDLREALAqkeDMEERITTLEKR---Y 305
Cdd:PRK04863   358 EELEERLEEQNEVVEEADEQQEENEARAEAAEEE------------------VDELKSQLA---DYQQALDVQQTRaiqY 416

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  306 LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQ-------------QTMRKAetLPEVEAELA 372
Cdd:PRK04863   417 QQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSvaqaahsqfeqayQLVRKI--AGEVSRSEA 494

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  373 QRIA--ALTKAEErHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDrllseSNERLQLHLKERMAALE 450
Cdd:PRK04863   495 WDVAreLLRRLRE-QRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD-----DEDELEQLQEELEARLE 568

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1474844183  451 EkntLIQELESSQRQIEEQHHHKGRLSEEIEKLRQ 485
Cdd:PRK04863   569 S---LSESVSEARERRMALRQQLEQLQARIQRLAA 600
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
22-493 1.64e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.92  E-value: 1.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   22 ADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQrhlnsALPQEFATLTRELSMCREQLLEREEEI 101
Cdd:PRK03918   187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-----ELKEEIEELEKELESLEGSKRKLEEKI 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  102 SELKAERNNTRLLLEHLECLVSRHE--RSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRErLRAALERV 179
Cdd:PRK03918   262 RELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERL 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  180 TTLEEQLAGAHQQVSALQQGAVVRDGVAEEEGTVELGPKRLWKDDTGRVEELQELLEKQNFELSQARERLVTLTATVTEL 259
Cdd:PRK03918   341 EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  260 EEDLGTARRDLIKSE--------ELSSKHQRDL-REALAQKEDMEERITTLEKRYLAAQREATsihdlndKLENELANKE 330
Cdd:PRK03918   421 IKELKKAIEELKKAKgkcpvcgrELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLRKELR-------ELEKVLKKES 493

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  331 SLHRQCE--EKARHLQELLEVAE-QKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELA 407
Cdd:PRK03918   494 ELIKLKElaEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELA 573

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  408 RVrqrekmnedhNKRLSdtvdRLLSESNERLQLHLKErmaaLEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEV 487
Cdd:PRK03918   574 EL----------LKELE----ELGFESVEELEERLKE----LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL 635


                   ....*.
gi 1474844183  488 DQLKGR 493
Cdd:PRK03918   636 AETEKR 641
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
135-494 1.93e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 1.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  135 KRQAQSPSGVSSEVEVL-KALKSLFEHHKALDEKvRERLRAALERVTTLEEQLAGAHQQVSALQQGAVVRDGVAEEEGTv 213
Cdd:COG4717     60 KPQGRKPELNLKELKELeEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL- 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  214 elgpKRLWKDDTGRVEELQELLEkqnfELSQARERLVTLTATVTELEEDLGTARRDLikseelSSKHQRDLREALAQKED 293
Cdd:COG4717    138 ----EAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQL------SLATEEELQDLAEELEE 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKAR-------------------------------- 341
Cdd:COG4717    204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvl 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  342 ----HLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE-----------EHLRQLEGQLEEKNQEL 406
Cdd:COG4717    284 gllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeellelldriEELQELLREAEELEEEL 363

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  407 ARVRQREKMNEDHNKRLSDTVDRL----------------LSESNERLQLHLKERMAALE--EKNTLIQELESSQRQIEE 468
Cdd:COG4717    364 QLEELEQEIAALLAEAGVEDEEELraaleqaeeyqelkeeLEELEEQLEELLGELEELLEalDEEELEEELEELEEELEE 443

                          410       420
                   ....*....|....*....|....*.
gi 1474844183  469 QHHHKGRLSEEIEKLRQEVDQLKGRG 494
Cdd:COG4717    444 LEEELEELREELAELEAELEQLEEDG 469
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 229-430 1.97e-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: 57.85  E-value: 1.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  229 EELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYlAA 308
Cdd:COG4942     30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-AE 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  309 QREATSIHDLNDKLENELANKESLhrQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnI 388
Cdd:COG4942    109 LLRALYRLGRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE---L 183

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1474844183  389 EEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL 430
Cdd:COG4942    184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 281-486 1.98e-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: 57.85  E-value: 1.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  361 AETLpevEAELAQRIAALTK------------------AEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKR 422
Cdd:COG4942     99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474844183  423 LSDTVDRlLSESNERLQLHLKERMAALEEKNtliQELESSQRQIEEQHHHKGRLSEEIEKLRQE 486
Cdd:COG4942    176 LEALLAE-LEEERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAE 235
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
16-493 2.59e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.39  E-value: 2.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   16 PPHGADADA---NFEQLM---VNMLDEREK--LLESLRESQETLAATQSRLQdalherdqLQRHLNSALPQEFATLTREL 87
Cdd:COG4913    221 PDTFEAADAlveHFDDLErahEALEDAREQieLLEPIRELAERYAAARERLA--------ELEYLRAALRLWFAQRRLEL 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   88 smcreqlleREEEISELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPSGvssevEVLKALKSLFEHHKALDEK 167
Cdd:COG4913    293 ---------LEAELEELRAELARLEAELERLEARLDALREELD--ELEAQIRGNGG-----DRLEQLEREIERLERELEE 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  168 VRERLRAALERVTTLEEQLAGAHQQVSALQQGAV-VRDGVAEEEGTVEL---GPKRLWKDDTGRVEELQ-EL--LEKQNF 240
Cdd:COG4913    357 RERRRARLEALLAALGLPLPASAEEFAALRAEAAaLLEALEEELEALEEalaEAEAALRDLRRELRELEaEIasLERRKS 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  241 ----ELSQARERLVT-LTATVTEL----------EED----------LGTARRDLIkseeLSSKHQRDLREALAQkEDME 295
Cdd:COG4913    437 nipaRLLALRDALAEaLGLDEAELpfvgelievrPEEerwrgaiervLGGFALTLL----VPPEHYAAALRWVNR-LHLR 511

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  296 ERITTLE-----KRYLAAQREATSI--------HDLNDKLENELANKESLHR-------QCEEKA--------------- 340
Cdd:COG4913    512 GRLVYERvrtglPDPERPRLDPDSLagkldfkpHPFRAWLEAELGRRFDYVCvdspeelRRHPRAitragqvkgngtrhe 591

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  341 ---RHL-----------QELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEH------LRQLEGQLE 400
Cdd:COG4913    592 kddRRRirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidVASAEREIA 671

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  401 EKNQELARvrqrekmnedhnkrlsdtvdrlLSESNERLQlHLKERMAALEEkntliqELESSQRQIEEQHHHKGRLSEEI 480
Cdd:COG4913    672 ELEAELER----------------------LDASSDDLA-ALEEQLEELEA------ELEELEEELDELKGEIGRLEKEL 722

                          570
                   ....*....|...
gi 1474844183  481 EKLRQEVDQLKGR 493
Cdd:COG4913    723 EQAEEELDELQDR 735
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 33-487 3.22e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 3.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   33 MLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREEEISELKAERNNTR 112
Cdd:COG1196    230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR-LELEELELELEEAQAEEYELLAELARLEQDIARLE 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  113 LLLEHLEclvsrherslrmtvvKRQAQspsgvssEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQ 192
Cdd:COG1196    309 ERRRELE---------------ERLEE-------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  193 VSALQQGAVVRDGVAEEEGTVELGPKRlwkddtgRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIK 272
Cdd:COG1196    367 LLEAEAELAEAEEELEELAEELLEALR-------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  273 SEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQ 352
Cdd:COG1196    440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  353 KLQQtmRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRqREKMNEDHNKRLSDTVDRLLS 432
Cdd:COG1196    520 RGLA--GAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT-FLPLDKIRARAALAAALARGA 596

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1474844183  433 ESNERLQLHLKERmaALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEV 487
Cdd:COG1196    597 IGAAVDLVASDLR--EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
169-489 3.31e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.00  E-value: 3.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAVVRDGVAEeegtvelgpkRLWKD-DTGRVE-ELQEL------LEKQNF 240
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAE----------YSWDEiDVASAErEIAELeaelerLDASSD 685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  241 ELSQARERLVTLTATVTELEEDLGTARRDLIKSEelssKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLND 320
Cdd:COG4913    686 DLAALEEQLEELEAELEELEEELDELKGEIGRLE----KELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  321 KLENELAnkeslhRQCEEKARHLQELLEVAEQKLQQTMR------------------------------KAETLPEVEAE 370
Cdd:COG4913    762 AVERELR------ENLEERIDALRARLNRAEEELERAMRafnrewpaetadldadleslpeylalldrlEEDGLPEYEER 835

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  371 LAQriaALTKAEER-----HGNIEEHLRQLEGQLEEKNQELARVRqrekMNEDHnkrlsdtvdrllsesneRLQLHLKER 445
Cdd:COG4913    836 FKE---LLNENSIEfvadlLSKLRRAIREIKERIDPLNDSLKRIP----FGPGR-----------------YLRLEARPR 891

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1474844183  446 maALEEKNTLIQELESSQRQI-----EEQHHHKGRLSEEIEKLRQEVDQ 489
Cdd:COG4913    892 --PDPEVREFRQELRAVTSGAslfdeELSEARFAALKRLIERLRSEEEE 938
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 848-914 4.81e-08

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: 51.14  E-value: 4.81e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474844183   848 FAQWDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 914
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
30-487 5.56e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.38  E-value: 5.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   30 MVNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERN 109
Cdd:PRK03918   336 KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  110 NTRLLLEHLECLVSRHERSLRMTVVKRqaqspsgvssevevlkalKSLFEHHKaldEKVRERLRAALERVttlEEQLAGA 189
Cdd:PRK03918   416 ELKKEIKELKKAIEELKKAKGKCPVCG------------------RELTEEHR---KELLEEYTAELKRI---EKELKEI 471

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  190 HQQVSALQQGAVVRDGVAEEEGTVelgpkRLWKDDTGRVEELQELLEKQNFE-LSQARERLVTLTATVTELEEDLGTARR 268
Cdd:PRK03918   472 EEKERKLRKELRELEKVLKKESEL-----IKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKK 546

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  269 DLIKSEELSSKhqrdLREALAQKEDMEERITTLEKRYLaaQREATSIHDLNDKLE---------NELANKESLHRQCEEK 339
Cdd:PRK03918   547 ELEKLEELKKK----LAELEKKLDELEEELAELLKELE--ELGFESVEELEERLKelepfyneyLELKDAEKELEREEKE 620

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  340 ARHLQELLEVAEQKLQQTMRKAEtlpeveaELAQRIAALtkaeERHGNIEEHlRQLEGQLEEKNQELARVRQREKMNEDH 419
Cdd:PRK03918   621 LKKLEEELDKAFEELAETEKRLE-------ELRKELEEL----EKKYSEEEY-EELREEYLELSRELAGLRAELEELEKR 688

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474844183  420 NKRLSDTVDRllsesnerlqlhLKERMAALEEKNTLIQELESSQRQIEEqhhhkgrLSEEIEKLRQEV 487
Cdd:PRK03918   689 REEIKKTLEK------------LKEELEEREKAKKELEKLEKALERVEE-------LREKVKKYKALL 737
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
301-491 6.76e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.70  E-value: 6.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  301 LEKRYLAAQREATSIHDLNDKLE-NELANKESLHRQCEEKARHLQELlevaEQKLQQTMRKAETLPEVEAELAQRIAALT 379
Cdd:COG4717     47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLE 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  380 KAEERHGNIEEhLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQEL 459
Cdd:COG4717    123 KLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1474844183  460 ESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG4717    202 EELQQRLAELEEELEEAQEELEELEEELEQLE 233
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 232-469 7.47e-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: 55.93  E-value: 7.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  232 QELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQRE 311
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  312 atsIHDLNDKLENELANKESLHRQCEEKarhlqelLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnieeh 391
Cdd:COG4942     99 ---LEAQKEELAELLRALYRLGRQPPLA-------LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE------- 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474844183  392 LRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ 469
Cdd:COG4942    162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 230-491 8.55e-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: 56.57  E-value: 8.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  230 ELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERIttlekrylaaQ 309
Cdd:TIGR04523  311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN----------Q 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  310 REATSIHDLNDK---LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHG 386
Cdd:TIGR04523  381 SYKQEIKNLESQindLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD 460

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  387 NIEEHLRQ----LEGQ-------LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAALE----E 451
Cdd:TIGR04523  461 NTRESLETqlkvLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEsekkE 535

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  452 KNTLIQELES--------------------SQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR04523  536 KESKISDLEDelnkddfelkkenlekeideKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 984-1039 9.45e-08

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: 9.45e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1474844183   984 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1039
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
40-491 1.01e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.31  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   40 LLESLRESQETLAATQSRL-QDALHERDQLQRHLNSA--LPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLE 116
Cdd:COG4717     47 LLERLEKEADELFKPQGRKpELNLKELKELEEELKEAeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  117 HLECL--VSRHERSL-----RMTVVKRQAQSPSGVSSEVEVLKAlkSLFEHHKALDEKVRERLRAALERVTTLEEQLAGA 189
Cdd:COG4717    127 LLPLYqeLEALEAELaelpeRLEELEERLEELRELEEELEELEA--ELAELQEELEELLEQLSLATEEELQDLAEELEEL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  190 HQQVSALQQG-AVVRDGVAEEEGTVE-LGPKRLWKDDTGRVEELQEL---------LEKQNFELSQARERLVTLTATVTE 258
Cdd:COG4717    205 QQRLAELEEElEEAQEELEELEEELEqLENELEAAALEERLKEARLLlliaaallaLLGLGGSLLSLILTIAGVLFLVLG 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  259 LeedLGTARRDLIKSEELSSKHQRDLREALAQKE-DMEERITTLEKRYLAAQREATSIHDLNDKLEnelaNKESLHRQCE 337
Cdd:COG4717    285 L---LALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDRIE----ELQELLREAE 357

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  338 EKARHLQelLEVAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEErhgnIEEHLRQLEGQLEEKNQELARVRQREKmNE 417
Cdd:COG4717    358 ELEEELQ--LEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQE----LKEELEELEEQLEELLGELEELLEALD-EE 428

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474844183  418 DHNKRLSDTVDRLLSESNERLQLHlkERMAALEEKntlIQELESSQRqIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG4717    429 ELEEELEELEEELEELEEELEELR--EELAELEAE---LEQLEEDGE-LAELLQELEELKAELRELAEEWAALK 496
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 22-486 1.46e-07

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: 56.00  E-value: 1.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   22 ADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEI 101
Cdd:pfam12128  454 NQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQA 533

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  102 SELKA-ERNNTRLLLEHLECLVSR---HERSLRMTVVKRQAQSPS---GVSSEVEVLKALKSLFeHHKALDE---KVRER 171
Cdd:pfam12128  534 GTLLHfLRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELnlyGVKLDLKRIDVPEWAA-SEEELRErldKAEEA 612

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  172 LRAALERVTTLEEQLAGAHQQVSALQQGavVRDGVAEEEGTvELGPKRLwkddTGRVEELQELLEKQ-NFELSQARERLV 250
Cdd:pfam12128  613 LQSAREKQAAAEEQLVQANGELEKASRE--ETFARTALKNA-RLDLRRL----FDEKQSEKDKKNKAlAERKDSANERLN 685

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  251 TLTATVTELEEDLGTA----RRDLIkseELSSKHQRDLREALAQKEDMEERI-TTLEKRYLAAQREATSIHDLNDkleNE 325
Cdd:pfam12128  686 SLEAQLKQLDKKHQAWleeqKEQKR---EARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWYK---RD 759

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  326 LANK--------------ESLHRQCEEKARHLQELLE----VAEQKLQQTMRKAETLPEVEA---ELAQRIAALTK-AEE 383
Cdd:pfam12128  760 LASLgvdpdviaklkreiRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERaisELQQQLARLIAdTKL 839

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  384 RHGNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHnkrlsdtvdrlLSESNERLQLHLKERMAALEE-KNTLIQELES 461
Cdd:pfam12128  840 RRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGERLAQLEDlKLKRDYLSES 908

                          490       500       510
                   ....*....|....*....|....*....|
gi 1474844183  462 SQRQIEE-----QHHHKGRLSEEIEKLRQE 486
Cdd:pfam12128  909 VKKYVEHfknviADHSGSGLAETWESLREE 938
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 243-493 2.24e-07

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: 55.46  E-value: 2.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  243 SQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDME-ERITTLEKRYLAAQREATSIHDLNDK 321
Cdd:TIGR02169  152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRrEREKAERYQALLKEKREYEGYELLKE 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  322 LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLpeveAELAQRIAALTkaEERHGNIEEHLRQLEGQLEE 401
Cdd:TIGR02169  232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL----EELNKKIKDLG--EEEQLRVKEKIGELEAEIAS 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  402 knqelarvrqrekmnedhnkrlsdtVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIE 481
Cdd:TIGR02169  306 -------------------------LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360

                          250
                   ....*....|..
gi 1474844183  482 KLRQEVDQLKGR 493
Cdd:TIGR02169  361 ELKEELEDLRAE 372
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 225-491 3.02e-07

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: 54.98  E-value: 3.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  225 TGRVEELQELLEKQNFELS-------QARERLVTLTATV--TELEEDLGTARRDLIKSEELsskhqRDLREALAQKEDME 295
Cdd:pfam02463  115 NVTKKEVAELLESQGISPEaynflvqGGKIEIIAMMKPErrLEIEEEAAGSRLKRKKKEAL-----KKLIEETENLAELI 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  296 ERITTLEKRYLAAQREAtsihdlndKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRI 375
Cdd:pfam02463  190 IDLEELKLQELKLKEQA--------KKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIE 261

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  376 AALTKAEERHGNIEEHLRQLEGQLEEKNQeLARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTL 455
Cdd:pfam02463  262 KEEEKLAQVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL 340

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1474844183  456 IQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam02463  341 EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 281-469 3.40e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.07  E-value: 3.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELankESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG3883     22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALYRS 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  361 AETLPEVEA--------ELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS 432
Cdd:COG3883     99 GGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1474844183  433 ESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ 469
Cdd:COG3883    179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-380 4.71e-07

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: 54.30  E-value: 4.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   33 MLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAErnntr 112
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----- 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  113 llLEHLECLVSRHERSLrmtvVKRQAQ--------SPSGVSsevEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEE 184
Cdd:TIGR02169  760 --LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKE 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  185 QLAGAHQQvsALQQGAVVRDGVAEEEGTVElgpkrlwkDDTGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLG 264
Cdd:TIGR02169  830 YLEKEIQE--LQEQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  265 TARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQ 344
Cdd:TIGR02169  900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1474844183  345 ELLEVAEqKLQQTMRKAETLPEVEAELAQRIAALTK 380
Cdd:TIGR02169  980 EYEEVLK-RLDELKEKRAKLEEERKAILERIEEYEK 1014
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
34-440 5.87e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 5.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   34 LDEREKLLESLRESQETLAATQSRLQDALherDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRL 113
Cdd:COG4717    151 LEERLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  114 LLEHLECLVSRHErslrmtvvkrqaqspsgvssEVEVLKALKSLFehhkaLDEKVRERLRAALERVTTLEEQLAGAHQQV 193
Cdd:COG4717    228 ELEQLENELEAAA--------------------LEERLKEARLLL-----LIAAALLALLGLGGSLLSLILTIAGVLFLV 282

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  194 SALQQGAVVRDGVAEEEGTVELGP-KRLWKDDTGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLik 272
Cdd:COG4717    283 LGLLALLFLLLAREKASLGKEAEElQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-- 360

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  273 sEELSSKHQRDLREALAQKEDM--EERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKArhLQELLEVA 350
Cdd:COG4717    361 -EELQLEELEQEIAALLAEAGVedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEEL 437

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  351 EQKLQQTMRKAETLPEVEAELAQRIAALtKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDT-VDR 429
Cdd:COG4717    438 EEELEELEEELEELREELAELEAELEQL-EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREErLPP 516

                          410
                   ....*....|.
gi 1474844183  430 LLSESNERLQL 440
Cdd:COG4717    517 VLERASEYFSR 527
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 284-451 7.60e-07

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: 51.46  E-value: 7.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  284 LREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELL-EVAEQKLQQTMRKae 362
Cdd:COG1579     19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgNVRNNKEYEALQK-- 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  363 tlpEVEAelaqriaaltkAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHL 442
Cdd:COG1579     97 ---EIES-----------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162


                   ....*....
gi 1474844183  443 KERMAALEE 451
Cdd:COG1579    163 AEREELAAK 171
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 227-377 7.67e-07

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: 51.46  E-value: 7.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  227 RVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEEL--SSKHQRDLREALAQKEDMEERITTLEKR 304
Cdd:COG1579     32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEALQKEIESLKRRISDLEDE 111

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1474844183  305 YLaaqreatsihDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAA 377
Cdd:COG1579    112 IL----------ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 35-493 1.74e-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: 52.76  E-value: 1.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   35 DEREKLLESLRESQETLAAT-------QSRLQDALHERDQLQRHLnSALPQEFATLTRELSMCREQLLEREEEISELKAE 107
Cdd:TIGR02169  364 EELEDLRAELEEVDKEFAETrdelkdyREKLEKLKREINELKREL-DRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  108 RNNTRLLLEHLE-------CLVSRHERSLRMTVVKRQAQSP--SGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALER 178
Cdd:TIGR02169  443 KEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKelSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  179 VTTLEEQLAGAHQQ-VSALQQGA--------VVRDGVAEE-------------------EGTVELGPKRLWKDDtGRVEE 230
Cdd:TIGR02169  523 VHGTVAQLGSVGERyATAIEVAAgnrlnnvvVEDDAVAKEaiellkrrkagratflplnKMRDERRDLSILSED-GVIGF 601

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  231 LQELLE-KQNFE---------------LSQARE-----RLVTLTAtvtELEEDLG--TARRDLIKSEELSSKHQRD-LRE 286
Cdd:TIGR02169  602 AVDLVEfDPKYEpafkyvfgdtlvvedIEAARRlmgkyRMVTLEG---ELFEKSGamTGGSRAPRGGILFSRSEPAeLQR 678

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  287 ALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAET--- 363
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvks 758

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  364 -LPEVEAELAQRIAALTKAEERHGNIEEHLRQleGQLEEKNQELARVRQREKMNEdhnKRLSDtVDRLLSESNERLQLhL 442
Cdd:TIGR02169  759 eLKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE---ARLRE-IEQKLNRLTLEKEY-L 831

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1474844183  443 KERMAALEEKNTLIQELESS-QRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSiEKEIENLNGKKEELEEELEELEAALRDLESR 883
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 35-493 2.59e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 2.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   35 DEREKLLESLRESQETLAATQSRLQ----------DALHERDQLQRHLNS---ALPQEFATLTRELSMCREQLLEREEEI 101
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQeleekleelrLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  102 SELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSgVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTT 181
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-LEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  182 LEEQLAGAHQQVSALQQGavvRDGVAEEEGTVELGPKRLWKDDT-GRVEELQELLEKQNFELSQARERLVTLTATVTELE 260
Cdd:TIGR02168  398 LNNEIERLEARLERLEDR---RERLQQEIEELLKKLEEAELKELqAELEELEEELEELQEELERLEEALEELREELEEAE 474

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  261 EDLGTARRDLIKS----------EELSSKHQRDLREALAQKEDME-------ERITTLEK------RYLAAQREATSIHD 317
Cdd:TIGR02168  475 QALDAAERELAQLqarldslerlQENLEGFSEGVKALLKNQSGLSgilgvlsELISVDEGyeaaieAALGGRLQAVVVEN 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  318 LNDKLENELANKESLHRQC------EEKARHLQELLEVAEQKLQQTMRKAETLPEVEAEL-------------------A 372
Cdd:TIGR02168  555 LNAAKKAIAFLKQNELGRVtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyllggvlvvddldnA 634

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  373 QRIAALTKAEER-----------HG---------------------NIEEHLRQLEGQLEEKNQELARVR----QREKMN 416
Cdd:TIGR02168  635 LELAKKLRPGYRivtldgdlvrpGGvitggsaktnssilerrreieELEEKIEELEEKIAELEKALAELRkeleELEEEL 714

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  417 EDHNKRLSDTvDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQH-------HHKGRLSEEIEKLRQEVDQ 489
Cdd:TIGR02168  715 EQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEerleeaeEELAEAEAEIEELEAQIEQ 793


                   ....
gi 1474844183  490 LKGR 493
Cdd:TIGR02168  794 LKEE 797
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-385 2.91e-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: 51.99  E-value: 2.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   33 MLDEREKLLESLRESQETLAATQSrLQDALHERDQLQRHLN-SALPQEFATLTRELSMCREQLLEREEEISELKAERNNT 111
Cdd:TIGR02169  192 IIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYELLKEkEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  112 RLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSLFEHHKALDEKVR---ERLRAALERVTTLEEQLA 187
Cdd:TIGR02169  271 EQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEKERELEDAEERLAkleAEIDKLLAEIEELEREIE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  188 GAHQQVSALQqgavvrDGVAEEEGTVELGPKRLWKDDTgrveELQELLEkqnfELSQARERLVTLTatvTELEEDLGTAR 267
Cdd:TIGR02169  347 EERKRRDKLT------EEYAELKEELEDLRAELEEVDK----EFAETRD----ELKDYREKLEKLK---REINELKRELD 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  268 RDLIKSEELSSKhQRDLREALAQKED----MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHL 343
Cdd:TIGR02169  410 RLQEELQRLSEE-LADLNAAIAGIEAkineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1474844183  344 QELLEVAEQKLQQTMRKAETLPEVEAELAQRI-------AALTKAEERH 385
Cdd:TIGR02169  489 QRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERY 537
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
376-493 2.95e-06

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 49.44  E-value: 2.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  376 AALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesNERLQLHLK---ERMA--ALE 450
Cdd:COG1842     16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreALE 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1474844183  451 EKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:COG1842     92 RKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 320-491 3.16e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.92  E-value: 3.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  320 DKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAetlpeveAELAQRIAALtkaEERHGNIEEHLRQLEGQL 399
Cdd:COG4942     30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-------RALEQELAAL---EAELAELEKEIAELRAEL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  400 EEKNQELA-RVRQREKMNED-------HNKRLSDTVDRLlsesnERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHH 471
Cdd:COG4942    100 EAQKEELAeLLRALYRLGRQpplalllSPEDFLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRAELEAERA 174

                          170       180
                   ....*....|....*....|
gi 1474844183  472 HKGRLSEEIEKLRQEVDQLK 491
Cdd:COG4942    175 ELEALLAELEEERAALEALK 194
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1062-1132 3.20e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 45.72  E-value: 3.20e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1474844183 1062 VLVWTNDQVVHWVQSIGLRDYAGNLQESGVHGALLALdeNFDHNTLAlvlQIPTQNTQARQVMEREFNNLL 1132
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
228-491 3.30e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 50.29  E-value: 3.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  228 VEELQELLEKQNFELSQARERLVTLTATVTELEEdlgtARRDLI-KSEELSSKhqrdLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1340     10 LEELEEKIEELREEIEELKEKRDELNEELKELAE----KRDELNaQVKELREE----AQELREKRDELNEKVKELKEERD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  307 AAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELlevaeQKLQQTMrkaETLPEVEAELAQRIAALTK-AEERh 385
Cdd:COG1340     82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL-----EWRQQTE---VLSPEEEKELVEKIKELEKeLEKA- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  386 gnieEHLRQLEGQLEEKNQELARVRQREkmnEDHNKRLSDTVDRLLSESNERLQLhLKERMAALEEKNTLIQELESSQRQ 465
Cdd:COG1340    153 ----KKALEKNEKLKELRAELKELRKEA---EEIHKKIKELAEEAQELHEEMIEL-YKEADELRKEADELHKEIVEAQEK 224

                          250       260
                   ....*....|....*....|....*.
gi 1474844183  466 IEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG1340    225 ADELHEEIIELQKELRELRKELKKLR 250
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 30-415 4.44e-06

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: 50.45  E-value: 4.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   30 MVNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNS------ALPQEFATLTRELSmcreqllereeeisE 103
Cdd:pfam19220   15 MADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQeraaygKLRRELAGLTRRLS--------------A 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  104 LKAERNNTRLLLEHLECLVSRHER---SLRMTVVKRQAQSPS---GVSSEVEVLKALKslfEHHKALdekvRERLRAALE 177
Cdd:pfam19220   81 AEGELEELVARLAKLEAALREAEAakeELRIELRDKTAQAEAlerQLAAETEQNRALE---EENKAL----REEAQAAEK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  178 RVTTLEEQLAGAHQqvsalqqgavvRDGVAEEEGTVelgpkrlwkddtgrveeLQELLEKQNFELSQarerlvtLTATVT 257
Cdd:pfam19220  154 ALQRAEGELATARE-----------RLALLEQENRR-----------------LQALSEEQAAELAE-------LTRRLA 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  258 ELEEDLGTARRDLIKSE----ELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLH 333
Cdd:pfam19220  199 ELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAI 278

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  334 RQCEEKARH--------------LQELLEVAEQKLQQTMRKAETLPEVEAELAQRIA----ALTKAEERHGNIEEHLRQL 395
Cdd:pfam19220  279 RAAERRLKEasierdtlerrlagLEADLERRTQQFQEMQRARAELEERAEMLTKALAakdaALERAEERIASLSDRIAEL 358

                          410       420
                   ....*....|....*....|....*..
gi 1474844183  396 EGQ-------LEEKNQELARVRQREKM 415
Cdd:pfam19220  359 TKRfeveraaLEQANRRLKEELQRERA 385
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 230-491 5.45e-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: 51.13  E-value: 5.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  230 ELQELLEKQNFELSQARERLVTLTATVTELEEDLgtarrdliKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQ 309
Cdd:pfam02463  166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQE--------LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEE 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  310 REATSIHDLNDK------------LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIaa 377
Cdd:pfam02463  238 RIDLLQELLRDEqeeiesskqeieKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK-- 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  378 LTKAEERHGNIEEHLRQLEGQLEEKNQELARV-RQREKMNE---------DHNKRLSDTVDRLLSESNERLQLHLKERMA 447
Cdd:pfam02463  316 LKESEKEKKKAEKELKKEKEEIEELEKELKELeIKREAEEEeeeeleklqEKLEQLEEELLAKKKLESERLSSAAKLKEE 395

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1474844183  448 ALEEKNTLIQE------LESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam02463  396 ELELKSEEEKEaqllleLARQLEDLLKEEKKEELEILEEEEESIELKQGK 445
PTZ00121 PTZ00121
MAEBL; Provisional
 135-486 5.52e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 5.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  135 KRQAQSPSGVSSEVEVLKALKSLFEHHKALDE--KVRERLRAALERVTTLEEQLAGAHQQVSALQQGAVVRDGVAEEEGT 212
Cdd:PTZ00121  1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK 1496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  213 VELGPKRLWKDDTGRVEELQELLEKQNF-ELSQARERLvtlTATVTELEEDLGTARrDLIKSEELssKHQRDLREALAQK 291
Cdd:PTZ00121  1497 KKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAK---KADEAKKAEEKKKAD-ELKKAEEL--KKAEEKKKAEEAK 1570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  292 EDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAETLPEVEAEL 371
Cdd:PTZ00121  1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK-----KKVEQLKKKEAEE 1645

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  372 AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesnERLQLHLKERMAALEE 451
Cdd:PTZ00121  1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA-----EELKKKEAEEKKKAEE 1720

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1474844183  452 kntLIQELESSQRQIEEQHHHKGRLSEEIEKLRQE 486
Cdd:PTZ00121  1721 ---LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
PTZ00121 PTZ00121
MAEBL; Provisional
 153-493 5.52e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 5.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  153 ALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAVVRDGVAEEEGTVELGPKRLwKDDTGRVEELQ 232
Cdd:PTZ00121  1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA-EEDKKKADELK 1411

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  233 ELLE--KQNFELSQARERlvtlTATVTELEEDLGTARrdliKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQR 310
Cdd:PTZ00121  1412 KAAAakKKADEAKKKAEE----KKKADEAKKKAEEAK----KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  311 EAtsiHDLNDKLENELANKESLHRQCEEKARhlQELLEVAEQKlqqtmRKAETLPEveAELAQRIAALTKAEERHGniEE 390
Cdd:PTZ00121  1484 KA---DEAKKKAEEAKKKADEAKKAAEAKKK--ADEAKKAEEA-----KKADEAKK--AEEAKKADEAKKAEEKKK--AD 1549

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  391 HLRQLEGQleEKNQELARVRQREKMNEDHNKRLsdtvdRLLSESNERLQLHLKERMAALEEKntliQELESSQRQIEEQH 470
Cdd:PTZ00121  1550 ELKKAEEL--KKAEEKKKAEEAKKAEEDKNMAL-----RKAEEAKKAEEARIEEVMKLYEEE----KKMKAEEAKKAEEA 1618

                          330       340
                   ....*....|....*....|...
gi 1474844183  471 HHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PTZ00121  1619 KIKAEELKKAEEEKKKVEQLKKK 1641
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 218-491 6.85e-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: 50.40  E-value: 6.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  218 KRLWKDDTGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLgtarrDLIKSEELSSKHQR-DLREALAQKEDMEE 296
Cdd:TIGR04523  137 KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK-----LNIQKNIDKIKNKLlKLELLLSNLKKKIQ 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  297 RITTLEKRYLAAQREATSIHD----LNDKL---ENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLP---- 365
Cdd:TIGR04523  212 KNKSLESQISELKKQNNQLKDniekKQQEInekTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEkqln 291

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  366 EVEAELA----QRIAALTKA-EERHGNIEEHLRQLEGQLEEKNQELARVRQ------REKMNEDHNKRlsdTVDRLLSES 434
Cdd:TIGR04523  292 QLKSEISdlnnQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEqisqlkKELTNSESENS---EKQRELEEK 368

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1474844183  435 NERLQLHLKERMAALEEKNTL---IQELESS-----------QRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR04523  369 QNEIEKLKKENQSYKQEIKNLesqINDLESKiqnqeklnqqkDEQIKKLQQEKELLEKEIERLKETIIKNN 439
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1062-1133 8.01e-06

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: 44.59  E-value: 8.01e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474844183  1062 VLVWTNDQVVHWVQSIGLRDYAGNLQESGVHGALLALDENFDHntlalVLQIPTQNTQARQVMEREFNNLLA 1133
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEED-----LKELGITKLGHRKKILKAIQKLKE 67
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 227-486 8.36e-06

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 49.42  E-value: 8.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  227 RVEELQELLEKQNFELSQARERLVTLTATVTELEEDLgtarRDLIKSEE-LSSKHQRDLREALAQKEDMEerITTLEKRY 305
Cdd:pfam15905   95 RLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL----LELTRVNElLKAKFSEDGTQKKMSSLSME--LMKLRNKL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  306 LAAQREATsihDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTmrKAETLpeveaELAQRIAALTKAEERH 385
Cdd:pfam15905  169 EAKMKEVM---AKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEE--KSETE-----KLLEYITELSCVSEQV 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  386 GNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHnkrLSDTVDRLlsesNERLQL--HLKERMAALEE--KNTLIQELES 461
Cdd:pfam15905  239 EKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQE---LSKQIKDL----NEKCKLleSEKEELLREYEekEQTLNAELEE 311

                          250       260
                   ....*....|....*....|....*
gi 1474844183  462 SQRQIEEQhhhkgrlSEEIEKLRQE 486
Cdd:pfam15905  312 LKEKLTLE-------EQEHQKLQQK 329
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 283-493 9.47e-06

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 49.69  E-value: 9.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMR--- 359
Cdd:pfam05622    1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRlet 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  360 -------KAETLPEVEAELAQRIAALTKAeerhgniEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVD---- 428
Cdd:pfam05622   81 arddyriKCEELEKEVLELQHRNEELTSL-------AEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDlrrq 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1474844183  429 -RLLSESNerlqLHLKERMAALEEK----NTLIQELESSQRQIEEQHHhkgRLSEEI---EKLRQEVDQLKGR 493
Cdd:pfam05622  154 vKLLEERN----AEYMQRTLQLEEElkkaNALRGQLETYKRQVQELHG---KLSEESkkaDKLEFEYKKLEEK 219
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 984-1035 9.76e-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: 9.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1474844183  984 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1035
Cdd:cd09487      4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 136-490 1.08e-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: 49.79  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  136 RQAQSPSGVSSEVEVLKALKSLFEHHKAL----------DEKVRERLRAALERV----TTLEEQLAGAHQQVSALQ---- 197
Cdd:pfam01576  160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMisdleerlkkEEKGRQELEKAKRKLegesTDLQEQIAELQAQIAELRaqla 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  198 ------QGAVVRdgvAEEEGTVELGPKRLWKDDTGRVEELQELLEKQNFELSQA----RERLVTLTATVTELEEDLGTAR 267
Cdd:pfam01576  240 kkeeelQAALAR---LEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAekqrRDLGEELEALKTELEDTLDTTA 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  268 rdliKSEELSSKHQRDLREAlaqKEDMEERITTLEKRYLA-AQREATSIHDLNDKLENELANKESLHRQ---CEEKARHL 343
Cdd:pfam01576  317 ----AQQELRSKREQEVTEL---KKALEEETRSHEAQLQEmRQKHTQALEELTEQLEQAKRNKANLEKAkqaLESENAEL 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  344 QELLEV--------------AEQKLQQTMRKAETLPEVEAELAQRIA-----------ALTKAEERHGNIEEHLRQLEGQ 398
Cdd:pfam01576  390 QAELRTlqqakqdsehkrkkLEGQLQELQARLSESERQRAELAEKLSklqselesvssLLNEAEGKNIKLSKDVSSLESQ 469

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  399 L--------EEKNQELA---RVRQ--------REKMNEDHNKRLS-----DTVDRLLSESNERLQLHLKERMAALEEKNT 454
Cdd:pfam01576  470 LqdtqellqEETRQKLNlstRLRQledernslQEQLEEEEEAKRNverqlSTLQAQLSDMKKKLEEDAGTLEALEEGKKR 549

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1474844183  455 LIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQL 490
Cdd:pfam01576  550 LQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDL 585
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 229-486 1.29e-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: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  229 EELQELLEKQNFELSQARERLVTLTATVTELEedlgtarRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAA 308
Cdd:TIGR04523  366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLE-------SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  309 QREatsIHDLNDK---LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMR-------KAETLPEVEAELAQRIAAL 378
Cdd:TIGR04523  439 NSE---IKDLTNQdsvKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKelkskekELKKLNEEKKELEEKVKDL 515

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  379 TKaeeRHGNIEEHLRQLEGQLEEKNQELARV-RQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQ 457
Cdd:TIGR04523  516 TK---KISSLKEKIEKLESEKKEKESKISDLeDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1474844183  458 ELESSQ----RQIEEQHHHKGRLSEEIEKLRQE 486
Cdd:TIGR04523  593 QKEKEKkdliKEIEEKEKKISSLEKELEKAKKE 625
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 227-493 1.30e-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: 49.44  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  227 RVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTarrdlikseelsskhqrdLREALAQKEDMEERITtlEKRYL 306
Cdd:pfam10174  402 KIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTT------------------LEEALSEKERIIERLK--EQRER 461

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  307 AAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH- 385
Cdd:pfam10174  462 EDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLk 541

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  386 ----------GNIE--EHLRQLEGQLEEKNQELAR-----------VRQREKMNEDHNKRLSDTVDRLLSESNERLQLHL 442
Cdd:pfam10174  542 kahnaeeavrTNPEinDRIRLLEQEVARYKEESGKaqaeverllgiLREVENEKNDKDKKIAELESLTLRQMKEQNKKVA 621

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1474844183  443 KERMAALEEKNTLIQELESSQRQIEE-----QHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:pfam10174  622 NIKHGQQEMKKKGAQLLEEARRREDNladnsQQLQLEELMGALEKTRQELDATKAR 677
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 33-490 1.31e-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: 49.44  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   33 MLDEREKLLESLRESQETLAATQSRLQDALherDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAERNNTR 112
Cdd:pfam10174  360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDML---DVKERKIN-VLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTD 435

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  113 LLLEHLECLVSRHERslrmtvvkrqaqspsgvsseveVLKALKslfeHHKALDEKVRerlraaLERVTTLEEQLAGAHQQ 192
Cdd:pfam10174  436 TALTTLEEALSEKER----------------------IIERLK----EQREREDRER------LEELESLKKENKDLKEK 483

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  193 VSALQQGAVVRDGVAEE--EGTVELGPKRLWKDDT-----GRVEELQELLEKQNFELSQARERLVTLTATvTELEEDLGT 265
Cdd:pfam10174  484 VSALQPELTEKESSLIDlkEHASSLASSGLKKDSKlksleIAVEQKKEECSKLENQLKKAHNAEEAVRTN-PEINDRIRL 562

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  266 ARRDLIKSEELSSKHQRD-------LREALAQKEDMEERITTLEKRYLAAQREATSihdlndklenELANKEslHRQCEE 338
Cdd:pfam10174  563 LEQEVARYKEESGKAQAEverllgiLREVENEKNDKDKKIAELESLTLRQMKEQNK----------KVANIK--HGQQEM 630

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  339 KARHLQELLEVAEQKlqqtmrKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ-REKMNE 417
Cdd:pfam10174  631 KKKGAQLLEEARRRE------DNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAeRRKQLE 704

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1474844183  418 dhnkrlsdtvdrllsesnERLQLHLKERMAALEEKNTLIQELESSQRQieeqhhhKGRLSEEIEKLRQEVDQL 490
Cdd:pfam10174  705 ------------------EILEMKQEALLAAISEKDANIALLELSSSK-------KKKTQEEVMALKREKDRL 752
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 115-478 1.34e-05

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: 49.66  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  115 LEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEV-------------LKALKSLFEHHKALDEKVRERLRAA---LER 178
Cdd:TIGR00606  711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIpelrnklqkvnrdIQRLKNDIEEQETLLGTIMPEEESAkvcLTD 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  179 VTTLEEQLAGAHQQVSALQQGAVVRDGVAEEEGTVELGPKRLWKDD-----TGRVEELQELLEKQNFELSQARERLVTLT 253
Cdd:TIGR00606  791 VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHeldtvVSKIELNRKLIQDQQEQIQHLKSKTNELK 870

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  254 ATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELankESLH 333
Cdd:TIGR00606  871 SEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKV---NDIK 947

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  334 RQCEEKARHLQELlevaEQKLQQTmrKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQE-------L 406
Cdd:TIGR00606  948 EKVKNIHGYMKDI----ENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQerwlqdnL 1021

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474844183  407 ARVRQREKMNEdhnkrLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELES----SQRQIEEQ-HHHKGRLSE 478
Cdd:TIGR00606 1022 TLRKRENELKE-----VEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVlalgRQKGYEKEiKHFKKELRE 1093
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 228-493 1.41e-05

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: 49.08  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  228 VEELQELLEKQNFelSQARERLVTLTATVTELEEDLGTARR---DLIKSEELSSKHQRDLREalaqkedmeeRITTLEKR 304
Cdd:pfam06160   69 LFEAEELNDKYRF--KKAKKALDEIEELLDDIEEDIKQILEeldELLESEEKNREEVEELKD----------KYRELRKT 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  305 YLAaQREA--TSIhdlnDKLENELANKESLHRQCEE--------KARHLQELLEVAEQKLQQTMRK--------AETLPE 366
Cdd:pfam06160  137 LLA-NRFSygPAI----DELEKQLAEIEEEFSQFEEltesgdylEAREVLEKLEEETDALEELMEDipplyeelKTELPD 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  367 VEAELAQRIAALTKAEER--HGNIEEHLRQLEGQLEE-----KNQELARVrqrEKMNEDHNKRLSDTVDRLLSESNERLQ 439
Cdd:pfam06160  212 QLEELKEGYREMEEEGYAleHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKY 288

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474844183  440 LH-----LKERMAALEEKNTLIQ-ELES-SQRQI---EEQHHHKGrLSEEIEKLRQEVDQLKGR 493
Cdd:pfam06160  289 VEknlpeIEDYLEHAEEQNKELKeELERvQQSYTlneNELERVRG-LEKQLEELEKRYDEIVER 351
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 178-487 1.49e-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: 49.12  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  178 RVTTLEEQLAGAHQQVSALQQGAVVRDGVAEEEGTVELGPKRLWKddtGRVEELQELLEKQNFELSQARERLVTLTATVT 257
Cdd:pfam07888   28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE---RQRRELESRVAELKEELRQSREKHEELEEKYK 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  258 ELEEDLGTARRDLIKSEELSSKHQRDLREalaqkedMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHR--- 334
Cdd:pfam07888  105 ELSASSEELSEEKDALLAQRAAHEARIRE-------LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKqlq 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  335 ----QCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLegqleeknQELARVR 410
Cdd:pfam07888  178 aklqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSL--------QERLNAS 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  411 QR--EKMNEDhnkrLSDTV---DRLLSESNE-RLQ-----LHLKE-RMAALEEKNTLIQELESSQRQIEEQHHHKGRLSE 478
Cdd:pfam07888  250 ERkvEGLGEE----LSSMAaqrDRTQAELHQaRLQaaqltLQLADaSLALREGRARWAQERETLQQSAEADKDRIEKLSA 325


                   ....*....
gi 1474844183  479 EIEKLRQEV 487
Cdd:pfam07888  326 ELQRLEERL 334
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 320-463 1.65e-05

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: 47.37  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  320 DKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 388
Cdd:pfam04012   39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474844183  389 EEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQ 463
Cdd:pfam04012  117 RKQLAALETKIQQLKAKKNLLKARLKAAK-AQEAVQTSLGSLSTSSATDSFERIEEKIEEREARADAAAELASAV 190
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 232-482 2.14e-05

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: 48.97  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  232 QELLEKQNFE-LSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDL--REALAQKEDMEERITTLEK-RYLA 307
Cdd:pfam17380  290 QEKFEKMEQErLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAmeRERELERIRQEERKRELERiRQEE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  308 AQREATSIHDLnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRiaaltkaeerhgn 387
Cdd:pfam17380  370 IAMEISRMREL-ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR------------- 435

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  388 ieeHLRQLEgqlEEKNQELARVRQREKMNEDHNKRLsdtvdRLLSESNERLQLHL---KERMAALEEKNTLI--QELESS 462
Cdd:pfam17380  436 ---EVRRLE---EERAREMERVRLEEQERQQQVERL-----RQQEEERKRKKLELekeKRDRKRAEEQRRKIleKELEER 504

                          250       260
                   ....*....|....*....|
gi 1474844183  463 QRQIEEQHHHKGRLSEEIEK 482
Cdd:pfam17380  505 KQAMIEEERKRKLLEKEMEE 524
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 166-485 2.20e-05

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: 49.18  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  166 EKVRERLRAALERVTTLEEQLAGAHQ-----QVSALQ-QGAVVRDGVAEEE-GTVELGPKRLwkddTGRVEELQELLEKQ 238
Cdd:COG3096    378 AEAEARLEAAEEEVDSLKSQLADYQQaldvqQTRAIQyQQAVQALEKARALcGLPDLTPENA----EDYLAAFRAKEQQA 453

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  239 NFELSQARERLVTLTATVTELEEDLGTARRdlIKSE-ELSSKHQRdLREALAQKEdmeerittlEKRYLAAQREAtsihd 317
Cdd:COG3096    454 TEEVLELEQKLSVADAARRQFEKAYELVCK--IAGEvERSQAWQT-ARELLRRYR---------SQQALAQRLQQ----- 516

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  318 lndkLENELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEG 397
Cdd:COG3096    517 ----LRAQLAELE----QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  398 QLEEKNQELarvRQREKMNEDHNKRLSdtvdRLLSESNERLQlHLKERMAALEEKNTLIQELESSQRQIEEQhhhKGRLS 477
Cdd:COG3096    589 QLRARIKEL---AARAPAWLAAQDALE----RLREQSGEALA-DSQEVTAAMQQLLEREREATVERDELAAR---KQALE 657


                   ....*...
gi 1474844183  478 EEIEKLRQ 485
Cdd:COG3096    658 SQIERLSQ 665
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 227-490 2.57e-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: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  227 RVEELQELLEKQNFELSQARERLVTLTATVTELEEDLgtARRDLIKSEELSSKHQRDLREA----LAQKEDMEERITTLE 302
Cdd:COG5185    276 SSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATE--SLEEQLAAAEAEQELEESKRETetgiQNLTAEIEQGQESLT 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  303 KRYLAAQREATSIHDLND------KLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlpeveaelaqria 376
Cdd:COG5185    354 ENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD-------------- 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  377 alTKAEERHGNIEEHLRQLEgQLEEKNQELAR--VRQREKMNEDHNKRLSDTVDRLLSEsnerlqlhLKERMAALEEKNT 454
Cdd:COG5185    420 --RQIEELQRQIEQATSSNE-EVSKLLNELISelNKVMREADEESQSRLEEAYDEINRS--------VRSKKEDLNEELT 488

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1474844183  455 LIQELESSQRQIEEQhhHKGRLSEEIEKLRQEVDQL 490
Cdd:COG5185    489 QIESRVSTLKATLEK--LRAKLERQLEGVRSKLDQV 522
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 274-491 2.67e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.48  E-value: 2.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  274 EELSSKHQRDLREALAQKE---DMEERITTLEKRY--LAAQREA--TSIHDLNDKLENELANKESLHRQCEEKArhlQEL 346
Cdd:TIGR04523  422 ELLEKEIERLKETIIKNNSeikDLTNQDSVKELIIknLDNTRESleTQLKVLSRSINKIKQNLEQKQKELKSKE---KEL 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  347 LEVAEQKlQQTMRKAETLPEVEAELAQRIAALTKAEERhgnIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNK--RLS 424
Cdd:TIGR04523  499 KKLNEEK-KELEEKVKDLTKKISSLKEKIEKLESEKKE---KESKISDLEDELNKDDFELKKENLEKEIDEKNKEieELK 574

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  425 DTVDRLLSeSNERLQLHLKERMA-------ALEEKNTLIQELESSQRQIEEQHHhkgRLSEEI-------EKLRQEVDQL 490
Cdd:TIGR04523  575 QTQKSLKK-KQEEKQELIDQKEKekkdlikEIEEKEKKISSLEKELEKAKKENE---KLSSIIknikskkNKLKQEVKQI 650


                   .
gi 1474844183  491 K 491
Cdd:TIGR04523  651 K 651
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
164-412 3.32e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 3.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  164 LDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQgAVVRdgVAEEEGTVELGPKRlwKDDTGRVEELQEllekqnfELS 243
Cdd:COG3206    162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEA-ALEE--FRQKNGLVDLSEEA--KLLLQQLSELES-------QLA 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  244 QARERLVTLTATVTELEEDLGTARRDLikSEELSSKHQRDLREALAQkedMEERITTLEKRYLAAQREATSihdlndkLE 323
Cdd:COG3206    230 EARAELAEAEARLAALRAQLGSGPDAL--PELLQSPVIQQLRAQLAE---LEAELAELSARYTPNHPDVIA-------LR 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  324 NELANKEslhrqceekarhlQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKN 403
Cdd:COG3206    298 AQIAALR-------------AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAR 364


                   ....*....
gi 1474844183  404 QELARVRQR 412
Cdd:COG3206    365 ELYESLLQR 373
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
318-493 5.18e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 5.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  318 LNDKLENElanKESLHRQCEEKARHLQELLEVAEQKLQQtmrkaetLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEG 397
Cdd:COG4717     47 LLERLEKE---ADELFKPQGRKPELNLKELKELEEELKE-------AEEKEEEYAELQEELEELEEELEELEAELEELRE 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  398 QLEEKNQELARVRQREKMnEDHNKRLSDTVDRLlsesnERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ-------- 469
Cdd:COG4717    117 ELEKLEKLLQLLPLYQEL-EALEAELAELPERL-----EELEERLEELRELEEELEELEAELAELQEELEELleqlslat 190

                          170       180
                   ....*....|....*....|....
gi 1474844183  470 HHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:COG4717    191 EEELQDLAEELEELQQRLAELEEE 214
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
154-491 5.20e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 5.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQgavvrdgvaeeegtvelgpkrlwkddtgRVEELQE 233
Cdd:COG4372     15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE----------------------------ELEQLEE 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  234 LLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREAT 313
Cdd:COG4372     67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  314 SIHDLNDKLENELANKESLHRQCEEKARHL--QELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEH 391
Cdd:COG4372    147 EREEELKELEEQLESLQEELAALEQELQALseAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  392 LRqLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHH 471
Cdd:COG4372    227 LE-AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305

                          330       340
                   ....*....|....*....|
gi 1474844183  472 HKGRLSEEIEKLRQEVDQLK 491
Cdd:COG4372    306 ALSLIGALEDALLAALLELA 325
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 169-493 5.97e-05

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: 47.64  E-value: 5.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAV-VRDGVAEeegtvelgpkrlwkddtgrVEELQELLEKqnfELSQARE 247
Cdd:COG3096    277 ANERRELSERALELRRELFGARRQLAEEQYRLVeMARELEE-------------------LSARESDLEQ---DYQAASD 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  248 RLvTLTATVTELEEDLGTARRDLiksEELSSKhqrdLREALAQKEDMEERITTLEKRYLAAQREAtsihdlnDKLENELA 327
Cdd:COG3096    335 HL-NLVQTALRQQEKIERYQEDL---EELTER----LEEQEEVVEEAAEQLAEAEARLEAAEEEV-------DSLKSQLA 399

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  328 NK----ESLHR---------QCEEKARHLQEL----LEVAEQKLQQTMRKAETLPEVEAELAQR---------------- 374
Cdd:COG3096    400 DYqqalDVQQTraiqyqqavQALEKARALCGLpdltPENAEDYLAAFRAKEQQATEEVLELEQKlsvadaarrqfekaye 479

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  375 ----IAALTKAEERHGNIEEHLRQ------LEGQLEEKNQELARVRQREKMNEDhnkrlsdtVDRLLSESNERLQLHLKE 444
Cdd:COG3096    480 lvckIAGEVERSQAWQTARELLRRyrsqqaLAQRLQQLRAQLAELEQRLRQQQN--------AERLLEEFCQRIGQQLDA 551

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1474844183  445 RMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:COG3096    552 AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR 600
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 233-490 6.21e-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: 47.32  E-value: 6.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  233 ELLEKQ----NFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEK----- 303
Cdd:TIGR04523   78 KILEQQikdlNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKelekl 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  304 --RYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQ--------------QTMRKAETLPEV 367
Cdd:TIGR04523  158 nnKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQknkslesqiselkkQNNQLKDNIEKK 237

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  368 EAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELarvRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMA 447
Cdd:TIGR04523  238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL---EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS 314

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1474844183  448 ALEEKNTLIQELESSQRQIEEQhhhKGRLSEEIEKLRQEVDQL 490
Cdd:TIGR04523  315 ELKNQEKKLEEIQNQISQNNKI---ISQLNEQISQLKKELTNS 354
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 151-493 1.21e-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: 46.50  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  151 LKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAVVRDGVAEEEGTVElgpkRLWKDDTGRVEE 230
Cdd:TIGR00618  196 AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQ----QLLKQLRARIEE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  231 LQEL---LEKQNFELSQAR--ERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKry 305
Cdd:TIGR00618  272 LRAQeavLEETQERINRARkaAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT-- 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  306 laAQREATSIHDLNDKLENELANKESLHRQcEEKARHLQELLEVAEQKLQQTMRKAETLPE----VEAELAQRIAALTKA 381
Cdd:TIGR00618  350 --LHSQEIHIRDAHEVATSIREISCQQHTL-TQHIHTLQQQKTTLTQKLQSLCKELDILQReqatIDTRTSAFRDLQGQL 426

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  382 EERHGNIEEHLRQLEGQ----------LEEKNQELARVRQR---EKMNEDHNKRLSDTVDRLLSESNERLQLH------L 442
Cdd:TIGR00618  427 AHAKKQQELQQRYAELCaaaitctaqcEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKAVVLARLLELqeepcpL 506

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1474844183  443 KERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR00618  507 CGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ 557
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 164-492 1.22e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 46.32  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  164 LDEKVRERLRAALERVTT------LEEQLAGAHQQVSALQQG--------AVVRDGVAEEEGTVELGPK----------- 218
Cdd:pfam01576  112 LDEEEAARQKLQLEKVTTeakikkLEEDILLLEDQNSKLSKErklleeriSEFTSNLAEEEEKAKSLSKlknkheamisd 191

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  219 ---RLWKDDTGRvEELQELLEKQNFELSQARERLVTLTATVTELeedlgtaRRDLIKSEElsskhqrDLREALAQKEDME 295
Cdd:pfam01576  192 leeRLKKEEKGR-QELEKAKRKLEGESTDLQEQIAELQAQIAEL-------RAQLAKKEE-------ELQAALARLEEET 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  296 ERITTLEKRYlaaqREATS-IHDLNDKLENELANKESLHRQCeekaRHLQELLEVAEQKLQQTMRKAETLPEVEAELAQR 374
Cdd:pfam01576  257 AQKNNALKKI----RELEAqISELQEDLESERAARNKAEKQR----RDLGEELEALKTELEDTLDTTAAQQELRSKREQE 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  375 IAALTKAEERHGNIEE----HLRQLEGQ-LEEKNQELARVRqREKMNEDHNKRlsdtvdRLLSESNErLQLHLKERMAAL 449
Cdd:pfam01576  329 VTELKKALEEETRSHEaqlqEMRQKHTQaLEELTEQLEQAK-RNKANLEKAKQ------ALESENAE-LQAELRTLQQAK 400

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1474844183  450 EE----KNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKG 492
Cdd:pfam01576  401 QDsehkRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSS 447
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 313-423 1.22e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 46.36  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  313 TSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGN 387
Cdd:PRK00409   509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1474844183  388 IEEHLRQLE--GQLEEKNQELARVRQR-EKMNEDHNKRL 423
Cdd:PRK00409   589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 347-589 1.70e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  347 LEVAEQKLQQTMRKAETlpeVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHNKRL-- 423
Cdd:COG3883     18 IQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERAra 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  424 --------------------SDTVDRL-----LSESNERLQLHLKERMAALEE-KNTLIQELESSQRQIEEQHHHKGRLS 477
Cdd:COG3883     95 lyrsggsvsyldvllgsesfSDFLDRLsalskIADADADLLEELKADKAELEAkKAELEAKLAELEALKAELEAAKAELE 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  478 EEIEKLRQEVDQLKGRGGPFVDGIHSRSHMGSAADVRFSLSTTTHAPPGlhRRYSALREDSAKDWEPSPLPGLLASTATP 557
Cdd:COG3883    175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA--AAAAAAAAAAAAAAAAAAAAASAAGAGAA 252

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1474844183  558 AFDSDPEISDVDEDEPGGLVGSVDVVSPGGHS 589
Cdd:COG3883    253 GAAGAAAGSAGAAGAAAGAAGAGAAAASAAGG 284
Caldesmon pfam02029
Caldesmon;
169-486 1.79e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 45.63  E-value: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAVVRDGVAEEEGTVELGPKRLWKDDTGRVEE-----LQELLEKQ-NFEL 242
Cdd:pfam02029   12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREErrqkrLQEALERQkEFDP 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  243 SQARERL-VTLTATVTELEEDLGTARRDLIKSEELSSK-----------HQRDLREALAQ---KEDMEERITTLEKRYLA 307
Cdd:pfam02029   92 TIADEKEsVAERKENNEEEENSSWEKEEKRDSRLGRYKeeeteirekeyQENKWSTEVRQaeeEGEEEEDKSEEAEEVPT 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  308 AQREATSIHDLNDKLENELA--NKESLHRQ---CEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 382
Cdd:pfam02029  172 ENFAKEEVKDEKIKKEKKVKyeSKVFLDQKrghPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLE 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  383 ErhgnieehLRQLEGQLEEKNQELARVRQREKMNE-DHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKntliqeles 461
Cdd:pfam02029  252 E--------LRRRRQEKESEEFEKLRQKQQEAELElEELKKKREERRKLLEEEEQRRKQEEAERKLREEEE--------- 314

                          330       340
                   ....*....|....*....|....*
gi 1474844183  462 sqrqieeqhhhKGRLSEEIEKLRQE 486
Cdd:pfam02029  315 -----------KRRMKEEIERRRAE 328
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 325-486 1.89e-04

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: 45.88  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  325 ELANKESLHRQCEEKARHLQELLEVAEQklqQTMRKAETlpeveaelaQRIAALTKAEERHGniEEHLRQLEG-QLEEKN 403
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREVERRRKLEEA---EKARQAEM---------DRQAAIYAEQERMA--MERERELERiRQEERK 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  404 QELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKermAALEEKntlIQElESSQRQIEEQHHHKGRLSEEIEKL 483
Cdd:pfam17380  360 RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELE---AARKVK---ILE-EERQRKIQQQKVEMEQIRAEQEEA 432


                   ...
gi 1474844183  484 RQE 486
Cdd:pfam17380  433 RQR 435
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 135-484 2.21e-04

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 45.52  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  135 KRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAVVRdgvAEEEGTv 213
Cdd:pfam09731   88 QVKIPRQSGVSSEVaEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQ---AVKAHT- 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  214 ELGPKRLWKDDTGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSeelsSKHQRDLREALAQKED 293
Cdd:pfam09731  164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPK----LPEHLDNVEEKVEKAQ 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  294 MEERITTLEKRYLAA-----QREATSIH-DLNDKL-ENELANKESLHRQCEekarHLQELLEVAEQKLQqTMRKAETLpE 366
Cdd:pfam09731  240 SLAKLVDQYKELVASerivfQQELVSIFpDIIPVLkEDNLLSNDDLNSLIA----HAHREIDQLSKKLA-ELKKREEK-H 313

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  367 VEAELAQRIAALTKAEER-HGNIEEHLRQLEGQLEEKNQElARVRQREKM-----------NEDHNKRLSDTVDRLLSES 434
Cdd:pfam09731  314 IERALEKQKEELDKLAEElSARLEEVRAADEAQLRLEFER-EREEIRESYeeklrtelerqAEAHEEHLKDVLVEQEIEL 392

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1474844183  435 NERLQLHLKERMAalEEKNTL---IQELESSQRQIEEQhhHKGRLSEEIEKLR 484
Cdd:pfam09731  393 QREFLQDIKEKVE--EERAGRllkLNELLANLKGLEKA--TSSHSEVEDENRK 441
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
160-412 2.22e-04

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 45.45  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  160 HHKALD-----EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGA-VVRDGVAEEEgtvELGPKrlwkddtgrVEELQE 233
Cdd:COG0497    143 QRELLDafaglEELLEEYREAYRAWRALKKELEELRADEAERARELdLLRFQLEELE---AAALQ---------PGEEEE 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  234 LLEKQNfELSQARERLVTLTATVTELEED-------LGTARRDLIK----SEELSSKHQRdLREALAQKEDMeerittle 302
Cdd:COG0497    211 LEEERR-RLSNAEKLREALQEALEALSGGeggaldlLGQALRALERlaeyDPSLAELAER-LESALIELEEA-------- 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  303 krylaaqreATSIHDLNDKLENElankeslhrqceekarhlQELLEVAEQKLQ---QTMRK----AETLPEVEAELAQRI 375
Cdd:COG0497    281 ---------ASELRRYLDSLEFD------------------PERLEEVEERLAllrRLARKygvtVEELLAYAEELRAEL 333

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1474844183  376 AALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG0497    334 AELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 229-413 2.91e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 2.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  229 EELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREAlaqKEDMEERITTLEKRYLAA 308
Cdd:COG3883     19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERARAL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  309 QR------------EATSIHDLNDKLEN----ELANKESLHRQCEEKAR--HLQELLEVAEQKLQQTMRKAET------- 363
Cdd:COG3883     96 YRsggsvsyldvllGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAakaelea 175

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1474844183  364 -LPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRE 413
Cdd:COG3883    176 qQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 338-493 3.13e-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: 43.59  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  338 EKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNE 417
Cdd:cd00176     40 KKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEELNQRWEELRELAEERRQRLEEALDLQQFFR 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  418 DH---NKRLSDTVDRLLSESN-------ERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGR--LSEEIEKLRQ 485
Cdd:cd00176    114 DAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeeIEEKLEELNE 193


                   ....*...
gi 1474844183  486 EVDQLKGR 493
Cdd:cd00176    194 RWEELLEL 201
mukB PRK04863
chromosome partition protein MukB;
28-497 3.25e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.33  E-value: 3.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   28 QLMVNMLDEREKLLESLRESQ-------ETLAATQSRL-QDALHERDQLQRHLNSALpqefaTLTRELSMCREQLLEREE 99
Cdd:PRK04863   233 QDMEAALRENRMTLEAIRVTQsdrdlfkHLITESTNYVaADYMRHANERRVHLEEAL-----ELRRELYTSRRQLAAEQY 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  100 EISELKAE---RNNTRLLLE--------HLECLvsrherslrMTVVKRQAQspsGVSSEVEVLKALKSLFEHHKALDE-- 166
Cdd:PRK04863   308 RLVEMARElaeLNEAESDLEqdyqaasdHLNLV---------QTALRQQEK---IERYQADLEELEERLEEQNEVVEEad 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  167 ----KVRERLRAALERVTTLEEQLAGAHQ-----QVSALQ-QGAVvrdgvaeeegtvelgpkrlwkddtGRVEELQELLE 236
Cdd:PRK04863   376 eqqeENEARAEAAEEEVDELKSQLADYQQaldvqQTRAIQyQQAV------------------------QALERAKQLCG 431

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  237 KQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLR---------EALAQKEDMEERITTLEK-RYL 306
Cdd:PRK04863   432 LPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvrkiagevSRSEAWDVARELLRRLREqRHL 511

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  307 AAQREAtsihdlndkLENELANKESLHRQceekARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHG 386
Cdd:PRK04863   512 AEQLQQ---------LRMRLSELEQRLRQ----QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  387 NIEEHLRQlegQLEEKNQELARVRQREkmnedhnkrlsdTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQI 466
Cdd:PRK04863   579 ERRMALRQ---QLEQLQARIQRLAARA------------PAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLEREREL 643

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1474844183  467 EEQhhhKGRLSEEIEKLRQEVDQLKGRGGPF 497
Cdd:PRK04863   644 TVE---RDELAARKQALDEEIERLSQPGGSE 671
mukB PRK04863
chromosome partition protein MukB;
37-490 3.31e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.33  E-value: 3.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   37 REKLLESlrESQETLAATQSRLQDALHE---RDQLQRHLNSAL----------PQEFATLTRELSMCREQLLEREEEISE 103
Cdd:PRK04863   499 RELLRRL--REQRHLAEQLQQLRMRLSEleqRLRQQQRAERLLaefckrlgknLDDEDELEQLQEELEARLESLSESVSE 576

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  104 LKAERNNTRLLLEHLECLVSRHE------RSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALdEKVRERLRAA-- 175
Cdd:PRK04863   577 ARERRMALRQQLEQLQARIQRLAarapawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLEREREL-TVERDELAARkq 655

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  176 ----------------LERVTTLEEQLAGA-----HQQV--------SALQQGA----VVRD--GVAE----EEGT---- 212
Cdd:PRK04863   656 aldeeierlsqpggseDPRLNALAERFGGVllseiYDDVsledapyfSALYGPArhaiVVPDlsDAAEqlagLEDCpedl 735

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  213 --VELGPKRLwkDDTG-RVEEL-----QELLEKQnFELSQ----------ARE-RLVTLTATVTELEEDLGTARRDLIKS 273
Cdd:PRK04863   736 ylIEGDPDSF--DDSVfSVEELekavvVKIADRQ-WRYSRfpevplfgraAREkRIEQLRAEREELAERYATLSFDVQKL 812

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  274 EELSSKHQRDLRE--ALAQKEDMEERIttlekRYLAAQREatsihdlndKLENELANKESLHRQCEEKARHLQELLEVAE 351
Cdd:PRK04863   813 QRLHQAFSRFIGShlAVAFEADPEAEL-----RQLNRRRV---------ELERALADHESQEQQQRSQLEQAKEGLSALN 878

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  352 QKLQQTMRKA-ETLPEVEAELAQRIAALTKAE---ERHGNieeHLRQLEGQ---LEEKNQELARVRQREKMNEDHNKRLS 424
Cdd:PRK04863   879 RLLPRLNLLAdETLADRVEEIREQLDEAEEAKrfvQQHGN---ALAQLEPIvsvLQSDPEQFEQLKQDYQQAQQTQRDAK 955

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474844183  425 DTVdRLLSESNERlQLHLKERMAA--LEEKNTLIQELESSQRQIEEQhhhkgrLSEEIEKLRQEVDQL 490
Cdd:PRK04863   956 QQA-FALTEVVQR-RAHFSYEDAAemLAKNSDLNEKLRQRLEQAEQE------RTRAREQLRQAQAQL 1015
PRK11281 PRK11281
mechanosensitive channel MscK;
286-466 3.40e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.90  E-value: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  286 EALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEnELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLP 365
Cdd:PRK11281    33 GDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALK 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  366 EVEA-ELAQRIAALTkaeerhgnieehLRQLEGQLEEKNQELARVRqrekmnedhnKRLSDTVDRLLSESN--ERLQLHL 442
Cdd:PRK11281   108 DDNDeETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQAAL 165

                          170       180
                   ....*....|....*....|....
gi 1474844183  443 KERMAALEEKNTLIQELESSQRQI 466
Cdd:PRK11281   166 YANSQRLQQIRNLLKGGKVGGKAL 189
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 172-360 3.41e-04

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: 42.97  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  172 LRAALERVTTLEEQLAGAHQQVSALQqgavvrdgvaEEEGTVelgpKRLWKDDT-------GRVEELQELLEKQNFELSQ 244
Cdd:pfam15619    6 LSARLHKIKELQNELAELQSKLEELR----------KENRLL----KRLQKRQEkalgkyeGTESELPQLIARHNEEVRV 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  245 ARERLVTLTATVTELEEDLGTARRDLIKSEElSSKHQRDLREA--LAQKEDMEERITTLEKRYLAAQREatsIHDLNDKL 322
Cdd:pfam15619   72 LRERLRRLQEKERDLERKLKEKEAELLRLRD-QLKRLEKLSEDknLAEREELQKKLEQLEAKLEDKDEK---IQDLERKL 147

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1474844183  323 EN-------ELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:pfam15619  148 ELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 226-493 4.05e-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: 45.04  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  226 GRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDL--IKSEELSSKhqrDLREALAQKEDMEERITTLEK 303
Cdd:TIGR00606  730 GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLgtIMPEEESAK---VCLTDVTIMERFQMELKDVER 806

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  304 RY--LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlpeveaELAQRIAALTKA 381
Cdd:TIGR00606  807 KIaqQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTN-------ELKSEKLQIGTN 879

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  382 EERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS---ESNERLQLHLKERMAALEEKNTLIQE 458
Cdd:TIGR00606  880 LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISskeTSNKKAQDKVNDIKEKVKNIHGYMKD 959

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1474844183  459 LESSQR-------------------QIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR00606  960 IENKIQdgkddylkqketelntvnaQLEECEKHQEKINEDMRLMRQDIDTQKIQ 1013
PLN02939 PLN02939
transferase, transferring glycosyl groups
 22-340 5.16e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 44.51  E-value: 5.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   22 ADANFEQLMvNMLDEREKllESLRESQETLAATQsRLQDALHERDQLQRHLNsalpqefaTLTRELSmcreqllEREEEI 101
Cdd:PLN02939   126 SDFQLEDLV-GMIQNAEK--NILLLNQARLQALE-DLEKILTEKEALQGKIN--------ILEMRLS-------ETDARI 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  102 SELKAERNNTRLLLEHLEclvsrherSLRMTVVKRQAQSPSGVSSEVEVLKALKslfEHHKALDEKVrERLRAALERVTT 181
Cdd:PLN02939   187 KLAAQEKIHVEILEEQLE--------KLRNELLIRGATEGLCVHSLSKELDVLK---EENMLLKDDI-QFLKAELIEVAE 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  182 LEEQLAGAHQQVSALQqgAVVRD----GVAEEEGTVELGPKR---LWKddtgRVEELQELLEKQNFELSQArerlvtltA 254
Cdd:PLN02939   255 TEERVFKLEKERSLLD--ASLREleskFIVAQEDVSKLSPLQydcWWE----KVENLQDLLDRATNQVEKA--------A 320

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  255 TVTELEEDLgtarRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQRE--------ATSIHDLNDKLENel 326
Cdd:PLN02939   321 LVLDQNQDL----RDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEihsyiqlyQESIKEFQDTLSK-- 394

                          330
                   ....*....|....
gi 1474844183  327 ANKESLHRQCEEKA 340
Cdd:PLN02939   395 LKEESKKRSLEHPA 408
PRK01156 PRK01156
chromosome segregation protein; Provisional
 31-450 5.56e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.12  E-value: 5.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   31 VNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQ-------------RHLNSALPQEFATLTRELSMCREQLLER 97
Cdd:PRK01156   321 INKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEgyemdynsylksiESLKKKIEEYSKNIERMSAFISEILKIQ 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   98 EEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkrqaqspSGVSSEVEVLKALKSLFEHHKAL-------DEKVRE 170
Cdd:PRK01156   401 EIDPDAIKKELNEINVKLQDISSKVSSLNQRIR-----------ALRENLDELSRNMEMLNGQSVCPvcgttlgEEKSNH 469

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  171 RLRAALERVTTLEEQLAGAHQQVSALQQGavVRDGVAEEEgtvelgpkRLWKDDTGRVEELQELLEKQNFELSQARERLV 250
Cdd:PRK01156   470 IINHYNEKKSRLEEKIREIEIEVKDIDEK--IVDLKKRKE--------YLESEEINKSINEYNKIESARADLEDIKIKIN 539

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  251 TLTATVTELE-----------EDLGTARRDLIKSeeLSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLN 319
Cdd:PRK01156   540 ELKDKHDKYEeiknrykslklEDLDSKRTSWLNA--LAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYI 617

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  320 D----KLENELANKESLHRQCEEKARHLQELLEvaeqklqqtmrKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQL 395
Cdd:PRK01156   618 DksirEIENEANNLNNKYNEIQENKILIEKLRG-----------KIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKS 686

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1474844183  396 EGQLEEKNQELARVRQREKMNEDHNKRLSDTVdrllSESNERLqlhlkERMAALE 450
Cdd:PRK01156   687 RKALDDAKANRARLESTIEILRTRINELSDRI----NDINETL-----ESMKKIK 732
DUF4472 pfam14739
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members ...
 231-326 5.59e-04

Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members also carry Kinesin-motor domains at their N-terminus, Kinesin, pfam00225.


Pssm-ID: 464291 [Multi-domain]  Cd Length: 107  Bit Score: 40.75  E-value: 5.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  231 LQELLEKQNFELSQareRLVTLTATVTELEEDLGTARRdlikseELSSKHQRdLREALAQKEDMEERITTLEKRYLAAQR 310
Cdd:pfam14739   22 LREQYEAEKFELKN---KLLNLENRVLELELRLEKAAE------EIQDLRER-LRELEDDRRELAEEFVALKKNYQALSK 91

                           90
                   ....*....|....*.
gi 1474844183  311 EATSIHDLNDKLENEL 326
Cdd:pfam14739   92 ELEAEVAKNQELSLEL 107
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 297-491 5.83e-04

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 43.06  E-value: 5.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  297 RITTLEKRYLAAQREATSIHDLNDKLENELANKESlhrqcEEKARHLQELLEVAEQKLQQTMRKAETL------------ 364
Cdd:pfam12795    1 KLDELEKAKLDEAAKKKLLQDLQQALSLLDKIDAS-----KQRAAAYQKALDDAPAELRELRQELAALqakaeaapkeil 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  365 -----PEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTvDRLLSESnerLQ 439
Cdd:pfam12795   76 aslslEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPP-GEPLSEA---QR 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474844183  440 LHLKERMAALEEK----------NTLIQELESSQRQIEEQHHHkgRLSEEIEKLRQEVDQLK 491
Cdd:pfam12795  152 WALQAELAALKAQidmleqellsNNNRQDLLKARRDLLTLRIQ--RLEQQLQALQELLNEKR 211
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 286-493 7.19e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.80  E-value: 7.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  286 EALAQKEDMEERITTLEKRY----LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQqtmrKA 361
Cdd:TIGR00618  184 MEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK----KQ 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  362 ETLPEVEAElaqriaaltkaeerhgniEEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDtVDRLLSESNERLQlh 441
Cdd:TIGR00618  260 QLLKQLRAR------------------IEELRAQEAVLEETQERINRARKAAPLAA-HIKAVTQ-IEQQAQRIHTELQ-- 317

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1474844183  442 lkERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR00618  318 --SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
31-305 7.40e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 7.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   31 VNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRhlnsalpqefatLTRELSMCREQLLEREEEISELKAERNN 110
Cdd:PRK02224   467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE------------AEDRIERLEERREDLEELIAERRETIEE 534

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  111 TRLLLEHLECLVSRHERSLRmtvVKRQAQSPSGVSSEvEVLKALKSLFEHHKALDEKvrerlRAALERVTTLEEQLAGAH 190
Cdd:PRK02224   535 KRERAEELRERAAELEAEAE---EKREAAAEAEEEAE-EAREEVAELNSKLAELKER-----IESLERIRTLLAAIADAE 605

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  191 QQVSALQQGavvRDGVAE--EEGTVELGPKRLWKD------DTGRVEELQEllEKQNFE--LSQARERLVTLTATVTELE 260
Cdd:PRK02224   606 DEIERLREK---REALAElnDERRERLAEKRERKReleaefDEARIEEARE--DKERAEeyLEQVEEKLDELREERDDLQ 680

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1474844183  261 EDLGTARRDLIKSEELsskhqRDLREALAQK----EDMEERITTLEKRY 305
Cdd:PRK02224   681 AEIGAVENELEELEEL-----RERREALENRvealEALYDEAEELESMY 724
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 851-909 7.46e-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: 39.24  E-value: 7.46e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474844183  851 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNALHRLKLRL 909
Cdd:cd09504      5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 247-406 7.52e-04

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 41.87  E-value: 7.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  247 ERLVTLTATVTELEEDLGTARRDLIkseELSSKHQRDLREALAQK-EDMEERITTlekrYLAAQRE--ATSIHDLNDKLE 323
Cdd:pfam01442    4 DSLDELSTYAEELQEQLGPVAQELV---DRLEKETEALRERLQKDlEEVRAKLEP----YLEELQAklGQNVEELRQRLE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  324 NELankESLHRQCEEKARHLQELLEVAEQKLQQTMRK---------AETLPEVEAELAQRIAAL-----TKAEERHGNIE 389
Cdd:pfam01442   77 PYT---EELRKRLNADAEELQEKLAPYGEELRERLEQnvdalrarlAPYAEELRQKLAERLEELkeslaPYAEEVQAQLS 153

                          170
                   ....*....|....*..
gi 1474844183  390 EHLRQLEGQLEEKNQEL 406
Cdd:pfam01442  154 QRLQELREKLEPQAEDL 170
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
388-491 7.61e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.69  E-value: 7.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  388 IEEHLRQLEGQLEEKNQELARVRQREK-MNEDHNKRLSDTVDRLLSEsNERLQLHLKERMAALEEkntLIQELESSQRQI 466
Cdd:COG2433    382 LEELIEKELPEEEPEAEREKEHEERELtEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---LERELSEARSEE 457

                           90       100
                   ....*....|....*....|....*
gi 1474844183  467 EEQHhhkgRLSEEIEKLRQEVDQLK 491
Cdd:COG2433    458 RREI----RKDREISRLDREIERLE 478
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 254-483 9.39e-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: 42.40  E-value: 9.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  254 ATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRylaAQREATSIHDLNDKLENELANKESLH 333
Cdd:pfam06008   12 PAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKK---ATQTLAKAQQVNAESERTLGHAKELA 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  334 RQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAltkaEERHGNIEEHLRQLEGQLEEKNQELARVRQRE 413
Cdd:pfam06008   89 EAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLG----EIRSRDFGTQLQNAEAELKAAQDLLSRIQTWF 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1474844183  414 KMNEDHNKRLSDTVDRLLSESNERLQ---LHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKL 483
Cdd:pfam06008  165 QSPQEENKALANALRDSLAEYEAKLSdlrELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
326-487 1.18e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 41.73  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  326 LANKESLHRQCEEKARHLQELLEVAEQKLQQT---------MRKAEtlpeVEAELAQRIAALTKAEERHGNIEEHLRQLE 396
Cdd:COG1842     50 IANQKRLERQLEELEAEAEKWEEKARLALEKGredlarealERKAE----LEAQAEALEAQLAQLEEQVEKLKEALRQLE 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  397 GQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQEL---ESSQRQIEEQhHHK 473
Cdd:COG1842    126 SKLEELKAKKDTLKARAKAAK-AQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEAAAELaagDSLDDELAEL-EAD 203

                          170
                   ....*....|....
gi 1474844183  474 GRLSEEIEKLRQEV 487
Cdd:COG1842    204 SEVEDELAALKAKM 217
COG5022 COG5022
Myosin heavy chain [General function prediction only];
219-492 1.42e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.14  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  219 RLWKDDTGRVEELQ--ELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKS--EELSSKHQRDLR-EALAQKED 293
Cdd:COG5022    862 SLLKKETIYLQSAQrvELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDliENLEFKTELIARlKKLLNNID 941

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  294 MEERIT---TLEKRYLAAQREATSIHDLNDKLENELANKESLHRQ----CEEKARHLQELLEVAEQKLQQTmRKAETLPE 366
Cdd:COG5022    942 LEEGPSieyVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREgnkaNSELKNFKKELAELSKQYGALQ-ESTKQLKE 1020

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  367 VEAELAQRIAALTKAEERHGN--IEEHLRQLEGQLEEKNQELarvrqREKMNEDHNKRLSDTVDRLLSESNERLQLHLKE 444
Cdd:COG5022   1021 LPVEVAELQSASKIISSESTElsILKPLQKLKGLLLLENNQL-----QARYKALKLRRENSLLDDKQLYQLESTENLLKT 1095

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1474844183  445 RMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEK-LRQEVDQLKG 492
Cdd:COG5022   1096 INVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKfLSQLVNTLEP 1144
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 168-326 1.62e-03

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


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 41.55  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  168 VRERLRAALERVTTLEEQLAGAHQQVSALQQGAVVRD--GVAEEEGTVELGP-----KRLWKDDTGRVEELQELLEKQNF 240
Cdd:pfam00261   48 LEEELERTEERLAEALEKLEEAEKAADESERGRKVLEnrALKDEEKMEILEAqlkeaKEIAEEADRKYEEVARKLVVVEG 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  241 ELSQARERLVTLTATVTELEEDLGTAR---RDLIKSEELSSKHQRDLREALaqkEDMEERITTLEKRYLAAQREATSIHD 317
Cdd:pfam00261  128 DLERAEERAELAESKIVELEEELKVVGnnlKSLEASEEKASEREDKYEEQI---RFLTEKLKEAETRAEFAERSVQKLEK 204


                   ....*....
gi 1474844183  318 LNDKLENEL 326
Cdd:pfam00261  205 EVDRLEDEL 213
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 850-914 1.70e-03

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: 38.02  E-value: 1.70e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474844183  850 QWDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 914
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 166-365 1.71e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQ-QGAVVRDGVAEEEGTVELGPKRLWKddTGRVEELQELLEKQNFelSQ 244
Cdd:COG4942     58 AALERRIAALARRIRALEQELAALEAELAELEkEIAELRAELEAQKEELAELLRALYR--LGRQPPLALLLSPEDF--LD 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  245 ARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKryLAAQREatsihDLNDKLEN 324
Cdd:COG4942    134 AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA--LKAERQ-----KLLARLEK 206

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1474844183  325 ELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLP 365
Cdd:COG4942    207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 229-353 1.99e-03

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 42.35  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  229 EELQEL-LEKQNFE--LSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKhqrdlreALAQKEDMEERITTLEKRY 305
Cdd:pfam05911  688 EEFEQLkSEKENLEveLASCTENLESTKSQLQESEQLIAELRSELASLKESNSL-------AETQLKCMAESYEDLETRL 760

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1474844183  306 LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQK 353
Cdd:pfam05911  761 TELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKK 808
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 228-468 2.01e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  228 VEELQELL--EKQNFElSQARERLVTLTATVTELEEDLGTARR---DLIKS----EELSSKHQRDLREALAQKEDMEER- 297
Cdd:pfam01576  329 VTELKKALeeETRSHE-AQLQEMRQKHTQALEELTEQLEQAKRnkaNLEKAkqalESENAELQAELRTLQQAKQDSEHKr 407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  298 ------ITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQ--QTMRKAET------ 363
Cdd:pfam01576  408 kklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtQELLQEETrqklnl 487

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  364 ---LPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL---------- 430
Cdd:pfam01576  488 strLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALtqqleekaaa 567

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1474844183  431 ---LSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEE 468
Cdd:pfam01576  568 ydkLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQ 608
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
984-1039 2.09e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 37.63  E-value: 2.09e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1474844183  984 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1039
Cdd:pfam07647   11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 227-491 2.30e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  227 RVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARR-------DLIKSEELSSKHQRDLREA-------LAQKE 292
Cdd:pfam01576  750 QVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKgreeavkQLKKLQAQMKDLQRELEEArasrdeiLAQSK 829

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  293 DMEERITTLEKRYL-------AAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLP 365
Cdd:pfam01576  830 ESEKKLKNLEAELLqlqedlaASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLN 909

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  366 EVEAELAQRIAALT---KAEERHGNIEEHLRQlegQLEEKNQEL-ARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLH 441
Cdd:pfam01576  910 DRLRKSTLQVEQLTtelAAERSTSQKSESARQ---QLERQNKELkAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQE 986

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1474844183  442 LKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam01576  987 SRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLK 1036
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 1062-1101 2.34e-03

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 37.63  E-value: 2.34e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1474844183 1062 VLVWTNDQVVHWVQSIGLRDYAGNLQESGVHG-ALLALDEN 1101
Cdd:cd09512      4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS 44
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 227-490 2.51e-03

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: 42.04  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  227 RVEELQELLEKQN---FELSQARERLvtltATVTELEEDLGTAR------RDLIKSEELSSKHQRDLREALAQKEDMEER 297
Cdd:pfam05557  171 RIKELEFEIQSQEqdsEIVKNSKSEL----ARIPELEKELERLRehnkhlNENIENKLLLKEEVEDLKRKLEREEKYREE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  298 ITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKarhLQELLEVAEQK---LQQTMRKAETLPEVEAELAQR 374
Cdd:pfam05557  247 AATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQL---QQREIVLKEENsslTSSARQLEKARRELEQELAQY 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  375 IAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ------REKMNEDHNKRLSDTVdRLLSESNERLQLHLKE---R 445
Cdd:pfam05557  324 LKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAilesydKELTMSNYSPQLLERI-EEAEDMTQKMQAHNEEmeaQ 402

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1474844183  446 MAALEEK--------NTLIQELESSQRQieEQHHHKGRLSEEIEKLRQEVDQL 490
Cdd:pfam05557  403 LSVAEEElggykqqaQTLERELQALRQQ--ESLADPSYSKEEVDSLRRKLETL 453
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 38-487 3.09e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 3.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   38 EKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSALPQeFATLTRELsmcreqlleREEEISELKAERNNtRLLLEH 117
Cdd:pfam01576  232 AELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQ-ISELQEDL---------ESERAARNKAEKQR-RDLGEE 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  118 LECLVSRHERSLRMTVVKRQAQSPSgvSSEVEVLK-ALKSLFEHHKALDEKVRERLRAALErvtTLEEQLAGAHQQVSAL 196
Cdd:pfam01576  301 LEALKTELEDTLDTTAAQQELRSKR--EQEVTELKkALEEETRSHEAQLQEMRQKHTQALE---ELTEQLEQAKRNKANL 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  197 QQGAVVRDG-----------VAEEEGTVELGPKRLwkddTGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGT 265
Cdd:pfam01576  376 EKAKQALESenaelqaelrtLQQAKQDSEHKRKKL----EGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNE 451

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  266 ARRDLIK-SEELSS------KHQRDLREALAQKEDMEERITTLE----------------KRYLAAQREATSIH--DLND 320
Cdd:pfam01576  452 AEGKNIKlSKDVSSlesqlqDTQELLQEETRQKLNLSTRLRQLEdernslqeqleeeeeaKRNVERQLSTLQAQlsDMKK 531

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  321 KLENELANKESLhrqcEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH----GNIEEHLRQLE 396
Cdd:pfam01576  532 KLEEDAGTLEAL----EEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQrqlvSNLEKKQKKFD 607

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  397 GQL-EEKNQELARVRQREKMNEDHNKR------LSDTVDRL------LSESNERLQLHLKERMAALEEKNTLIQELESSQ 463
Cdd:pfam01576  608 QMLaEEKAISARYAEERDRAEAEAREKetralsLARALEEAleakeeLERTNKQLRAEMEDLVSSKDDVGKNVHELERSK 687

                          490       500       510
                   ....*....|....*....|....*....|...
gi 1474844183  464 RQIEEQHHHKGRLSEEIE---------KLRQEV 487
Cdd:pfam01576  688 RALEQQVEEMKTQLEELEdelqatedaKLRLEV 720
mukB PRK04863
chromosome partition protein MukB;
166-423 3.13e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAvvrDGVAEEEGTVelgpkRLWKDDT--GRVEELQELLEkqnfELS 243
Cdd:PRK04863   840 RQLNRRRVELERALADHESQEQQQRSQLEQAKEGL---SALNRLLPRL-----NLLADETlaDRVEEIREQLD----EAE 907

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  244 QARERLVTLTATVTELEEDLGTARRDLIKSEELsskhQRDLREALAQKEDMEERITTL----EKR----YLAAQREATSI 315
Cdd:PRK04863   908 EAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQL----KQDYQQAQQTQRDAKQQAFALtevvQRRahfsYEDAAEMLAKN 983

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  316 HDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALT---------KAEERHG 386
Cdd:PRK04863   984 SDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvpadsgaeeRARARRD 1063

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1474844183  387 NIEEHLRQLEGQleeKNQ-ELARVRQREKMNEdHNKRL 423
Cdd:PRK04863  1064 ELHARLSANRSR---RNQlEKQLTFCEAEMDN-LTKKL 1097
PRK09039 PRK09039
peptidoglycan -binding protein;
273-410 3.85e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.10  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  273 SEELSSKHQR---------DLREALA----QKEDMEERITTLEKRYLAAQREatsihdlNDKLENELANKESLHRQCEEK 339
Cdd:PRK09039    45 SREISGKDSAldrlnsqiaELADLLSlerqGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGR 117

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474844183  340 ARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL--------TKAEERHGNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:PRK09039   118 AGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 258-460 3.98e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 3.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  258 ELEEDLGTARRDLI-KSEELSSKHQRDLREALAQkeDMEERITTLE-------KRYLAAQREATSIHDLNDK-------- 321
Cdd:cd16269     94 KLMEQLEEKKEEFCkQNEEASSKRCQALLQELSA--PLEEKISQGSysvpggyQLYLEDREKLVEKYRQVPRkgvkaeev 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  322 LENELANKESlhrqcEEKArHLQ--ELLEVAEQKLQQTMRKAETLpEVEAELAQRIAALT--KAEERHGNIEEHLRQLEG 397
Cdd:cd16269    172 LQEFLQSKEA-----EAEA-ILQadQALTEKEKEIEAERAKAEAA-EQERKLLEEQQRELeqKLEDQERSYEEHLRQLKE 244

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1474844183  398 QLEEKnqelarvrqREKMNEDHNKRLsdtvDRLLSESNERLQLHLKERMAALEEKntlIQELE 460
Cdd:cd16269    245 KMEEE---------RENLLKEQERAL----ESKLKEQEALLEEGFKEQAELLQEE---IRSLK 291
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 257-489 4.64e-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: 41.31  E-value: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  257 TELEEDLGTARRDLIKSEELSSKHQRDLRE-ALAQKEDMEERITTLEK----------------RYLAAQREATSI-HDL 318
Cdd:pfam01576    1 TRQEEEMQAKEEELQKVKERQQKAESELKElEKKHQQLCEEKNALQEQlqaetelcaeaeemraRLAARKQELEEIlHEL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  319 NDKLENELANKESLHRQCEEKARHLQEL------LEVAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEEH 391
Cdd:pfam01576   81 ESRLEEEEERSQQLQNEKKKMQQHIQDLeeqldeEEAARQKLQLEKVTTEAkIKKLEEDILLLEDQNSKLSKERKLLEER 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  392 LRQLEGQLEEknqELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLH-LKERMAAleEKNTLIQELESSQRQIEEQH 470
Cdd:pfam01576  161 ISEFTSNLAE---EEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEkAKRKLEG--ESTDLQEQIAELQAQIAELR 235

                          250
                   ....*....|....*....
gi 1474844183  471 HHKGRLSEEIEKLRQEVDQ 489
Cdd:pfam01576  236 AQLAKKEEELQAALARLEE 254
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 26-407 5.58e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.26  E-value: 5.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   26 FEQLMVNMLDEREKLLESL--RESQETLAATQS-RLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEIS 102
Cdd:pfam15921  368 FSQESGNLDDQLQKLLADLhkREKELSLEKEQNkRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQME 447

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  103 ELKAERNNTRLLLEHLECLVSRHERS---LRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDE------KVRERLR 173
Cdd:pfam15921  448 RQMAAIQGKNESLEKVSSLTAQLESTkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAtnaeitKLRSRVD 527

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  174 AALERVTTL---EEQLAGAHQQVSALQQGAVVRDGVAE------------------EEGTVELGPKRLWKDDTGRVEELQ 232
Cdd:pfam15921  528 LKLQELQHLkneGDHLRNVQTECEALKLQMAEKDKVIEilrqqienmtqlvgqhgrTAGAMQVEKAQLEKEINDRRLELQ 607

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  233 ELLEKQNFELSQARErlvtLTATVTELE----------------------------EDLGTARRDLIKSEELSSKHQRDL 284
Cdd:pfam15921  608 EFKILKDKKDAKIRE----LEARVSDLElekvklvnagserlravkdikqerdqllNEVKTSRNELNSLSEDYEVLKRNF 683

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  285 REalaQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENE--LANKESLHRQCEEKARH-----LQELLEVAEQKLQQT 357
Cdd:pfam15921  684 RN---KSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSdgHAMKVAMGMQKQITAKRgqidaLQSKIQFLEEAMTNA 760

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1474844183  358 MRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEK--NQELA 407
Cdd:pfam15921  761 NKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKvaNMEVA 812
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 35-493 5.79e-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: 40.93  E-value: 5.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   35 DEREKLLESLREsQETLAATQSR-LQDALHERDQLQRHlNSALPQEFATLT--------------RELSMCREQLLEREE 99
Cdd:pfam01576  622 EERDRAEAEARE-KETRALSLARaLEEALEAKEELERT-NKQLRAEMEDLVsskddvgknvheleRSKRALEQQVEEMKT 699

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  100 EISELKAERNNT---RLLLE-HLECLVSRHERSLrmtvvkrQAQSPSGVSSEVEVLKALKslfEHHKALDEKVRERLRAA 175
Cdd:pfam01576  700 QLEELEDELQATedaKLRLEvNMQALKAQFERDL-------QARDEQGEEKRRQLVKQVR---ELEAELEDERKQRAQAV 769

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  176 LERvTTLEEQLAGAHQQVSALQQGavvRDGVAEEEGTVELGPKRLWKddtgrveELQELLEKQNFELSQARE---RLVTL 252
Cdd:pfam01576  770 AAK-KKLELDLKELEAQIDAANKG---REEAVKQLKKLQAQMKDLQR-------ELEEARASRDEILAQSKEsekKLKNL 838

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  253 TATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEErittlEKRYLAAQreatsIHDLNDKLENELANKESL 332
Cdd:pfam01576  839 EAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD-----EKRRLEAR-----IAQLEEELEEEQSNTELL 908

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  333 H---RQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL-----TKAEERHGNIEEHLRQLEGQLEEKNQ 404
Cdd:pfam01576  909 NdrlRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMegtvkSKFKSSIAALEAKIAQLEEQLEQESR 988

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  405 ELAR----VRQREK------MNEDHNKRLSDTVDRLLSESNERLQlHLKERMAALEEKNTLIQELESS-QRQIEEqhhhk 473
Cdd:pfam01576  989 ERQAanklVRRTEKklkevlLQVEDERRHADQYKDQAEKGNSRMK-QLKRQLEEAEEEASRANAARRKlQRELDD----- 1062

                          490       500
                   ....*....|....*....|
gi 1474844183  474 grLSEEIEKLRQEVDQLKGR 493
Cdd:pfam01576 1063 --ATESNESMNREVSTLKSK 1080
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
142-414 7.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 7.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  142 SGVSSEVEVLKALKSlfehhkaldekvreRLRAALERVTTLEEQLAGAHQQVSALQQGAVvrDGVAEEEGTVELGPKRL- 220
Cdd:PRK03918   542 KSLKKELEKLEELKK--------------KLAELEKKLDELEEELAELLKELEELGFESV--EELEERLKELEPFYNEYl 605

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  221 -WKDDTGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLgtarrdliksEELSSKH-QRDLREALAQKEDMEERI 298
Cdd:PRK03918   606 eLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL----------EELEKKYsEEEYEELREEYLELSREL 675

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  299 TTLEKRYLAAQREATSIHDLNDKLENELANKeslhrqceEKARHLQELLEVAEQKLQQTMRKaetLPEVEAELAQRiaAL 378
Cdd:PRK03918   676 AGLRAELEELEKRREEIKKTLEKLKEELEER--------EKAKKELEKLEKALERVEELREK---VKKYKALLKER--AL 742

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1474844183  379 TKAEERHGNIEEHLRqlegqlEEKNQELARVRQREK 414
Cdd:PRK03918   743 SKVGEIASEIFEELT------EGKYSGVRVKAEENK 772
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-303 7.17e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 7.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   27 EQLMVNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLnSALPQEFATLTRELSMCREQLLEREEEISELKA 106
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI-AATERRLEDLEEQIEELSEDIESLAAEIEELEE 866

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  107 ERNNTRLLLEHLECLVSRHERSLRmtvvkrqaqspsgvssevEVLKALKSLFEHHKALDEKVRE---RLRAALERVTTLE 183
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALA------------------LLRSELEELSEELRELESKRSElrrELEELREKLAQLE 928

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  184 EQLAGAHQQVSALQQgavvrdgVAEEEGTVELgpkrlwkddtgrvEELQELLEKQNFELSQARERLVTLTATVTELeedl 263
Cdd:TIGR02168  929 LRLEGLEVRIDNLQE-------RLSEEYSLTL-------------EEAEALENKIEDDEEEARRRLKRLENKIKEL---- 984

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1474844183  264 gtARRDLIKSEELSSKHQRdLREALAQKEDMEERITTLEK 303
Cdd:TIGR02168  985 --GPVNLAAIEEYEELKER-YDFLTAQKEDLTEAKETLEE 1021
RNase_Y_N pfam12072
RNase Y N-terminal region;
366-488 7.73e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.10  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  366 EVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLqlhlkER 445
Cdd:pfam12072   68 EAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ER 142

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1474844183  446 MAAL---EEKNTLIQELEssqrqiEEQHHHKGRLSEEIE-KLRQEVD 488
Cdd:pfam12072  143 ISGLtseEAKEILLDEVE------EELRHEAAVMIKEIEeEAKEEAD 183
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 984-1028 7.92e-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: 7.92e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1474844183  984 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 1028
Cdd:cd09501     11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 274-490 8.20e-03

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: 40.42  E-value: 8.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  274 EELSSKHQRDLREALAQKEDMEERITTLEKRY---LAAQREATSIHDLNDKLENELANK-ESLHRQCEEKARHLQEllev 349
Cdd:TIGR00606  694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRdemLGLAPGRQSIIDLKEKEIPELRNKlQKVNRDIQRLKNDIEE---- 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  350 aEQKLQQTMRKAETLPEVeaeLAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELArVRQREKMNEDHNKRLsdtvdR 429
Cdd:TIGR00606  770 -QETLLGTIMPEEESAKV---CLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRT-VQQVNQEKQEKQHEL-----D 839

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1474844183  430 LLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQL 490
Cdd:TIGR00606  840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSL 900
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 229-461 8.70e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.20  E-value: 8.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  229 EELQEL------LEKQNFELSQarerlVTLTATVTELEEDLGTARRDLiksEELsskhqrDLREALAQKEDMEERITTL- 301
Cdd:PRK04778   230 DQLQELkagyreLVEEGYHLDH-----LDIEKEIQDLKEQIDENLALL---EEL------DLDEAEEKNEEIQERIDQLy 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  302 ---EKRYLAAQREATSIHDLNDKLEN-------------------ELANKESLHRQCEEKarHLQELLEVAEQKLQQTMR 359
Cdd:PRK04778   296 dilEREVKARKYVEKNSDTLPDFLEHakeqnkelkeeidrvkqsyTLNESELESVRQLEK--QLESLEKQYDEITERIAE 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  360 KAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR--------EKMN-----EDHNKRLSDT 426
Cdd:PRK04778   374 QEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKlheikrylEKSNlpglpEDYLEMFFEV 453

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1474844183  427 VDRL--LSESNERLQLHLKERMAALEEKNTLIQELES 461
Cdd:PRK04778   454 SDEIeaLAEELEEKPINMEAVNRLLEEATEDVETLEE 490
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
231-412 9.38e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.04  E-value: 9.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  231 LQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEE----LSSKHQRDL-REALAQKEDMEERITTLEKRY 305
Cdd:COG1842     28 LDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEkarlALEKGREDLaREALERKAELEAQAEALEAQL 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  306 LAAQREATSIHDLNDKLENELANKESlhRQCEEKARHlqellEVAE--QKLQQTMRKAETLpEVEAELAQ---RIAALT- 379
Cdd:COG1842    108 AQLEEQVEKLKEALRQLESKLEELKA--KKDTLKARA-----KAAKaqEKVNEALSGIDSD-DATSALERmeeKIEEMEa 179

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1474844183  380 KAE-----ERHGNIEEHLRQLEGQlEEKNQELARVRQR 412
Cdd:COG1842    180 RAEaaaelAAGDSLDDELAELEAD-SEVEDELAALKAK 216
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 40-492 9.40e-03

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: 40.19  E-value: 9.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183   40 LLESLRESQETLAATQSRLQdALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNT-------R 112
Cdd:pfam10174   58 LKEQYRVTQEENQHLQLTIQ-ALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQakelfllR 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  113 LLLEHLECLVSRHERSL--RMTVVKR-----QAQS-PSGVSSEVEVLKALKSLFEHHKA-----LDEKVRE--RLRAALE 177
Cdd:pfam10174  137 KTLEEMELRIETQKQTLgaRDESIKKllemlQSKGlPKKSGEEDWERTRRIAEAEMQLGhlevlLDQKEKEniHLREELH 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  178 RvttlEEQLAGAHQQVSALQQgavvrdgVAEEEGTVELGPKRLWKDdtgrVEELQELLeKQNFELS--QARERLVTLTAT 255
Cdd:pfam10174  217 R----RNQLQPDPAKTKALQT-------VIEMKDTKISSLERNIRD----LEDEVQML-KTNGLLHteDREEEIKQMEVY 280

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  256 VTE---LEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKES- 331
Cdd:pfam10174  281 KSHskfMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESf 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  332 -------LHRQCEEKA------RHLQELLEVAEQKLQQTMRKAETLPEV-------EAELAQRIAALtkaEERHGNIEEH 391
Cdd:pfam10174  361 lnkktkqLQDLTEEKStlageiRDLKDMLDVKERKINVLQKKIENLQEQlrdkdkqLAGLKERVKSL---QTDSSNTDTA 437

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474844183  392 LRQLEGQLEEKNQELARVRQ------REKMNE--DHNKRLSDtvdrlLSESNERLQLHLKERMAALEEkntlIQELESSQ 463
Cdd:pfam10174  438 LTTLEEALSEKERIIERLKEqreredRERLEEleSLKKENKD-----LKEKVSALQPELTEKESSLID----LKEHASSL 508

                          490       500       510
                   ....*....|....*....|....*....|
gi 1474844183  464 RQ-IEEQHHHKGRLSEEIEKLRQEVDQLKG 492
Cdd:pfam10174  509 ASsGLKKDSKLKSLEIAVEQKKEECSKLEN 538
 
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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