NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2024438909|ref|XP_040513752|]
View 

liprin-alpha-2 isoform X1 [Gallus gallus]

Protein Classification

liprin-alpha( domain architecture ID 13377566)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1133-1204 4.44e-44

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


:

Pssm-ID: 188967  Cd Length: 72  Bit Score: 153.63  E-value: 4.44e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909 1133 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1204
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
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 ...
 1048-1113 8.36e-44

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: 152.63  E-value: 8.36e-44
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024438909 1048 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1113
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 ...
 930-1000 8.62e-44

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


:

Pssm-ID: 188961  Cd Length: 71  Bit Score: 153.10  E-value: 8.62e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024438909  930 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 1000
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-513 1.80e-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: 88.58  E-value: 1.80e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  111 KELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSrherslrmTVVKRQAQSPSGVSSEVEVLKALkslfehhkal 190
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELE--------QLRKELEELSRQISALRKDLARL---------- 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  191 dEKVRERLRvslERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGPAESEhiegmepgqkvhEKRLSNGSIDSNDET 270
Cdd:TIGR02168  739 -EAEVEQLE---ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL------------EAQIEQLKEELKALR 802

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  271 SQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRY 350
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  351 LSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQT----MRKAETLPEVEAELAQRIAALTKS 426
Cdd:TIGR02168  883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLevriDNLQERLSEEYSLTLEEAEALENK 962

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  427 DPTSSTSSGDYQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTV 501
Cdd:TIGR02168  963 IEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTF 1038

                          410
                   ....*....|..
gi 2024438909  502 DRLltesNERLQ 513
Cdd:TIGR02168 1039 DQV----NENFQ 1046
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
462-573 6.55e-04

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


The actual alignment was detected with superfamily member COG2433:

Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 6.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  462 IEERM-RHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTEsNERLQLHLKERMAALEEknvLIQESESFRKNL 540
Cdd:COG2433    382 LEELIeKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---LERELSEARSEE 457

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2024438909  541 EESLH-DKE--RLAEEIEKLRSELDQMKLRAGSLIE 573
Cdd:COG2433    458 RREIRkDREisRLDREIERLERELEEERERIEELKR 493
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 453-720 3.50e-03

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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  453 RKAEERHGNIEERMRHLEAQLEEKNQELQR-ARQREKMNEehnkrlsdtVDRLLTESNE-RLQLHLKERMAALEEKNVLI 530
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLKEKEALERQKEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  531 QESESFRKNLEESLHDKERLAEEIEKLRSELDQMKLRAGSLIEPTLSRPHLDsSAELRYSVGSLVDSQSDYRSTKVIRRP 610
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK-IGELEAEIASLERSIAEKERELEDAEE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  611 RRGRMGVRRDEPKVKSLGDHEWNRTQQIGVlsshpfESDTEMSDIDDDDRETLFSSMDLLSPSG------HSDAQTLAMM 684
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEREIEEERKRR------DKLTEEYAELKEELEDLRAELEEVDKEFaetrdeLKDYREKLEK 396

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2024438909  685 LQEQLDAINKEIRLIQEEKESTELRAEEIENRVASV 720
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1133-1204 4.44e-44

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


Pssm-ID: 188967  Cd Length: 72  Bit Score: 153.63  E-value: 4.44e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909 1133 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1204
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
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 ...
 1048-1113 8.36e-44

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: 152.63  E-value: 8.36e-44
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024438909 1048 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1113
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 ...
 930-1000 8.62e-44

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


Pssm-ID: 188961  Cd Length: 71  Bit Score: 153.10  E-value: 8.62e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024438909  930 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 1000
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-513 1.80e-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: 88.58  E-value: 1.80e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  111 KELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSrherslrmTVVKRQAQSPSGVSSEVEVLKALkslfehhkal 190
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELE--------QLRKELEELSRQISALRKDLARL---------- 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  191 dEKVRERLRvslERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGPAESEhiegmepgqkvhEKRLSNGSIDSNDET 270
Cdd:TIGR02168  739 -EAEVEQLE---ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL------------EAQIEQLKEELKALR 802

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  271 SQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRY 350
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  351 LSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQT----MRKAETLPEVEAELAQRIAALTKS 426
Cdd:TIGR02168  883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLevriDNLQERLSEEYSLTLEEAEALENK 962

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  427 DPTSSTSSGDYQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTV 501
Cdd:TIGR02168  963 IEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTF 1038

                          410
                   ....*....|..
gi 2024438909  502 DRLltesNERLQ 513
Cdd:TIGR02168 1039 DQV----NENFQ 1046
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 1047-1111 5.85e-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: 5.85e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024438909 1047 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1111
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 272-573 1.10e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.05  E-value: 1.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  272 QVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYL 351
Cdd:COG1196    247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  352 SAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALtksdptss 431
Cdd:COG1196    327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-------- 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  432 tssgdyqyvmEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNER 511
Cdd:COG1196    399 ----------AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909  512 LQLHLKERmAALEEKNVLIQESESfRKNLEESLHDKERLAEEIEKLRSELDQMKLRAGSLIE 573
Cdd:COG1196    469 LEEAALLE-AALAELLEELAEAAA-RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
105-565 9.82e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 69.71  E-value: 9.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  105 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVvkRQAQSPSGVSSEVEVLKALKSLF 184
Cdd:PRK03918   232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK----KEIEELEEKV--KELKELKEKAEEYIKLSEFYEEY 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  185 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGPAES-EHIEGMEPGQKVHEKRLSNGS 263
Cdd:PRK03918   306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTGLT 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  264 IDSNDETSQVI-----ELQELLEKQNYEMAQMKERMAALSSRVGEVEQE-----------AETARKELIK--TEEMnSKY 325
Cdd:PRK03918   386 PEKLEKELEELekakeEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelTEEHRKELLEeyTAEL-KRI 464

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  326 QRDIREAMAQKEDMEERITTLEKrYLSAQRESTSIHDMNDKLEN-----------ELANKEAILRQLEDKNRQLQ----- 389
Cdd:PRK03918   465 EKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKEleeklkkynleELEKKAEEYEKLKEKLIKLKgeiks 543

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  390 -----ERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKSDPTSstssgdyqyvMEAKLQEMISIRRK------AEER 458
Cdd:PRK03918   544 lkkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE----------LEERLKELEPFYNEylelkdAEKE 613

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  459 HGNIEERMRHLEAQLEEKNQELQRARQR----EKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESE 534
Cdd:PRK03918   614 LEREEKELKKLEEELDKAFEELAETEKRleelRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693

                          490       500       510
                   ....*....|....*....|....*....|.
gi 2024438909  535 SFRKNLEESLHDKERLAEEIEKLRSELDQMK 565
Cdd:PRK03918   694 KTLEKLKEELEEREKAKKELEKLEKALERVE 724
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 268-562 4.92e-10

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


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 63.16  E-value: 4.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  268 DETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLE 347
Cdd:pfam19220   45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  348 KRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKSD 427
Cdd:pfam19220  125 RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  428 PTSSTSSGDyqyvMEAKLQEMISIRRKAEERHGNIEERMRHleaqleeknqelQRARQREKMnEEHNKRLSDTvDRLLTE 507
Cdd:pfam19220  205 DATRARLRA----LEGQLAAEQAERERAEAQLEEAVEAHRA------------ERASLRMKL-EALTARAAAT-EQLLAE 266

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024438909  508 SNERLQlHLKERMAALEEKNV-LIQESESFRKNLEESLHDKERLAE---EIEKLRSELD 562
Cdd:pfam19220  267 ARNQLR-DRDEAIRAAERRLKeASIERDTLERRLAGLEADLERRTQqfqEMQRARAELE 324
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 930-996 5.10e-09

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 53.84  E-value: 5.10e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024438909   930 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 996
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1056-1111 1.10e-07

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.99  E-value: 1.10e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024438909  1056 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1111
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1134-1205 6.49e-07

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 47.68  E-value: 6.49e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909  1134 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1205
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 932-996 1.16e-04

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 41.49  E-value: 1.16e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024438909  932 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 996
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1134-1204 1.37e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.37e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024438909 1134 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1204
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
462-573 6.55e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 6.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  462 IEERM-RHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTEsNERLQLHLKERMAALEEknvLIQESESFRKNL 540
Cdd:COG2433    382 LEELIeKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---LERELSEARSEE 457

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2024438909  541 EESLH-DKE--RLAEEIEKLRSELDQMKLRAGSLIE 573
Cdd:COG2433    458 RREIRkDREisRLDREIERLERELEEERERIEELKR 493
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 453-720 3.50e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  453 RKAEERHGNIEERMRHLEAQLEEKNQELQR-ARQREKMNEehnkrlsdtVDRLLTESNE-RLQLHLKERMAALEEKNVLI 530
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLKEKEALERQKEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  531 QESESFRKNLEESLHDKERLAEEIEKLRSELDQMKLRAGSLIEPTLSRPHLDsSAELRYSVGSLVDSQSDYRSTKVIRRP 610
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK-IGELEAEIASLERSIAEKERELEDAEE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  611 RRGRMGVRRDEPKVKSLGDHEWNRTQQIGVlsshpfESDTEMSDIDDDDRETLFSSMDLLSPSG------HSDAQTLAMM 684
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEREIEEERKRR------DKLTEEYAELKEELEDLRAELEEVDKEFaetrdeLKDYREKLEK 396

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2024438909  685 LQEQLDAINKEIRLIQEEKESTELRAEEIENRVASV 720
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1133-1204 4.44e-44

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


Pssm-ID: 188967  Cd Length: 72  Bit Score: 153.63  E-value: 4.44e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909 1133 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1204
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
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 ...
 1048-1113 8.36e-44

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: 152.63  E-value: 8.36e-44
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024438909 1048 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1113
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 ...
 930-1000 8.62e-44

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


Pssm-ID: 188961  Cd Length: 71  Bit Score: 153.10  E-value: 8.62e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024438909  930 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 1000
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 1052-1111 1.34e-31

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


Pssm-ID: 188894  Cd Length: 60  Bit Score: 117.63  E-value: 1.34e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909 1052 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1111
Cdd:cd09495      1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 937-995 3.27e-27

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


Pssm-ID: 188893  Cd Length: 58  Bit Score: 105.39  E-value: 3.27e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024438909  937 TVVAWLELWLGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 995
Cdd:cd09494      1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 1141-1202 7.03e-25

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


Pssm-ID: 188895  Cd Length: 62  Bit Score: 98.77  E-value: 7.03e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909 1141 RVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNN 1202
Cdd:cd09496      1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 1133-1204 1.47e-18

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


Pssm-ID: 188969  Cd Length: 72  Bit Score: 80.95  E-value: 1.47e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909 1133 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1204
Cdd:cd09570      1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-513 1.80e-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: 88.58  E-value: 1.80e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  111 KELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSrherslrmTVVKRQAQSPSGVSSEVEVLKALkslfehhkal 190
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELE--------QLRKELEELSRQISALRKDLARL---------- 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  191 dEKVRERLRvslERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGPAESEhiegmepgqkvhEKRLSNGSIDSNDET 270
Cdd:TIGR02168  739 -EAEVEQLE---ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL------------EAQIEQLKEELKALR 802

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  271 SQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRY 350
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  351 LSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQT----MRKAETLPEVEAELAQRIAALTKS 426
Cdd:TIGR02168  883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLevriDNLQERLSEEYSLTLEEAEALENK 962

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  427 DPTSSTSSGDYQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTV 501
Cdd:TIGR02168  963 IEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTF 1038

                          410
                   ....*....|..
gi 2024438909  502 DRLltesNERLQ 513
Cdd:TIGR02168 1039 DQV----NENFQ 1046
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 931-995 5.98e-17

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


Pssm-ID: 188963  Cd Length: 70  Bit Score: 76.34  E-value: 5.98e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024438909  931 AQWDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 995
Cdd:cd09564      2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 1047-1111 1.35e-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: 75.04  E-value: 1.35e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024438909 1047 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1111
Cdd:cd09566      1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 1047-1111 1.37e-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: 75.14  E-value: 1.37e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024438909 1047 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1111
Cdd:cd09567      1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 256-565 5.03e-16

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: 83.96  E-value: 5.03e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  256 EKRLSNGSIDSNDETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQ 335
Cdd:TIGR02169  701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  336 KEDMEERIttlekrylsAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAE 415
Cdd:TIGR02169  781 LNDLEARL---------SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  416 LAQRIAALTKSDPTSSTSSGDYQYV---MEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEE 492
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAAlrdLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  493 HNKRLSDTVDRLLTESNERLQL--------HLKERMAALEEKNVL-IQESESFRKNLEESLHDKERLAEE---IEKLRSE 560
Cdd:TIGR02169  932 ELSEIEDPKGEDEEIPEEELSLedvqaelqRVEEEIRALEPVNMLaIQEYEEVLKRLDELKEKRAKLEEErkaILERIEE 1011


                   ....*
gi 2024438909  561 LDQMK 565
Cdd:TIGR02169 1012 YEKKK 1016
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 1133-1204 2.01e-15

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 72.10  E-value: 2.01e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909 1133 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1204
Cdd:cd09569      1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 117-492 1.25e-14

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: 79.34  E-value: 1.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  117 REQLLEKEEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAqspSGVSSEVEVLKAlkslfEHhkaldEKVRE 196
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKI---GEIEKEIEQLEQ-----EE-----EKLKE 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  197 RLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIaagegpaesehiegmepgqkvHEKRLSNGSIDSNDETSQVIEL 276
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL---------------------HKLEEALNDLEARLSHSRIPEI 796

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  277 QELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKE-------LIKTEEMNSKYQRDIREAMAQKEDMEERITTLEK- 348
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEiqelqeqRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAa 876

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  349 -RYLSAQREstsihdmndKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALtKSD 427
Cdd:TIGR02169  877 lRDLESRLG---------DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED-EEI 946

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909  428 PTSSTSSGDYQYV---MEAKLQEMISIRRKAEERHGNIEERMRHLEAQL----EEKNQELQRARQREKMNEE 492
Cdd:TIGR02169  947 PEEELSLEDVQAElqrVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRakleEERKAILERIEEYEKKKRE 1018
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 268-625 2.38e-14

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: 78.57  E-value: 2.38e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  268 DETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMN--SKYQRDIR--EAMAQKEDMEERI 343
Cdd:TIGR02169  160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQalLKEKREYEgyELLKEKEALERQK 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  344 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQL--------EDKNRQLQERLELAEQKLQQTMR----KAETLPE 411
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLERsiaeKERELED 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  412 VEAELAQRIAALTKSDPTSSTSSGDyqyvmeakLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQR----- 486
Cdd:TIGR02169  320 AEERLAKLEAEIDKLLAEIEELERE--------IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDElkdyr 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  487 ---EKMNEEHNKrLSDTVDRLLTE----SNERLQLH-----LKERMAALE-EKNVLIQESESFRKNLEESLHDKERLAEE 553
Cdd:TIGR02169  392 eklEKLKREINE-LKRELDRLQEElqrlSEELADLNaaiagIEAKINELEeEKEDKALEIKKQEWKLEQLAADLSKYEQE 470

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024438909  554 IEKLRSELDQMKLRAGSLIEPTlsrphldssAELRYSVGSLVDSQSDYRST-KVIRRPRRGRMGVRRDEPKVK 625
Cdd:TIGR02169  471 LYDLKEEYDRVEKELSKLQREL---------AEAEAQARASEERVRGGRAVeEVLKASIQGVHGTVAQLGSVG 534
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 1047-1111 5.85e-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: 5.85e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024438909 1047 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1111
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 258-564 1.01e-13

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 76.26  E-value: 1.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  258 RLSNGSIDSNDETSQVIELQELLEKqnyemaqMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKE 337
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  338 DMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERleLAEQKLQQTMRKAETLPEVEAELA 417
Cdd:TIGR02169  734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKLEEEVSRIE 811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  418 QRIAALTKSdptSSTSSGDYQYvMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRL 497
Cdd:TIGR02169  812 ARLREIEQK---LNRLTLEKEY-LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  498 SDTVDRL-------------LTESNERLQLHLKERMAALEEKNVLIQESESFRKNLEES---LHDKERLAEEIEKLRSEL 561
Cdd:TIGR02169  888 KKERDELeaqlrelerkieeLEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeELSLEDVQAELQRVEEEI 967


                   ...
gi 2024438909  562 DQM 564
Cdd:TIGR02169  968 RAL 970
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 285-565 1.04e-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: 76.25  E-value: 1.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  285 YEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEmnskyqrDIREAMAQKEDMEERITTLEKRYLSAQREstsIHDmn 364
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEE-------KLEELRLEVSELEEEIEELQKELYALANE---ISR-- 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  365 dkLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKSDPTsstssgdyqyvMEAK 444
Cdd:TIGR02168  300 --LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE-----------LEAE 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  445 LQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqLHLKERMAALE 524
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---AELKELQAELE 443

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2024438909  525 EKNVLIQESESFRKNLEESLhdkERLAEEIEKLRSELDQMK 565
Cdd:TIGR02168  444 ELEEELEELQEELERLEEAL---EELREELEEAEQALDAAE 481
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 272-573 1.10e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.05  E-value: 1.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  272 QVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYL 351
Cdd:COG1196    247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  352 SAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALtksdptss 431
Cdd:COG1196    327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-------- 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  432 tssgdyqyvmEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNER 511
Cdd:COG1196    399 ----------AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909  512 LQLHLKERmAALEEKNVLIQESESfRKNLEESLHDKERLAEEIEKLRSELDQMKLRAGSLIE 573
Cdd:COG1196    469 LEEAALLE-AALAELLEELAEAAA-RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 930-994 1.47e-12

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


Pssm-ID: 188962  Cd Length: 64  Bit Score: 63.79  E-value: 1.47e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024438909  930 FAQWDGPTVVAWL-ELWLGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 994
Cdd:cd09563      1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 213-564 2.04e-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: 72.01  E-value: 2.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  213 AAANQEIVALREQNAHIQRKIAAGEGPAESEHIEgmepgQKVHEKRLSNGsidsndeTSQVIELQELLEKQNYEMAQMKE 292
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKA-----LAELRKELEEL-------EEELEQLRKELEELSRQISALRK 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  293 RMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELA 372
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  373 NKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKSDPTSSTSsgdyqyvMEAKLQEMISI- 451
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-------LEALLNERASLe 886

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  452 --RRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLkERMAALEEKNVL 529
Cdd:TIGR02168  887 eaLALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL-EEAEALENKIED 965

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2024438909  530 iqesesfrknleeslhDKERLAEEIEKLRSELDQM 564
Cdd:TIGR02168  966 ----------------DEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 177-492 2.47e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 2.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  177 LKALKSLFEHHKAL--DEKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAgegpaESEHIEGMEPGQKV 254
Cdd:COG1196    218 LKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE-----LELELEEAQAEEYE 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  255 HEKRLSNGSIDSNDETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMA 334
Cdd:COG1196    293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  335 QKEDMEERITTLEKRYLSAQREstsihdmndklENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEA 414
Cdd:COG1196    373 ELAEAEEELEELAEELLEALRA-----------AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024438909  415 ELAQRIaaltksdptsstssgdyqyvmEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEE 492
Cdd:COG1196    442 EALEEA---------------------AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 275-565 4.45e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 70.86  E-value: 4.45e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  275 ELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYLSAQ 354
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  355 RESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLEL-------AEQKLQQTMRKAETLPEVEAELAQRIAALTKSD 427
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealdeLRAELTLLNEEAANLRERLESLERRIAATERRL 840

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  428 PTSSTSSGDyqyvMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL--- 504
Cdd:TIGR02168  841 EDLEEQIEE----LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrre 916

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909  505 LTESNERL-QLHLKERMAALEEKNVLIQESESFRKNLEESLHDKERLAEEIEKLRSELDQMK 565
Cdd:TIGR02168  917 LEELREKLaQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 39-564 5.44e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.74  E-value: 5.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALpQMTVAAGTSIENNIQRTIScpnEFAALTKELNACRE 118
Cdd:COG1196    262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-ARLEERRRELEERLEELEE---ELAELEEELEELEE 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  119 QLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTV------VKRQAQSPSGVSSEVEVLKALKSLFEHHKALDE 192
Cdd:COG1196    338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEeeleelAEELLEALRAAAELAAQLEELEEAEEALLERLE 417

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  193 KVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGPAESEHIEGMEPGQKVHEKRLSNGSIDSNDETSQ 272
Cdd:COG1196    418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  273 VIELQELLEKQNYEMAQMKERMAALSSRVGE---VEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKR 349
Cdd:COG1196    498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVligVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  350 YLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEqklqqtmrkaETLPEVEAELAQRIAALTKSDPT 429
Cdd:COG1196    578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG----------RTLVAARLEAALRRAVTLAGRLR 647

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  430 SSTSSGDyqyVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESN 509
Cdd:COG1196    648 EVTLEGE---GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024438909  510 ERLQLHLKERMAALEEKNVLIQESESFRKNLEESLHDKERLAEEIEKLRSELDQM 564
Cdd:COG1196    725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
105-565 9.82e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 69.71  E-value: 9.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  105 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVvkRQAQSPSGVSSEVEVLKALKSLF 184
Cdd:PRK03918   232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK----KEIEELEEKV--KELKELKEKAEEYIKLSEFYEEY 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  185 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGPAES-EHIEGMEPGQKVHEKRLSNGS 263
Cdd:PRK03918   306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTGLT 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  264 IDSNDETSQVI-----ELQELLEKQNYEMAQMKERMAALSSRVGEVEQE-----------AETARKELIK--TEEMnSKY 325
Cdd:PRK03918   386 PEKLEKELEELekakeEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelTEEHRKELLEeyTAEL-KRI 464

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  326 QRDIREAMAQKEDMEERITTLEKrYLSAQRESTSIHDMNDKLEN-----------ELANKEAILRQLEDKNRQLQ----- 389
Cdd:PRK03918   465 EKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKEleeklkkynleELEKKAEEYEKLKEKLIKLKgeiks 543

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  390 -----ERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKSDPTSstssgdyqyvMEAKLQEMISIRRK------AEER 458
Cdd:PRK03918   544 lkkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE----------LEERLKELEPFYNEylelkdAEKE 613

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  459 HGNIEERMRHLEAQLEEKNQELQRARQR----EKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESE 534
Cdd:PRK03918   614 LEREEKELKKLEEELDKAFEELAETEKRleelRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693

                          490       500       510
                   ....*....|....*....|....*....|.
gi 2024438909  535 SFRKNLEESLHDKERLAEEIEKLRSELDQMK 565
Cdd:PRK03918   694 KTLEKLKEELEEREKAKKELEKLEKALERVE 724
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 266-573 1.18e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.70  E-value: 1.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  266 SNDETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITT 345
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  346 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTk 425
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR- 823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  426 sdptsstssgdyqyvmeaklqemiSIRRKAEERHGNIEERMRHLEAQLEEKNQELQR-ARQREKMNEEHNKrLSDTVDRL 504
Cdd:TIGR02168  824 ------------------------ERLESLERRIAATERRLEDLEEQIEELSEDIESlAAEIEELEELIEE-LESELEAL 878

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024438909  505 LTESnERLQLHLKERMAALEEKNVLIQESESFRKNLEeslHDKERLAEEIEKLRSELDQMKLRAGSLIE 573
Cdd:TIGR02168  879 LNER-ASLEEALALLRSELEELSEELRELESKRSELR---RELEELREKLAQLELRLEGLEVRIDNLQE 943
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
105-563 1.27e-11

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 69.30  E-value: 1.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  105 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLF 184
Cdd:PRK02224   200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----------------EELETLEAEIEDL 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  185 EHHKALDEKVRErlrvslervsALEEELAAANQEIVALREQNAHIQRKIAAGEGPAE--SEHIEGMEpgqkvhekrlsng 262
Cdd:PRK02224   264 RETIAETERERE----------ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEavEARREELE------------- 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  263 siDSNDETSQVIELQEL-LEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEmnskyqrDIREAMAQKEDMEE 341
Cdd:PRK02224   321 --DRDEELRDRLEECRVaAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE-------AVEDRREEIEELEE 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  342 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQ--------QTMRK---AETLP 410
Cdd:PRK02224   392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGsphVETIE 471

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  411 EVEAELAQRIAALTKSDPTSSTSSGDYQYVMEAKLQEmiSIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMN 490
Cdd:PRK02224   472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAE--DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024438909  491 EEHNKRLSDTVDRLLTESNERLqlhlkERMAALEEKNVLIQESESFRKNLEESLHDKERLAEEIEKLRSELDQ 563
Cdd:PRK02224   550 EAEAEEKREAAAEAEEEAEEAR-----EEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREA 617
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 323-573 2.66e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.42  E-value: 2.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  323 SKYQRDIREAMAQKEDMEERIT-------TLEKRY--LSAQRESTSIHdmnDKLENELANKEAILRQLEDknRQLQERLE 393
Cdd:COG1196    168 SKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEKAERY---RELKEELKELEAELLLLKL--RELEAELE 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  394 LAEQKLQQTMRKAE----TLPEVEAELAQRIAALTKSDPTSSTSSGDYqYVMEAKLQEMISIRRKAEERHGNIEERMRHL 469
Cdd:COG1196    243 ELEAELEELEAELEeleaELAELEAELEELRLELEELELELEEAQAEE-YELLAELARLEQDIARLEERRRELEERLEEL 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  470 EAQLEEKNQELQRARQREKMNEEHNKRLsdtvDRLLTESNERLQLHLKERMAALEEKNVLIQESESFRKNLEESLHDKER 549
Cdd:COG1196    322 EEELAELEEELEELEEELEELEEELEEA----EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                          250       260
                   ....*....|....*....|....
gi 2024438909  550 LAEEIEKLRSELDQMKLRAGSLIE 573
Cdd:COG1196    398 LAAQLEELEEAEEALLERLERLEE 421
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 90-572 4.21e-11

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: 67.35  E-value: 4.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   90 TSIENNIQRTIscpNEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHeRSLrmtvvkrqaqspsg 169
Cdd:TIGR04523  155 EKLNNKYNDLK---KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSL-------------- 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  170 vSSEVEVLKALKSLFEhhKALDEKVRErlrvslerVSALEEELAAANQEIVALREQNAHIQRKIAAGEGPAE--SEHIEG 247
Cdd:TIGR04523  217 -ESQISELKKQNNQLK--DNIEKKQQE--------INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEqnNKKIKE 285

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  248 MEPGQKVHEKRLSngsiDSNDETSQVI--ELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKY 325
Cdd:TIGR04523  286 LEKQLNQLKSEIS----DLNNQKEQDWnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  326 QRDIREamaqKEDMEERIttlekrylsaQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRK 405
Cdd:TIGR04523  362 QRELEE----KQNEIEKL----------KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE 427

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  406 AETLPEVEAELAQRIAALTKSDptsstssgdyqYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQ 485
Cdd:TIGR04523  428 IERLKETIIKNNSEIKDLTNQD-----------SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  486 REKMNEEHNKRLSDTVDRLLTESNErlqlhLKERMAALE----EKNVLIQESESFRKNLEESLhDKERLAEEIEKLRSEL 561
Cdd:TIGR04523  497 ELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEsekkEKESKISDLEDELNKDDFEL-KKENLEKEIDEKNKEI 570

                          490
                   ....*....|.
gi 2024438909  562 DQMKLRAGSLI 572
Cdd:TIGR04523  571 EELKQTQKSLK 581
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 112-419 7.55e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 7.55e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  112 ELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvSRHERslrmtvvKRQAQSpsgvSSEVEVLKALKSLFEHHKALd 191
Cdd:COG1196    233 KLRELEAELEELEAELEELEAELEELEAELAELE---AELEE-------LRLELE----ELELELEEAQAEEYELLAEL- 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  192 EKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEgpaesEHIEGMEPGQKVHEKRLSNGSIDSNDETS 271
Cdd:COG1196    298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE-----EELEEAEEELEEAEAELAEAEEALLEAEA 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  272 QVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYL 351
Cdd:COG1196    373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024438909  352 SAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQR 419
Cdd:COG1196    453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 326-570 1.80e-10

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: 64.40  E-value: 1.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  326 QRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRK 405
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  406 AETLpevEAELAQRIAALTKsdptsstsSGDYQYVMEAKLQEMISirrKAEERHGNIEERMRHLEAQLEEKNQELQRARQ 485
Cdd:COG4942     99 LEAQ---KEELAELLRALYR--------LGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAA 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  486 REKMNEEHNKRLSDTVDRLLTEsNERLQLHLKERMAALEEKNvliQESESFRKNLEESLHDKERLAEEIEKLRSELDQMK 565
Cdd:COG4942    165 LRAELEAERAELEALLAELEEE-RAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAA 240


                   ....*
gi 2024438909  566 LRAGS 570
Cdd:COG4942    241 ERTPA 245
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-515 2.59e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.08  E-value: 2.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  174 VEVLKALKSLFEHHKALDEKVRE-RLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAgegpAESEHIEgmepgq 252
Cdd:TIGR02168  202 LKSLERQAEKAERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQE----LEEKLEE------ 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  253 kvHEKRLSNGSIDSNDETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREA 332
Cdd:TIGR02168  272 --LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  333 MAQKEDMEERITtlEKRYLSAQRESTsihdmNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEV 412
Cdd:TIGR02168  350 KEELESLEAELE--ELEAELEELESR-----LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  413 EAELAQRIAALTKSDPTSSTSSgdyqyvMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEE 492
Cdd:TIGR02168  423 IEELLKKLEEAELKELQAELEE------LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496

                          330       340
                   ....*....|....*....|...
gi 2024438909  493 HNKRLSDTVDRLLTESNERLQLH 515
Cdd:TIGR02168  497 LQENLEGFSEGVKALLKNQSGLS 519
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 49-563 3.60e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 3.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   49 LRETQESLslaqQRLQDVIYD----RDSLQRQ-------------LNSALPQMTVAAGTSIENNIQRTIscpNEFAALTK 111
Cdd:COG1196    181 LEATEENL----ERLEDILGElerqLEPLERQaekaeryrelkeeLKELEAELLLLKLRELEAELEELE---AELEELEA 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  112 ELNACREQLLEKEEEISELKAERNNTRLLLEHLeclvsrheRSLRMTVVKRQAQSPSGVSSEVEVLKALkslfehhKALD 191
Cdd:COG1196    254 ELEELEAELAELEAELEELRLELEELELELEEA--------QAEEYELLAELARLEQDIARLEERRREL-------EERL 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  192 EKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGpAESEHIEGMEPgqkvHEKRLSNGSIDSNDETS 271
Cdd:COG1196    319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE-ALLEAEAELAE----AEEELEELAEELLEALR 393

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  272 QVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYL 351
Cdd:COG1196    394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  352 SAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKL----------------------------QQTM 403
Cdd:COG1196    474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavligveaayeaaleaalaaalqNIVV 553

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  404 RKAETLPEVEAELAQRIAA------LTKSDPTSSTSSG-----------------DYQYVMEAKLQEMISIRRKAEERHG 460
Cdd:COG1196    554 EDDEVAAAAIEYLKAAKAGratflpLDKIRARAALAAAlargaigaavdlvasdlREADARYYVLGDTLLGRTLVAARLE 633

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  461 NIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESESFRKNL 540
Cdd:COG1196    634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713

                          570       580
                   ....*....|....*....|...
gi 2024438909  541 EESLHDKERLAEEIEKLRSELDQ 563
Cdd:COG1196    714 EERLEEELEEEALEEQLEAEREE 736
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 268-562 4.92e-10

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


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 63.16  E-value: 4.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  268 DETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLE 347
Cdd:pfam19220   45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  348 KRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKSD 427
Cdd:pfam19220  125 RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  428 PTSSTSSGDyqyvMEAKLQEMISIRRKAEERHGNIEERMRHleaqleeknqelQRARQREKMnEEHNKRLSDTvDRLLTE 507
Cdd:pfam19220  205 DATRARLRA----LEGQLAAEQAERERAEAQLEEAVEAHRA------------ERASLRMKL-EALTARAAAT-EQLLAE 266

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024438909  508 SNERLQlHLKERMAALEEKNV-LIQESESFRKNLEESLHDKERLAE---EIEKLRSELD 562
Cdd:pfam19220  267 ARNQLR-DRDEAIRAAERRLKeASIERDTLERRLAGLEADLERRTQqfqEMQRARAELE 324
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
309-571 8.44e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.54  E-value: 8.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  309 ETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLED----- 383
Cdd:PRK03918   161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeei 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  384 -----KNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKSDPTSSTSSgdyqyVMEAKLQEMISIRRKAEER 458
Cdd:PRK03918   241 eelekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI-----KLSEFYEEYLDELREIEKR 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  459 HGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdrlLTESNERLQ--LHLKERMAALEEKnVLIQESESF 536
Cdd:PRK03918   316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----LEERHELYEeaKAKKEELERLKKR-LTGLTPEKL 389

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2024438909  537 RKNLEESLHDKERLAEEIEKLRSELDQMKLRAGSL 571
Cdd:PRK03918   390 EKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 287-727 9.11e-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: 63.21  E-value: 9.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  287 MAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEerITTLEKRYLSAQRESTSIHDMNDK 366
Cdd:pfam15921  226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEI 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  367 LENELANKEAI-LRQLEDknrqlqerLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKSDPTSSTSSGDyQYVMEAkl 445
Cdd:pfam15921  304 IQEQARNQNSMyMRQLSD--------LESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERD-QFSQES-- 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  446 qemisirrkaeerhGNIEERMRHLEAQLEEKNQELQrarqrekMNEEHNKRLSD-------TVDRLLTESNER------- 511
Cdd:pfam15921  373 --------------GNLDDQLQKLLADLHKREKELS-------LEKEQNKRLWDrdtgnsiTIDHLRRELDDRnmevqrl 431

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  512 ----------LQLHLKERMAALEEKNVLIQESESFRKNLEESlhdKERLAEEIEKLRSEldQMKLRAGsliEPTLSrphl 581
Cdd:pfam15921  432 eallkamkseCQGQMERQMAAIQGKNESLEKVSSLTAQLEST---KEMLRKVVEELTAK--KMTLESS---ERTVS---- 499

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  582 DSSAELRYSVGSLVDSQSDYrsTKVirrprRGRMGVRRDEPK-VKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIddddR 660
Cdd:pfam15921  500 DLTASLQEKERAIEATNAEI--TKL-----RSRVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL----R 568

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024438909  661 ETLFSSMDLLSPSGHSDA--QTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNL 727
Cdd:pfam15921  569 QQIENMTQLVGQHGRTAGamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL 637
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
107-571 1.09e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.16  E-value: 1.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  107 AALTKELNACREQL---LEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVvkrqaqspSGVSSEVEVLKALKSL 183
Cdd:PRK03918   168 GEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--------EKLEKEVKELEELKEE 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  184 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQR-KIAAGEGPAESEHIEGMEPGQKVHEKRLSNG 262
Cdd:PRK03918   240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  263 SidsnDETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNskyQRDIREAMAQKEDMEER 342
Cdd:PRK03918   320 E----EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE---RLKKRLTGLTPEKLEKE 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  343 ITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDK-------NRQLQE--RLELAEQKLQQTMRKAETLPEVE 413
Cdd:PRK03918   393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcGRELTEehRKELLEEYTAELKRIEKELKEIE 472

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  414 AELAQRIAALTKSDPTSSTSSgdYQYVMEAKLQEMISIRRK-----------AEERHGNIEERMRHLEAQLEEKNQELQR 482
Cdd:PRK03918   473 EKERKLRKELRELEKVLKKES--ELIKLKELAEQLKELEEKlkkynleelekKAEEYEKLKEKLIKLKGEIKSLKKELEK 550

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  483 ARQREKMNEEHNKRLsDTVDRLLTESNERLQLHLKERMAALEEKnvlIQESESF----------RKNLEESLHDKERLAE 552
Cdd:PRK03918   551 LEELKKKLAELEKKL-DELEEELAELLKELEELGFESVEELEER---LKELEPFyneylelkdaEKELEREEKELKKLEE 626

                          490
                   ....*....|....*....
gi 2024438909  553 EIEKLRSELDQMKLRAGSL 571
Cdd:PRK03918   627 ELDKAFEELAETEKRLEEL 645
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 172-442 1.52e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 62.78  E-value: 1.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  172 SEVEVLKALKSLFEHHKALDEKVRERLrvslERVSALEEELAAANQEIVAL-REQNAHIQRKIAAGEGPAES--EHIEGM 248
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELE----KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASleRSIAEK 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  249 EPGQKVHEKRLSNGSIDSNDETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRD 328
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  329 IREAmaqKEDMEERITTLEKRYLSAQRESTSIHDMNdkleNELANKEAILRQLEDKNRQLQERLELAEQKLQQT------ 402
Cdd:TIGR02169  394 LEKL---KREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLaadlsk 466

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2024438909  403 -----MRKAETLPEVEAEL---AQRIAALTKSDPTSSTSSGDYQYVME 442
Cdd:TIGR02169  467 yeqelYDLKEEYDRVEKELsklQRELAEAEAQARASEERVRGGRAVEE 514
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 32-503 1.88e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 1.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   32 EQLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQMTVAAGTSIENNIQRTiscpNEFAALTK 111
Cdd:COG1196    371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE----EEEEALEE 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  112 ELNACREQLLEKEEEISELKAERNNTRLLLEHL-ECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLfehhKAL 190
Cdd:COG1196    447 AAEEEAELEEEEEALLELLAELLEEAALLEAALaELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL----RGL 522

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  191 DEKVRERLRVSLERVSALEEELAAANQEIVALREQNA-----HIQRKIAAGEGPAESEHIEGMEPGQKVHEKRLSNGSID 265
Cdd:COG1196    523 AGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAaaaieYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  266 SND-------ETSQVIELQELLEKQNYEMAQM-KERMAALSSRVGEVEQEAETA----RKELIKTEEMNSKYQRDIREAM 333
Cdd:COG1196    603 LVAsdlreadARYYVLGDTLLGRTLVAARLEAaLRRAVTLAGRLREVTLEGEGGsaggSLTGGSRRELLAALLEAEAELE 682

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  334 AQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVE 413
Cdd:COG1196    683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  414 AELAQRIAALtksdptsstssgdyqyvmEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEeknqELQRARQR-----EK 488
Cdd:COG1196    763 EELERELERL------------------EREIEALGPVNLLAIEEYEELEERYDFLSEQRE----DLEEARETleeaiEE 820

                          490
                   ....*....|....*
gi 2024438909  489 MNEEHNKRLSDTVDR 503
Cdd:COG1196    821 IDRETRERFLETFDA 835
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 53-558 2.18e-09

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: 62.37  E-value: 2.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   53 QESLSLAQQRLQDVIYDRDSLQRQLNSALPQMTVAAGTSIENNIQRTISC-----PNEFAALTKELNACREQLLEKEEEI 127
Cdd:TIGR00606  349 QGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLvierqEDEAKTAAQLCADLQSKERLKQEQA 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  128 SELKAERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPSGVSSEV-EVLKAL-KSLFEHHKALDEKVRERLrvsLERV 205
Cdd:TIGR00606  429 DEIRDEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSDRIlELDQELrKAERELSKAEKNSLTETL---KKEV 503

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  206 SALEEELAAANQEIVALREQNAHIQRKIAAgEGPAESEHIEGMEPGQKVHEkrlsNGSIDSNDETSQV------IELQEL 279
Cdd:TIGR00606  504 KSLQNEKADLDRKLRKLDQEMEQLNHHTTT-RTQMEMLTKDKMDKDEQIRK----IKSRHSDELTSLLgyfpnkKQLEDW 578

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  280 LEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQkEDMEERITTLEKRYLSAQRESTS 359
Cdd:TIGR00606  579 LHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQRAM 657

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  360 ihdmndkLENELANKEAILRQLEDKNRQ---LQERLELAEQKLQQTMRKAETlpeveaelaqriaaLTKSDPTSSTSSGD 436
Cdd:TIGR00606  658 -------LAGATAVYSQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQS--------------KLRLAPDKLKSTES 716

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  437 YQYVMEAKLQEMISirrKAEERHGNIEERMRHLEaQLEEKNQELQRARQREKMNEEHNKRLSDTV-------DRLLTESN 509
Cdd:TIGR00606  717 ELKKKEKRRDEMLG---LAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTImpeeesaKVCLTDVT 792

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024438909  510 --ERLQLHLKERMAALEEKNVLIQESE------SFRKNLEESLHDKERLAEEIEKLR 558
Cdd:TIGR00606  793 imERFQMELKDVERKIAQQAAKLQGSDldrtvqQVNQEKQEKQHELDTVVSKIELNR 849
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
40-502 3.26e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 61.59  E-value: 3.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQMTvAAGTSIENNIQ-------RTISCPNEFAALTKE 112
Cdd:PRK02224   293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ-AHNEEAESLREdaddleeRAEELREEAAELESE 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  113 LNACREQLLEKEEEISELKAERNNTRL-----------LLEHLECLVSRHERslrmtVVKRQAQSPSGVSSEVEVLKALK 181
Cdd:PRK02224   372 LEEAREAVEDRREEIEELEEEIEELRErfgdapvdlgnAEDFLEELREERDE-----LREREAELEATLRTARERVEEAE 446

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  182 SLFEHHKA-------LDEKVRERLRVSLERVSALEEELAaanqeivALREQNAHIQRKIAAGEGPAESE-HIEGMEPGQK 253
Cdd:PRK02224   447 ALLEAGKCpecgqpvEGSPHVETIEEDRERVEELEAELE-------DLEEEVEEVEERLERAEDLVEAEdRIERLEERRE 519

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  254 VHEKRLSNGSIDSNDETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELiktEEMNSKYQR--DIRE 331
Cdd:PRK02224   520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL---AELKERIESleRIRT 596

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  332 AMAQKEDMEERITTL-EKRylsaqresTSIHDMNDKLENELANKEAILRQLEDK---NR--QLQERLELAEQKLQQTMRK 405
Cdd:PRK02224   597 LLAAIADAEDEIERLrEKR--------EALAELNDERRERLAEKRERKRELEAEfdeARieEAREDKERAEEYLEQVEEK 668

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  406 AETLPEVEAELAQRIAALtksdptsstssgdyqyvmEAKLQEMISIRrkaeERHGNIEERMRHLEAqLEEKNQELQ---- 481
Cdd:PRK02224   669 LDELREERDDLQAEIGAV------------------ENELEELEELR----ERREALENRVEALEA-LYDEAEELEsmyg 725

                          490       500
                   ....*....|....*....|...
gi 2024438909  482 --RARQREKMNEEHNKRLSDTVD 502
Cdd:PRK02224   726 dlRAELRQRNVETLERMLNETFD 748
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 41-571 4.48e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 61.24  E-value: 4.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   41 ERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSAlpqmtvaaGTSIENNIQRTISCPNEFAALTKELNACREQL 120
Cdd:TIGR02169  302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL--------EREIEEERKRRDKLTEEYAELKEELEDLRAEL 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  121 LEKE--------------EEISELKAERNNTRLLLEHL-ECLVSRHERSLRM-----TVVKRQAQSPSGVSSEVEVLKAL 180
Cdd:TIGR02169  374 EEVDkefaetrdelkdyrEKLEKLKREINELKRELDRLqEELQRLSEELADLnaaiaGIEAKINELEEEKEDKALEIKKQ 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  181 KSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRkiAAGEGPAESEHIEGMEPG--------Q 252
Cdd:TIGR02169  454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE--RVRGGRAVEEVLKASIQGvhgtvaqlG 531

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  253 KVHEK-----------RLSNGSIDSNDETSQVIELqeLLEKQNYEMA-------QMKERMAALSSRVGEVE--------- 305
Cdd:TIGR02169  532 SVGERyataievaagnRLNNVVVEDDAVAKEAIEL--LKRRKAGRATflplnkmRDERRDLSILSEDGVIGfavdlvefd 609

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  306 -----------------QEAETARKELI-------------------------KTEEMNSKYQRD-IREAMAQKEDMEER 342
Cdd:TIGR02169  610 pkyepafkyvfgdtlvvEDIEAARRLMGkyrmvtlegelfeksgamtggsrapRGGILFSRSEPAeLQRLRERLEGLKRE 689

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  343 ITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA 422
Cdd:TIGR02169  690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  423 LTKSDPTSSTSSGD-YQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRArqREKMNEEHNKRlsdtv 501
Cdd:TIGR02169  770 LEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQR----- 842

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  502 dRLLTESNERLQLHLKERMAALEEKNVLIQESESFRKNLEESLHDkerLAEEIEKLRSELDQMKLRAGSL 571
Cdd:TIGR02169  843 -IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEEL 908
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 930-996 5.10e-09

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 53.84  E-value: 5.10e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024438909   930 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 996
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
105-537 5.57e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 60.55  E-value: 5.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  105 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHE------------RSLRMTVVKRQAQSPSGVSS 172
Cdd:COG4717     89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleaelaelperlEELEERLEELRELEEELEEL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  173 EVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGPAESEHIEgmepgQ 252
Cdd:COG4717    169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-----E 243

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  253 KVHEKRLS-------------NGSIDSNDETSQ---------VIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAET 310
Cdd:COG4717    244 RLKEARLLlliaaallallglGGSLLSLILTIAgvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE 323

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  311 ARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKnRQLQE 390
Cdd:COG4717    324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKE 402

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  391 RLELAEQKLQQTMRKAETLPEV--EAELAQRIAALtksdptsstssgdyqyvmEAKLQEMISIRRKAEERHGNIEERMRH 468
Cdd:COG4717    403 ELEELEEQLEELLGELEELLEAldEEELEEELEEL------------------EEELEELEEELEELREELAELEAELEQ 464

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  469 LEAQ--LEEKNQELQRARQREKMNEEHNKRL---SDTVDRLLTESNERLQLHLKERMAAL-------EEKNVLIQESESF 536
Cdd:COG4717    465 LEEDgeLAELLQELEELKAELRELAEEWAALklaLELLEEAREEYREERLPPVLERASEYfsrltdgRYRLIRIDEDLSL 544


                   .
gi 2024438909  537 R 537
Cdd:COG4717    545 K 545
PTZ00121 PTZ00121
MAEBL; Provisional
 171-568 6.07e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.93  E-value: 6.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  171 SSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGPAESEHIEGMEP 250
Cdd:PTZ00121  1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  251 GQKVHEKRLSNGSIDSNDETSQVIELQELLEKQnyEMAQMKERMAALSSRVGEVEQEAETARK--ELIKTEEMNSKYQRD 328
Cdd:PTZ00121  1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA--KKAEEAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADE 1501

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  329 IREAMAQKEDMEERITTLEKRYL------SAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLElaEQKLQQT 402
Cdd:PTZ00121  1502 AKKAAEAKKKADEAKKAEEAKKAdeakkaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA--EEDKNMA 1579

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  403 MRKAETLPEVEAELAQRIAALTKSDPTSSTSSGDYQYVMEAKLQEMI---SIRRKAEERHGNIEERMRHLEaQLEEKNQE 479
Cdd:PTZ00121  1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKkaeEEKKKVEQLKKKEAEEKKKAE-ELKKAEEE 1658

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  480 LQRARQREKMNEEHNKRLSDTVDRllTESNERLQLHLKERMAalEEKnvliQESESFRKNLEESLHDKERLAEEIEKLRS 559
Cdd:PTZ00121  1659 NKIKAAEEAKKAEEDKKKAEEAKK--AEEDEKKAAEALKKEA--EEA----KKAEELKKKEAEEKKKAEELKKAEEENKI 1730


                   ....*....
gi 2024438909  560 ELDQMKLRA 568
Cdd:PTZ00121  1731 KAEEAKKEA 1739
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 41-573 1.13e-08

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: 59.69  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   41 ERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNsalpqmtvAAGTSIENNIQRTISCPNEFAALTKELNACREQL 120
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQ--------ELEEKLEELRLEVSELEEEIEELQKELYALANEI 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  121 LEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvKRQAQSPSGVSSEVEVLKALKSLFEhhKALDEKvRERLRV 200
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEELEAQLEELESKL-----DELAEELAELEEKLEELKEELESLE--AELEEL-EAELEE 369

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  201 SLERVSALEEELAAANQEIVALREQ----NAHIQR---KIAAGEGPAESEHIEGMEPGQKVHEKRLSNGSIDSNDETSQV 273
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQiaslNNEIERleaRLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL 449

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  274 IELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEM---NSKYQRDIREAMAQKEDMEERITTLEKRY 350
Cdd:TIGR02168  450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqenLEGFSEGVKALLKNQSGLSGILGVLSELI 529

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  351 LSAQRESTSIH-----DMNDKL-ENELANKEAI--LRQLE-----------DKNRQLQERLELAEQKLQQTMRKAETLPE 411
Cdd:TIGR02168  530 SVDEGYEAAIEaalggRLQAVVvENLNAAKKAIafLKQNElgrvtflpldsIKGTEIQGNDREILKNIEGFLGVAKDLVK 609

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  412 VEAEL-------------------AQRIAALTKSDPTSSTSSGD-----YQYVMEAKLQEMISIRRKAEERhgNIEERMR 467
Cdd:TIGR02168  610 FDPKLrkalsyllggvlvvddldnALELAKKLRPGYRIVTLDGDlvrpgGVITGGSAKTNSSILERRREIE--ELEEKIE 687

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  468 HLEAQLEEKNQELQRAR-QREKMNEEHNK--RLSDTVDRLLTESNERLQLHLKERMAALE-------EKNVLIQESESFR 537
Cdd:TIGR02168  688 ELEEKIAELEKALAELRkELEELEEELEQlrKELEELSRQISALRKDLARLEAEVEQLEEriaqlskELTELEAEIEELE 767

                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 2024438909  538 KNLEESLHDKERLAEEIEKLRSELDQMKLRAGSLIE 573
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 30-485 1.65e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 59.36  E-value: 1.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   30 HFEQLMVNMLDERDRLLDTLRETQESLSLAQQRlQDVIYDRDS--------LQRQLN------SALPQMTVAAGTSIENN 95
Cdd:pfam15921  367 QFSQESGNLDDQLQKLLADLHKREKELSLEKEQ-NKRLWDRDTgnsitidhLRRELDdrnmevQRLEALLKAMKSECQGQ 445

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   96 IQR---TISCPNE----FAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKrQAQSPS 168
Cdd:pfam15921  446 MERqmaAIQGKNEslekVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE-ITKLRS 524

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  169 GVSSEVEVLKALKSLFEHhkaldekvrerLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGPAESEHIEGM 248
Cdd:pfam15921  525 RVDLKLQELQHLKNEGDH-----------LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  249 EPGQKVHEKR--LSNGSIDSNDETSQVIELQELLEKQNYEMAQM----KERMAALSSRVGEVEQ---EAETARKELIKTE 319
Cdd:pfam15921  594 QLEKEINDRRleLQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQllnEVKTSRNELNSLS 673

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  320 EMNSKYQRDIREamaQKEDMEERITTLEKRYLSAQRE----STSIHDMNDKLENELANKEAILRQLEDKNRQ---LQERL 392
Cdd:pfam15921  674 EDYEVLKRNFRN---KSEEMETTTNKLKMQLKSAQSEleqtRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidaLQSKI 750

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  393 ELAEQKLQQTMRKAETLPEVEAELAQRIAaltksdpTSSTSSGDyqyvMEAKLQEMISIRRKAEERHGNIEERMRHLEAQ 472
Cdd:pfam15921  751 QFLEEAMTNANKEKHFLKEEKNKLSQELS-------TVATEKNK----MAGELEVLRSQERRLKEKVANMEVALDKASLQ 819

                          490
                   ....*....|...
gi 2024438909  473 LEEKNQELQRARQ 485
Cdd:pfam15921  820 FAECQDIIQRQEQ 832
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 40-571 1.71e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 59.36  E-value: 1.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   40 DERDRLLDTLRETQESLSLAQQRLQD----------VIYDRDSLQRQLNSALPQMTVAAGTSI-ENNIQRTISCPNEFAA 108
Cdd:pfam15921  142 DLRNQLQNTVHELEAAKCLKEDMLEDsntqieqlrkMMLSHEGVLQEIRSILVDFEEASGKKIyEHDSMSTMHFRSLGSA 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  109 LTK-------ELNACREQLLEKEEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-----RMTVVKRQAQSpsgVS 171
Cdd:pfam15921  222 ISKilreldtEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglteKASSARSQANS---IQ 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  172 SEVEV------------LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQR-------- 231
Cdd:pfam15921  299 SQLEIiqeqarnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnlddq 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  232 --KIAAGEGPAESEHIEGMEPGQKVHEKRLSNG-SIDS-----NDETSQVIELQELLEKQNYE-MAQMKERMAAL----- 297
Cdd:pfam15921  379 lqKLLADLHKREKELSLEKEQNKRLWDRDTGNSiTIDHlrrelDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIqgkne 458

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  298 -----SSRVGEVEQEAETARK---ELIK---TEEMNSKYQRDIREAMAQKEDMEE----RITTLEKRYLSAQRESTSIHD 362
Cdd:pfam15921  459 slekvSSLTAQLESTKEMLRKvveELTAkkmTLESSERTVSDLTASLQEKERAIEatnaEITKLRSRVDLKLQELQHLKN 538

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  363 MNDKLENELANKEAILRQLEDKNR-------------------------------QLQE-----RLELAEQKLQQTMRKA 406
Cdd:pfam15921  539 EGDHLRNVQTECEALKLQMAEKDKvieilrqqienmtqlvgqhgrtagamqvekaQLEKeindrRLELQEFKILKDKKDA 618

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  407 EtLPEVEAELA--------------QRIAALTKSDPTS-------STSSGDYQYVMEAKLQEMISIRRKAEErhgnIEER 465
Cdd:pfam15921  619 K-IRELEARVSdlelekvklvnagsERLRAVKDIKQERdqllnevKTSRNELNSLSEDYEVLKRNFRNKSEE----METT 693

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  466 MRHLEAQLEEKNQELQRARQREKMNEE---HNKRLSDTVDRLLTES-------NERLQLhLKERMA-ALEEKNVLIQESE 534
Cdd:pfam15921  694 TNKLKMQLKSAQSELEQTRNTLKSMEGsdgHAMKVAMGMQKQITAKrgqidalQSKIQF-LEEAMTnANKEKHFLKEEKN 772

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 2024438909  535 SFRKNLEESLHDKERLAEEIEKLRSELDQMKLRAGSL 571
Cdd:pfam15921  773 KLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANM 809
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 244-581 1.89e-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: 1.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  244 HIEGMEPGQKVHEKRLSNGSIdSNDETSQVIELQELLEKQNYEMAqmkERMAALSS-RVGEVEQEAETARKELIKTEEMN 322
Cdd:TIGR00618  100 HRKTEQPEQLYLEQKKGRGRI-LAAKKSETEEVIHDLLKLDYKTF---TRVVLLPQgEFAQFLKAKSKEKKELLMNLFPL 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  323 SKYQRDIREAMAQKEDMEERITTLEKRY----LSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQK 398
Cdd:TIGR00618  176 DQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ 255

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  399 LQQTMRKAETLPEVEaELAQRIAALTKSDPTSSTSSGDYQYVMEAKlqEMISIRRKAEERHGNIEERMRHLE-------- 470
Cdd:TIGR00618  256 LKKQQLLKQLRARIE-ELRAQEAVLEETQERINRARKAAPLAAHIK--AVTQIEQQAQRIHTELQSKMRSRAkllmkraa 332

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  471 -AQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlQLHLKERMAALEEKNVLIQESESFRKNLEESLHDKER 549
Cdd:TIGR00618  333 hVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ--QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQA 410

                          330       340       350
                   ....*....|....*....|....*....|..
gi 2024438909  550 LAEEIEKLRSELDQMKLRAGSLIEPTLSRPHL 581
Cdd:TIGR00618  411 TIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 48-587 1.99e-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: 58.93  E-value: 1.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   48 TLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALP--QMTVAAGTSIENNIQRTISCPNEFAALTKELnacREQLLEKEE 125
Cdd:TIGR02169  379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEelQRLSEELADLNAAIAGIEAKINELEEEKEDK---ALEIKKQEW 455

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  126 EISELKAERNNTRLLLEHLECLVSRHERSLRMT------VVKRQAQSPSGVSSEVEVLKALKSLFEHHKALdekVRERLR 199
Cdd:TIGR02169  456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLqrelaeAEAQARASEERVRGGRAVEEVLKASIQGVHGT---VAQLGS 532

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  200 VSLERVSALEEELAAANQEIVALREQNAH--IQRKIAAGEGPAESEHIEGMEPGQKVHEKRLSNGSI---------DSND 268
Cdd:TIGR02169  533 VGERYATAIEVAAGNRLNNVVVEDDAVAKeaIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIgfavdlvefDPKY 612

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  269 ETSQVIELQELLEKQNYEMAQ---MKERMAALSSRVGEvEQEAETARKELIKTEEMNSKYQRDIREAMAQK-EDMEERIT 344
Cdd:TIGR02169  613 EPAFKYVFGDTLVVEDIEAARrlmGKYRMVTLEGELFE-KSGAMTGGSRAPRGGILFSRSEPAELQRLRERlEGLKRELS 691

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  345 TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALT 424
Cdd:TIGR02169  692 SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  425 KSDPTSSTSSGD-YQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEA----------QLEEKNQELQRARQREKMNEEH 493
Cdd:TIGR02169  772 EDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrltlekeYLEKEIQELQEQRIDLKEQIKS 851

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  494 NKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESESFRKNLEESLHDKERLAEEIEKLRSELDQMKLRAGSL-- 571
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALee 931

                          570       580
                   ....*....|....*....|
gi 2024438909  572 ----IEPTLSRPHLDSSAEL 587
Cdd:TIGR02169  932 elseIEDPKGEDEEIPEEEL 951
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 277-539 3.09e-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: 57.47  E-value: 3.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  277 QELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYLSAQRE 356
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  357 StsihdmnDKLENELANkeaILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALtksdptsstssgd 436
Cdd:COG4942     99 L-------EAQKEELAE---LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL------------- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  437 yqyvmEAKLQEMISIRRKAEERHgnieERMRHLEAQLEEKNQELQRAR-QREKMNEEHNKRLSDTVDRL--LTESNERLQ 513
Cdd:COG4942    156 -----RADLAELAALRAELEAER----AELEALLAELEEERAALEALKaERQKLLARLEKELAELAAELaeLQQEAEELE 226

                          250       260
                   ....*....|....*....|....*.
gi 2024438909  514 lHLKERMAALEEKNVLIQESESFRKN 539
Cdd:COG4942    227 -ALIARLEAEAAAAAERTPAAGFAAL 251
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
39-425 3.62e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.86  E-value: 3.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQMTVAAGTSIENNIQRTISCPNEFAALTKELNACRE 118
Cdd:COG4717    141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  119 QLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERL 198
Cdd:COG4717    221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  199 RVSLERVSALEEELAAANQEivalreqnahIQRKIAAGEGPAESEHIEGMEPGQKVHEKRLSNGSIDSNDETSQVI---- 274
Cdd:COG4717    301 GKEAEELQALPALEELEEEE----------LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEeleq 370

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  275 ELQELLEKQN-------YEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKyqrdiREAMAQKEDMEERITTLE 347
Cdd:COG4717    371 EIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELE 445

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  348 KRYLSAQRESTSIHDMNDKLEN--ELANKEAILRQLEDKNRQLQER---LELAEQKLQQTMRKA--ETLPEVEAELAQRI 420
Cdd:COG4717    446 EELEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEwaaLKLALELLEEAREEYreERLPPVLERASEYF 525


                   ....*
gi 2024438909  421 AALTK 425
Cdd:COG4717    526 SRLTD 530
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 45-564 4.68e-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: 57.67  E-value: 4.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   45 LLDTLRE---TQESLSLAQQRLQ-DVIYDRDSLQRQLNSAlPQMTVAAGTSIENNIQRTISCPNEFAALT--KELNACRE 118
Cdd:TIGR00618  401 ELDILQReqaTIDTRTSAFRDLQgQLAHAKKQQELQQRYA-ELCAAAITCTAQCEKLEKIHLQESAQSLKerEQQLQTKE 479

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  119 QLLEKEEEISELKAERNNtrlLLEHLECLVsrhERSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKALdEKVRERL 198
Cdd:TIGR00618  480 QIHLQETRKKAVVLARLL---ELQEEPCPL---CGSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSE-EDVYHQL 551

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  199 RVSLERVSALEEELAAANQEIVALREQnahiqrkiaagegpaESEHIEGMEPGQKVHEKRLSNGSIDSNDETSQVIELQE 278
Cdd:TIGR00618  552 TSERKQRASLKEQMQEIQQSFSILTQC---------------DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA 616

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  279 LLEKQNYEMAqmKERMAALSSRVGEVEQEAETArkeliKTEEMNSKYQRDIREAMAqkedmeeRITTLEKRYLsAQREST 358
Cdd:TIGR00618  617 LLRKLQPEQD--LQDVRLHLQQCSQELALKLTA-----LHALQLTLTQERVREHAL-------SIRVLPKELL-ASRQLA 681

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  359 SihdmnDKLENELANKEAILRQLEDKNRQLQERlelaEQKLQQTMRKAEtlpEVEAELAQRIAALTKSDPTSSTSSGDYQ 438
Cdd:TIGR00618  682 L-----QKMQSEKEQLTYWKEMLAQCQTLLREL----ETHIEEYDREFN---EIENASSSLGSDLAAREDALNQSLKELM 749

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  439 YVMEAKLQEMISIRRKAEERHGNIEER---MRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH 515
Cdd:TIGR00618  750 HQARTVLKARTEAHFNNNEEVTAALQTgaeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQE 829

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2024438909  516 LKERMAALEEKNVLIQESESFRKNLEESLHDKERLAEEIEKLRSELDQM 564
Cdd:TIGR00618  830 EEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
mukB PRK04863
chromosome partition protein MukB;
195-559 4.85e-08

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 57.66  E-value: 4.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  195 RERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAA---GEGPAESEHIEGMEPGQKVHEKRLSNGSIDSNDEts 271
Cdd:PRK04863   278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAElneAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA-- 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  272 QVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELikteemnSKYQR--DIREAMAQKedmeerittlekr 349
Cdd:PRK04863   356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQL-------ADYQQalDVQQTRAIQ------------- 415

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  350 YLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTmRKAETLPEVEAELAQRIAaltksDPT 429
Cdd:PRK04863   416 YQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRKIA-----GEV 489

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  430 SSTssgdyqyvmEAKLQEMISIRRKAEERHgnIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSN 509
Cdd:PRK04863   490 SRS---------EAWDVARELLRRLREQRH--LAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD-----DE 553

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024438909  510 ERLQLHLKERMAALEEknvLIQESESFRKNLEESLHDKERLAEEIEKLRS 559
Cdd:PRK04863   554 DELEQLQEELEARLES---LSESVSEARERRMALRQQLEQLQARIQRLAA 600
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
107-459 5.28e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.62  E-value: 5.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  107 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQspsgvssevevlkalkslfeh 186
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIA--------------------- 671

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  187 hkALDEKvRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEgpaesEHIEGMEPGQKVHEKRLSNGSIDS 266
Cdd:COG4913    672 --ELEAE-LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE-----KELEQAEEELDELQDRLEAAEDLA 743

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  267 NDETSQviELQELLEKQNYEmAQMKERMAALSSRVGEVEQEAETARKELIKT-EEMNSKYQRDIREAMAQKEDMEE---R 342
Cdd:COG4913    744 RLELRA--LLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERAmRAFNREWPAETADLDADLESLPEylaL 820

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  343 ITTLEKRYLSAQREstsihDMNDKL-ENELANKEAILRQLEDKNRQLQERLELAEQKLQQ------TMRKAETLPEVEAE 415
Cdd:COG4913    821 LDRLEEDGLPEYEE-----RFKELLnENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRipfgpgRYLRLEARPRPDPE 895

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 2024438909  416 LAQRIAALTKSDPTSSTSSGDYQYVMEAKLQEMISIRRKAEERH 459
Cdd:COG4913    896 VREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRSEEEES 939
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 44-425 9.84e-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: 56.61  E-value: 9.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   44 RLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQMTVAAGT--SIENNIQRTiscPNEFAALTKELNACREQLL 121
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigEIEKEIEQL---EQEEEKLKERLEELEEDLS 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  122 EKEEEISELKAErnntrllLEHLECLVSRHERSLrmtvvkrqaqspSGVSSEVEVLKA--LKSLFEHHKALDEKVRERLR 199
Cdd:TIGR02169  748 SLEQEIENVKSE-------LKELEARIEELEEDL------------HKLEEALNDLEArlSHSRIPEIQAELSKLEEEVS 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  200 VSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGPAESEhiegmepGQKVHEKRLsngsidsndetsQVIELQEL 279
Cdd:TIGR02169  809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-------EKEIENLNG------------KKEELEEE 869

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  280 LEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTS 359
Cdd:TIGR02169  870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE 949

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024438909  360 IHDMnDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 425
Cdd:TIGR02169  950 ELSL-EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1056-1111 1.10e-07

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.99  E-value: 1.10e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024438909  1056 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1111
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 274-425 1.13e-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: 54.16  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  274 IELQELLEkqnyEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKR---- 349
Cdd:COG1579     10 LDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnv 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  350 -----YLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALT 424
Cdd:COG1579     86 rnnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEELE 162


                   .
gi 2024438909  425 K 425
Cdd:COG1579    163 A 163
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
176-567 1.60e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  176 VLKALKSLFEhhKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEgpAESEHIEGMEPGQKVH 255
Cdd:COG4717     39 LLAFIRAMLL--ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE--ELEEELEELEAELEEL 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  256 EKRLsngsidsnDETSQVIELQELLEkqnyEMAQMKERMAALSSRVGEVEQEAEtARKELIKTEEMNSKYQRDIREAMAQ 335
Cdd:COG4717    115 REEL--------EKLEKLLQLLPLYQ----ELEALEAELAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEE 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  336 KED-----MEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDknrqlqerlELAEQKLQQTMRKAETLP 410
Cdd:COG4717    182 LLEqlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN---------ELEAAALEERLKEARLLL 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  411 EVEAELAQrIAALTKSDPTSSTSSGDYQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMN 490
Cdd:COG4717    253 LIAAALLA-LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  491 EEhnkrLSDTVDRLLTESNERLQLHLKERMAALEEknVLIQESESFRKNL--------EESLHDKERLAEEIEKLRSELD 562
Cdd:COG4717    332 PD----LSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEIAALlaeagvedEEELRAALEQAEEYQELKEELE 405


                   ....*
gi 2024438909  563 QMKLR 567
Cdd:COG4717    406 ELEEQ 410
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
177-565 3.48e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.77  E-value: 3.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  177 LKALKSLFEHHKALDEKVrERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGPAE----SEHIEGMEPGQ 252
Cdd:COG4717     70 LKELKELEEELKEAEEKE-EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQElealEAELAELPERL 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  253 KVHEKRLSngsidsndetsQVIELQELLEKQNYEMAQMKERMAALSSRVG-EVEQEAETARKELIKTEEMNSKYQRDIRE 331
Cdd:COG4717    149 EELEERLE-----------ELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEE 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  332 AMAQKEDMEERITTLEKRYLSAQREST------------------SIHDMNDKLENELANKEAILRQLEDKNRQLQERLE 393
Cdd:COG4717    218 AQEELEELEEELEQLENELEAAALEERlkearlllliaaallallGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  394 LAEQKLQQTMRKAETLPEVEAELAQRIAALTKSDPTSSTSSGDYQYVMEAKLQEMISIRRKAEERHgNIEERMRHLEAQL 473
Cdd:COG4717    298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-QLEELEQEIAALL 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  474 EEKNQE--------LQRARQREKMNEEhnkrlsdtvdrlLTESNERLQLHLKERMAALE--EKNVLIQESESFRKNLEES 543
Cdd:COG4717    377 AEAGVEdeeelraaLEQAEEYQELKEE------------LEELEEQLEELLGELEELLEalDEEELEEELEELEEELEEL 444

                          410       420
                   ....*....|....*....|..
gi 2024438909  544 LHDKERLAEEIEKLRSELDQMK 565
Cdd:COG4717    445 EEELEELREELAELEAELEQLE 466
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
289-561 4.28e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 4.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  289 QMKERMAALSsrvgEVEQEAETARKELIKTEEMNSKYQRdIREAMAQKEDMEERITTLekRYLSAQREStsihdmnDKLE 368
Cdd:COG4913    229 ALVEHFDDLE----RAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAAL--RLWFAQRRL-------ELLE 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  369 NELANKEAILRQLEDKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQ----RIAALtksdptsstssgdyqyvmEAK 444
Cdd:COG4913    295 AELEELRAELARLEAELERLEARLDALREELD----------ELEAQIRGnggdRLEQL------------------ERE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  445 LQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREkmneehnKRLSDTVDRLLTESNERLQLHLKERMAALE 524
Cdd:COG4913    347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA-------AALLEALEEELEALEEALAEAEAALRDLRR 419

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2024438909  525 EKNVLIQESESFRK---NLEESLHD-KERLAEEIEKLRSEL 561
Cdd:COG4913    420 ELRELEAEIASLERrksNIPARLLAlRDALAEALGLDEAEL 460
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 175-356 4.61e-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: 52.23  E-value: 4.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  175 EVLKALKSLFEHHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEgpaesEHIEGMEPGQKV 254
Cdd:COG1579      4 EDLRALLDLQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE-----LEIEEVEARIKK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  255 HEKRLsnGSIDSNDEtsqvielQELLEKqnyEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMA 334
Cdd:COG1579     78 YEEQL--GNVRNNKE-------YEALQK---EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145

                          170       180
                   ....*....|....*....|..
gi 2024438909  335 QKEDMEERITTLEKRyLSAQRE 356
Cdd:COG1579    146 ELDEELAELEAELEE-LEAERE 166
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 53-636 4.83e-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: 54.46  E-value: 4.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   53 QESLSLAQQRLQDVIYDRDSLQRQLNSAlPQMTvaagtSIENNIQRTISCPNEFAALTKELNACREQLLEKEEEISELKA 132
Cdd:pfam12128  213 PPKSRLNRQQVEHWIRDIQAIAGIMKIR-PEFT-----KLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSA 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  133 ERNnTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVEVLKalkslfEHHKALDEKVRERLRVSLERVSALEEEL 212
Cdd:pfam12128  287 ELN-QLLRTLDDQWKEKRDELNGELSAADAAVAK---DRSELEALE------DQHGAFLDADIETAAADQEQLPSWQSEL 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  213 AAANQEIVALREQNAHIQRKIAAGEGPAESEH---IEGMEPGQ-KVHEKRLSNGSIDSNDETSQVIELQELLEKQNYEMA 288
Cdd:pfam12128  357 ENLEERLKALTGKHQDVTAKYNRRRSKIKEQNnrdIAGIKDKLaKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  289 QMKERmaaLSSRVGE--VEQEAETARKELIKteemnskyqrDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDK 366
Cdd:pfam12128  437 EEEYR---LKSRLGElkLRLNQATATPELLL----------QLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ 503

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  367 LENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKaeTLPEVEAELAQRIA-AL---TKSDPTSSTSSG------- 435
Cdd:pfam12128  504 ASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRK--EAPDWEQSIGKVISpELlhrTDLDPEVWDGSVggelnly 581

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  436 ----DYQYV-------MEAKLQEMISIRRK----AEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDT 500
Cdd:pfam12128  582 gvklDLKRIdvpewaaSEEELRERLDKAEEalqsAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDE 661

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  501 VDRL---LTESNERLQLHLKERMAALE-EKNVLIQESESF-----RKNLEESLHDKERLAEEIEKLRSELDQMKlrAGSL 571
Cdd:pfam12128  662 KQSEkdkKNKALAERKDSANERLNSLEaQLKQLDKKHQAWleeqkEQKREARTEKQAYWQVVEGALDAQLALLK--AAIA 739

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024438909  572 IEPTLSRPHLDSSAELRY-SVGSL-VDSQSDYRSTKVIRRPRRGRMGVRRDEPKVKSLgdHEWNRTQ 636
Cdd:pfam12128  740 ARRSGAKAELKALETWYKrDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY--FDWYQET 804
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
37-560 5.37e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 5.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   37 NMLDERD---------RLLDTLRETQESLSLAQQR---LQDVIYDRDSLQRQLNSALPQMTVAAGTSIENNIQRtiscpn 104
Cdd:COG4913    216 YMLEEPDtfeaadalvEHFDDLERAHEALEDAREQielLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR------ 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  105 eFAALTKELNACREQLLEKEEEISELKAERNNTRLL---------------LEHLECLVSRHERSLRMTVVKRQAQS--- 166
Cdd:COG4913    290 -LELLEAELEELRAELARLEAELERLEARLDALREEldeleaqirgnggdrLEQLEREIERLERELEERERRRARLEall 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  167 -------PSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQN-------AHIQRK 232
Cdd:COG4913    369 aalglplPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniparlLALRDA 448

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  233 IAAGEGPAES------EHIEgMEPGQKV---------------------HEKRLSNgSIDSNDETSQVIELQELLEKQNY 285
Cdd:COG4913    449 LAEALGLDEAelpfvgELIE-VRPEEERwrgaiervlggfaltllvppeHYAAALR-WVNRLHLRGRLVYERVRTGLPDP 526

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  286 EMAQMKERM-------------AALSSRVGE------VEQEAETARKE-------LIKTEemNSKYQRDIREAMAQK--- 336
Cdd:COG4913    527 ERPRLDPDSlagkldfkphpfrAWLEAELGRrfdyvcVDSPEELRRHPraitragQVKGN--GTRHEKDDRRRIRSRyvl 604

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  337 -EDMEERITTLEKRYlsaqrestsihdmnDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAEtLPEVEAE 415
Cdd:COG4913    605 gFDNRAKLAALEAEL--------------AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAERE 669

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  416 LA---QRIAALTKSDPTSSTssgdyqyvMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQRekmnee 492
Cdd:COG4913    670 IAeleAELERLDASSDDLAA--------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR------ 735

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024438909  493 hnkrlsdtVDRLLTESNERLQLHLKERMAALEEKNVLIQESESFRKNLEESLHDKERLAEEIEKLRSE 560
Cdd:COG4913    736 --------LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1134-1205 6.49e-07

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 47.68  E-value: 6.49e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909  1134 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1205
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 323-571 7.21e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 7.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  323 SKYQRDIREAMAQKEDMEERITTLE---------KRYLSAQRESTSI-HDMNDKLENelANKEAILRQLEDKNRQLqERL 392
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDRLEdilnelerqLKSLERQAEKAERyKELKAELRE--LELALLVLRLEELREEL-EEL 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  393 ELAEQKLQQTMRKAET-LPEVEAELAQRIAALTKSDptssTSSGDYQyvmeAKLQEMISIRRKAEERHGNIEERMRHLEA 471
Cdd:TIGR02168  245 QEELKEAEEELEELTAeLQELEEKLEELRLEVSELE----EEIEELQ----KELYALANEISRLEQQKQILRERLANLER 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  472 QLEEKNQELQRARQRekmneehnkrlSDTVDRLLTESNERLQLhLKERMAALEEKnvlIQESESFRKNLEESLHDKErla 551
Cdd:TIGR02168  317 QLEELEAQLEELESK-----------LDELAEELAELEEKLEE-LKEELESLEAE---LEELEAELEELESRLEELE--- 378

                          250       260
                   ....*....|....*....|
gi 2024438909  552 EEIEKLRSELDQMKLRAGSL 571
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASL 398
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
353-562 7.21e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.89  E-value: 7.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  353 AQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELA---QRIAALTKSDPT 429
Cdd:PRK02224   197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEdlrETIAETEREREE 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  430 SSTSSGDYQYVMEAKLQEMISIRRKAEERHGNIE---ERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT 506
Cdd:PRK02224   277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEaveARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024438909  507 ESNErlqlhLKERMAALEEknvliqESESFRKNLEESLHDKERLAEEIEKLRSELD 562
Cdd:PRK02224   357 RAEE-----LREEAAELES------ELEEAREAVEDRREEIEELEEEIEELRERFG 401
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 41-566 7.78e-07

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 53.82  E-value: 7.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   41 ERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQMTVAAGTSIENNIQ---RTISC------------PNE 105
Cdd:TIGR00618  308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsiREISCqqhtltqhihtlQQQ 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  106 FAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAqSPSGVSSEVEVLKALKSLFE 185
Cdd:TIGR00618  388 KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAA-ITCTAQCEKLEKIHLQESAQ 466

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  186 HHKALDEKV--RERLRVSLERVSALEEELAAANQEI-VALREQNAHI-QRKIAAGEGPAESEHIEGMEPGQKVHEKRLSN 261
Cdd:TIGR00618  467 SLKEREQQLqtKEQIHLQETRKKAVVLARLLELQEEpCPLCGSCIHPnPARQDIDNPGPLTRRMQRGEQTYAQLETSEED 546

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  262 GSIDSNDETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELikteEMNSKYQRDIREAM-AQKEDME 340
Cdd:TIGR00618  547 VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT----EKLSEAEDMLACEQhALLRKLQ 622

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  341 ERITTLEKRYLSAQrestsihdmndkLENELANKEAILRQLEDKNRQLQERLELAEQKLQQtMRKAETLPEVEAELAQRI 420
Cdd:TIGR00618  623 PEQDLQDVRLHLQQ------------CSQELALKLTALHALQLTLTQERVREHALSIRVLP-KELLASRQLALQKMQSEK 689

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  421 AALTKSDPTSSTSsgdyQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARqrekmneehnkRLSDT 500
Cdd:TIGR00618  690 EQLTYWKEMLAQC----QTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM-----------HQART 754

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024438909  501 VDRLLTESNERLQLHLKERMAALEEKNVLIQESESFRKNLEESLHDKERLAEEIEKLRSELDQMKL 566
Cdd:TIGR00618  755 VLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILN 820
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
271-593 8.04e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 8.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  271 SQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRY 350
Cdd:COG4372     45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  351 LSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQtMRKAETLPEVEAELAQriaALTKSDPTS 430
Cdd:COG4372    125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA-LSEAEAEQALDELLKE---ANRNAEKEE 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  431 STSSGDYQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNE 510
Cdd:COG4372    201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  511 RLQLHLKERMAALEEKNVLIQESESFRKNLEESLHDKERLAEEIEKLRSELDQMKLRAGSLIEPTLSRPHLDSSAELRYS 590
Cdd:COG4372    281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360


                   ...
gi 2024438909  591 VGS 593
Cdd:COG4372    361 KGA 363
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 105-562 1.53e-06

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: 52.87  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  105 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHE-RSLRMTVVKRQAQSpsgvssevevlkALKSL 183
Cdd:pfam01576   41 EKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEeRSQQLQNEKKKMQQ------------HIQDL 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  184 FEHhkaLDEKVRERLRVSLERVSaLEEELAAANQEIVALREQNAHIQRKiaagegpaesehiegmepgQKVHEKRLSNGS 263
Cdd:pfam01576  109 EEQ---LDEEEAARQKLQLEKVT-TEAKIKKLEEDILLLEDQNSKLSKE-------------------RKLLEERISEFT 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  264 IDSNDETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERI 343
Cdd:pfam01576  166 SNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEEL 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  344 TTLEKRY-------LSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL 416
Cdd:pfam01576  246 QAALARLeeetaqkNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKR 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  417 AQRIAALTKSDPTSSTSSgdyqyvmEAKLQEMisirrkaeerhgnieeRMRHLEAqLEEKNQELQRARqREKMNEEHNKr 496
Cdd:pfam01576  326 EQEVTELKKALEEETRSH-------EAQLQEM----------------RQKHTQA-LEELTEQLEQAK-RNKANLEKAK- 379

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024438909  497 lsdtvdRLLTESNERLQLHLKERMAALeeknvliQESESFRKNLEESLHD-----------KERLAEEIEKLRSELD 562
Cdd:pfam01576  380 ------QALESENAELQAELRTLQQAK-------QDSEHKRKKLEGQLQElqarlseserqRAELAEKLSKLQSELE 443
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
208-418 1.94e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 52.33  E-value: 1.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  208 LEEELAAANQEIVALREQNAHIQRKIAAGEgpaesehiegmepgQKVHEKRLSNGSIDSNDETSQVIELQELLEKQnyeM 287
Cdd:COG3206    166 LELRREEARKALEFLEEQLPELRKELEEAE--------------AALEEFRQKNGLVDLSEEAKLLLQQLSELESQ---L 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  288 AQMKERMAALSSRVGEVEQEAETARKEL--IKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsIHDMND 365
Cdd:COG3206    229 AEARAELAEAEARLAALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRA 305

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024438909  366 KLENELankEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 418
Cdd:COG3206    306 QLQQEA---QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
195-482 2.10e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.22  E-value: 2.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  195 RERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGPAEsehiegmepgqkvhekrLSNGSIDSNDETSQVI 274
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-----------------YSWDEIDVASAEREIA 671

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  275 ELQ---ELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYL 351
Cdd:COG4913    672 ELEaelERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  352 SAQRESTSIhdmnDKLENELAnkeailRQLEDKNRQLQERLELAEQKLQQTMRK---------------AETLPEVEAEL 416
Cdd:COG4913    752 EERFAAALG----DAVERELR------ENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldadLESLPEYLALL 821

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909  417 AQriaaLTKSD-PtsstssgDYQ-----YVMEAKLQEMISIRRKAEERHGNIEERMRHLeaqleekNQELQR 482
Cdd:COG4913    822 DR----LEEDGlP-------EYEerfkeLLNENSIEFVADLLSKLRRAIREIKERIDPL-------NDSLKR 875
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 177-410 5.95e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.15  E-value: 5.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  177 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEgpaesEHIEGMEPGQKVHE 256
Cdd:COG4942     29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE-----KEIAELRAELEAQK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  257 KRLSNgSIDSNDETSQVIELQELLEKQNyeMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQK 336
Cdd:COG4942    104 EELAE-LLRALYRLGRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024438909  337 EDMEERITTLEKryLSAQRESTSihdmnDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLP 410
Cdd:COG4942    181 AELEEERAALEA--LKAERQKLL-----ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 1056-1107 7.10e-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: 44.54  E-value: 7.10e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024438909 1056 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1107
Cdd:cd09487      4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 205-589 1.14e-05

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 49.69  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  205 VSALEEELAAANQEIVALREQNAHIQRKIAAGEgPAESEHIEGMEPGQKVHEK--RLSNGSID----SNDETSQVIELQ- 277
Cdd:pfam05622   23 VSLLQEEKNSLQQENKKLQERLDQLESGDDSGT-PGGKKYLLLQKQLEQLQEEnfRLETARDDyrikCEELEKEVLELQh 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  278 --ELLEKQNYEMAQMKERMAAL---SSRVGEVEQEAETARKEL---------IKT-EEMNSKYqrdireaMAQKEDMEE- 341
Cdd:pfam05622  102 rnEELTSLAEEAQALKDEMDILresSDKVKKLEATVETYKKKLedlgdlrrqVKLlEERNAEY-------MQRTLQLEEe 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  342 --RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQ---ERLELAEQKLQQTMRKAETLPEVEAEL 416
Cdd:pfam05622  175 lkKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQkekERLIIERDTLRETNEELRCAQLQQAEL 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  417 AQRIAALTKSDPTSSTSSGDyqyVMEAKLQEMIsIRRKAEER------HGNIEERMRHLEAQLEEKNQELQRARQREKMN 490
Cdd:pfam05622  255 SQADALLSPSSDPGDNLAAE---IMPAEIREKL-IRLQHENKmlrlgqEGSYRERLTELQQLLEDANRRKNELETQNRLA 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  491 EEHNKRLSDTVdrlltesnERLQLHLKERMAALEEKNVLIQESESFRKNLEESLHDKERLAEEIEKLRSELDQMKLRAGS 570
Cdd:pfam05622  331 NQRILELQQQV--------EELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKID 402

                          410       420
                   ....*....|....*....|
gi 2024438909  571 LIEPTLSRPHLDSSA-ELRY 589
Cdd:pfam05622  403 ELQEALRKKDEDMKAmEERY 422
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 36-526 1.22e-05

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: 49.72  E-value: 1.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   36 VNMLDERDRLLD-TLRETQESLSLAQQRLQDViydRDSLQRqlnsalpqmTVAAGTSIENNIQ---RTI-SCPNEFAALT 110
Cdd:pfam05483  270 ANQLEEKTKLQDeNLKELIEKKDHLTKELEDI---KMSLQR---------SMSTQKALEEDLQiatKTIcQLTEEKEAQM 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  111 KELNACREQlleKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFE 185
Cdd:pfam05483  338 EELNKAKAA---HSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEE 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  186 HHKALDEKvrERLRVSLERVSALEEELAAANQEIVAL---REQNAH---IQRKIAAGEGPAESEHIEGMEpgQKVHEKRL 259
Cdd:pfam05483  410 LKKILAED--EKLLDEKKQFEKIAEELKGKEQELIFLlqaREKEIHdleIQLTAIKTSEEHYLKEVEDLK--TELEKEKL 485

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  260 SNGSIDSN-------------DETSQVIEL---QELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELI------- 316
Cdd:pfam05483  486 KNIELTAHcdklllenkeltqEASDMTLELkkhQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdevk 565

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  317 ----KTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN---------------------DKLENEL 371
Cdd:pfam05483  566 ckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLELEL 645

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  372 ANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltksdptsstssgdyQYVMEAKLQEMISI 451
Cdd:pfam05483  646 ASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEI-----------------DKRCQHKIAEMVAL 708

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  452 RRKAEERHGNI-EERMRHLEAQleeKNQELQRARQREKMNEEhnkrLSDTVDRLLT---------ESNERLQLHLKERMA 521
Cdd:pfam05483  709 MEKHKHQYDKIiEERDSELGLY---KNKEQEQSSAKAALEIE----LSNIKAELLSlkkqleiekEEKEKLKMEAKENTA 781


                   ....*
gi 2024438909  522 ALEEK 526
Cdd:pfam05483  782 ILKDK 786
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 271-492 1.27e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.06  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  271 SQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAmaqKEDMEERITTLEKRY 350
Cdd:COG3883     16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  351 LSAQR------------ESTSIHDMNDKLEnelaNKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 418
Cdd:COG3883     93 RALYRsggsvsyldvllGSESFSDFLDRLS----ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024438909  419 RIAALtksdptsstssgdyqyvmEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEE 492
Cdd:COG3883    169 AKAEL------------------EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 106-489 1.35e-05

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


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 48.91  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  106 FAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrheRSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFE 185
Cdd:pfam19220   29 FSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLR-------RELAGLTRRLSAAEGELEELVARLAKLEAALRE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  186 HHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQ-RKIAAGEGPAESEHiegmepgqkvhekrlsngSI 264
Cdd:pfam19220  102 AEAAKEE-LRIELRDKTAQAEALERQLAAETEQNRALEEENKALReEAQAAEKALQRAEG------------------EL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  265 DSNDETSQVIE-----LQELLEKQNYEMAQmkermaaLSSRVGEVEQEAETARKELIKTE----EMNSKYQRDIREAMAQ 335
Cdd:pfam19220  163 ATARERLALLEqenrrLQALSEEQAAELAE-------LTRRLAELETQLDATRARLRALEgqlaAEQAERERAEAQLEEA 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  336 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQ-------LQERLELAEQKLQQTMRKAET 408
Cdd:pfam19220  236 VEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEasierdtLERRLAGLEADLERRTQQFQE 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  409 LPEVEAELAQRIAALTKSDPTSstssgdyqyvmEAKLQemisirrKAEERHGNIEERMRHLE-------AQLEEKNQELQ 481
Cdd:pfam19220  316 MQRARAELEERAEMLTKALAAK-----------DAALE-------RAEERIASLSDRIAELTkrfeverAALEQANRRLK 377


                   ....*...
gi 2024438909  482 RARQREKM 489
Cdd:pfam19220  378 EELQRERA 385
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 252-449 1.36e-05

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 47.59  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  252 QKVHEKRLSNGSIDSNDETSQVIELQELLEKqnyEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIRE 331
Cdd:pfam13851    3 MKNHEKAFNEIKNYYNDITRNNLELIKSLKE---EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  332 AMAQKEDME---ERITTLEKRYLSAQRESTSIHDMNDKLENElanKEAILRQLEDKNRQLQERLELAEQKLQQTMRK-AE 407
Cdd:pfam13851   80 YEKDKQSLKnlkARLKVLEKELKDLKWEHEVLEQRFEKVERE---RDELYDKFEAAIQDVQQKTGLKNLLLEKKLQAlGE 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2024438909  408 TLPEVEAELAQRIAAlTKSDPTSSTSsgdyqyvMEAKLQEMI 449
Cdd:pfam13851  157 TLEKKEAQLNEVLAA-ANLDPDALQA-------VTEKLEDVL 190
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
271-572 1.69e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 1.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  271 SQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRY 350
Cdd:COG4372     31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  351 LSAQREstsihdmNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKSDPTS 430
Cdd:COG4372    111 EELQEE-------LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  431 STSsgdyQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNE 510
Cdd:COG4372    184 ALD----ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909  511 RLQLHLKERMAALEEKNVLIQESESFRKNLEESLHDKERLAEEIEKLRSELDQMKLRAGSLI 572
Cdd:COG4372    260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 277-562 1.76e-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: 49.35  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  277 QELLEKQNYEMAQMKERMAAL----SSRVGEVEQEA----ETARKELIKTEEMNSKYQRDIREAMAQKEDME-----ERI 343
Cdd:pfam17380  298 QERLRQEKEEKAREVERRRKLeeaeKARQAEMDRQAaiyaEQERMAMERERELERIRQEERKRELERIRQEEiameiSRM 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  344 TTLEKRYLSAQRESTSIhdmndKLENELANKEAILRqlEDKNRQLQERLELAEQ-KLQQTMRKAETLPEVEAELAQRIAA 422
Cdd:pfam17380  378 RELERLQMERQQKNERV-----RQELEAARKVKILE--EERQRKIQQQKVEMEQiRAEQEEARQREVRRLEEERAREMER 450

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  423 LTKSDPTSSTSSGDYQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQE-LQRARQR---EKMNEEHNKRLS 498
Cdd:pfam17380  451 VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmIEEERKRkllEKEMEERQKAIY 530

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024438909  499 DTVDRLLTESNERLQLHLKERMAALEEKNVLIQEsesfRKNLEESLHDKERLAE--EIEKLRSELD 562
Cdd:pfam17380  531 EEERRREAEEERRKQQEMEERRRIQEQMRKATEE----RSRLEAMEREREMMRQivESEKARAEYE 592
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 270-478 1.86e-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: 1.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  270 TSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEA--ETARKELIKTEEMNSKYQR---------DIREAMAQKED 338
Cdd:COG3096    454 TEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQQALAQRlqqlraqlaELEQRLRQQQN 533

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  339 MEERITTLEKRyLSAQREStsihdmNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 418
Cdd:COG3096    534 AERLLEEFCQR-IGQQLDA------AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLA 606

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  419 RIAALTKSDPTSSTSSGDYQYVMEAkLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQ 478
Cdd:COG3096    607 AQDALERLREQSGEALADSQEVTAA-MQQLLEREREATVERDELAARKQALESQIERLSQ 665
PTZ00121 PTZ00121
MAEBL; Provisional
 118-571 2.00e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  118 EQLLEKEEEISELKAERNNTRLllEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALkslfEHHKALDEKVRER 197
Cdd:PTZ00121  1233 EEAKKDAEEAKKAEEERNNEEI--RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD----EAKKAEEKKKADE 1306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  198 LRVSLERVSALEE-----ELAAANQEIVALREQNAHIQRKIAAGEGPAESEHIEGMEPGQKVHEKRLSNGSIDSN----- 267
Cdd:PTZ00121  1307 AKKKAEEAKKADEakkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaakkk 1386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  268 -DETSQVIELQELLEKQNYEMAQMKERMAAlSSRVGEVEQEAETARK--ELIKTEEMNSKYQRDIREAMAQKEDMEERIT 344
Cdd:PTZ00121  1387 aEEKKKADEAKKKAEEDKKKADELKKAAAA-KKKADEAKKKAEEKKKadEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  345 TLEKRY---LSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRIA 421
Cdd:PTZ00121  1466 AEEAKKadeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE--AKKADEAKKAE 1543

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  422 ALTKSDPtsstssgdyqyVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSdtv 501
Cdd:PTZ00121  1544 EKKKADE-----------LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--- 1609

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  502 drlltesnERLQLHLKERMAALEeknvlIQESESFRKNLEESLHDKERLAEEIEKLRSELDQMKLRAGSL 571
Cdd:PTZ00121  1610 --------EEAKKAEEAKIKAEE-----LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 118-563 2.42e-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: 48.89  E-value: 2.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  118 EQLLEKEEEISELKAERNNTRLL----LEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVE-VLKALKSLFEHHKALDE 192
Cdd:TIGR00606  684 QRVFQTEAELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQ-----SIIDlKEKEIPELRNKLQKVNR 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  193 KVrERLRVSLERVSAL------EEELAAANQEIVA----LREQNAHIQRKIAagEGPAESEHIEGMEPGQKVHEKRlSNG 262
Cdd:TIGR00606  759 DI-QRLKNDIEEQETLlgtimpEEESAKVCLTDVTimerFQMELKDVERKIA--QQAAKLQGSDLDRTVQQVNQEK-QEK 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  263 SIDSNDETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEER 342
Cdd:TIGR00606  835 QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPL 914

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  343 ITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLElaEQKLQQTMRKAETLPEVEAELA--QRI 420
Cdd:TIGR00606  915 ETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ--DGKDDYLKQKETELNTVNAQLEecEKH 992

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  421 AALTKSDPTSSTSSGDYQYVMEAKLQEMISIRRKAEErhgnIEERMRHLEAQLEEKNQElqrarQREKMNEEHNKrLSDT 500
Cdd:TIGR00606  993 QEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENE----LKEVEEELKQHLKEMGQM-----QVLQMKQEHQK-LEEN 1062

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024438909  501 VDRLLTESNE---RLQLHLKERMAALEE-KNVLIQESESFRKNLEESLHDKERLAEEIEKLRSELDQ 563
Cdd:TIGR00606 1063 IDLIKRNHVLalgRQKGYEKEIKHFKKElREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQ 1129
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 201-405 3.16e-05

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


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 46.05  E-value: 3.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  201 SLERVSALEEELAAANQEIVALREQNAHIQRKiaagegpaesehiegmepgQKVHEKRLSNGSIDSNdetsqviELQELL 280
Cdd:pfam15619    9 RLHKIKELQNELAELQSKLEELRKENRLLKRL-------------------QKRQEKALGKYEGTES-------ELPQLI 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  281 EKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREA-MAQKEDMEERITTLEKRYLSAQREsts 359
Cdd:pfam15619   63 ARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDKDEK--- 139

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024438909  360 IHDMNDKLEN-------ELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRK 405
Cdd:pfam15619  140 IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 192-438 4.10e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.52  E-value: 4.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  192 EKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAgegpaesehiegmepgqkvhekrlSNGSIDSNDEts 271
Cdd:COG3883     19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA------------------------LQAEIDKLQA-- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  272 QVIELQELLEKQNyemAQMKERMAAL---SSRVGEVEQ--EAETA-----RKELIKTeeMNSKYQRDIREAMAQKEDMEE 341
Cdd:COG3883     73 EIAEAEAEIEERR---EELGERARALyrsGGSVSYLDVllGSESFsdfldRLSALSK--IADADADLLEELKADKAELEA 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  342 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIA 421
Cdd:COG3883    148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227

                          250
                   ....*....|....*..
gi 2024438909  422 ALTKSDPTSSTSSGDYQ 438
Cdd:COG3883    228 AAAAAAAAAAAAAAAAA 244
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 45-570 4.32e-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: 47.89  E-value: 4.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   45 LLDTLRETQES---LSLAQQRLQDVIydrdSLQRQLNSALPQMTVAAGTSIENNIQRTISCPNEFAAL-------TKELN 114
Cdd:pfam10174   58 LKEQYRVTQEEnqhLQLTIQALQDEL----RAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLqseherqAKELF 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  115 ACREQLLEKEEEISE----LKAERNNTRLLLEHLEC-------LVSRHERSLRMTVVKRQAQspsgvssEVEVLKALKSL 183
Cdd:pfam10174  134 LLRKTLEEMELRIETqkqtLGARDESIKKLLEMLQSkglpkksGEEDWERTRRIAEAEMQLG-------HLEVLLDQKEK 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  184 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVAL----REQNAHIQRKIAAGEGPAE--SEHIEGMEPgQKVHEK 257
Cdd:pfam10174  207 ENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLerniRDLEDEVQMLKTNGLLHTEdrEEEIKQMEV-YKSHSK 285

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  258 RLSNG----SIDSNDETSQVIELQ---ELLEKQNYEMAQ----MKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQ 326
Cdd:pfam10174  286 FMKNKidqlKQELSKKESELLALQtklETLTNQNSDCKQhievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKT 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  327 -----------------RDIREAMAQKE------------------DMEERITTLEKRYLSAQRESTSIHDMNDKLENEL 371
Cdd:pfam10174  366 kqlqdlteekstlageiRDLKDMLDVKErkinvlqkkienlqeqlrDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEAL 445

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  372 ANKEAILRQL-EDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALT--KSDPTSSTSSGDYQyvmEAKLQEM 448
Cdd:pfam10174  446 SEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIdlKEHASSLASSGLKK---DSKLKSL 522

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  449 -ISIRRKAEERHG-------------------NIEERMRHLEAQLEEKNQELQRARQ---------REKMNEEHNK--RL 497
Cdd:pfam10174  523 eIAVEQKKEECSKlenqlkkahnaeeavrtnpEINDRIRLLEQEVARYKEESGKAQAeverllgilREVENEKNDKdkKI 602

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024438909  498 SDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESESFRKNLEESLHDK-----ERLAEEIEKLRSELDQMKLRAGS 570
Cdd:pfam10174  603 AELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSqqlqlEELMGALEKTRQELDATKARLSS 680
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 271-416 4.47e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.46  E-value: 4.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  271 SQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEE----------------MNSKYQRDIREAMA 334
Cdd:COG1579     17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELeieevearikkyeeqlGNVRNNKEYEALQK 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  335 QKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQtmRKAETLPEVEA 414
Cdd:COG1579     97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA--EREELAAKIPP 174


                   ..
gi 2024438909  415 EL 416
Cdd:COG1579    175 EL 176
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 104-564 4.75e-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: 47.89  E-value: 4.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  104 NEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkRQAQSPSGVSSEVEVLKAL--- 180
Cdd:pfam10174  317 NQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ-----DLTEEKSTLAGEIRDLKDMldv 391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  181 ---KSLFEHHK--ALDEKVRERLRV---------SLERVSA--------LEEELAAANQEIVALREQNAHIQRkiaageg 238
Cdd:pfam10174  392 kerKINVLQKKieNLQEQLRDKDKQlaglkervkSLQTDSSntdtalttLEEALSEKERIIERLKEQREREDR------- 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  239 pAESEHIEGMEPGQKVHEKRLSNGSIDSNDETSQVIELQELLEKQNyemaqmkERMAALSSRVGEVEQEAETARKELIKT 318
Cdd:pfam10174  465 -ERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLA-------SSGLKKDSKLKSLEIAVEQKKEECSKL 536

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  319 EEMNSKYQrDIREAMAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAILRQLE----DKNRQLQERLEL 394
Cdd:pfam10174  537 ENQLKKAH-NAEEAVRTNPEINDRIRLLEQEVARYKEESG-------KAQAEVERLLGILREVEneknDKDKKIAELESL 608

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  395 AEQKLQQTMRKAETLPEVEAELAQRIAALTK--SDPTSSTSSGDYQYVMEAKLQEMISIRRKAEErhgnIEERMRHLEAQ 472
Cdd:pfam10174  609 TLRQMKEQNKKVANIKHGQQEMKKKGAQLLEeaRRREDNLADNSQQLQLEELMGALEKTRQELDA----TKARLSSTQQS 684

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  473 LEEKNQELqrarqrEKMNEEHNKRLSdtvdrlltesnERLQLHLKERMAALEEKNVLIQEsesfrknLEESLHDKERLAE 552
Cdd:pfam10174  685 LAEKDGHL------TNLRAERRKQLE-----------EILEMKQEALLAAISEKDANIAL-------LELSSSKKKKTQE 740

                          490
                   ....*....|..
gi 2024438909  553 EIEKLRSELDQM 564
Cdd:pfam10174  741 EVMALKREKDRL 752
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 332-543 5.65e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.13  E-value: 5.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  332 AMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTmrkaetlpe 411
Cdd:COG3883     14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER--------- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  412 vEAELAQRIAALTKSDPTSSTSSgdyqYVMEAK-LQEMIS---IRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQRE 487
Cdd:COG3883     85 -REELGERARALYRSGGSVSYLD----VLLGSEsFSDFLDrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024438909  488 KMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESESFRKNLEES 543
Cdd:COG3883    160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 272-561 5.68e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.86  E-value: 5.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  272 QVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETAR-------KELIKTEEMNSKYQRDIREAMAQKEDM----- 339
Cdd:pfam01576  750 QVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANkgreeavKQLKKLQAQMKDLQRELEEARASRDEIlaqsk 829

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  340 --EERITTLEKRYL-------SAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLP 410
Cdd:pfam01576  830 esEKKLKNLEAELLqlqedlaASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLN 909

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  411 EVEAELAQRIAALT---KSDPTSSTSSGDYQYVME-------AKLQEMIS-IRRKAEERHGNIEERMRHLEAQLEEKNQE 479
Cdd:pfam01576  910 DRLRKSTLQVEQLTtelAAERSTSQKSESARQQLErqnkelkAKLQEMEGtVKSKFKSSIAALEAKIAQLEEQLEQESRE 989

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  480 LQRA----RQREK------MNEEHNKRLSDTVDRLLTESNERLQlHLKERMAALEEKNVLIQESE-SFRKNLEESLHDKE 548
Cdd:pfam01576  990 RQAAnklvRRTEKklkevlLQVEDERRHADQYKDQAEKGNSRMK-QLKRQLEEAEEEASRANAARrKLQRELDDATESNE 1068

                          330
                   ....*....|...
gi 2024438909  549 RLAEEIEKLRSEL 561
Cdd:pfam01576 1069 SMNREVSTLKSKL 1081
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 209-568 7.60e-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: 47.25  E-value: 7.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  209 EEELAAANQEIVAL-REQNAHiqrkiaAGEGPAESEHIEGMEPGQKVHEKRLSNGSI-DSNDETSQVIELQELLEKQNYE 286
Cdd:COG3096    835 EAELAALRQRRSELeRELAQH------RAQEQQLRQQLDQLKEQLQLLNKLLPQANLlADETLADRLEELREELDAAQEA 908

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  287 MAQMKERMAALSsrvgEVEQEAETARKELIKTEEMNSKYQRdireAMAQKEDMEERITTLEkrYLSAQRESTSIHD---- 362
Cdd:COG3096    909 QAFIQQHGKALA----QLEPLVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALS--EVVQRRPHFSYEDavgl 978

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  363 ------MNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKSDPTSstssgd 436
Cdd:COG3096    979 lgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAE------ 1052

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  437 yqyvmeaklqemisirrkAEERhgnIEERMRHLEAQL----EEKNQ-ELQRARQREKMnEEHNKRLSDtVDRLLTESNER 511
Cdd:COG3096   1053 ------------------AEER---ARIRRDELHEELsqnrSRRSQlEKQLTRCEAEM-DSLQKRLRK-AERDYKQEREQ 1109

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024438909  512 LQLHLKERMAALEeknvLIQESesfrkNLEESLHDKERLAEEIEKLRSELDQmKLRA 568
Cdd:COG3096   1110 VVQAKAGWCAVLR----LARDN-----DVERRLHRRELAYLSADELRSMSDK-ALGA 1156
PTZ00121 PTZ00121
MAEBL; Provisional
 180-557 9.36e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 9.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  180 LKSLFEHHKALDEKVRERLRVSlERVSALEEELAAANQEIVALR--EQNAHIQRK-IAAGEGPAESEHIEGMEPGQKVHE 256
Cdd:PTZ00121  1539 AKKAEEKKKADELKKAEELKKA-EEKKKAEEAKKAEEDKNMALRkaEEAKKAEEArIEEVMKLYEEEKKMKAEEAKKAEE 1617

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  257 KRLSNGSIDSNDETSQVIElqELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQK 336
Cdd:PTZ00121  1618 AKIKAEELKKAEEEKKKVE--QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  337 EDMEERITTLEKRylsaqrestsihdmndKLENELANKEAILRQLEDKNRQlqeRLELAEQKLQQTMRKAETLpEVEAEL 416
Cdd:PTZ00121  1696 KEAEEAKKAEELK----------------KKEAEEKKKAEELKKAEEENKI---KAEEAKKEAEEDKKKAEEA-KKDEEE 1755

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  417 AQRIAALTKSDPTSSTS-SGDYQYVMEAKLQEMISIRRKAEERhgNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNK 495
Cdd:PTZ00121  1756 KKKIAHLKKEEEKKAEEiRKEKEAVIEEELDEEDEKRRMEVDK--KIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIK 1833

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909  496 RLSDTVDRLLTESNErLQLHLKERMAALEEKNVLIQESESFRKNLEESLHDKERlAEEIEKL 557
Cdd:PTZ00121  1834 EVADSKNMQLEEADA-FEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE-ADEIEKI 1893
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 932-996 1.16e-04

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 41.49  E-value: 1.16e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024438909  932 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 996
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1134-1204 1.37e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.37e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024438909 1134 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1204
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 105-564 1.38e-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: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  105 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSlRMTVVKRQAQSPSGVSSEVEVLKALKSLF 184
Cdd:pfam01576  153 ERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG-RQELEKAKRKLEGESTDLQEQIAELQAQI 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  185 EHHKALDEKVRERLRVSLERvsaLEEELAAANQEIVALREQNAHI---QRKIAAGEGPAESEHIEGMEPGQKVheKRLSN 261
Cdd:pfam01576  232 AELRAQLAKKEEELQAALAR---LEEETAQKNNALKKIRELEAQIselQEDLESERAARNKAEKQRRDLGEEL--EALKT 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  262 GSIDSNDETS-----------QVIELQELLEKQ----NYEMAQMKERMAALSSRVGEVEQEAETARKELIKT----EEMN 322
Cdd:pfam01576  307 ELEDTLDTTAaqqelrskreqEVTELKKALEEEtrshEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAkqalESEN 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  323 SKYQRDIREAMAQKEDMEER-------ITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKN---------- 385
Cdd:pfam01576  387 AELQAELRTLQQAKQDSEHKrkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNiklskdvssl 466

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  386 -RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKSDPTSSTSSGDYQyVMEAKLQEMisiRRKAEERHGNI-- 462
Cdd:pfam01576  467 eSQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLS-TLQAQLSDM---KKKLEEDAGTLea 542

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  463 -EERMRHLEAQLEEKNQEL-QRARQREKMnEEHNKRLSDTVDRLLTESNERLQ----LHLKER----MAAlEEKNVLIQE 532
Cdd:pfam01576  543 lEEGKKRLQRELEALTQQLeEKAAAYDKL-EKTKNRLQQELDDLLVDLDHQRQlvsnLEKKQKkfdqMLA-EEKAISARY 620

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2024438909  533 SE-----------------SFRKNLEESLHDKERLAEEIEKLRSELDQM 564
Cdd:pfam01576  621 AEerdraeaeareketralSLARALEEALEAKEELERTNKQLRAEMEDL 669
PTZ00121 PTZ00121
MAEBL; Provisional
 243-568 1.57e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 1.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  243 EHIEGMEPGQKVHEKRLSNGSIDSNDET-----SQVIELQELL-EKQNYEMAQMKErmaalsSRVGEVEQEAETARKELI 316
Cdd:PTZ00121  1031 ELTEYGNNDDVLKEKDIIDEDIDGNHEGkaeakAHVGQDEGLKpSYKDFDFDAKED------NRADEATEEAFGKAEEAK 1104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  317 KTEEMNSKYQRDIREAMAQKEDMeerittlekRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKnRQLQERLELAE 396
Cdd:PTZ00121  1105 KTETGKAEEARKAEEAKKKAEDA---------RKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA-RKAEEARKAED 1174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  397 QKLQQTMRKAETLPEVE----AELAQRIAALTKsdptsstssgdYQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQ 472
Cdd:PTZ00121  1175 AKKAEAARKAEEVRKAEelrkAEDARKAEAARK-----------AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK 1243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  473 LEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESESFRKNLEESlHDKERLAE 552
Cdd:PTZ00121  1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA-KKADEAKK 1322

                          330
                   ....*....|....*.
gi 2024438909  553 EIEKLRSELDQMKLRA 568
Cdd:PTZ00121  1323 KAEEAKKKADAAKKKA 1338
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 210-563 1.59e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.25  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  210 EELAAANQEIvALREQNAHIQRKIAAGEGPAESEHIEgMEPGQKVH--EKRLSNGSIDSNDETSQVIELQELLEKQNYEM 287
Cdd:pfam05483  193 EKMILAFEEL-RVQAENARLEMHFKLKEDHEKIQHLE-EEYKKEINdkEKQVSLLLIQITEKENKMKDLTFLLEESRDKA 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  288 AQMKERMAALSSRVGEVEQEAETARKELiktEEMNSKYQRDIREAMAQKEDME---ERITTLEKRYLSAQRESTSIHDMN 364
Cdd:pfam05483  271 NQLEEKTKLQDENLKELIEKKDHLTKEL---EDIKMSLQRSMSTQKALEEDLQiatKTICQLTEEKEAQMEELNKAKAAH 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  365 DKLENELankEAILRQLEDKNRQLQERLELAEQKLQ-------------QTMRKAETLPEVEAELAQRIAALTKSDPTSS 431
Cdd:pfam05483  348 SFVVTEF---EATTCSLEELLRTEQQRLEKNEDQLKiitmelqkksselEEMTKFKNNKEVELEELKKILAEDEKLLDEK 424

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  432 TSSGDYQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNER 511
Cdd:pfam05483  425 KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEL 504

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024438909  512 LQ------LHLKERMaalEEKNVLIQESESFRKNLEESLHDKERLAEEIEKLRSELDQ 563
Cdd:pfam05483  505 TQeasdmtLELKKHQ---EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ 559
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 302-585 1.85e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.12  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  302 GEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKrylsaqrestsihdmNDKLENELANKEAILRQL 381
Cdd:pfam02463  142 GKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAEL---------------IIDLEELKLQELKLKEQA 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  382 EDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKSdptSSTSSGDYQYVMEAKLQEMISIRRKAEERHGN 461
Cdd:pfam02463  207 KKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE---EIESSKQEIEKEEEKLAQVLKENKEEEKEKKL 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  462 IEERMRHLEAQLEEKNQELQRARQREKMNEEhNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESESFRKNLE 541
Cdd:pfam02463  284 QEEELKLLAKEEEELKSELLKLERRKVDDEE-KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE 362

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2024438909  542 ESLHDKERLAEEIEKLRSELDQMKLRAGSLIEPTLSRPHLDSSA 585
Cdd:pfam02463  363 KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 195-559 1.97e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.10  E-value: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  195 RERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEG---------PAESEHIEGMEPGQKVHEKrlsngsID 265
Cdd:COG3096    277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSAresdleqdyQAASDHLNLVQTALRQQEK------IE 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  266 SNDEtsQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELikteemnSKYQRDIREAMAQKEDMEERITT 345
Cdd:COG3096    351 RYQE--DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL-------ADYQQALDVQQTRAIQYQQAVQA 421

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  346 LEKrylsaQRESTSIHDMN-DKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQtMRKAetlpeveAELAQRIAalt 424
Cdd:COG3096    422 LEK-----ARALCGLPDLTpENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQ-FEKA-------YELVCKIA--- 485

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  425 ksDPTSSTSSGDyqyvmEAKLQemisIRRKAEERHgnIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDrl 504
Cdd:COG3096    486 --GEVERSQAWQ-----TAREL----LRRYRSQQA--LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-- 550

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024438909  505 lteSNERLQLHLKERMAALEEknvLIQESESFRKNLEESLHDKERLAEEIEKLRS 559
Cdd:COG3096    551 ---AAEELEELLAELEAQLEE---LEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 275-573 2.04e-04

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: 45.66  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  275 ELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYLSAQ 354
Cdd:pfam07888  105 ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  355 RESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQK---LQQTMRKAETLPEVeAELAQRIAALTKSDPTSS 431
Cdd:pfam07888  185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaeNEALLEELRSLQER-LNASERKVEGLGEELSSM 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  432 TSSGDYQYVmeaklqEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesNER 511
Cdd:pfam07888  264 AAQRDRTQA------ELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRL----EER 333

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909  512 LQlhlKERMAALEEKNVLIQESESFRKNLEESLHDKERLAEEIEKLRSELDQMKLRAGSLIE 573
Cdd:pfam07888  334 LQ---EERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 161-559 2.32e-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: 2.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  161 KRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVRERLRVSLERVsaLEEELAAANQEIVALREQNAHIQRKIAAGEGP 239
Cdd:pfam09731   88 QVKIPRQSGVSSEVaEEEKEATKDAAEAKAQLPKSEQEKEKALEEV--LKEAISKAESATAVAKEAKDDAIQAVKAHTDS 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  240 AESEHIEGMEPGQK-VHEKRLSNGSIDSNDETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKT 318
Cdd:pfam09731  166 LKEASDTAEISREKaTDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLV 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  319 EemnsKYQRDIREAmAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLE--LAE 396
Cdd:pfam09731  246 D----QYKELVASE-RIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIEraLEK 320

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  397 QKLQQTMRKAETLPEVEAELAQRIAALTKSdptsstssgdyqyvMEAKLQEmisIRRKAEERHGNIEERMR-----HLEA 471
Cdd:pfam09731  321 QKEELDKLAEELSARLEEVRAADEAQLRLE--------------FEREREE---IRESYEEKLRTELERQAeaheeHLKD 383

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  472 QLEEKNQELQRARQR---EKMNEEHNKRLSDtVDRLLTESNERLQLhLKERMAALEEKN---VLIQESESFRKNLEESLH 545
Cdd:pfam09731  384 VLVEQEIELQREFLQdikEKVEEERAGRLLK-LNELLANLKGLEKA-TSSHSEVEDENRkaqQLWLAVEALRSTLEDGSA 461

                          410
                   ....*....|....*.
gi 2024438909  546 DKER--LAEEIEKLRS 559
Cdd:pfam09731  462 DSRPrpLVRELKALKE 477
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 103-235 2.63e-04

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: 44.15  E-value: 2.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  103 PNEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVEVLKALKS 182
Cdd:COG1579     30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA---LQKEIESLKRRIS 106

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024438909  183 LFEhhkaldekvrERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAA 235
Cdd:COG1579    107 DLE----------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
271-588 3.82e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 3.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  271 SQVIELQELLEKQNYEMAQMKERMAALSSRvGEVEQEAETARKELIKTEEmnskYQRDIREAMAQKED----------ME 340
Cdd:COG4913    617 AELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVAS----AEREIAELEAELERldassddlaaLE 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  341 ERITTLEKRYlsaqrestsihdmnDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRI 420
Cdd:COG4913    692 EQLEELEAEL--------------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERF 755

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  421 AALTKSDPtsstssgdyqyvmEAKLQEmisirrkaeerhgNIEERMRHLEAQLEEKNQELQRARQrekmneEHNKRLSDT 500
Cdd:COG4913    756 AAALGDAV-------------ERELRE-------------NLEERIDALRARLNRAEEELERAMR------AFNREWPAE 803

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  501 VDRLLT--ESNERLQLHLK----ERMAALEEK--NVLIQESESFRKNLEESLHDKERLAEE-IEKLRSELDQMKLRAGSL 571
Cdd:COG4913    804 TADLDAdlESLPEYLALLDrleeDGLPEYEERfkELLNENSIEFVADLLSKLRRAIREIKErIDPLNDSLKRIPFGPGRY 883

                          330
                   ....*....|....*..
gi 2024438909  572 IEPTLSRPHLDSSAELR 588
Cdd:COG4913    884 LRLEARPRPDPEVREFR 900
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 365-525 4.00e-04

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: 43.37  E-value: 4.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  365 DKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKSDPTSSTSSgDYQyvmeAK 444
Cdd:COG1579     20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYE----AL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  445 LQEMISirrkAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 524
Cdd:COG1579     95 QKEIES----LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170


                   .
gi 2024438909  525 E 525
Cdd:COG1579    171 K 171
PRK12704 PRK12704
phosphodiesterase; Provisional
 301-427 4.13e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  301 VGEVEQEAETARKELIKteEMNSKYQRDIREAMAQKEDMEERITTLEKRYLsaQREST--SIHDMNDKLENELANKEAIL 378
Cdd:PRK12704    44 LEEAKKEAEAIKKEALL--EAKEEIHKLRNEFEKELRERRNELQKLEKRLL--QKEENldRKLELLEKREEELEKKEKEL 119

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2024438909  379 RQLEDKNRQLQERLELAEQKLQQTMrkaetlpeveaelaQRIAALTKSD 427
Cdd:PRK12704   120 EQKQQELEKKEEELEELIEEQLQEL--------------ERISGLTAEE 154
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 933-991 4.65e-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: 40.01  E-value: 4.65e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909  933 WDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 991
Cdd:cd09504      5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 300-510 5.74e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 44.15  E-value: 5.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  300 RVGEVEQEAETARKELIKTEEMNSKYQRDIREAM-AQKEDMEERITTLEKRYlsaqrestsihdmnDKLENELANKEAIL 378
Cdd:PRK05771    44 RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKkVSVKSLEELIKDVEEEL--------------EKIEKEIKELEEEI 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  379 RQLEDKNRQLQERLELAE---------QKLQQ---TMRKAETLPEVEAELAQRIAALTKSDPTSSTSSGDYQYVMEAK-- 444
Cdd:PRK05771   110 SELENEIKELEQEIERLEpwgnfdldlSLLLGfkyVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKel 189

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024438909  445 LQEMISIRRKAEER------HGNIEERMRHLEAQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDRLLTESNE 510
Cdd:PRK05771   190 SDEVEEELKKLGFErleleeEGTPSELIREIKEELEEIEKERESLLEElKELAKKYLEELLALYEYLEIELER 262
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 323-486 5.81e-04

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 43.57  E-value: 5.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  323 SKYQRDIREAMAQKEDMEERITTLE---KRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKL 399
Cdd:pfam00529   54 TDYQAALDSAEAQLAKAQAQVARLQaelDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLA 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  400 QQTMRKAETLPEVEAELAQriaaltkSDPTSSTSSGDYQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQE 479
Cdd:pfam00529  134 PIGGISRESLVTAGALVAQ-------AQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLD 206


                   ....*..
gi 2024438909  480 LQRARQR 486
Cdd:pfam00529  207 LERTEIR 213
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 267-563 6.14e-04

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: 44.24  E-value: 6.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  267 NDETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKT-----------EEMNSKYQRDIReamaQ 335
Cdd:TIGR04523   92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFlteikkkekelEKLNNKYNDLKK----Q 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  336 KEDMEERITTLEKRYLSAQRESTSIH-----------------DMNDKLENELANKEAILRQLEDKNRQLQERLELAEQK 398
Cdd:TIGR04523  168 KEELENELNLLEKEKLNIQKNIDKIKnkllklelllsnlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTE 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  399 LQQTMRKAETL----PEVEAELAQRIAALTKSDPTSSTSSGDYQYVmEAKLQEMIS-----IRRKAEERHGNIEERMRHL 469
Cdd:TIGR04523  248 ISNTQTQLNQLkdeqNKIKKQLSEKQKELEQNNKKIKELEKQLNQL-KSEISDLNNqkeqdWNKELKSELKNQEKKLEEI 326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  470 EAQLEEKNQELQRARQ------REKMNEEHNKRlsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESESFRKNLEES 543
Cdd:TIGR04523  327 QNQISQNNKIISQLNEqisqlkKELTNSESENS---EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403

                          330       340
                   ....*....|....*....|
gi 2024438909  544 LHDKERLAEEIEKLRSELDQ 563
Cdd:TIGR04523  404 EKLNQQKDEQIKKLQQEKEL 423
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 303-567 6.53e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.94  E-value: 6.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  303 EVEQEAETARKElikteeMNSKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAILRQLE 382
Cdd:pfam05483  201 ELRVQAENARLE------MHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQIT-------EKENKMKDLTFLLEESR 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  383 DKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKSDPTSSTSSGDYQ------YVMEAKLQEMISIRRKAE 456
Cdd:pfam05483  268 DKANQLEEKTKLQDENLKELIEKKDHL---TKELEDIKMSLQRSMSTQKALEEDLQiatktiCQLTEEKEAQMEELNKAK 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  457 ERHGNIEERMRHLEAQLEEKnqeLQRARQREKMNEEHNKRLSDTVDRLLTESNERLQL------HLKERMAALEEKNVLI 530
Cdd:pfam05483  345 AAHSFVVTEFEATTCSLEEL---LRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFknnkevELEELKKILAEDEKLL 421

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024438909  531 QESESFRKNLEE-----------------SLHD-----------KERLAEEIEKLRSELDQMKLR 567
Cdd:pfam05483  422 DEKKQFEKIAEElkgkeqelifllqarekEIHDleiqltaiktsEEHYLKEVEDLKTELEKEKLK 486
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
462-573 6.55e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 6.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  462 IEERM-RHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTEsNERLQLHLKERMAALEEknvLIQESESFRKNL 540
Cdd:COG2433    382 LEELIeKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---LERELSEARSEE 457

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2024438909  541 EESLH-DKE--RLAEEIEKLRSELDQMKLRAGSLIE 573
Cdd:COG2433    458 RREIRkDREisRLDREIERLERELEEERERIEELKR 493
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 90-426 6.85e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.86  E-value: 6.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   90 TSIENNIQRTISCPNEFAALTKELN-------ACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvKR 162
Cdd:TIGR04523  328 NQISQNNKIISQLNEQISQLKKELTnsesensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI-----QN 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  163 QAQSPSGVSSEVEVLKALKSLFEHHKaldEKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGpaes 242
Cdd:TIGR04523  403 QEKLNQQKDEQIKKLQQEKELLEKEI---ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR---- 475

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  243 eHIEGMEPGQKVHEKRLSNGSIDSNDETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMN 322
Cdd:TIGR04523  476 -SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL 554

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  323 SKYQrdireamaqkedmeerittLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQT 402
Cdd:TIGR04523  555 KKEN-------------------LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL 615

                          330       340
                   ....*....|....*....|....
gi 2024438909  403 MRKAETLPEVEAELAQRIAALTKS 426
Cdd:TIGR04523  616 EKELEKAKKENEKLSSIIKNIKSK 639
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 272-723 7.11e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.27  E-value: 7.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  272 QVIELQELLEKQNYEMAQMKERMAALSSRVG------EVEQEAETARKELIKTEEMNSKY---------QRDIREAMA-Q 335
Cdd:TIGR00606  320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGrlqlqaDRHQEHIRARDSLIQSLATRLELdgfergpfsERQIKNFHTlV 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  336 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAE 415
Cdd:TIGR00606  400 IERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQE 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  416 LAQRIAALTKSDPTSSTssgdyqyvmEAKLQEMISIRRKaeerHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNk 495
Cdd:TIGR00606  480 LRKAERELSKAEKNSLT---------ETLKKEVKSLQNE----KADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKM- 545

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  496 rlsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESESFRKNLEESLHDKERLAEEIEKLRSELDQMKLRAGSLIEpt 575
Cdd:TIGR00606  546 ----DKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE-- 619

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  576 lsrpHLDSSAELRYSVGSLVDSQSDY-RSTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLSSHPFESDTEMSD 654
Cdd:TIGR00606  620 ----QLSSYEDKLFDVCGSQDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQE 695

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024438909  655 IDDDdretlFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLE 723
Cdd:TIGR00606  696 FISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRD 759
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
180-553 1.02e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  180 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGegpaesehiegmepgqkvhEKRL 259
Cdd:COG4372     15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA-------------------RSEL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  260 SNGSIDSNDETSQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQKEDM 339
Cdd:COG4372     76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  340 EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQR 419
Cdd:COG4372    156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  420 IAALTKSDPTSSTSSGDYQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSD 499
Cdd:COG4372    236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024438909  500 TVDRLLTESNERLQLHLKERMAALEEKNVLIQESESFRKNLEESLHDKERLAEE 553
Cdd:COG4372    316 ALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
PRK01156 PRK01156
chromosome segregation protein; Provisional
 92-539 1.05e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 43.35  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   92 IENNIQRTISCPNEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHErSLRMtvvKRQAQSPSGVS 171
Cdd:PRK01156   313 ILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE-SLKK---KIEEYSKNIER 388

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  172 SEVEVLKALKSLFEHHKALDeKVRERLRVSLERVSAleeELAAANQEIVALREQNAHIQRKIAAGEGPA----------- 240
Cdd:PRK01156   389 MSAFISEILKIQEIDPDAIK-KELNEINVKLQDISS---KVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlge 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  241 -ESEHI--EGMEPGQKVHEK--RLSNGSIDSNDETSQVIELQELLEKQNYEMA-----QMKERMAALS------SRVGEV 304
Cdd:PRK01156   465 eKSNHIinHYNEKKSRLEEKirEIEIEVKDIDEKIVDLKKRKEYLESEEINKSineynKIESARADLEdikikiNELKDK 544

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  305 EQEAETARKEL--IKTEEMNSKYQrDIREAMAQKEDMEerITTLEKRYlsaQRESTSIHDMNDKLENELANKEAILRQLE 382
Cdd:PRK01156   545 HDKYEEIKNRYksLKLEDLDSKRT-SWLNALAVISLID--IETNRSRS---NEIKKQLNDLESRLQEIEIGFPDDKSYID 618

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  383 DKNRQLQERLELAEQK---LQQTMRKAETLPEVEAELAQRIAaltksdptsstssgdyqyvmeaKLQEMISIRRKAEERH 459
Cdd:PRK01156   619 KSIREIENEANNLNNKyneIQENKILIEKLRGKIDNYKKQIA----------------------EIDSIIPDLKEITSRI 676

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  460 GNIEERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdrllTESNERLqlhlkERMAALEEK-NVLIQESESFRK 538
Cdd:PRK01156   677 NDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETL-----ESMKKIKKAiGDLKRLREAFDK 747


                   .
gi 2024438909  539 N 539
Cdd:PRK01156   748 S 748
COG5022 COG5022
Myosin heavy chain [General function prediction only];
312-573 1.11e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.53  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  312 RKELIKTEEMNSKYQRDIREAMAQKEdMEERITTLekrylsaqrESTSIHdmNDKLENELANKEAILRQLEDKNRQLQER 391
Cdd:COG5022    809 RKEYRSYLACIIKLQKTIKREKKLRE-TEEVEFSL---------KAEVLI--QKFGRSLKAKKRFSLLKKETIYLQSAQR 876

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  392 LELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKSdpTSSTSSGDYQYVME--AKLQEMISIRRKAEERhgNIEERM 466
Cdd:COG5022    877 VELAERQlqeLKIDVKSISSLKLVNLELESEIIELKKS--LSSDLIENLEFKTEliARLKKLLNNIDLEEGP--SIEYVK 952

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  467 RHLEAQLEEKNQELQRArQREKMNEehNKRLSDTVDRLLTeSNERLQLHLKERMAALEEKNVLIQESESFRKNLEESLH- 545
Cdd:COG5022    953 LPELNKLHEVESKLKET-SEEYEDL--LKKSTILVREGNK-ANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAEl 1028

                          250       260       270
                   ....*....|....*....|....*....|
gi 2024438909  546 --DKERLAEEIEKLRSELDQMKLRAGSLIE 573
Cdd:COG5022   1029 qsASKIISSESTELSILKPLQKLKGLLLLE 1058
PRK12704 PRK12704
phosphodiesterase; Provisional
 387-556 1.44e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  387 QLQERLELAEQKLQQTMRKAETLPEvEAELAQRIAALtksdptsstssgDYQYVMEAKLQEMISIRRKAEERHGNIEERM 466
Cdd:PRK12704    32 KIKEAEEEAKRILEEAKKEAEAIKK-EALLEAKEEIH------------KLRNEFEKELRERRNELQKLEKRLLQKEENL 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  467 RHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEsfrknlEES 543
Cdd:PRK12704    99 DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEA 167

                          170
                   ....*....|...
gi 2024438909  544 LHDKERLAEEIEK 556
Cdd:PRK12704   168 RHEAAVLIKEIEE 180
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
463-571 1.57e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  463 EERMRHLEaQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESESFRKNLEE 542
Cdd:COG4913    248 REQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2024438909  543 SLH---------DKERLAEEIEKLRSELDQMKLRAGSL 571
Cdd:COG4913    327 ELEaqirgnggdRLEQLEREIERLERELEERERRRARL 364
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 58-567 1.61e-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: 43.11  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   58 LAQQRLQDVIYDRDSLQRQLNSALPQMTvAAGTSIENNIQRTISCPNEFAALTKELN---ACREQLLEKEEEISelKAER 134
Cdd:TIGR00606  409 TAAQLCADLQSKERLKQEQADEIRDEKK-GLGRTIELKKEILEKKQEELKFVIKELQqleGSSDRILELDQELR--KAER 485

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  135 NNTRLLLEHL-ECLVSR-----HERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRE-RLRVSLERVS- 206
Cdd:TIGR00606  486 ELSKAEKNSLtETLKKEvkslqNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKiKSRHSDELTSl 565

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  207 --------ALEEELAAANQEIVALREQNAHIQRKIAAGEgpAESEHIEGMEPGQKVHEKRLSNGSID---SNDETSQVIE 275
Cdd:TIGR00606  566 lgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLE--QNKNHINNELESKEEQLSSYEDKLFDvcgSQDEESDLER 643

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  276 LQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETAR---KELIKTE----EMNSKYQRDIREAMAQKEDMEERITTLEK 348
Cdd:TIGR00606  644 LKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCpvcQRVFQTEaelqEFISDLQSKLRLAPDKLKSTESELKKKEK 723

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  349 RY---LSAQRESTSIHDMNDKLENELANKeaiLRQLEDKNRQLQERLELAEQKLQQTMRKAET----------------- 408
Cdd:TIGR00606  724 RRdemLGLAPGRQSIIDLKEKEIPELRNK---LQKVNRDIQRLKNDIEEQETLLGTIMPEEESakvcltdvtimerfqme 800

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  409 LPEVEAELAQRIAALTKSDPTSSTSS-----GDYQYVMEAKLQEMISIRRKAEERHGNIE-------------------- 463
Cdd:TIGR00606  801 LKDVERKIAQQAAKLQGSDLDRTVQQvnqekQEKQHELDTVVSKIELNRKLIQDQQEQIQhlksktnelkseklqigtnl 880

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  464 ERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESES---FRKN- 539
Cdd:TIGR00606  881 QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgYMKDi 960

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024438909  540 -------------------------LEESLHDKERLAEEIEKLRSELDQMKLR 567
Cdd:TIGR00606  961 enkiqdgkddylkqketelntvnaqLEECEKHQEKINEDMRLMRQDIDTQKIQ 1013
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 441-565 1.64e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  441 MEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQR-----EKMNEEHNKRLSDTVDR---LLTESNERL 512
Cdd:COG1579     29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeEQLGNVRNNKEYEALQKeieSLKRRISDL 108

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024438909  513 QLHLKERMAALEEKNVLIQESESFRKNLEESL-HDKERLAEEIEKLRSELDQMK 565
Cdd:COG1579    109 EDEILELMERIEELEEELAELEAELAELEAELeEKKAELDEELAELEAELEELE 162
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 290-561 1.80e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 42.53  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  290 MKERMAAlSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAMAQK--EDMEERITT------LEKRYLSAQRE----S 357
Cdd:PLN03229   421 MKKREAV-KTPVRELEGEVEKLKEQILKAKESSSKPSELALNEMIEKlkKEIDLEYTEaviamgLQERLENLREEfskaN 499

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  358 TSIHDMN-------DKLENEL------ANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAET---LPEV--EAELAQR 419
Cdd:PLN03229   500 SQDQLMHpvlmekiEKLKDEFnkrlsrAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEInkkFKEVmdRPEIKEK 579

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  420 IAALTKSDPTSSTSSGDyqyVMEAKLQEMIS-IRRKAEERHGNIEERM---------RHLEAQLEEKNQELQraRQREKM 489
Cdd:PLN03229   580 MEALKAEVASSGASSGD---ELDDDLKEKVEkMKKEIELELAGVLKSMglevigvtkKNKDTAEQTPPPNLQ--EKIESL 654

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024438909  490 NEEHNKRLSDTVDrlLTESNERLQLhLKERMA------ALEEKNVLIQESESFRKNLEESLHDKErLAEEIEKLRSEL 561
Cdd:PLN03229   655 NEEINKKIERVIR--SSDLKSKIEL-LKLEVAkasktpDVTEKEKIEALEQQIKQKIAEALNSSE-LKEKFEELEAEL 728
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 176-567 1.93e-03

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 42.53  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  176 VLKALKSLFEHHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGE---GPAES---EHIEGME 249
Cdd:pfam06160   81 FKKAKKALDEIEELLDD-IEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRfsyGPAIDeleKQLAEIE 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  250 PGQKVHEKRLSNGsidsndetsQVIELQELLEKQNYEMAQMKERMAALSSRVGEVEQEAETARKELIKTeemnskyqrdI 329
Cdd:pfam06160  160 EEFSQFEELTESG---------DYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEG----------Y 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  330 REAMAQKEDMEErittlekryLSAQRESTSIHDMNDKLENELANKEaiLRQLEDKNRQLQERLElaeqKLQQTMRKaetl 409
Cdd:pfam06160  221 REMEEEGYALEH---------LNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERID----QLYDLLEK---- 281

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  410 pEVEAelaqriaaltksdptsstssgdYQYVmeaklqemisirrkaEERHGNIEERMRHLEAQLEEKNQELQRARQREKM 489
Cdd:pfam06160  282 -EVDA----------------------KKYV---------------EKNLPEIEDYLEHAEEQNKELKEELERVQQSYTL 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  490 NEEH-------NKRLsDTVDRLLTESNERLQLH------LKERMAALEEKNVLIQES-ESFRKNLeESLHDKERLA-EEI 554
Cdd:pfam06160  324 NENElervrglEKQL-EELEKRYDEIVERLEEKevayseLQEELEEILEQLEEIEEEqEEFKESL-QSLRKDELEArEKL 401

                          410
                   ....*....|...
gi 2024438909  555 EKLRSELDQMKLR 567
Cdd:pfam06160  402 DEFKLELREIKRL 414
46 PHA02562
endonuclease subunit; Provisional
 215-416 1.96e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.31  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  215 ANQEIVALREQNAHIQRKIAAGEgpaesEHIEGMEPGQKVHEKRLSNgSIDSNDET-----SQVIELQELLEKQNYEMAQ 289
Cdd:PHA02562   179 LNQQIQTLDMKIDHIQQQIKTYN-----KNIEEQRKKNGENIARKQN-KYDELVEEaktikAEIEELTDELLNLVMDIED 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  290 MKERMAALSSRVGEVEQEAETARKE----------------LIKTEEMNSKYQRDIREAMAQKEDMEERITTLEKRYLSA 353
Cdd:PHA02562   253 PSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcptctqqISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEF 332

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024438909  354 QRESTSIHDMNDKLENelaNKEAILRqLEDKNRQLQERLELAEqklQQTMRKAETLPEVEAEL 416
Cdd:PHA02562   333 NEQSKKLLELKNKIST---NKQSLIT-LVDKAKKVKAAIEELQ---AEFVDNAEELAKLQDEL 388
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1056-1111 2.46e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 37.63  E-value: 2.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024438909 1056 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1111
Cdd:pfam07647   11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
pepcterm_ChnLen TIGR03007
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ...
 209-418 3.16e-03

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


Pssm-ID: 274386 [Multi-domain]  Cd Length: 498  Bit Score: 41.58  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  209 EEELAAANQEI-VALR---EQNAHIQRKIAAGEGPAES---EHIEGMepgqkvhekrlsngSIDSNDETSQVIELQELLE 281
Cdd:TIGR03007  149 EETLGSKRQDSdSAQRfidEQIKTYEKKLEAAENRLKAfkqENGGIL--------------PDQEGDYYSEISEAQEELE 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  282 KQNYEMAQMKERMAALSSRVG----EVEQEAETARKEL-IKTEEMNSKYQR----------DIREAMAQKEDMEERITTL 346
Cdd:TIGR03007  215 AARLELNEAIAQRDALKRQLGgeepVLLAGSSVANSELdGRIEALEKQLDAlrlrytdkhpDVIATKREIAQLEEQKEEE 294

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024438909  347 EKRYLSAQRESTSIHDMNDKLENELANKEAILRQLEDKNRQLQERLElaeqklqQTMRKAETLPEVEAELAQ 418
Cdd:TIGR03007  295 GSAKNGGPERGEIANPVYQQLQIELAEAEAEIASLEARVAELTARIE-------RLESLLRTIPEVEAELTQ 359
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 259-398 3.41e-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: 41.97  E-value: 3.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  259 LSNGSIDSNDETSQVIE---LQELLEKQNYEMAQMK--ERMAALSSRVGEVEQEAETARKELIKTEEMNSKYQRDIREAM 333
Cdd:pfam05911  671 LVSGSNDLKTEENKRLKeefEQLKSEKENLEVELASctENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMA 750

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024438909  334 AQKEDMEERITTLEKRYLSAQRESTSihdmndkLENELANKEAILRQLEDKNRQLQERLELAEQK 398
Cdd:pfam05911  751 ESYEDLETRLTELEAELNELRQKFEA-------LEVELEEEKNCHEELEAKCLELQEQLERNEKK 808
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 453-720 3.50e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  453 RKAEERHGNIEERMRHLEAQLEEKNQELQR-ARQREKMNEehnkrlsdtVDRLLTESNE-RLQLHLKERMAALEEKNVLI 530
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLKEKEALERQKEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  531 QESESFRKNLEESLHDKERLAEEIEKLRSELDQMKLRAGSLIEPTLSRPHLDsSAELRYSVGSLVDSQSDYRSTKVIRRP 610
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK-IGELEAEIASLERSIAEKERELEDAEE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  611 RRGRMGVRRDEPKVKSLGDHEWNRTQQIGVlsshpfESDTEMSDIDDDDRETLFSSMDLLSPSG------HSDAQTLAMM 684
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEREIEEERKRR------DKLTEEYAELKEELEDLRAELEEVDKEFaetrdeLKDYREKLEK 396

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2024438909  685 LQEQLDAINKEIRLIQEEKESTELRAEEIENRVASV 720
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 328-542 4.26e-03

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: 41.21  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  328 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAI----------LRQLEDKNRQLQE---RLEL 394
Cdd:pfam05622    1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGddsgtpggkkYLLLQKQLEQLQEenfRLET 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  395 AEQKLQQtmrKAETLPEVEAELAQRIAALTKSDPTSSTSSGDYQYVMEA-----KLQEMISIRRKAEERHGNIEERMRHL 469
Cdd:pfam05622   81 ARDDYRI---KCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESsdkvkKLEATVETYKKKLEDLGDLRRQVKLL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  470 E----------AQLEEknqELQRARQREKMNEEHNKRLSDTVDRLLTESN--ERLQL---HLKERMAALE-EKNVLIQES 533
Cdd:pfam05622  158 EernaeymqrtLQLEE---ELKKANALRGQLETYKRQVQELHGKLSEESKkaDKLEFeykKLEEKLEALQkEKERLIIER 234


                   ....*....
gi 2024438909  534 ESFRKNLEE 542
Cdd:pfam05622  235 DTLRETNEE 243
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 272-418 4.34e-03

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


Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 39.66  E-value: 4.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  272 QVIELQELLEKQNYEMAQMKERMAA-LSSRVGEVEQEAETArkELIKTEEMNSKYQRDIREAMAQKEDmeERITTLEKRY 350
Cdd:pfam08703   10 LEQELLELREEQYEQEKKRKEQHLTeQIQKLKELAREKQAA--ELKALKESSESEKKEMKKKLERKRL--ESIQEAKKRT 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024438909  351 LSAQRESTSIHDMNDKLENELANkeaILRQLEDKNRQLQERLELAEQKLQQTMRkaETLPEVEAELAQ 418
Cdd:pfam08703   86 SDKAAQERLKKEINNSHIQEVVQ---SIKQLEEKQKRRQEKLEEKQAECLQQIK--EEEPQLQAELNA 148
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
 464-652 4.64e-03

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


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 41.26  E-value: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  464 ERMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK---NVLIQESESFRKN- 539
Cdd:COG5192    590 EGEEELIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEElrgNFELEERGDPEKKd 669

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  540 LEESLHDKERLAEEIEKLRSELDQM---------KLRAGSLIEPTLSRPHLD----SSAELRYSVGSLVDSQSDYRSTKV 606
Cdd:COG5192    670 VDWYTEEKRKIEEQLKINRSEFETMvpesrvvieGYRAGRYVRIVLSHVPLEfvdeFNSRYPIVLGGLLPAEKEMGIVQG 749

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2024438909  607 -IRRPRRGRMGVRRDEPKVKSLGdheWNRTQQIGVLSSHPFESDTEM 652
Cdd:COG5192    750 rIKRHRWHKKILKTNDPLIFSVG---WRRFQSIPVYSMKDSRTRNRM 793
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 938-995 4.97e-03

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 36.45  E-value: 4.97e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024438909  938 VVAWLElWLGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 995
Cdd:cd09487      2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 292-564 5.58e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 40.78  E-value: 5.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  292 ERMAALSSRVGEVEQEAETARKELIKTEEmnsKYQRDIREAMAQKedMEERITTlekrylSAQRESTSIhdmndklenEL 371
Cdd:pfam05667  210 ERNAAELAAAQEWEEEWNSQGLASRLTPE---EYRKRKRTKLLKR--IAEQLRS------AALAGTEAT---------SG 269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  372 ANKEAI-LRQLEDKNRQLQERLELAEQKLQQTMRKAETLpeveaelAQRIAALTKSDPTSSTSSGDYQyvmEAKLQEMIS 450
Cdd:pfam05667  270 ASRSAQdLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQF-------TNEAPAATSSPPTKVETEEELQ---QQREEELEE 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  451 IRRKAEERHGNIEE---RMRHLEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLL-TESN-ERLQL---HLKERMAA 522
Cdd:pfam05667  340 LQEQLEDLESSIQElekEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPdAEENiAKLQAlvdASAQRLVE 419

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2024438909  523 L----EEKNV-LIQESESFRKNLEESLHDKERLAEEIEKLRSELDQM 564
Cdd:pfam05667  420 LagqwEKHRVpLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEV 466
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 1056-1100 7.45e-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: 36.51  E-value: 7.45e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2024438909 1056 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 1100
Cdd:cd09501     11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 40-225 7.97e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 40.30  E-value: 7.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909   40 DERDRLLDTLRETQ----ESLS--LAQQRLQDVIYDRDSLQR---QLNSALPqmtvAAGTSIENNIQRTISCPNEFAA-L 109
Cdd:PRK05771    16 SYKDEVLEALHELGvvhiEDLKeeLSNERLRKLRSLLTKLSEaldKLRSYLP----KLNPLREEKKKVSVKSLEELIKdV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  110 TKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVS-----RHERSLRMTV-----VKRQAQSPSGVSSEVEVLKA 179
Cdd:PRK05771    92 EEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNfdldlSLLLGFKYVSvfvgtVPEDKLEELKLESDVENVEY 171

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024438909  180 LKSLFEH-------HKALDEKVRERLR-------------VSLERVSALEEELAAANQEIVALREQ 225
Cdd:PRK05771   172 ISTDKGYvyvvvvvLKELSDEVEEELKklgferleleeegTPSELIREIKEELEEIEKERESLLEE 237
Tmemb_cc2 pfam10267
Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil ...
 426-564 8.01e-03

Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil containing proteins is conserved from worms to humans. Its function is unknown.


Pssm-ID: 463036  Cd Length: 401  Bit Score: 40.02  E-value: 8.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  426 SDPTSSTSSGDYQYVMEAKLQEMISIRrkaeERHGNIEERMRHLEAQLEEKNQELQRARQREKMNEEhnkRLSDTVDRLl 505
Cdd:pfam10267  207 ADNGGQQAESDSQNGLAAILEELQEIK----EAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYE---RLEEQLNDL- 278

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024438909  506 TESNERLQLHLKERMAALEEKnVLIQESESFRkNLEESLhdkERLAEEIEKLrsELDQM 564
Cdd:pfam10267  279 TELHQNEIANLKQELASMEEK-VAYQSYERAR-DIQEAL---ESCQTRISKM--ELQQQ 330
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 105-573 8.67e-03

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: 40.73  E-value: 8.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  105 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLF 184
Cdd:pfam02463  237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  185 EHHKA----------LDEKVRERLRVSLERVSALEEELAAANQEIVALREQNAHIQRKIAAGEGPAESEHIEGMEPGQKV 254
Cdd:pfam02463  317 KESEKekkkaekelkKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  255 HEKRLSNGSIDS-------NDETSQVIELQELLEKQNYEmaqmKERMAALSSRVGEVEQEAETARKELIKTEEMNSKyqr 327
Cdd:pfam02463  397 LELKSEEEKEAQlllelarQLEDLLKEEKKEELEILEEE----EESIELKQGKLTEEKEELEKQELKLLKDELELKK--- 469

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  328 diREAMAQKEDMEERITTLEKRYLSAQRESTSihdMNDKLENELANKEAILRQLEDKNRQLQERLELAEQKLQQTMRKAE 407
Cdd:pfam02463  470 --SEDLLKETQLVKLQEQLELLLSRQKLEERS---QKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  408 TLPEVEAELAQRIAALTKSDptSSTSSGDYQYVMEAKLQEMISIRRKAEERHGNIEERMRHLEAQLEEKNQELQRARQRE 487
Cdd:pfam02463  545 ISTAVIVEVSATADEVEERQ--KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024438909  488 KMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESE--SFRKNLEESLHDKERLAEEIEKLRSELDQMK 565
Cdd:pfam02463  623 KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSelTKELLEIQELQEKAESELAKEEILRRQLEIK 702


                   ....*...
gi 2024438909  566 LRAGSLIE 573
Cdd:pfam02463  703 KKEQREKE 710
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH