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Conserved domains on  [gi|2017363533|ref|NP_001380881|]
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liprin-alpha-4 isoform 5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 965-1030 1.20e-43

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


:

Pssm-ID: 188964  Cd Length: 66  Bit Score: 152.24  E-value: 1.20e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363533  965 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1030
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 848-918 3.36e-42

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


:

Pssm-ID: 188961  Cd Length: 71  Bit Score: 148.48  E-value: 3.36e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363533  848 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 918
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_superfamily super family cl15755
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 1050-1108 2.10e-32

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.


The actual alignment was detected with superfamily member cd09568:

Pssm-ID: 472832  Cd Length: 72  Bit Score: 120.50  E-value: 2.10e-32
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363533 1050 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQ 1108
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQ 59
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 221-501 6.08e-14

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.90  E-value: 6.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  221 WKEDTGRVEELQELLEKQNFELSQARERlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITT 300
Cdd:COG1196    241 LEELEAELEELEAELEELEAELAELEAE--------------LEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  301 LEKRYLAAQ----REATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIA 376
Cdd:COG1196    307 LEERRRELEerleELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  377 ALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERmAALEEKNTLI 456
Cdd:COG1196    387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELL 465

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2017363533  457 QELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGRGGPFVDGV 501
Cdd:COG1196    466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 33-380 8.31e-05

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: 46.98  E-value: 8.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   33 MLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAErnntr 112
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----- 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  113 llLEHLECLVSRHERSLrmtvVKRQAQ--------SPSGVSsevEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEE 184
Cdd:TIGR02169  760 --LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKE 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  185 QLAGAHQQvsALQQGAGVRDGAAEEEGTVElgpkrlwkEDTGRVEELQELLEKQNFELSQARERlvtltttvteleedLG 264
Cdd:TIGR02169  830 YLEKEIQE--LQEQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEELEAALRDLESR--------------LG 885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  265 TARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANK---ESLHRQCEEKAR 341
Cdd:TIGR02169  886 DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDVQAELQRVEE 965

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2017363533  342 HLQELLEV---AEQKLQQTMR-------KAETLPEVEAELAQRIAALTK 380
Cdd:TIGR02169  966 EIRALEPVnmlAIQEYEEVLKrldelkeKRAKLEEERKAILERIEEYEK 1014
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 965-1030 1.20e-43

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


Pssm-ID: 188964  Cd Length: 66  Bit Score: 152.24  E-value: 1.20e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363533  965 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1030
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 848-918 3.36e-42

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


Pssm-ID: 188961  Cd Length: 71  Bit Score: 148.48  E-value: 3.36e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363533  848 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 918
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1050-1108 2.10e-32

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: 120.50  E-value: 2.10e-32
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363533 1050 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQ 1108
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQ 59
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 964-1028 5.44e-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: 5.44e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363533  964 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1028
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 221-501 6.08e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.90  E-value: 6.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  221 WKEDTGRVEELQELLEKQNFELSQARERlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITT 300
Cdd:COG1196    241 LEELEAELEELEAELEELEAELAELEAE--------------LEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  301 LEKRYLAAQ----REATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIA 376
Cdd:COG1196    307 LEERRRELEerleELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  377 ALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERmAALEEKNTLI 456
Cdd:COG1196    387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELL 465

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2017363533  457 QELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGRGGPFVDGV 501
Cdd:COG1196    466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-493 1.45e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.86  E-value: 1.45e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  170 ERLRAALERVT----TLEEQLAGAHQQVSALQQGAGVRdgaaEEEGTVELgpkRLWkedTGRVEELQELLEKQNFELSQA 245
Cdd:TIGR02168  182 ERTRENLDRLEdilnELERQLKSLERQAEKAERYKELK----AELRELEL---ALL---VLRLEELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  246 RERLVtltttvteleedlgTARRDLIKSEELSSKHQRDLREalaqkedMEERITTLEKRYLAAQREatsIHDLNDKLENE 325
Cdd:TIGR02168  252 EEELE--------------ELTAELQELEEKLEELRLEVSE-------LEEEIEELQKELYALANE---ISRLEQQKQIL 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  326 LANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  406 LARVRQREKM-------NEDHNKRLSDTVDRLLSESNERLQ----LHLKERMAALEEKNTLIQELESSQRQIEEQhhhKG 474
Cdd:TIGR02168  388 VAQLELQIASlnneierLEARLERLEDRRERLQQEIEELLKkleeAELKELQAELEELEEELEELQEELERLEEA---LE 464

                          330
                   ....*....|....*....
gi 2017363533  475 RLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02168  465 ELREELEEAEQALDAAERE 483
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
38-493 3.87e-11

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 67.76  E-value: 3.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   38 EKLLESLRESQETLAATQSRLQDA-IHERdqlqrhLNsALPQEFATLTRElsmcreqllereeeISELKAERNNTRLLLE 116
Cdd:PRK02224   179 ERVLSDQRGSLDQLKAQIEEKEEKdLHER------LN-GLESELAELDEE--------------IERYEEQREQARETRD 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  117 HLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalERVTTLEEQLAGAHQQVSAL 196
Cdd:PRK02224   238 EADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDDL 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  197 QQGAGVRDGAAEeegTVELGPKRLWKEDtgrvEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEEL 276
Cdd:PRK02224   299 LAEAGLDDADAE---AVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  277 SSKHQRDLREALAQKEDMEERITTLEKRYLAAqreATSIHDLNDKLENELANKESLHRQCEEkarhlqelLEVAEQKLQQ 356
Cdd:PRK02224   372 LEEAREAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELREREAE--------LEATLRTARE 440

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  357 TMRKAETL------PEVEAEL--AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMnEDHNKRLSD--- 425
Cdd:PRK02224   441 RVEEAEALleagkcPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEErre 519

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363533  426 TVDRLLSESNERLQlhlkERMAALEEKNTLIQELESSQrqiEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PRK02224   520 DLEELIAERRETIE----EKRERAEELRERAAELEAEA---EEKREAAAEAEEEAEEAREEVAELNSK 580
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 31-491 1.23e-09

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: 62.82  E-value: 1.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   31 VNMLDEREKLL-ESLRESQETLAATQSRLQDAiheRDQLQRHLNS--ALPQEFATLTRELSMCREQLLEREEE------- 100
Cdd:pfam05483  270 ANQLEEKTKLQdENLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKTICQLTEEKEAQMEElnkakaa 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  101 ----ISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEHHKALDEKvrER 171
Cdd:pfam05483  347 hsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  172 LRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDtgrVEELQELLEKQ---NFELSQARER 248
Cdd:pfam05483  420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE---VEDLKTELEKEklkNIELTAHCDK 496

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  249 LVTLTTTVTELEEDLgtarrdlikSEELSsKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD----LNDKLEN 324
Cdd:pfam05483  497 LLLENKELTQEASDM---------TLELK-KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqKGDEVKC 566

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  325 ELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTK---AEERHGNIEE-HLRQLEGQLE 400
Cdd:pfam05483  567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKkgsAENKQLNAYEiKVNKLELELA 646

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  401 EKNQ---ELARVRQRE----KMNEDH-------NKRLSDTVDRLLSESNERLQLHLKErMAALEEK-----NTLIQELES 461
Cdd:pfam05483  647 SAKQkfeEIIDNYQKEiedkKISEEKlleevekAKAIADEAVKLQKEIDKRCQHKIAE-MVALMEKhkhqyDKIIEERDS 725

                          490       500       510
                   ....*....|....*....|....*....|....
gi 2017363533  462 S----QRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam05483  726 ElglyKNKEQEQSSAKAALEIELSNIKAELLSLK 759
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 848-914 4.63e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 51.14  E-value: 4.63e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363533   848 FAQWDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 914
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 973-1028 9.28e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.99  E-value: 9.28e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363533   973 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1028
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-380 8.31e-05

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: 46.98  E-value: 8.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   33 MLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAErnntr 112
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----- 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  113 llLEHLECLVSRHERSLrmtvVKRQAQ--------SPSGVSsevEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEE 184
Cdd:TIGR02169  760 --LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKE 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  185 QLAGAHQQvsALQQGAGVRDGAAEEEGTVElgpkrlwkEDTGRVEELQELLEKQNFELSQARERlvtltttvteleedLG 264
Cdd:TIGR02169  830 YLEKEIQE--LQEQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEELEAALRDLESR--------------LG 885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  265 TARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANK---ESLHRQCEEKAR 341
Cdd:TIGR02169  886 DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDVQAELQRVEE 965

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2017363533  342 HLQELLEV---AEQKLQQTMR-------KAETLPEVEAELAQRIAALTK 380
Cdd:TIGR02169  966 EIRALEPVnmlAIQEYEEVLKrldelkeKRAKLEEERKAILERIEEYEK 1014
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1051-1093 2.17e-04

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: 40.74  E-value: 2.17e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2017363533  1051 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDH 1093
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEED 43
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1051-1097 2.41e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 40.33  E-value: 2.41e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2017363533 1051 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALdeNFDHNTLA 1097
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK 45
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 338-493 3.71e-04

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.20  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  338 EKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNE 417
Cdd:cd00176     40 KKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEELNQRWEELRELAEERRQRLEEALDLQQFFR 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  418 DH---NKRLSDTVDRLLSESN-------ERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGR--LSEEIEKLRQ 485
Cdd:cd00176    114 DAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeeIEEKLEELNE 193


                   ....*...
gi 2017363533  486 EVDQLKGR 493
Cdd:cd00176    194 RWEELLEL 201
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 850-914 1.67e-03

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 38.02  E-value: 1.67e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363533  850 QWDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 914
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 965-1030 1.20e-43

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


Pssm-ID: 188964  Cd Length: 66  Bit Score: 152.24  E-value: 1.20e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363533  965 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1030
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 848-918 3.36e-42

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


Pssm-ID: 188961  Cd Length: 71  Bit Score: 148.48  E-value: 3.36e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363533  848 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 918
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1050-1108 2.10e-32

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: 120.50  E-value: 2.10e-32
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363533 1050 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQ 1108
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQ 59
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 969-1028 9.50e-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: 115.32  E-value: 9.50e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  969 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1028
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 ...
 855-913 4.65e-25

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


Pssm-ID: 188893  Cd Length: 58  Bit Score: 98.84  E-value: 4.65e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363533  855 TVVSWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 913
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 ...
 1058-1108 9.26e-21

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: 86.83  E-value: 9.26e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2017363533 1058 QVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQ 1108
Cdd:cd09496      1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQ 51
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 1050-1103 3.20e-17

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: 77.10  E-value: 3.20e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2017363533 1050 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIP 1103
Cdd:cd09570      1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIP 54
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 964-1028 3.82e-16

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 73.98  E-value: 3.82e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363533  964 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1028
Cdd:cd09567      1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 964-1028 3.84e-16

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 73.88  E-value: 3.84e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363533  964 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1028
Cdd:cd09566      1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 849-913 1.19e-15

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


Pssm-ID: 188963  Cd Length: 70  Bit Score: 72.48  E-value: 1.19e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363533  849 AQWDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 913
Cdd:cd09564      2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 1050-1107 1.43e-14

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: 69.41  E-value: 1.43e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363533 1050 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNT 1107
Cdd:cd09569      1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKT 58
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 964-1028 5.44e-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: 5.44e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363533  964 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1028
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 221-501 6.08e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.90  E-value: 6.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  221 WKEDTGRVEELQELLEKQNFELSQARERlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITT 300
Cdd:COG1196    241 LEELEAELEELEAELEELEAELAELEAE--------------LEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  301 LEKRYLAAQ----REATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIA 376
Cdd:COG1196    307 LEERRRELEerleELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  377 ALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERmAALEEKNTLI 456
Cdd:COG1196    387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELL 465

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2017363533  457 QELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGRGGPFVDGV 501
Cdd:COG1196    466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-493 1.45e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.86  E-value: 1.45e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  170 ERLRAALERVT----TLEEQLAGAHQQVSALQQGAGVRdgaaEEEGTVELgpkRLWkedTGRVEELQELLEKQNFELSQA 245
Cdd:TIGR02168  182 ERTRENLDRLEdilnELERQLKSLERQAEKAERYKELK----AELRELEL---ALL---VLRLEELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  246 RERLVtltttvteleedlgTARRDLIKSEELSSKHQRDLREalaqkedMEERITTLEKRYLAAQREatsIHDLNDKLENE 325
Cdd:TIGR02168  252 EEELE--------------ELTAELQELEEKLEELRLEVSE-------LEEEIEELQKELYALANE---ISRLEQQKQIL 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  326 LANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  406 LARVRQREKM-------NEDHNKRLSDTVDRLLSESNERLQ----LHLKERMAALEEKNTLIQELESSQRQIEEQhhhKG 474
Cdd:TIGR02168  388 VAQLELQIASlnneierLEARLERLEDRRERLQQEIEELLKkleeAELKELQAELEELEEELEELQEELERLEEA---LE 464

                          330
                   ....*....|....*....
gi 2017363533  475 RLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02168  465 ELREELEEAEQALDAAERE 483
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 147-418 1.23e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 1.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  147 EVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEdtg 226
Cdd:COG1196    233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE--- 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1196    310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  307 AAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHG 386
Cdd:COG1196    390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---EAAEEEAELEEEEEALLELLA 466

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2017363533  387 NIEEHLRQLEGQLEEKNQELARVRQREKMNED 418
Cdd:COG1196    467 ELLEEAALLEAALAELLEELAEAAARLLLLLE 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 267-491 2.33e-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: 2.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  267 RRDLIksEELS--SKHQRDLREALAQKEDMEERIT-------TLEKRY--LAAQRE-ATSIHDLNDKLEnELANKESLHR 334
Cdd:COG1196    157 RRAII--EEAAgiSKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEkAERYRELKEELK-ELEAELLLLK 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  335 qceekARHLQELLEVAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREK 414
Cdd:COG1196    234 -----LRELEAELEELEAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  415 MNEDHNKRLSDTVDRL---LSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG1196    306 RLEERRRELEERLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
38-493 3.87e-11

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 67.76  E-value: 3.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   38 EKLLESLRESQETLAATQSRLQDA-IHERdqlqrhLNsALPQEFATLTRElsmcreqllereeeISELKAERNNTRLLLE 116
Cdd:PRK02224   179 ERVLSDQRGSLDQLKAQIEEKEEKdLHER------LN-GLESELAELDEE--------------IERYEEQREQARETRD 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  117 HLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalERVTTLEEQLAGAHQQVSAL 196
Cdd:PRK02224   238 EADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDDL 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  197 QQGAGVRDGAAEeegTVELGPKRLWKEDtgrvEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEEL 276
Cdd:PRK02224   299 LAEAGLDDADAE---AVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  277 SSKHQRDLREALAQKEDMEERITTLEKRYLAAqreATSIHDLNDKLENELANKESLHRQCEEkarhlqelLEVAEQKLQQ 356
Cdd:PRK02224   372 LEEAREAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELREREAE--------LEATLRTARE 440

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  357 TMRKAETL------PEVEAEL--AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMnEDHNKRLSD--- 425
Cdd:PRK02224   441 RVEEAEALleagkcPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEErre 519

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363533  426 TVDRLLSESNERLQlhlkERMAALEEKNTLIQELESSQrqiEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PRK02224   520 DLEELIAERRETIE----EKRERAEELRERAAELEAEA---EEKREAAAEAEEEAEEAREEVAELNSK 580
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-490 4.29e-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: 67.77  E-value: 4.29e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  147 EVEVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVElgpkrlwKEDTG 226
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL-------AEAEA 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  307 AAQREATSIHDLNDKLENELANkeslhrqceekarhLQELLEVAEQKLQQTMrkaETLPEVEAELAQRIAALTKAEERHG 386
Cdd:TIGR02168  863 ELEELIEELESELEALLNERAS--------------LEEALALLRSELEELS---EELRELESKRSELRRELEELREKLA 925

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  387 NIEEHLRQLEGQLEEKNQelaRVRQREKMNEDHNKRLSDTVDRLLSESNERLQLhLKERMAALEEKN-TLIQELESSQRQ 465
Cdd:TIGR02168  926 QLELRLEGLEVRIDNLQE---RLSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNlAAIEEYEELKER 1001

                          330       340
                   ....*....|....*....|....*
gi 2017363533  466 IEEQHHHKGRLSEEIEKLRQEVDQL 490
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAKETLEEAIEEI 1026
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 20-439 9.95e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.50  E-value: 9.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   20 ADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSmcreqlleREE 99
Cdd:COG1196    406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL--------LEA 477

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  100 EISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHH------KALDEKVRERLR 173
Cdd:COG1196    478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAleaalaAALQNIVVEDDE 557

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  174 AALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKrlwkedtGRVEELQELLEKQNFELSQARERLVTLT 253
Cdd:COG1196    558 VAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD-------LVASDLREADARYYVLGDTLLGRTLVAA 630

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  254 TTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLH 333
Cdd:COG1196    631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  334 RQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEK---N----QEL 406
Cdd:COG1196    711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvNllaiEEY 790

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 2017363533  407 ARVRQR-EKMNEDHN------KRLSDTVDRLLSESNERLQ 439
Cdd:COG1196    791 EELEERyDFLSEQREdleearETLEEAIEEIDRETRERFL 830
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 848-912 1.36e-10

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


Pssm-ID: 188962  Cd Length: 64  Bit Score: 58.01  E-value: 1.36e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363533  848 FAQWDGPTVVSWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQ 912
Cdd:cd09563      1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 20-468 2.12e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 2.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   20 ADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREE 99
Cdd:COG1196    329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-EELLEALRAAAELAAQLEELEE 407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  100 EISELKAERNNTRLLLEHLEclvSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG1196    408 AEEALLERLERLEEELEELE---EALAELEEEEEEEEEALE-----EAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  180 TTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKR--------LWKEDTGRVEELQELLEKQNFELSQARERLVT 251
Cdd:COG1196    480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  252 LTTTVTELEEDLGTARR---DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDlNDKLENELAN 328
Cdd:COG1196    560 AAAIEYLKAAKAGRATFlplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV-AARLEAALRR 638

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  329 KESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELAR 408
Cdd:COG1196    639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  409 VRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEE 468
Cdd:COG1196    719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 218-491 3.08e-10

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 64.70  E-value: 3.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  218 KRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEE----LSSKHQRDLREALAQKED 293
Cdd:TIGR02169  155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEA 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHL--QELLEVAEQ--KLQQTMRKAE-TLPEVE 368
Cdd:TIGR02169  235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKigELEAEIASLErSIAEKE 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  369 AELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDhnkRLSDTVDRLLSESnerlqlhlKERMAA 448
Cdd:TIGR02169  315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE---ELEDLRAELEEVD--------KEFAET 383

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2017363533  449 LEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR02169  384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 281-491 8.18e-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: 63.54  E-value: 8.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQ-ELLEVAEQKLQQTMR 359
Cdd:TIGR02168  690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSkELTELEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  360 KAE---TLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesne 436
Cdd:TIGR02168  770 LEEaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL------ 843

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2017363533  437 rlqlhlKERMAALEEkntliqELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR02168  844 ------EEQIEELSE------DIESLAAEIEELEELIEELESELEALLNERASLE 886
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 31-491 1.23e-09

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: 62.82  E-value: 1.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   31 VNMLDEREKLL-ESLRESQETLAATQSRLQDAiheRDQLQRHLNS--ALPQEFATLTRELSMCREQLLEREEE------- 100
Cdd:pfam05483  270 ANQLEEKTKLQdENLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKTICQLTEEKEAQMEElnkakaa 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  101 ----ISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEHHKALDEKvrER 171
Cdd:pfam05483  347 hsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  172 LRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDtgrVEELQELLEKQ---NFELSQARER 248
Cdd:pfam05483  420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE---VEDLKTELEKEklkNIELTAHCDK 496

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  249 LVTLTTTVTELEEDLgtarrdlikSEELSsKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD----LNDKLEN 324
Cdd:pfam05483  497 LLLENKELTQEASDM---------TLELK-KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqKGDEVKC 566

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  325 ELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTK---AEERHGNIEE-HLRQLEGQLE 400
Cdd:pfam05483  567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKkgsAENKQLNAYEiKVNKLELELA 646

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  401 EKNQ---ELARVRQRE----KMNEDH-------NKRLSDTVDRLLSESNERLQLHLKErMAALEEK-----NTLIQELES 461
Cdd:pfam05483  647 SAKQkfeEIIDNYQKEiedkKISEEKlleevekAKAIADEAVKLQKEIDKRCQHKIAE-MVALMEKhkhqyDKIIEERDS 725

                          490       500       510
                   ....*....|....*....|....*....|....
gi 2017363533  462 S----QRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam05483  726 ElglyKNKEQEQSSAKAALEIELSNIKAELLSLK 759
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 35-491 1.30e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   35 DEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLL 114
Cdd:COG1196    253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-AELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  115 LEHLECLVSRHERSLRMTVVKRQAqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:COG1196    332 LEELEEELEELEEELEEAEEELEE-------AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  195 ALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSE 274
Cdd:COG1196    405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  275 ELSSKHQRDLREALAQKEDMEE---------------------RITTLEKRYLAAQREATSIHDLNDKLENELANKE--- 330
Cdd:COG1196    485 ELAEAAARLLLLLEAEADYEGFlegvkaalllaglrglagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAaie 564

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  331 -------------SLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEG 397
Cdd:COG1196    565 ylkaakagratflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  398 QLEEKNQELARVRQREKMNEDHNKRLSdtvdRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLS 477
Cdd:COG1196    645 RLREVTLEGEGGSAGGSLTGGSRRELL----AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720

                          490
                   ....*....|....
gi 2017363533  478 EEIEKLRQEVDQLK 491
Cdd:COG1196    721 LEEEALEEQLEAER 734
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
22-493 1.48e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.39  E-value: 1.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   22 ADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQrhlnsALPQEFATLTRELSMCREQLLEREEEI 101
Cdd:PRK03918   187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-----ELKEEIEELEKELESLEGSKRKLEEKI 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  102 SELKAERNNTRLLLEHLECLVSRHE--RSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRErLRAALERV 179
Cdd:PRK03918   262 RELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERL 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  180 TTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTEL 259
Cdd:PRK03918   341 EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  260 EEDLGTARRDLIKS----------------EELSSKHQRDLREALAQKEDMEERITTLEKR------YLAAQREATSIHD 317
Cdd:PRK03918   421 IKELKKAIEELKKAkgkcpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKERKLRKElrelekVLKKESELIKLKE 500

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  318 LNDKLEN-----ELANKESLHRQCEEkARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHL 392
Cdd:PRK03918   501 LAEQLKEleeklKKYNLEELEKKAEE-YEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL 579

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  393 RQL----EGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQL--HLKERMAALEEKNTLIQELES--SQR 464
Cdd:PRK03918   580 EELgfesVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAfeELAETEKRLEELRKELEELEKkySEE 659

                          490       500
                   ....*....|....*....|....*....
gi 2017363533  465 QIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PRK03918   660 EYEELREEYLELSRELAGLRAELEELEKR 688
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 37-409 1.74e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 1.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   37 REKLLESLRESQETLAatqsRLQDAIHERD-QLQR-HLNSALPQEFATLTRELSmcREQLLEREEEISELKAERNNTRLL 114
Cdd:TIGR02168  174 RKETERKLERTRENLD----RLEDILNELErQLKSlERQAEKAERYKELKAELR--ELELALLVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  115 LEHLECLVSRHERSLRMTvvkrqaqspsgvSSEVEVLKALKSlfEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:TIGR02168  248 LKEAEEELEELTAELQEL------------EEKLEELRLEVS--ELEEEIEE-LQKELYALANEISRLEQQKQILRERLA 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  195 ALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSE 274
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  275 ELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATS-----IHDLNDKLENELANKESLHRQCEEKARHLQELLEV 349
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEELEEELEELQEELERLEEALEELREELEE 472

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  350 AEQKLQQTMRKaetlpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARV 409
Cdd:TIGR02168  473 AEQALDAAERE-------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
262-495 2.77e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.62  E-value: 2.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKAR 341
Cdd:PRK03918   159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  342 HLQEL----------LEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER----------HGNIEEHLRQLEGQLEE 401
Cdd:PRK03918   239 EIEELekeleslegsKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKaeeyiklsefYEEYLDELREIEKRLSR 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  402 KNQELARVRQREKMNEDHNKRLSDTVDRL------LSESNERLQLH-----LKERMAALEEKNTlIQELESSQRQIEEQH 470
Cdd:PRK03918   319 LEEEINGIEERIKELEEKEERLEELKKKLkelekrLEELEERHELYeeakaKKEELERLKKRLT-GLTPEKLEKELEELE 397

                          250       260
                   ....*....|....*....|....*
gi 2017363533  471 HHKGRLSEEIEKLRQEVDQLKGRGG 495
Cdd:PRK03918   398 KAKEEIEEEISKITARIGELKKEIK 422
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
9-470 3.20e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 60.94  E-value: 3.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533    9 NEGDRLGPPHGADADANFEQLmvnmlDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSA------------- 75
Cdd:COG4717     53 KEADELFKPQGRKPELNLKEL-----KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeleklekllql 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   76 --LPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVVKRQAQSPSGVSSEVEVLKA 153
Cdd:COG4717    128 lpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA----ELQEELEELLEQLSLATEEELQDLAEELEE 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAH--QQVSALQQGAGVRDGAAEEEGTVELGPKRLWKED------T 225
Cdd:COG4717    204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvL 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  226 GRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRY 305
Cdd:COG4717    284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  306 LAAQREATSIHDLND---KLENELANKESLHRQCEEkarhLQELLEVAEQKLqqtmrkAETLPEVEAELAQriAALTKAE 382
Cdd:COG4717    364 QLEELEQEIAALLAEagvEDEEELRAALEQAEEYQE----LKEELEELEEQL------EELLGELEELLEA--LDEEELE 431

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  383 ERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDhnkrlSDTVDRLLSEsnerlQLHLKERMAALEEK----NTLIQE 458
Cdd:COG4717    432 EELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQE-----LEELKAELRELAEEwaalKLALEL 501

                          490
                   ....*....|..
gi 2017363533  459 LESSQRQIEEQH 470
Cdd:COG4717    502 LEEAREEYREER 513
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
34-491 3.73e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.23  E-value: 3.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   34 LDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS---------ALPQEFATLTRELSMCREQLLEREEEISEL 104
Cdd:PRK03918   240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkelkEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  105 KAERNNTRLLLEHLECLVSR-HERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD-----EKVRERLRAALER 178
Cdd:PRK03918   320 EEEINGIEERIKELEEKEERlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKA 399

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  179 VTTLEEQLAGAHQQVSALQQGAGVRDGAAEE----EGTVELGPKRLWKEDTGRV-EELQELLEKQNFELSQARERLVTLT 253
Cdd:PRK03918   400 KEEIEEEISKITARIGELKKEIKELKKAIEElkkaKGKCPVCGRELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLR 479

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  254 TTVTELEEDLGTARR--------DLIKS--EELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK-- 321
Cdd:PRK03918   480 KELRELEKVLKKESEliklkelaEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKla 559

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  322 -LENELANKES----LHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLE 396
Cdd:PRK03918   560 eLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETE 639

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  397 GQLEEKNQELarvrqrekmnEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRL 476
Cdd:PRK03918   640 KRLEELRKEL----------EELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709

                          490
                   ....*....|....*
gi 2017363533  477 SEEIEKLRQEVDQLK 491
Cdd:PRK03918   710 KKELEKLEKALERVE 724
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 342-493 7.24e-09

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 57.63  E-value: 7.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  342 HLQELLEVAE--QKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVrqREKM 415
Cdd:COG1579      5 DLRALLDLQEldSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY--EEQL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  416 NEDHNKRLSDTVDR---LLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHH-KGRLSEEIEKLRQEVDQLK 491
Cdd:COG1579     83 GNVRNNKEYEALQKeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEkKAELDEELAELEAELEELE 162


                   ..
gi 2017363533  492 GR 493
Cdd:COG1579    163 AE 164
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 21-491 7.95e-09

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: 60.13  E-value: 7.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   21 DADANFEQLMVNMLDErEKLLESLREsqeTLAATQSRLQDAIHERDQLQ----RHLNSALPQEFATLTRELSMCREQLLE 96
Cdd:pfam15921  167 DSNTQIEQLRKMMLSH-EGVLQEIRS---ILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   97 REEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-----RMTVVKRQAQSpsgVSSEVEV------------LKAL 154
Cdd:pfam15921  243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQL 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  155 KSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHqqvSALQQGAGVRDGAAEEEGTV----------------ELG-- 216
Cdd:pfam15921  320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN---SELTEARTERDQFSQESGNLddqlqklladlhkrekELSle 396

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  217 ---PKRLWKEDTG-----------------RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLG--TARRDLIKS- 273
Cdd:pfam15921  397 keqNKRLWDRDTGnsitidhlrrelddrnmEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSslTAQLESTKEm 476

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  274 -----EELSSKHQ---------RDLREALAQKEDMEE----RITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQ 335
Cdd:pfam15921  477 lrkvvEELTAKKMtlessertvSDLTASLQEKERAIEatnaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 556

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  336 CEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQriaaLTKA-EERHGNIEEhLRQLEGQLEEKNQEL-ARVRQRE 413
Cdd:pfam15921  557 MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ----LEKEiNDRRLELQE-FKILKDKKDAKIRELeARVSDLE 631

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  414 ----KMNEDHNKRLSDTVDRllseSNERLQLhLKERMAALEEKNTLIQELESSQRQI----EEQHHHKGRLSEEIEKLRQ 485
Cdd:pfam15921  632 lekvKLVNAGSERLRAVKDI----KQERDQL-LNEVKTSRNELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQS 706


                   ....*.
gi 2017363533  486 EVDQLK 491
Cdd:pfam15921  707 ELEQTR 712
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 35-490 1.05e-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: 1.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   35 DEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS------ALPQEFATLTRELSMCREQLLEREEEISELKAER 108
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeeleSLEAELEELEAELEELESRLEELEEQLETLRSKV 388

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  109 NNTRL-----------LLEHLECLVSRHER------SLRMTVVKRQAQSPSGVSSEVE-VLKALKSLFEHHKALDEKVRE 170
Cdd:TIGR02168  389 AQLELqiaslnneierLEARLERLEDRRERlqqeieELLKKLEEAELKELQAELEELEeELEELQEELERLEEALEELRE 468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  171 RLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLwKEDTGRVEEL------------------- 231
Cdd:TIGR02168  469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL-SGILGVLSELisvdegyeaaieaalggrl 547

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  232 --------------QELLEKQN------FELSQARERLVTLTTTVTELEED--LGTARrDLIKSEELSSK-------HQR 282
Cdd:TIGR02168  548 qavvvenlnaakkaIAFLKQNElgrvtfLPLDSIKGTEIQGNDREILKNIEgfLGVAK-DLVKFDPKLRKalsyllgGVL 626

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  283 ---DLREALAQ--KEDMEERITTLE-----KRYLAAQREATSIHDLNDKlENELANKESLHRQCEEKARHLQELLEVAEQ 352
Cdd:TIGR02168  627 vvdDLDNALELakKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAELEKALAELRK 705

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  353 KLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVD 428
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363533  429 RL-----------------LSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQL 490
Cdd:TIGR02168  786 ELeaqieqlkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
280-486 1.53e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 59.16  E-value: 1.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  280 HQRDLREALAQK----EDMEERITTLEKRYLAAQREAtsihdlnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQ 355
Cdd:COG4913    590 HEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEEL-------AEAEERLEALEAELDALQERREALQRLAEYSWDEID 662

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  356 qTMRKAETLPEVEAELAQRIAA---LTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS 432
Cdd:COG4913    663 -VASAEREIAELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2017363533  433 ESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQE 486
Cdd:COG4913    742 LARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 281-486 2.35e-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: 2.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  361 AETLpevEAELAQRIAALTK------------------AEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKR 422
Cdd:COG4942     99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017363533  423 LSDTVDRlLSESNERLQLHLKERMAALEEKNtliQELESSQRQIEEQHHHKGRLSEEIEKLRQE 486
Cdd:COG4942    176 LEALLAE-LEEERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAE 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 34-493 2.70e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 2.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   34 LDEREKLLESLRESQETLAATQSRL-QDAIHERDQLQRHLNSA--LPQEFATLTRELSMCREQLLEREEEISELKAERNN 110
Cdd:COG1196    276 LEELELELEEAQAEEYELLAELARLeQDIARLEERRRELEERLeeLEEELAELEEELEELEEELEELEEELEEAEEELEE 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  111 TRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERvTTLEEQLAGAH 190
Cdd:COG1196    356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL-EELEEALAELE 434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  191 QQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDL 270
Cdd:COG1196    435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  271 IKS------------------------EELSSKHQRDLREALAQ--------KEDMEERITTLEKRyLAAQREATSIHDL 318
Cdd:COG1196    515 LLAglrglagavavligveaayeaaleAALAAALQNIVVEDDEVaaaaieylKAAKAGRATFLPLD-KIRARAALAAALA 593

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  319 NDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ 398
Cdd:COG1196    594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  399 LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSE 478
Cdd:COG1196    674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753

                          490       500
                   ....*....|....*....|..
gi 2017363533  479 E-------IEKLRQEVDQLKGR 493
Cdd:COG1196    754 EelpeppdLEELERELERLERE 775
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
149-412 3.20e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.00  E-value: 3.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  149 EVLKALKSLFEHHKALDEkVRERLRAALERVTTLEeQLAGAHQQVSALQQGAGVRDGAAEeegtvelgPKRLWKEDTgRV 228
Cdd:COG4913    222 DTFEAADALVEHFDDLER-AHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRA--------ALRLWFAQR-RL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  229 EELQELLEKQNFELSQARERlvtltttvteleedlgtarrdlikseelsskhqrdLREALAQKEDMEERITTLEKRYLAA 308
Cdd:COG4913    291 ELLEAELEELRAELARLEAE-----------------------------------LERLEARLDALREELDELEAQIRGN 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  309 QREATsihdlnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK-AETLPEVEAELAQRIAALTKAEERHGN 387
Cdd:COG4913    336 GGDRL------EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEfAALRAEAAALLEALEEELEALEEALAE 409

                          250       260
                   ....*....|....*....|....*
gi 2017363533  388 IEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG4913    410 AEAALRDLRRELRELEAEIASLERR 434
PTZ00121 PTZ00121
MAEBL; Provisional
 159-451 3.25e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.23  E-value: 3.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDgaAEEEGTVElgPKRLWKEDTG----RVEELQEL 234
Cdd:PTZ00121  1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK--AEEKKKAE--EAKKAEEDKNmalrKAEEAKKA 1589

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  235 LEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATs 314
Cdd:PTZ00121  1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK- 1668

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  315 ihdlndKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQ 394
Cdd:PTZ00121  1669 ------KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363533  395 lEGQLEEKNQELARVRQREKmnedhnkrlsDTVDRLLSESNERLQLHLKERMAALEE 451
Cdd:PTZ00121  1738 -EAEEDKKKAEEAKKDEEEK----------KKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
34-490 3.69e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 57.74  E-value: 3.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   34 LDEREKLLESLRESQE---TLAATQSRLQDAIHERDQlqrhlnsalpqEFATLTRELSMCREQLLEREEEISELKAERNN 110
Cdd:PRK02224   236 RDEADEVLEEHEERREeleTLEAEIEDLRETIAETER-----------EREELAEEVRDLRERLEELEEERDDLLAEAGL 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  111 TRL----LLEHLECLVSRHERSLRMTVVKRQAQSpsgvssevEVLKALKSLFEHHKALDEKVRErlraALERVTTLEEQL 186
Cdd:PRK02224   305 DDAdaeaVEARREELEDRDEELRDRLEECRVAAQ--------AHNEEAESLREDADDLEERAEE----LREEAAELESEL 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  187 AGAHQQVSALQ-QGAGVRDGAAEEEGTVELGPkrlwkEDTGRVEELQELLEKqnfELSQARERlvtltttVTELEEDLGT 265
Cdd:PRK02224   373 EEAREAVEDRReEIEELEEEIEELRERFGDAP-----VDLGNAEDFLEELRE---ERDELRER-------EAELEATLRT 437

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  266 ARRDLIKSEEL--------------SSKHQRDLREALAQKEDMEERITTLEkrylaaqreaTSIHDLNDKLE--NELANK 329
Cdd:PRK02224   438 ARERVEEAEALleagkcpecgqpveGSPHVETIEEDRERVEELEAELEDLE----------EEVEEVEERLEraEDLVEA 507

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  330 ESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETL----PEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:PRK02224   508 EDRIERLEERREDLEELIAERRETIEEKRERAEELreraAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER 587

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  406 LARVRQ-REKMNEDHNKRlsDTVDRlLSESNERLQLHLKERMAALEEKNTLIQELESS--QRQIEEQHHHKGRLSEEIEK 482
Cdd:PRK02224   588 IESLERiRTLLAAIADAE--DEIER-LREKREALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQ 664


                   ....*...
gi 2017363533  483 LRQEVDQL 490
Cdd:PRK02224   665 VEEKLDEL 672
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
278-494 3.73e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.00  E-value: 3.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  278 SKHQRDLREALAQKEDMEERITTLEKrylaaqreatsIHDLNDKLEnELANKESLHRQCEEKARHLQellevAEQKLQqt 357
Cdd:COG4913    231 VEHFDDLERAHEALEDAREQIELLEP-----------IRELAERYA-AARERLAELEYLRAALRLWF-----AQRRLE-- 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  358 mRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ--------LEEKNQELARVRQREKMNEDHNKRLSDTVDR 429
Cdd:COG4913    292 -LLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRRARLEALLAA 370

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363533  430 L---LSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHhkgRLSEEIEKLRQEVDQLKGRG 494
Cdd:COG4913    371 LglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR---DLRRELRELEAEIASLERRK 435
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 848-914 4.63e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 51.14  E-value: 4.63e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363533   848 FAQWDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 914
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 39-487 7.72e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 7.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   39 KLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSAlpqEFATLTRELSmcreqllEREEEISELKAERNNTRLLLEHL 118
Cdd:COG1196    217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEA---ELEELEAELA-------ELEAELEELRLELEELELELEEA 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  119 eclvsrheRSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQ 198
Cdd:COG1196    287 --------QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  199 GAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSS 278
Cdd:COG1196    359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  279 KHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEE-KARHLQELLEVAEQKLQQT 357
Cdd:COG1196    439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEaEADYEGFLEGVKAALLLAG 518

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  358 MRKAE----TLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRqREKMNEDHNKRLSDTVDRLLSE 433
Cdd:COG1196    519 LRGLAgavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT-FLPLDKIRARAALAAALARGAI 597

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2017363533  434 SNERLQLHLKERmaALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEV 487
Cdd:COG1196    598 GAAVDLVASDLR--EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
301-491 8.74e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.31  E-value: 8.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  301 LEKRYLAAQREATSIHDLNDKLE-NELANKESLHRQCEEKARHLQELlevaEQKLQQTMRKAETLPEVEAELAQRIAALT 379
Cdd:COG4717     47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLE 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  380 KAEERHGNIEEhLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQEL 459
Cdd:COG4717    123 KLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2017363533  460 ESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG4717    202 EELQQRLAELEEELEEAQEELEELEEELEQLE 233
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 34-487 8.81e-08

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 56.77  E-value: 8.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   34 LDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSmcrEQLLEREEEISELKAERNNTRl 113
Cdd:pfam12128  246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWK---EKRDELNGELSAADAAVAKDR- 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  114 llEHLECLVSRHERSLRMTVVKR---QAQSPSgVSSEVEVL-KALKSLFEHHKALDEKVrERLRAAleRVTTLEEQLAGA 189
Cdd:pfam12128  322 --SELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKY-NRRRSK--IKEQNNRDIAGI 395

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  190 HQQVSALQQGAgVRdGAAEEEGTVElgpkrlwkedtGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLgTARRD 269
Cdd:pfam12128  396 KDKLAKIREAR-DR-QLAVAEDDLQ-----------ALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQA-TATPE 461

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  270 LIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANK-ESLHRQCEEKARHLQELLE 348
Cdd:pfam12128  462 LLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSAlDELELQLFPQAGTLLHFLR 541

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  349 VAEQKLQQTMRK---AETL------PEV-----------------------------EAELAQRIAALTKA----EERHG 386
Cdd:pfam12128  542 KEAPDWEQSIGKvisPELLhrtdldPEVwdgsvggelnlygvkldlkridvpewaasEEELRERLDKAEEAlqsaREKQA 621

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  387 NIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllSESNERLQLHlKERMAALEEKNTLIQELESSQRQI 466
Cdd:pfam12128  622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD------EKQSEKDKKN-KALAERKDSANERLNSLEAQLKQL 694

                          490       500
                   ....*....|....*....|....*....
gi 2017363533  467 EEQH-----HHKGRLSE---EIEKLRQEV 487
Cdd:pfam12128  695 DKKHqawleEQKEQKREartEKQAYWQVV 723
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 973-1028 9.28e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.99  E-value: 9.28e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363533   973 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1028
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 169-490 1.92e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.84  E-value: 1.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAG-VRDGAAEEEGTVELGPKRLwkedtgrvEELQELLEKQNFELSQARE 247
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDeLSQELSDASRKIGEIEKEI--------EQLEQEEEKLKERLEELEE 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  248 RLVTLTTTVTELEEDLGTARRDLIKSEELSSKhqrdLREALAQKEDM--EERITTLEKRYlaaqreatsihdlnDKLENE 325
Cdd:TIGR02169  745 DLSSLEQEIENVKSELKELEARIEELEEDLHK----LEEALNDLEARlsHSRIPEIQAEL--------------SKLEEE 806

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  326 LANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL-TKAEERHGNIEEH---LRQLEGQLEE 401
Cdd:TIGR02169  807 VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLnGKKEELEEELEELeaaLRDLESRLGD 886

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  402 KNQElaRVRQREKMNEDHNKRlsdtvdRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHK---GRLSE 478
Cdd:TIGR02169  887 LKKE--RDELEAQLRELERKI------EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDVQA 958

                          330
                   ....*....|..
gi 2017363533  479 EIEKLRQEVDQL 490
Cdd:TIGR02169  959 ELQRVEEEIRAL 970
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 35-492 2.08e-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: 55.36  E-value: 2.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   35 DEREKLLeSLRESQETLAATQSRLQDAIHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLL 114
Cdd:TIGR00618  421 DLQGQLA-HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL-QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  115 LEHLECLVsrhERSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKALdEKVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:TIGR00618  499 LQEEPCPL---CGSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSE-EDVYHQLTSERKQRASLKEQMQEIQQSFS 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  195 ALQQ-----GAGVRDGAAEEEGTVELGPKRLWKEDTGRvEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARrd 269
Cdd:TIGR00618  574 ILTQcdnrsKEDIPNLQNITVRLQDLTEKLSEAEDMLA-CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA-- 650

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  270 liksEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQEL--- 346
Cdd:TIGR00618  651 ----LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIena 726

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  347 -----------LEVAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ---LEEKNQELArvrq 411
Cdd:TIGR00618  727 ssslgsdlaarEDALNQSLKELMHQARTvLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFnrlREEDTHLLK---- 802

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  412 rEKMNEDHNKRLSDTVDRLLSEsnERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR00618  803 -TLEAEIGQEIPSDEDILNLQC--ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879


                   .
gi 2017363533  492 G 492
Cdd:TIGR00618  880 G 880
mukB PRK04863
chromosome partition protein MukB;
123-493 2.26e-07

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 55.35  E-value: 2.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  123 SRHERSLRMTVVKRqaqspsgVSSEVEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEE--QLAGAHQQ--VSAL-Q 197
Cdd:PRK04863   275 MRHANERRVHLEEA-------LELRRELYTSRRQLAAEQYRLVEMARE-LAELNEAESDLEQdyQAASDHLNlvQTALrQ 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  198 QGAGVRdgaAEEEgtvelgpkrlwkedtgrVEELQELLEKQNFELSQARERlvtltttvteleedlgtarrdLIKSEELS 277
Cdd:PRK04863   347 QEKIER---YQAD-----------------LEELEERLEEQNEVVEEADEQ---------------------QEENEARA 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  278 SKHQRDLREALAQKEDMEERITTLEKR---YLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKL 354
Cdd:PRK04863   386 EAAEEEVDELKSQLADYQQALDVQQTRaiqYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKL 465

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  355 QQTmRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLE------GQLEEKNQELARVRQREkmnedhnkRLSDTVD 428
Cdd:PRK04863   466 SVA-QAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLReqrhlaEQLQQLRMRLSELEQRL--------RQQQRAE 536

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363533  429 RLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PRK04863   537 RLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR 601
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
26-493 3.41e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 3.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   26 FEQLMVNMLDER-EKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRElsmcreqllereeeISEL 104
Cdd:COG4913    285 FAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLERE--------------IERL 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  105 KAERNNTRLLLEHLECLVsrheRSLRMTVvkrqaqsPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEE 184
Cdd:COG4913    351 ERELEERERRRARLEALL----AALGLPL-------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  185 QLAGAHQQVSALQQGAGVRDGAAEEEgtvelgpKRLWKEDTG-RVEELQ---ELLE-KQNFELSQ-ARERLvtltttvte 258
Cdd:COG4913    420 ELRELEAEIASLERRKSNIPARLLAL-------RDALAEALGlDEAELPfvgELIEvRPEEERWRgAIERV--------- 483

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  259 leedLGTARRDLIkseeLSSKHQRDLREALAQkEDMEERITTLE-----KRYLAAQREATSI--------HDLNDKLENE 325
Cdd:COG4913    484 ----LGGFALTLL----VPPEHYAAALRWVNR-LHLRGRLVYERvrtglPDPERPRLDPDSLagkldfkpHPFRAWLEAE 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  326 LANKESLHR-------QCEEKA------------------RHL-----------QELLEVAEQKLQQTMRKAETLPEVEA 369
Cdd:COG4913    555 LGRRFDYVCvdspeelRRHPRAitragqvkgngtrhekddRRRirsryvlgfdnRAKLAALEAELAELEEELAEAEERLE 634

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  370 ELAQRIAALTKAEERHGNIEEH------LRQLEGQLEEKNQELARvrqrekmnedhnkrlsdtvdrlLSESNERLQlHLK 443
Cdd:COG4913    635 ALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELER----------------------LDASSDDLA-ALE 691

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 2017363533  444 ERMAALEEkntliqELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:COG4913    692 EQLEELEA------ELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 32-484 4.27e-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: 54.59  E-value: 4.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   32 NMLDEREKLLESLRESQETLAATQsRLQDAIHERDQLQRHLNSALPQEfATLTRELSmcreqllereeEISELKAERNNT 111
Cdd:TIGR00618  223 VLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARI-EELRAQEA-----------VLEETQERINRA 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  112 RllleHLECLVsrhERSLRMTVVKRQAQspsgvssevevlkalkslfEHHKALDEKVRERLRAALERVTTLEEQLAGAHQ 191
Cdd:TIGR00618  290 R----KAAPLA---AHIKAVTQIEQQAQ-------------------RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  192 QVSA---LQQGAGVRDGAAEEEGTVELGPKRlwKEDTGRVEELQELLEKQNfELSQARERLVTLTTTVTELEEDLGTARR 268
Cdd:TIGR00618  344 RRLLqtlHSQEIHIRDAHEVATSIREISCQQ--HTLTQHIHTLQQQKTTLT-QKLQSLCKELDILQREQATIDTRTSAFR 420

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  269 DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHdlnDKLENELANKESLHRQCEEK-ARHLQELL 347
Cdd:TIGR00618  421 DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL---KEREQQLQTKEQIHLQETRKkAVVLARLL 497

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  348 EVAEQklQQTMRKAETLPEVEAELAQRIAALT----KAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRL 423
Cdd:TIGR00618  498 ELQEE--PCPLCGSCIHPNPARQDIDNPGPLTrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL 575

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363533  424 SDTVDRLLSESNERLQLhlkermaaLEEKNTLIQELESSQRQI-EEQHHHKGRLSEEIEKLR 484
Cdd:TIGR00618  576 TQCDNRSKEDIPNLQNI--------TVRLQDLTEKLSEAEDMLaCEQHALLRKLQPEQDLQD 629
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 281-469 4.36e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 53.68  E-value: 4.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELankESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG3883     22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALYRS 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  361 AETLPEVEA--------ELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS 432
Cdd:COG3883     99 GGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2017363533  433 ESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ 469
Cdd:COG3883    179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 25-491 5.27e-07

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: 54.35  E-value: 5.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   25 NFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHErdqlqrhlnsalpQEFATLTRELSMcreqllereeeisel 104
Cdd:pfam15921  114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHE-------------LEAAKCLKEDML--------------- 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  105 kaerNNTRLLLEHLECLVSRHE---RSLRMTVVKRQAQSPSGVsSEVEVLKALkslfeHHKALDEKVRERLRAALERVTT 181
Cdd:pfam15921  166 ----EDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKI-YEHDSMSTM-----HFRSLGSAISKILRELDTEISY 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  182 LEEQLAGAHQQVSALQqgagvrdgaAEEEGTVELgpkrLWKEDTGRVE--------ELQELLEKQNFELSQARERLVTLT 253
Cdd:pfam15921  236 LKGRIFPVEDQLEALK---------SESQNKIEL----LLQQHQDRIEqlisehevEITGLTEKASSARSQANSIQSQLE 302

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  254 TTVTELEEDLGTARRDLIKSEELSSKHQRDLREAlaqKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELAN-KESL 332
Cdd:pfam15921  303 IIQEQARNQNSMYMRQLSDLESTVSQLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNlDDQL 379

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  333 HRQCEEKARHLQELLEVAEQKLQ---QTMRKAETLPEVEAEL------AQRIAALTKA--EERHGNIEEHLRQLEGqlee 401
Cdd:pfam15921  380 QKLLADLHKREKELSLEKEQNKRlwdRDTGNSITIDHLRRELddrnmeVQRLEALLKAmkSECQGQMERQMAAIQG---- 455

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  402 KNQELARVRQREKMNEDHNKRLSDTVDRLLS-----ESNER----LQLHLKERMAALEEKNTLIQELESS-QRQIEEQHH 471
Cdd:pfam15921  456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAkkmtlESSERtvsdLTASLQEKERAIEATNAEITKLRSRvDLKLQELQH 535

                          490       500
                   ....*....|....*....|
gi 2017363533  472 HKGRlSEEIEKLRQEVDQLK 491
Cdd:pfam15921  536 LKNE-GDHLRNVQTECEALK 554
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 284-451 9.27e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.46  E-value: 9.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  284 LREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELL-EVAEQKLQQTMRKae 362
Cdd:COG1579     19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgNVRNNKEYEALQK-- 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  363 tlpEVEAelaqriaaltkAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHL 442
Cdd:COG1579     97 ---EIES-----------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162


                   ....*....
gi 2017363533  443 KERMAALEE 451
Cdd:COG1579    163 AEREELAAK 171
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 262-493 1.00e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.15  E-value: 1.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHR------- 334
Cdd:TIGR02169  689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKelearie 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  335 QCEEKARHLQELLE-----VAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnieehLRQLEGQLEEKNQELARV 409
Cdd:TIGR02169  769 ELEEDLHKLEEALNdlearLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-------LTLEKEYLEKEIQELQEQ 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  410 RQREKMNEDHNKRLSDTVDRLLSESNERlqlhLKERMAALEEkntLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQ 489
Cdd:TIGR02169  842 RIDLKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRD---LESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914


                   ....
gi 2017363533  490 LKGR 493
Cdd:TIGR02169  915 KRKR 918
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 264-493 1.24e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.15  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  264 GTARRDLIksEELS--SKHQRDLREALAQKEDMEERITTLEkrylaaqreaTSIHDLNDKLENELANKESLHRQCEEKAR 341
Cdd:TIGR02169  152 PVERRKII--DEIAgvAEFDRKKEKALEELEEVEENIERLD----------LIIDEKRQQLERLRREREKAERYQALLKE 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  342 hLQEL--------LEVAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARvRQRE 413
Cdd:TIGR02169  220 -KREYegyellkeKEALERQKEAIERQLASL---EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL-RVKE 294

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  414 KMNEDHNKRLSdtVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02169  295 KIGELEAEIAS--LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
40-491 1.32e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   40 LLESLRESQETLAATQSRL-QDAIHERDQLQRHLNSA--LPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLE 116
Cdd:COG4717     47 LLERLEKEADELFKPQGRKpELNLKELKELEEELKEAeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  117 HLECL--VSRHERSL-----RMTVVKRQAQSPSGVSSEVEVLKAlkSLFEHHKALDEKVRERLRAALERVTTLEEQLAGA 189
Cdd:COG4717    127 LLPLYqeLEALEAELaelpeRLEELEERLEELRELEEELEELEA--ELAELQEELEELLEQLSLATEEELQDLAEELEEL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  190 HQQVSALQQgagvRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQAR----ERLVTLTTTVTELEEDLGT 265
Cdd:COG4717    205 QQRLAELEE----ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAllalLGLGGSLLSLILTIAGVLF 280

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  266 ARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK-----LENELANKESLHRQCEEKA 340
Cdd:COG4717    281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeelleLLDRIEELQELLREAEELE 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  341 RHLQelLEVAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEErhgnIEEHLRQLEGQLEEKNQELARVRQREKmNEDHN 420
Cdd:COG4717    361 EELQ--LEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQE----LKEELEELEEQLEELLGELEELLEALD-EEELE 431

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363533  421 KRLSDTVDRLLSESNERLQLHlkERMAALEEKntlIQELESSQRqIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG4717    432 EELEELEEELEELEEELEELR--EELAELEAE---LEQLEEDGE-LAELLQELEELKAELRELAEEWAALK 496
PTZ00121 PTZ00121
MAEBL; Provisional
 135-486 1.33e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  135 KRQAQSPSGVSSEVEVLKALKSLFEHHKALDE--KVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGT 212
Cdd:PTZ00121  1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK 1496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  213 VELGPKRLWKEDTGRVEELQELLEKQNFElsQARERLVTLTTTVTELEEDLGTARrDLIKSEELssKHQRDLREALAQKE 292
Cdd:PTZ00121  1497 KKADEAKKAAEAKKKADEAKKAEEAKKAD--EAKKAEEAKKADEAKKAEEKKKAD-ELKKAEEL--KKAEEKKKAEEAKK 1571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  293 DMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAETLPEVEAELA 372
Cdd:PTZ00121  1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK-----KKVEQLKKKEAEEK 1646

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  373 QRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesnERLQLHLKERMAALEEk 452
Cdd:PTZ00121  1647 KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA-----EELKKKEAEEKKKAEE- 1720

                          330       340       350
                   ....*....|....*....|....*....|....
gi 2017363533  453 ntLIQELESSQRQIEEQHHHKGRLSEEIEKLRQE 486
Cdd:PTZ00121  1721 --LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
135-494 1.93e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.08  E-value: 1.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  135 KRQAQSPSGVSSEVEVL-KALKSLFEHHKALDEKV--RERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEG 211
Cdd:COG4717     60 KPQGRKPELNLKELKELeEELKEAEEKEEEYAELQeeLEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  212 TVELGPKRL--WKEDTGRVEELQELLEKQNFELSQARER-LVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREAL 288
Cdd:COG4717    140 ELAELPERLeeLEERLEELRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  289 AQKEDMEERITTLEKRYLAAQRE-------------------ATSIHDLNDKLEN-----------------ELANKESL 332
Cdd:COG4717    220 EELEELEEELEQLENELEAAALEerlkearlllliaaallalLGLGGSLLSLILTiagvlflvlgllallflLLAREKAS 299

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  333 HRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQR-IAALTKAEERHGNIEEHLRQLE-GQLEEKNQEL---A 407
Cdd:COG4717    300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLElLDRIEELQELLREAEELEEELQlEELEQEIAALlaeA 379

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  408 RVRQREKMNE--DHNKRLSDTVDRLlSESNERLQLHLKERMAALE--EKNTLIQELESSQRQIEEQHHHKGRLSEEIEKL 483
Cdd:COG4717    380 GVEDEEELRAalEQAEEYQELKEEL-EELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEELEELREELAEL 458

                          410
                   ....*....|.
gi 2017363533  484 RQEVDQLKGRG 494
Cdd:COG4717    459 EAELEQLEEDG 469
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 229-407 2.43e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.92  E-value: 2.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  229 EELQELLEKQNF--ELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRyl 306
Cdd:COG1579      4 EDLRALLDLQELdsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  307 aaQREATSIHDLNDkLENELANKESLHRQCEEKARHLQELLEVAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHG 386
Cdd:COG1579     82 --LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEKKAELD 148

                          170       180
                   ....*....|....*....|.
gi 2017363533  387 NIEEHLRQLEGQLEEKNQELA 407
Cdd:COG1579    149 EELAELEAELEELEAEREELA 169
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 229-430 2.53e-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: 51.30  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  229 EELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYlAA 308
Cdd:COG4942     30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-AE 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  309 QREATSIHDLNDKLENELANKESLhrQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnI 388
Cdd:COG4942    109 LLRALYRLGRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE---L 183

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2017363533  389 EEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL 430
Cdd:COG4942    184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
PTZ00121 PTZ00121
MAEBL; Provisional
 153-493 2.91e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 2.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  153 ALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLwKEDTGRVEELQ 232
Cdd:PTZ00121  1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA-EEDKKKADELK 1411

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  233 ELLE--KQNFELSQARERLVtltttvteleedlgtarrdliKSEELSSKHQrDLREALAQKEDMEERITTLEKRYLAaqR 310
Cdd:PTZ00121  1412 KAAAakKKADEAKKKAEEKK---------------------KADEAKKKAE-EAKKADEAKKKAEEAKKAEEAKKKA--E 1467

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  311 EATSIHDLNDKLEnELANKESLHRQCEEKARHLQELLEVAEQKLQ-QTMRKAETLPEVE----AELAQRIAALTKAEERH 385
Cdd:PTZ00121  1468 EAKKADEAKKKAE-EAKKADEAKKKAEEAKKKADEAKKAAEAKKKaDEAKKAEEAKKADeakkAEEAKKADEAKKAEEKK 1546

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  386 GniEEHLRQLEGQleEKNQELARVRQREKMNEDHNKRLsdtvdRLLSESNERLQLHLKERMAALEEKntliQELESSQRQ 465
Cdd:PTZ00121  1547 K--ADELKKAEEL--KKAEEKKKAEEAKKAEEDKNMAL-----RKAEEAKKAEEARIEEVMKLYEEE----KKMKAEEAK 1613

                          330       340
                   ....*....|....*....|....*...
gi 2017363533  466 IEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PTZ00121  1614 KAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 320-491 3.65e-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: 50.53  E-value: 3.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  320 DKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAetlpeveAELAQRIAALtkaEERHGNIEEHLRQLEGQL 399
Cdd:COG4942     30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-------RALEQELAAL---EAELAELEKEIAELRAEL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  400 EEKNQELA-RVRQREKMNED-------HNKRLSDTVDRLlsesnERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHH 471
Cdd:COG4942    100 EAQKEELAeLLRALYRLGRQpplalllSPEDFLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRAELEAERA 174

                          170       180
                   ....*....|....*....|
gi 2017363533  472 HKGRLSEEIEKLRQEVDQLK 491
Cdd:COG4942    175 ELEALLAELEEERAALEALK 194
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
376-493 4.14e-06

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 49.05  E-value: 4.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  376 AALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesNERLQLHLK---ERMA--ALE 450
Cdd:COG1842     16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreALE 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2017363533  451 EKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:COG1842     92 RKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 163-414 5.24e-06

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: 51.11  E-value: 5.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  163 ALDEKVRERLRAALERVTTLEEQLAgahQQVSALQQGAGVRDGAAEEEGTVE--LGPKRLWKEDT--GRVEELQELLEkq 238
Cdd:COG3096    829 AFAPDPEAELAALRQRRSELERELA---QHRAQEQQLRQQLDQLKEQLQLLNklLPQANLLADETlaDRLEELREELD-- 903

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  239 nfELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELsskhQRDLREALAQKEDMEERITTLEkrYLAAQREATSIHD- 317
Cdd:COG3096    904 --AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQL----QADYLQAKEQQRRLKQQIFALS--EVVQRRPHFSYEDa 975

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  318 ---------LNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL-----TKAEE 383
Cdd:COG3096    976 vgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadAEAEE 1055

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2017363533  384 RhgnIEEHLRQLEGQLeekNQELARVRQREK 414
Cdd:COG3096   1056 R---ARIRRDELHEEL---SQNRSRRSQLEK 1080
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 13-486 5.97e-06

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 50.61  E-value: 5.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   13 RLGPPHGADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSMCRE 92
Cdd:pfam12128  445 RLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE 524

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   93 QLLEREEEISELKA-ERNNTRLLLEHLECLVSR---HERSLRMTVVKRQAQSPS---GVSSEVEVLKALKSLFeHHKALD 165
Cdd:pfam12128  525 LELQLFPQAGTLLHfLRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELnlyGVKLDLKRIDVPEWAA-SEEELR 603

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  166 E---KVRERLRAALERVTTLEEQLAGAHQQVSALQqgAGVRDGAAEEEGTvELGPKRLWKEDTGRVEELQELLEKQNFEL 242
Cdd:pfam12128  604 ErldKAEEALQSAREKQAAAEEQLVQANGELEKAS--REETFARTALKNA-RLDLRRLFDEKQSEKDKKNKALAERKDSA 680

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  243 SQARERLVTLTTTVTELEEDLGTARRDliKSEELSSKHQRDLREALAQKEDMEERI-TTLEKRYLAAQREATSIHDLNDk 321
Cdd:pfam12128  681 NERLNSLEAQLKQLDKKHQAWLEEQKE--QKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWYK- 757

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  322 leNELANK--------------ESLHRQCEEKARHLQELLE----VAEQKLQQTMRKAETLPEVEA---ELAQRIAALTK 380
Cdd:pfam12128  758 --RDLASLgvdpdviaklkreiRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERaisELQQQLARLIA 835

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  381 -AEERHGNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHnkrlsdtvdrlLSESNERLQLHLKERMAALEE-KNTLIQ 457
Cdd:pfam12128  836 dTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGERLAQLEDlKLKRDY 904

                          490       500       510
                   ....*....|....*....|....*....|....
gi 2017363533  458 ELESSQRQIEE-----QHHHKGRLSEEIEKLRQE 486
Cdd:pfam12128  905 LSESVKKYVEHfknviADHSGSGLAETWESLREE 938
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 973-1024 8.52e-06

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 44.15  E-value: 8.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2017363533  973 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1024
Cdd:cd09487      4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 24-493 8.60e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 8.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   24 ANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLnSALPQEFATLTRELSMCREQLLEREEEISE 103
Cdd:TIGR02169  360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL-DRLQEELQRLSEELADLNAAIAGIEAKINE 438

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  104 LKAERNNTRLLLEHLE-------CLVSRHERSLRMTVVKRQAQSP--SGVSSEVEVLKALKSLFEHHKALDEKVRERLRA 174
Cdd:TIGR02169  439 LEEEKEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKelSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  175 ALERVTTLEEQLAGAHQQ-VSALQQGAGVRDGA--AEEEGTVELGPKRLWKEDTGRV-----------EELQELLEKQNF 240
Cdd:TIGR02169  519 SIQGVHGTVAQLGSVGERyATAIEVAAGNRLNNvvVEDDAVAKEAIELLKRRKAGRAtflplnkmrdeRRDLSILSEDGV 598

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  241 --------ELSQARERLVTLTTTVTELEEDLGTARRDLIKSE------EL-------------SSKHQRDLREALAQKED 293
Cdd:TIGR02169  599 igfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRmvtlegELfeksgamtggsraPRGGILFSRSEPAELQR 678

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHR-------QCEEKARHLQELLEVAEQKLQQTMRKAET--- 363
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGeiekeieQLEQEEEKLKERLEELEEDLSSLEQEIENvks 758

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  364 -LPEVEAELAQRIAALTKAEERHGNIEEHLRQleGQLEEKNQELARVRQREKMNEdhnKRLSDtVDRLLSESNERLQLhL 442
Cdd:TIGR02169  759 eLKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE---ARLRE-IEQKLNRLTLEKEY-L 831

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2017363533  443 KERMAALEEKNTLIQELESS-QRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSiEKEIENLNGKKEELEEELEELEAALRDLESR 883
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
42-485 8.91e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 8.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   42 ESLRESQETLAATQSRLQDAIHE-RDQLQRHLNSA----------------LPQEFATLTRELSMCREQLLEREEEISEL 104
Cdd:PRK02224   310 EAVEARREELEDRDEELRDRLEEcRVAAQAHNEEAeslredaddleeraeeLREEAAELESELEEAREAVEDRREEIEEL 389

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  105 KAERNNTRL-----------LLEHLECLVSRHERslrmtVVKRQAQSPSGVSSEVEVLKALKSLFEHHKA-------LDE 166
Cdd:PRK02224   390 EEEIEELRErfgdapvdlgnAEDFLEELREERDE-----LREREAELEATLRTARERVEEAEALLEAGKCpecgqpvEGS 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  167 KVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvRDGAAEEEGTVELGPKRLwKEdtgRVEELQELLEKQNFELSQAR 246
Cdd:PRK02224   465 PHVETIEEDRERVEELEAELEDLEEEVEEVEE----RLERAEDLVEAEDRIERL-EE---RREDLEELIAERRETIEEKR 536

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  247 ERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKrylaaqreatsIHDLNDKLENEL 326
Cdd:PRK02224   537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-----------IRTLLAAIADAE 605

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  327 ANKESLhrqcEEKARHLQELLEVAEQKLQQtmrKAETLPEVEAELAQriAALTKAEERHGNIEEHLRQLEGQLEEKNQEL 406
Cdd:PRK02224   606 DEIERL----REKREALAELNDERRERLAE---KRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREER 676

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363533  407 ARVRQREKMNEDHNKRLSDtvdrllsesnerlqlhLKERMAALEEKntlIQELESSQRQIEEQHHHKGRLSEEiekLRQ 485
Cdd:PRK02224   677 DDLQAEIGAVENELEELEE----------------LRERREALENR---VEALEALYDEAEELESMYGDLRAE---LRQ 733
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 283-493 1.02e-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: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMR--- 359
Cdd:pfam05622    1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRlet 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  360 -------KAETLPEVEAELAQRIAALTKAeerhgniEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVD---- 428
Cdd:pfam05622   81 arddyriKCEELEKEVLELQHRNEELTSL-------AEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDlrrq 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017363533  429 -RLLSESNerlqLHLKERMAALEEK----NTLIQELESSQRQIEEQHHhkgRLSEEI---EKLRQEVDQLKGR 493
Cdd:pfam05622  154 vKLLEERN----AEYMQRTLQLEEElkkaNALRGQLETYKRQVQELHG---KLSEESkkaDKLEFEYKKLEEK 219
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 42-493 1.60e-05

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: 49.28  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   42 ESLRESQETLAATqsRLQDAIHERDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECL 121
Cdd:TIGR02168  220 AELRELELALLVL--RLEELREELEELQEELK-EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  122 VSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLfEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAG 201
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKL-DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  202 VRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQnfELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQ 281
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL--EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  282 RDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEE--KARH--------LQELLEVAE 351
Cdd:TIGR02168  454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSglsgilgvLSELISVDE 533

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  352 Q-------------------------KLQQTMRKAET------------------------------------LPEVEAE 370
Cdd:TIGR02168  534 GyeaaieaalggrlqavvvenlnaakKAIAFLKQNELgrvtflpldsikgteiqgndreilkniegflgvakdLVKFDPK 613

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  371 L-------------------AQRIAALTKAEER-----------HG---------------------NIEEHLRQLEGQL 399
Cdd:TIGR02168  614 LrkalsyllggvlvvddldnALELAKKLRPGYRivtldgdlvrpGGvitggsaktnssilerrreieELEEKIEELEEKI 693

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  400 EEKNQELARVR----QREKMNEDHNKRLSDTvDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQH----- 470
Cdd:TIGR02168  694 AELEKALAELRkeleELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEerlee 772

                          570       580
                   ....*....|....*....|....*
gi 2017363533  471 --HHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02168  773 aeEELAEAEAEIEELEAQIEQLKEE 797
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 320-463 2.45e-05

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


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 46.60  E-value: 2.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  320 DKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 388
Cdd:pfam04012   39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363533  389 EEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQ 463
Cdd:pfam04012  117 RKQLAALETKIQQLKAKKNLLKARLKAAK-AQEAVQTSLGSLSTSSATDSFERIEEKIEEREARADAAAELASAV 190
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
169-489 3.39e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 3.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  169 RERLRAALERVTTLEEQLAGAHQQVSALQ-QGAGVRDGAAEEEGTVELGPKRL-WKEDTGRVEELQ---ELLEKQNFELS 243
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEaELDALQERREALQRLAEYSWDEIdVASAEREIAELEaelERLDASSDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  244 QARERLVTLTTTVTELEEDLGTARRDLIKSEelssKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLE 323
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIGRLE----KELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  324 NELAnkeslhRQCEEKARHLQELLEVAEQKLQQTMR------------------------------KAETLPEVEAELAQ 373
Cdd:COG4913    765 RELR------ENLEERIDALRARLNRAEEELERAMRafnrewpaetadldadleslpeylalldrlEEDGLPEYEERFKE 838

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  374 riaALTKAEER-----HGNIEEHLRQLEGQLEEKNQELARVRqrekMNEDHnkrlsdtvdrllsesneRLQLHLKERmaA 448
Cdd:COG4913    839 ---LLNENSIEfvadlLSKLRRAIREIKERIDPLNDSLKRIP----FGPGR-----------------YLRLEARPR--P 892

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2017363533  449 LEEKNTLIQELESSQRQI-----EEQHHHKGRLSEEIEKLRQEVDQ 489
Cdd:COG4913    893 DPEVREFRQELRAVTSGAslfdeELSEARFAALKRLIERLRSEEEE 938
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 232-482 5.47e-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: 47.43  E-value: 5.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  232 QELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREAlaQKEDMEERITTLEKRYLAAqrE 311
Cdd:pfam17380  298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQEEIAM--E 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  312 ATSIHDLnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRiaaltkaeerhgnieeH 391
Cdd:pfam17380  374 ISRMREL-ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR----------------E 436

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  392 LRQLEgqlEEKNQELARVRQREKMNEDHNKRLsdtvdRLLSESNERLQLHL---KERMAALEEKNTLI--QELESSQRQI 466
Cdd:pfam17380  437 VRRLE---EERAREMERVRLEEQERQQQVERL-----RQQEEERKRKKLELekeKRDRKRAEEQRRKIleKELEERKQAM 508

                          250
                   ....*....|....*.
gi 2017363533  467 EEQHHHKGRLSEEIEK 482
Cdd:pfam17380  509 IEEERKRKLLEKEMEE 524
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 270-491 6.11e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 6.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  270 LIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIH-----------------DLNDKLENELANKES- 331
Cdd:TIGR04523  147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKnkllklelllsnlkkkiQKNKSLESQISELKKq 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  332 ---LHRQCEEKARHLQEL---LEVAEQKLQQTMrkaETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLE----E 401
Cdd:TIGR04523  227 nnqLKDNIEKKQQEINEKtteISNTQTQLNQLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnQ 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  402 KNQELAR-----VRQREKMNEDHNKRLSDTvDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRL 476
Cdd:TIGR04523  304 KEQDWNKelkseLKNQEKKLEEIQNQISQN-NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382

                          250
                   ....*....|....*
gi 2017363533  477 SEEIEKLRQEVDQLK 491
Cdd:TIGR04523  383 KQEIKNLESQINDLE 397
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 295-491 6.54e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 6.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  295 EERITTLEKRYLAAQREATSIHD----LNDKL---ENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLP-- 365
Cdd:TIGR04523  210 IQKNKSLESQISELKKQNNQLKDniekKQQEInekTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEkq 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  366 --EVEAELA----QRIAALTKA-EERHGNIEEHLRQLEGQLEEKNQELARVRQ------REKMNEDHNKRlsdTVDRLLS 432
Cdd:TIGR04523  290 lnQLKSEISdlnnQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEqisqlkKELTNSESENS---EKQRELE 366

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017363533  433 ESNERLQLHLKERMAALEEKNTL---IQELESS-----------QRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR04523  367 EKQNEIEKLKKENQSYKQEIKNLesqINDLESKiqnqeklnqqkDEQIKKLQQEKELLEKEIERLKETIIKNN 439
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
318-493 7.11e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 7.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  318 LNDKLENElanKESLHRQCEEKARHLQELLEVAEQKLQQtmrkaetLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEG 397
Cdd:COG4717     47 LLERLEKE---ADELFKPQGRKPELNLKELKELEEELKE-------AEEKEEEYAELQEELEELEEELEELEAELEELRE 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  398 QLEEKNQELARVRQREKMnEDHNKRLSDTVDRLlsesnERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ-------- 469
Cdd:COG4717    117 ELEKLEKLLQLLPLYQEL-EALEAELAELPERL-----EELEERLEELRELEEELEELEAELAELQEELEELleqlslat 190

                          170       180
                   ....*....|....*....|....
gi 2017363533  470 HHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:COG4717    191 EEELQDLAEELEELQQRLAELEEE 214
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 291-491 7.96e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.94  E-value: 7.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  291 KEDMEERITTLEKRYLAAQREATSIHDLNDK---LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEV 367
Cdd:TIGR04523  362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQindLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  368 EAELAQRIAALTKAEERHGNIEEHLRQ----LEGQ-------LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNE 436
Cdd:TIGR04523  442 IKDLTNQDSVKELIIKNLDNTRESLETqlkvLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363533  437 rlqlhLKERMAALE----EKNTLIQELES--------------------SQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR04523  522 -----LKEKIEKLEsekkEKESKISDLEDelnkddfelkkenlekeideKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-380 8.31e-05

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: 46.98  E-value: 8.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   33 MLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAErnntr 112
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----- 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  113 llLEHLECLVSRHERSLrmtvVKRQAQ--------SPSGVSsevEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEE 184
Cdd:TIGR02169  760 --LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKE 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  185 QLAGAHQQvsALQQGAGVRDGAAEEEGTVElgpkrlwkEDTGRVEELQELLEKQNFELSQARERlvtltttvteleedLG 264
Cdd:TIGR02169  830 YLEKEIQE--LQEQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEELEAALRDLESR--------------LG 885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  265 TARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANK---ESLHRQCEEKAR 341
Cdd:TIGR02169  886 DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDVQAELQRVEE 965

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2017363533  342 HLQELLEV---AEQKLQQTMR-------KAETLPEVEAELAQRIAALTK 380
Cdd:TIGR02169  966 EIRALEPVnmlAIQEYEEVLKrldelkeKRAKLEEERKAILERIEEYEK 1014
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 274-486 1.05e-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: 46.55  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  274 EELSSKHQRDLREALAQKE---DMEERITTLEKRY--LAAQREA--TSIHDLNDKLENELANKESLHRQCEEKArhlQEL 346
Cdd:TIGR04523  422 ELLEKEIERLKETIIKNNSeikDLTNQDSVKELIIknLDNTRESleTQLKVLSRSINKIKQNLEQKQKELKSKE---KEL 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  347 LEVAEQKLQqtmrkaetLPEVEAELAQRIAALTKAEErhgNIEEHLRQLEGQLEEKNQELarvrqrEKMNEDHNKRLSDT 426
Cdd:TIGR04523  499 KKLNEEKKE--------LEEKVKDLTKKISSLKEKIE---KLESEKKEKESKISDLEDEL------NKDDFELKKENLEK 561

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363533  427 VdrlLSESNERL-QLHL--KERMAALEEKNTLIQELESSQ----RQIEEQHHHKGRLSEEIEKLRQE 486
Cdd:TIGR04523  562 E---IDEKNKEIeELKQtqKSLKKKQEEKQELIDQKEKEKkdliKEIEEKEKKISSLEKELEKAKKE 625
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 313-423 1.31e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 46.36  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  313 TSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGN 387
Cdd:PRK00409   509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2017363533  388 IEEHLRQLE--GQLEEKNQELARVRQR-EKMNEDHNKRL 423
Cdd:PRK00409   589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 263-491 1.61e-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: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  263 LGTARRDLIKSEELsskhqRDLREALAQKEDMEERITTLEKRYLAAQREAtsihdlndKLENELANKESLHRQCEEKARH 342
Cdd:pfam02463  162 AAGSRLKRKKKEAL-----KKLIEETENLAELIIDLEELKLQELKLKEQA--------KKALEYYQLKEKLELEEEYLLY 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  343 LQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQeLARVRQREKMNEDHNKR 422
Cdd:pfam02463  229 LDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLER 307

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363533  423 LSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam02463  308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 222-491 1.68e-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: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  222 KEDTGRVEELQELLEKQNFELSQARErlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREaLAQKEDMEERITTL 301
Cdd:pfam02463  166 RLKRKKKEALKKLIEETENLAELIID---------------LEELKLQELKLKEQAKKALEYYQL-KEKLELEEEYLLYL 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  302 EKRYLAAQREATSIHDLNDK------------LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEA 369
Cdd:pfam02463  230 DYLKLNEERIDLLQELLRDEqeeiesskqeieKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  370 ELAQRIaaLTKAEERHGNIEEHLRQLEGQLEEKNQELARV-RQREKMNE---------DHNKRLSDTVDRLLSESNERLQ 439
Cdd:pfam02463  310 VDDEEK--LKESEKEKKKAEKELKKEKEEIEELEKELKELeIKREAEEEeeeeleklqEKLEQLEEELLAKKKLESERLS 387

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363533  440 LHLKERMAALEEKNTLIQE------LESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam02463  388 SAAKLKEEELELKSEEEKEaqllleLARQLEDLLKEEKKEELEILEEEEESIELKQGK 445
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
154-417 1.96e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvrdgaaeeegtvelgpkrlwkedtgRVEELQE 233
Cdd:COG4372     15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE----------------------------ELEQLEE 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  234 LLEKQNFELSQARERlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREAT 313
Cdd:COG4372     67 ELEQARSELEQLEEE--------------LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  314 SIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMrkaetlpevEAELAQRIAALTKAEERHGNIEEHLR 393
Cdd:COG4372    133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKEANRNAEKEEELA 203

                          250       260
                   ....*....|....*....|....
gi 2017363533  394 QLEGQLEEKNQELARVRQREKMNE 417
Cdd:COG4372    204 EAEKLIESLPRELAEELLEAKDSL 227
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1051-1093 2.17e-04

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: 40.74  E-value: 2.17e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2017363533  1051 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDH 1093
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEED 43
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1051-1097 2.41e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 40.33  E-value: 2.41e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2017363533 1051 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALdeNFDHNTLA 1097
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK 45
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 136-490 2.45e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.55  E-value: 2.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  136 RQAQSPSGVSSEVEVLKALKSLFEHHKAL----------DEKVRERLRAALERV----TTLEEQLAGAHQQVSALQQGAG 201
Cdd:pfam01576  160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMisdleerlkkEEKGRQELEKAKRKLegesTDLQEQIAELQAQIAELRAQLA 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  202 VRD-------GAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNfelsQARERLVTLTTTVTELEEDLGTARRDLIKS- 273
Cdd:pfam01576  240 KKEeelqaalARLEEETAQKNNALKKIRELEAQISELQEDLESER----AARNKAEKQRRDLGEELEALKTELEDTLDTt 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  274 ---EELSSKHQRDLREAlaqKEDMEERITTLEKRYLA-AQREATSIHDLNDKLENELANKESLHRQ---CEEKARHLQEL 346
Cdd:pfam01576  316 aaqQELRSKREQEVTEL---KKALEEETRSHEAQLQEmRQKHTQALEELTEQLEQAKRNKANLEKAkqaLESENAELQAE 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  347 LEV--------------AEQKLQQTMRKAETLPEVEAELAQRIA-----------ALTKAEERHGNIEEHLRQLEGQL-- 399
Cdd:pfam01576  393 LRTlqqakqdsehkrkkLEGQLQELQARLSESERQRAELAEKLSklqselesvssLLNEAEGKNIKLSKDVSSLESQLqd 472

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  400 ------EEKNQELA---RVRQ--------REKMNEDHNKRLS-----DTVDRLLSESNERLQLHLKERMAALEEKNTLIQ 457
Cdd:pfam01576  473 tqellqEETRQKLNlstRLRQledernslQEQLEEEEEAKRNverqlSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQR 552

                          410       420       430
                   ....*....|....*....|....*....|...
gi 2017363533  458 ELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQL 490
Cdd:pfam01576  553 ELEALTQQLEEKAAAYDKLEKTKNRLQQELDDL 585
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 222-490 2.45e-04

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 45.33  E-value: 2.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  222 KEDTGRVEELQELLEKQNFELS-QARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRdlREALAQKEDMEERITT 300
Cdd:COG5185    274 AESSKRLNENANNLIKQFENTKeKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETE--TGIQNLTAEIEQGQES 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  301 LEKRYLAAQREATSIHDLND------KLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlpeveaelaqr 374
Cdd:COG5185    352 LTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD------------ 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  375 iaalTKAEERHGNIEEHLRQLEgQLEEKNQELAR--VRQREKMNEDHNKRLSDTVDRLLSEsnerlqlhLKERMAALEEK 452
Cdd:COG5185    420 ----RQIEELQRQIEQATSSNE-EVSKLLNELISelNKVMREADEESQSRLEEAYDEINRS--------VRSKKEDLNEE 486

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2017363533  453 NTLIQELESSQRQIEEQhhHKGRLSEEIEKLRQEVDQL 490
Cdd:COG5185    487 LTQIESRVSTLKATLEK--LRAKLERQLEGVRSKLDQV 522
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 135-484 2.63e-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: 45.13  E-value: 2.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  135 KRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRdgAAEEEgtV 213
Cdd:pfam09731   88 QVKIPRQSGVSSEVaEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQ--AVKAH--T 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  214 ELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSeelsSKHQRDLREALAQKED 293
Cdd:pfam09731  164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPK----LPEHLDNVEEKVEKAQ 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  294 MEERITTLEKRYLAA-----QREATSIH-DLNDKL-ENELANKESLHRQCEekarHLQELLEVAEQKLQqTMRKAETLpE 366
Cdd:pfam09731  240 SLAKLVDQYKELVASerivfQQELVSIFpDIIPVLkEDNLLSNDDLNSLIA----HAHREIDQLSKKLA-ELKKREEK-H 313

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  367 VEAELAQRIAALTKAEER-HGNIEEHLRQLEGQLEEKNQElARVRQREKM-----------NEDHNKRLSDTVDRLLSES 434
Cdd:pfam09731  314 IERALEKQKEELDKLAEElSARLEEVRAADEAQLRLEFER-EREEIRESYeeklrtelerqAEAHEEHLKDVLVEQEIEL 392

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2017363533  435 NERLQLHLKERMAalEEKNTL---IQELESSQRQIEEQhhHKGRLSEEIEKLR 484
Cdd:pfam09731  393 QREFLQDIKEKVE--EERAGRllkLNELLANLKGLEKA--TSSHSEVEDENRK 441
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 325-486 2.71e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.11  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  325 ELANKESLHRQCEEKARHLQELLEVAEQklqQTMRKAETlpeveaelaQRIAALTKAEERHGniEEHLRQLEG-QLEEKN 403
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREVERRRKLEEA---EKARQAEM---------DRQAAIYAEQERMA--MERERELERiRQEERK 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  404 QELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKermAALEEKntlIQElESSQRQIEEQHHHKGRLSEEIEKL 483
Cdd:pfam17380  360 RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELE---AARKVK---ILE-EERQRKIQQQKVEMEQIRAEQEEA 432


                   ...
gi 2017363533  484 RQE 486
Cdd:pfam17380  433 RQR 435
PRK11281 PRK11281
mechanosensitive channel MscK;
286-466 2.71e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 45.29  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  286 EALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEnELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLP 365
Cdd:PRK11281    33 GDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALK 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  366 EVEA-ELAQRIAALTkaeerhgnieehLRQLEGQLEEKNQELARVRqrekmnedhnKRLSDTVDRLLSESN--ERLQLHL 442
Cdd:PRK11281   108 DDNDeETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQAAL 165

                          170       180
                   ....*....|....*....|....
gi 2017363533  443 KERMAALEEKNTLIQELESSQRQI 466
Cdd:PRK11281   166 YANSQRLQQIRNLLKGGKVGGKAL 189
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 338-493 3.71e-04

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.20  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  338 EKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNE 417
Cdd:cd00176     40 KKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEELNQRWEELRELAEERRQRLEEALDLQQFFR 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  418 DH---NKRLSDTVDRLLSESN-------ERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGR--LSEEIEKLRQ 485
Cdd:cd00176    114 DAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeeIEEKLEELNE 193


                   ....*...
gi 2017363533  486 EVDQLKGR 493
Cdd:cd00176    194 RWEELLEL 201
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
267-491 3.81e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.75  E-value: 3.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  267 RRDLI-KSEELSSKhqrdLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQE 345
Cdd:COG1340     45 RDELNaQVKELREE----AQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  346 LlevaeQKLQQTMrkaETLPEVEAELAQRIAALTK-AEERhgnieEHLRQLEGQLEEKNQELARVRQREkmnEDHNKRLS 424
Cdd:COG1340    121 L-----EWRQQTE---VLSPEEEKELVEKIKELEKeLEKA-----KKALEKNEKLKELRAELKELRKEA---EEIHKKIK 184

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363533  425 DTVDRLLSESNERLQLhLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG1340    185 ELAEEAQELHEEMIEL-YKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLR 250
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 316-486 4.01e-04

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


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 44.03  E-value: 4.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  316 HDLNDKLENELANKESLHRQCEEKARHLQEL-LEVA--EQKLQQTMR-KAETLPEVEaELAQRIAALTKAEERHGNIEEH 391
Cdd:pfam15905  166 NKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSkGKVAqlEEKLVSTEKeKIEEKSETE-KLLEYITELSCVSEQVEKYKLD 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  392 LRQLEGQLEEKNQELARVRQREKMNEDHnkrLSDTVDRLlsesNERLQL--HLKERMAALEE--KNTLIQELESSQRQIE 467
Cdd:pfam15905  245 IAQLEELLKEKNDEIESLKQSLEEKEQE---LSKQIKDL----NEKCKLleSEKEELLREYEekEQTLNAELEELKEKLT 317

                          170
                   ....*....|....*....
gi 2017363533  468 EQhhhkgrlSEEIEKLRQE 486
Cdd:pfam15905  318 LE-------EQEHQKLQQK 329
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 347-589 4.16e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 4.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  347 LEVAEQKLQQTMRKAETlpeVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHNKRL-- 423
Cdd:COG3883     18 IQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERAra 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  424 --------------------SDTVDRL-----LSESNERLQLHLKERMAALEE-KNTLIQELESSQRQIEEQHHHKGRLS 477
Cdd:COG3883     95 lyrsggsvsyldvllgsesfSDFLDRLsalskIADADADLLEELKADKAELEAkKAELEAKLAELEALKAELEAAKAELE 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  478 EEIEKLRQEVDQLKGRGGPFVDGVHSRSHMGSAADVRFSLGTTTHAPPGvhRRYSALREESAKDWETSPLPGMLAPAAGP 557
Cdd:COG3883    175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA--AAAAAAAAAAAAAAAAAAAAASAAGAGAA 252

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2017363533  558 AFDSDPEISDVDEDEPGGLVGSADVVSPSGHS 589
Cdd:COG3883    253 GAAGAAAGSAGAAGAAAGAAGAGAAAASAAGG 284
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 297-491 4.59e-04

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


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 43.06  E-value: 4.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  297 RITTLEKRYLAAQREATSIHDLNDKLENELANKESlhrqcEEKARHLQELLEVAEQKLQQTMRKAETL------------ 364
Cdd:pfam12795    1 KLDELEKAKLDEAAKKKLLQDLQQALSLLDKIDAS-----KQRAAAYQKALDDAPAELRELRQELAALqakaeaapkeil 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  365 -----PEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTvDRLLSESnerLQ 439
Cdd:pfam12795   76 aslslEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPP-GEPLSEA---QR 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363533  440 LHLKERMAALEEK----------NTLIQELESSQRQIEEQHHHkgRLSEEIEKLRQEVDQLK 491
Cdd:pfam12795  152 WALQAELAALKAQidmleqellsNNNRQDLLKARRDLLTLRIQ--RLEQQLQALQELLNEKR 211
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 227-493 4.77e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.43  E-value: 4.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTarrdlikseelsskhqrdLREALAQKEDMEERITtlEKRYL 306
Cdd:pfam10174  402 KIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTT------------------LEEALSEKERIIERLK--EQRER 461

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  307 AAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH- 385
Cdd:pfam10174  462 EDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLk 541

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  386 ------------GNIEEHLRQLEGQLEEKNQELAR-----------VRQREKMNEDHNKRLSDTVDRLLSESNERLQLHL 442
Cdd:pfam10174  542 kahnaeeavrtnPEINDRIRLLEQEVARYKEESGKaqaeverllgiLREVENEKNDKDKKIAELESLTLRQMKEQNKKVA 621

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363533  443 KERMAALEEKNTLIQELESSQRQIEE-----QHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:pfam10174  622 NIKHGQQEMKKKGAQLLEEARRREDNladnsQQLQLEELMGALEKTRQELDATKAR 677
PRK01156 PRK01156
chromosome segregation protein; Provisional
 283-450 5.81e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.12  E-value: 5.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLND----KLENELANKESLHRQCEEKARHLQELLEvaeqklqqtm 358
Cdd:PRK01156   581 DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDksirEIENEANNLNNKYNEIQENKILIEKLRG---------- 650

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  359 rKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVdrllSESNERL 438
Cdd:PRK01156   651 -KIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETL 725

                          170
                   ....*....|..
gi 2017363533  439 qlhlkERMAALE 450
Cdd:PRK01156   726 -----ESMKKIK 732
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 851-909 6.39e-04

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 39.62  E-value: 6.39e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363533  851 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNALHRLKLRL 909
Cdd:cd09504      5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 165-478 7.52e-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: 43.88  E-value: 7.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  165 DEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEgtvelgpkRLWKEDTGRVEELQELLEKQNFELSQ 244
Cdd:TIGR00606  790 DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ--------HELDTVVSKIELNRKLIQDQQEQIQH 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  245 ARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN 324
Cdd:TIGR00606  862 LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  325 ELankESLHRQCEEKARHLQELlevaEQKLQQTmrKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQ 404
Cdd:TIGR00606  942 KV---NDIKEKVKNIHGYMKDI----ENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI 1012

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  405 E-------LARVRQREKMNEdhnkrLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELES----SQRQIEEQ-HHH 472
Cdd:TIGR00606 1013 QerwlqdnLTLRKRENELKE-----VEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVlalgRQKGYEKEiKHF 1087


                   ....*.
gi 2017363533  473 KGRLSE 478
Cdd:TIGR00606 1088 KKELRE 1093
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 286-493 8.46e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.80  E-value: 8.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  286 EALAQKEDMEERITTLEKRY----LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQqtmrKA 361
Cdd:TIGR00618  184 MEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK----KQ 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  362 ETLPEVEAElaqriaaltkaeerhgniEEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDtVDRLLSESNERLQlh 441
Cdd:TIGR00618  260 QLLKQLRAR------------------IEELRAQEAVLEETQERINRARKAAPLAA-HIKAVTQ-IEQQAQRIHTELQ-- 317

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2017363533  442 lkERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR00618  318 --SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
388-491 8.74e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.31  E-value: 8.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  388 IEEHLRQLEGQLEEKNQELARVRQREK-MNEDHNKRLSDTVDRLLSEsNERLQLHLKERMAALEEkntLIQELESSQRQI 466
Cdd:COG2433    382 LEELIEKELPEEEPEAEREKEHEERELtEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---LERELSEARSEE 457

                           90       100
                   ....*....|....*....|....*
gi 2017363533  467 EEQHhhkgRLSEEIEKLRQEVDQLK 491
Cdd:COG2433    458 RREI----RKDREISRLDREIERLE 478
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
274-412 1.06e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.14  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  274 EELSSKHQR-----DLREALAQ-KEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQ--- 344
Cdd:COG0497    209 EELEEERRRlsnaeKLREALQEaLEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRryl 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  345 -------ELLEVAEQKLQ---QTMRK----AETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:COG0497    289 dslefdpERLEEVEERLAllrRLARKygvtVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAAR 368


                   ..
gi 2017363533  411 QR 412
Cdd:COG0497    369 KK 370
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 850-914 1.67e-03

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 38.02  E-value: 1.67e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363533  850 QWDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 914
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
326-487 1.78e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 41.35  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  326 LANKESLHRQCEEKARHLQELLEVAEQKLQQT---------MRKAEtlpeVEAELAQRIAALTKAEERHGNIEEHLRQLE 396
Cdd:COG1842     50 IANQKRLERQLEELEAEAEKWEEKARLALEKGredlarealERKAE----LEAQAEALEAQLAQLEEQVEKLKEALRQLE 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  397 GQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQEL---ESSQRQIEEQhHHK 473
Cdd:COG1842    126 SKLEELKAKKDTLKARAKAAK-AQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEAAAELaagDSLDDELAEL-EAD 203

                          170
                   ....*....|....
gi 2017363533  474 GRLSEEIEKLRQEV 487
Cdd:COG1842    204 SEVEDELAALKAKM 217
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
973-1028 2.03e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 37.63  E-value: 2.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363533  973 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1028
Cdd:pfam07647   11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 1051-1090 2.77e-03

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


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 37.63  E-value: 2.77e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2017363533 1051 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHG-ALLALDEN 1090
Cdd:cd09512      4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS 44
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 230-452 2.81e-03

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: 42.02  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  230 ELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQK----EDMEERITTLEKRY 305
Cdd:pfam05483  545 NLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnkniEELHQENKALKKKG 624

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  306 LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRI--AALTKAEE 383
Cdd:pfam05483  625 SAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIdkRCQHKIAE 704

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  384 RHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNK----RLSDTVDRLLS---------ESNERLQLHLKERMAALE 450
Cdd:pfam05483  705 MVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAaleiELSNIKAELLSlkkqleiekEEKEKLKMEAKENTAILK 784


                   ..
gi 2017363533  451 EK 452
Cdd:pfam05483  785 DK 786
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 227-377 2.84e-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: 40.68  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEEL--SSKHQRDLREALAQKEDMEERITTLEKR 304
Cdd:COG1579     32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEALQKEIESLKRRISDLEDE 111

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017363533  305 YLaaqreatsihDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAA 377
Cdd:COG1579    112 IL----------ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 267-483 3.12e-03

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


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 40.86  E-value: 3.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  267 RRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRylaAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQEL 346
Cdd:pfam06008   25 TKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKK---ATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEI 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  347 LEVAEQKLQQTMRKAETLPEVEAELAQRIAAltkaEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDT 426
Cdd:pfam06008  102 NEKVATLGENDFALPSSDLSRMLAEAQRMLG----EIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANA 177

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  427 VDRLLSESNERLQ---LHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKL 483
Cdd:pfam06008  178 LRDSLAEYEAKLSdlrELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 104-490 3.18e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 41.73  E-value: 3.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  104 LKAERNNTRLLLEHLECLVSRHERSLRmtvvkRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLraaLERVTTLE 183
Cdd:pfam10174  343 LQTEVDALRLRLEEKESFLNKKTKQLQ-----DLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENL---QEQLRDKD 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  184 EQLAGAHQQVSALQQGAGVRDGA--------AEEEGTVELGPKRLWKEDTGRVEELqELLEKQNFELSQARERLVTLTTT 255
Cdd:pfam10174  415 KQLAGLKERVKSLQTDSSNTDTAlttleealSEKERIIERLKEQREREDRERLEEL-ESLKKENKDLKEKVSALQPELTE 493

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  256 VTELEEDL----------GTARRDLIKSEELSSKHQRD--------------LREALAQKEDMEERITTLEK-------- 303
Cdd:pfam10174  494 KESSLIDLkehasslassGLKKDSKLKSLEIAVEQKKEecsklenqlkkahnAEEAVRTNPEINDRIRLLEQevarykee 573

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  304 ---------RYLAAQREATSihDLNDKlENELANKESLH-RQCEEKARHLQELlevaeQKLQQTMRKAETlpeVEAELAQ 373
Cdd:pfam10174  574 sgkaqaeveRLLGILREVEN--EKNDK-DKKIAELESLTlRQMKEQNKKVANI-----KHGQQEMKKKGA---QLLEEAR 642

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  374 RIAALTKAEERHGNIEEhlrqLEGQLEEKNQELARVRQR----EKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAAL 449
Cdd:pfam10174  643 RREDNLADNSQQLQLEE----LMGALEKTRQELDATKARlsstQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAI 718

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2017363533  450 EEKNTLIQELESSQRQieeqhhhKGRLSEEIEKLRQEVDQL 490
Cdd:pfam10174  719 SEKDANIALLELSSSK-------KKKTQEEVMALKREKDRL 752
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 28-385 3.27e-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: 3.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   28 QLMVNMLDEREKLLESLRESQETLAATQSRLQDAihERDQLQRHLNSALPQEfATLTRELSMCREQLLEREEEISELKAE 107
Cdd:TIGR02169  190 DLIIDEKRQQLERLRREREKAERYQALLKEKREY--EGYELLKEKEALERQK-EAIERQLASLEEELEKLTEEISELEKR 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  108 RNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSLFEHHKALDEKVR---ERLRAALERVTTLE 183
Cdd:TIGR02169  267 LEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEKERELEDAEERLAkleAEIDKLLAEIEELE 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  184 EQLAGAHQQVSALQqgAGVRDGAAEEEGTVElgpkrlwkedtgRVEELQELLEKQNFELSQARERLVTLTTTVTELeedL 263
Cdd:TIGR02169  343 REIEEERKRRDKLT--EEYAELKEELEDLRA------------ELEEVDKEFAETRDELKDYREKLEKLKREINEL---K 405

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  264 GTARRDLIKSEELSSKhQRDLREALAQKED----MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEK 339
Cdd:TIGR02169  406 RELDRLQEELQRLSEE-LADLNAAIAGIEAkineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE 484

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2017363533  340 ARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRI-------AALTKAEERH 385
Cdd:TIGR02169  485 LSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERY 537
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 262-493 3.48e-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: 41.38  E-value: 3.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRY------LAAQREA--TSIhdlnDKLENELANKESLH 333
Cdd:pfam06160   87 ALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYrelrktLLANRFSygPAI----DELEKQLAEIEEEF 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  334 RQCEE--------KARHLQELLEVAEQKLQQTMRK--------AETLPEVEAELAQRIAALTKAEER--HGNIEEHLRQL 395
Cdd:pfam06160  163 SQFEEltesgdylEAREVLEKLEEETDALEELMEDipplyeelKTELPDQLEELKEGYREMEEEGYAleHLNVDKEIQQL 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  396 EGQLEE-----KNQELARVrqrEKMNEDHNKRLSDTVDRLLSESNERLQLH-----LKERMAALEEKNTLIQ-ELES-SQ 463
Cdd:pfam06160  243 EEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVEknlpeIEDYLEHAEEQNKELKeELERvQQ 319

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2017363533  464 RQI---EEQHHHKGrLSEEIEKLRQEVDQLKGR 493
Cdd:pfam06160  320 SYTlneNELERVRG-LEKQLEELEKRYDEIVER 351
PRK09039 PRK09039
peptidoglycan -binding protein;
273-410 3.83e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.10  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  273 SEELSSKHQR---------DLREALA----QKEDMEERITTLEKRYLAAQREatsihdlNDKLENELANKESLHRQCEEK 339
Cdd:PRK09039    45 SREISGKDSAldrlnsqiaELADLLSlerqGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGR 117

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363533  340 ARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL--------TKAEERHGNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:PRK09039   118 AGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
169-412 3.85e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  169 RERLRAAL----ERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVElgpkrlwkedtgRVEELQELLEKQNFELSQ 244
Cdd:COG3206    170 REEARKALefleEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQ------------QLSELESQLAEARAELAE 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  245 ARERLVTLTTTVteleedlgtARRDLIKSEELSSKHQRDLREALAQkedMEERITTLEKRYLAAQREATSihdlndkLEN 324
Cdd:COG3206    238 AEARLAALRAQL---------GSGPDALPELLQSPVIQQLRAQLAE---LEAELAELSARYTPNHPDVIA-------LRA 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  325 ELANKEslhrqceekarhlQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQ 404
Cdd:COG3206    299 QIAALR-------------AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365


                   ....*...
gi 2017363533  405 ELARVRQR 412
Cdd:COG3206    366 LYESLLQR 373
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 30-415 4.20e-03

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: 40.82  E-value: 4.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   30 MVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS------ALPQEFATLTRELSmcreqllereeeisE 103
Cdd:pfam19220   15 MADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQeraaygKLRRELAGLTRRLS--------------A 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  104 LKAERNNTRLLLEHLECLVSRHER---SLRMTVVKRQAQSPS---GVSSEVEVLKALKslfEHHKALdekvRERLRAALE 177
Cdd:pfam19220   81 AEGELEELVARLAKLEAALREAEAakeELRIELRDKTAQAEAlerQLAAETEQNRALE---EENKAL----REEAQAAEK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  178 RVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEG--TVELGpkRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTT 255
Cdd:pfam19220  154 ALQRAEGELATARERLALLEQENRRLQALSEEQAaeLAELT--RRLAELETQLDATRARLRALEGQLAAEQAERERAEAQ 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  256 VTELEEDLGTARRDL-IKSEELSSKH---QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKES 331
Cdd:pfam19220  232 LEEAVEAHRAERASLrMKLEALTARAaatEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQ 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  332 LHrQCEEKARhlQELLEVAEqklqqTMRKAetlpeveaeLAQRIAALTKAEERHGNIEEHLRQLEGQ-------LEEKNQ 404
Cdd:pfam19220  312 QF-QEMQRAR--AELEERAE-----MLTKA---------LAAKDAALERAEERIASLSDRIAELTKRfeveraaLEQANR 374

                          410
                   ....*....|.
gi 2017363533  405 ELARVRQREKM 415
Cdd:pfam19220  375 RLKEELQRERA 385
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 169-493 4.44e-03

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: 41.48  E-value: 4.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAG-VRD-----GAAEEEGTVELGPKRLW----------KEDTGR----V 228
Cdd:COG3096    277 ANERRELSERALELRRELFGARRQLAEEQYRLVeMAReleelSARESDLEQDYQAASDHlnlvqtalrqQEKIERyqedL 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  229 EELQELLEKQNFELSQARERLVTLTttvteleedlgtARRDLIKSEELSSKHQ-RDLREALaqkeDMEERITTLEKRYLA 307
Cdd:COG3096    357 EELTERLEEQEEVVEEAAEQLAEAE------------ARLEAAEEEVDSLKSQlADYQQAL----DVQQTRAIQYQQAVQ 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  308 AQREATSIHDLNDKlenELANKESLHRQCEEKARHLQELLEVAEQKLQqTMRKAETLPEVEAELAQRIAALTKAEERHGN 387
Cdd:COG3096    421 ALEKARALCGLPDL---TPENAEDYLAAFRAKEQQATEEVLELEQKLS-VADAARRQFEKAYELVCKIAGEVERSQAWQT 496

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  388 IEEHLRQ------LEGQLEEKNQELARVRQREkmNEDHNKRlsdtvdRLLSESNERLQLHLKERMAALEEKNTLIQELES 461
Cdd:COG3096    497 ARELLRRyrsqqaLAQRLQQLRAQLAELEQRL--RQQQNAE------RLLEEFCQRIGQQLDAAEELEELLAELEAQLEE 568

                          330       340       350
                   ....*....|....*....|....*....|..
gi 2017363533  462 SQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:COG3096    569 LEEQAAEAVEQRSELRQQLEQLRARIKELAAR 600
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 266-491 4.69e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  266 ARRDLIKSEELSSKHQRDLREA-------LAQKEDMEERITTLEKRYL-------AAQREATSIHDLNDKLENELANKES 331
Cdd:pfam01576  796 AVKQLKKLQAQMKDLQRELEEArasrdeiLAQSKESEKKLKNLEAELLqlqedlaASERARRQAQQERDELADEIASGAS 875

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  332 LHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALT---KAEERHGNIEEHLRQlegQLEEKNQEL-A 407
Cdd:pfam01576  876 GKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTtelAAERSTSQKSESARQ---QLERQNKELkA 952

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  408 RVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEV 487
Cdd:pfam01576  953 KLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRM 1032


                   ....
gi 2017363533  488 DQLK 491
Cdd:pfam01576 1033 KQLK 1036
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 271-490 5.58e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 5.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  271 IKSEELSSKHQRDLREALAQKEDMEERITTLEK-------RYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHL 343
Cdd:TIGR04523  120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleklnnKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  344 QELLEVAEQKLQ--------------QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELarv 409
Cdd:TIGR04523  200 ELLLSNLKKKIQknkslesqiselkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL--- 276

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  410 RQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQhhhKGRLSEEIEKLRQEVDQ 489
Cdd:TIGR04523  277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKI---ISQLNEQISQLKKELTN 353


                   .
gi 2017363533  490 L 490
Cdd:TIGR04523  354 S 354
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 35-490 5.90e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.88  E-value: 5.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533   35 DEREKLLESLRESQETLAATQSRLQDAIHERDQ---LQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNT 111
Cdd:pfam05557   17 EKKQMELEHKRARIELEKKASALKRQLDRESDRnqeLQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKE 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  112 RLLLEHLECLVS-RHERSLRMTVVKRQAQSPSGVSSEVEVLKalkslfEHHKALDEKVR--ERLRAALErvtTLEEQLAG 188
Cdd:pfam05557   97 SQLADAREVISClKNELSELRRQIQRAELELQSTNSELEELQ------ERLDLLKAKASeaEQLRQNLE---KQQSSLAE 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  189 AHQQVSALQQGAGVRDGAAEEEGTVelgpkrlwKEDTGRVEELQELLEKQNFELSQARErlvtltttvteleedlgTARR 268
Cdd:pfam05557  168 AEQRIKELEFEIQSQEQDSEIVKNS--------KSELARIPELEKELERLREHNKHLNE-----------------NIEN 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  269 DLIKSEELSskhqrDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKarhLQELLE 348
Cdd:pfam05557  223 KLLLKEEVE-----DLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQL---QQREIV 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  349 VAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ------REKMNEDH 419
Cdd:pfam05557  295 LKEENsslTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAilesydKELTMSNY 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  420 NKRLSDTVdRLLSESNERLQLHLKE---RMAALEEK--------NTLIQELESSQRQieEQHHHKGRLSEEIEKLRQEVD 488
Cdd:pfam05557  375 SPQLLERI-EEAEDMTQKMQAHNEEmeaQLSVAEEElggykqqaQTLERELQALRQQ--ESLADPSYSKEEVDSLRRKLE 451


                   ..
gi 2017363533  489 QL 490
Cdd:pfam05557  452 TL 453
PTZ00121 PTZ00121
MAEBL; Provisional
 159-491 6.43e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 6.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvrdgaAEEEGTVELGPKrlwKEDTGRVEELQELLE-- 236
Cdd:PTZ00121  1168 EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK--------AEEERKAEEARK---AEDAKKAEAVKKAEEak 1236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  237 KQNFELSQA-RERLVTLTTTVTELEEDLGTARRDLIKSEElsSKHQRDLREALAQKEDMEERITTLEKRYLAAQR---EA 312
Cdd:PTZ00121  1237 KDAEEAKKAeEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKKKADEAKKAEEKKKADEAKKkaeEA 1314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  313 TSIHDLNDKLENELANKESLHRQCEE-----------------KARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRI 375
Cdd:PTZ00121  1315 KKADEAKKKAEEAKKKADAAKKKAEEakkaaeaakaeaeaaadEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  376 AALTKAEERHGNIEEHLRQLEgqlEEKNQELARVRQREKMNEDHNKRLSD---TVDRLLSESNErlqlhlKERMAALEEK 452
Cdd:PTZ00121  1395 EAKKKAEEDKKKADELKKAAA---AKKKADEAKKKAEEKKKADEAKKKAEeakKADEAKKKAEE------AKKAEEAKKK 1465

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2017363533  453 NTLIQELESSQRQIEEQHHHKgRLSEEIEKLRQEVDQLK 491
Cdd:PTZ00121  1466 AEEAKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADEAK 1503
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 973-1017 6.71e-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: 6.71e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2017363533  973 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 1017
Cdd:cd09501     11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 166-485 7.62e-03

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: 40.71  E-value: 7.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEeegtvelgpkrlwkedtgRVEELQELLEKQNFELSQA 245
Cdd:COG3096    378 AEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ------------------ALEKARALCGLPDLTPENA 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  246 RERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQR--DLREALA---QKEDMEERITTL-----EKRYLAAQREAtsi 315
Cdd:COG3096    440 EDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayELVCKIAgevERSQAWQTARELlrryrSQQALAQRLQQ--- 516

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  316 hdlndkLENELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQL 395
Cdd:COG3096    517 ------LRAQLAELE----QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  396 EGQLEEKNQELarvRQREKMNEDHNKRLSdtvdRLLSESNERLQlHLKERMAALEEKNTLIQELESSQRQIEEQhhhKGR 475
Cdd:COG3096    587 LEQLRARIKEL---AARAPAWLAAQDALE----RLREQSGEALA-DSQEVTAAMQQLLEREREATVERDELAAR---KQA 655

                          330
                   ....*....|
gi 2017363533  476 LSEEIEKLRQ 485
Cdd:COG3096    656 LESQIERLSQ 665
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 320-491 8.05e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 8.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  320 DKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKA-EERHGNIEEHLRQL--E 396
Cdd:COG3883     19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERARALyrS 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  397 GQ--------LEEKNQE--LARVRQREKMNEDHNKRLSDTVDrlLSESNERLQLHLKERMAALEE-KNTLIQELESSQRQ 465
Cdd:COG3883     99 GGsvsyldvlLGSESFSdfLDRLSALSKIADADADLLEELKA--DKAELEAKKAELEAKLAELEAlKAELEAAKAELEAQ 176

                          170       180
                   ....*....|....*....|....*.
gi 2017363533  466 IEEQHHHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG3883    177 QAEQEALLAQLSAEEAAAEAQLAELE 202
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 274-490 8.08e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.42  E-value: 8.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  274 EELSSKHQRDLREALAQKEDMEERITTLEKRY---LAAQREATSIHDLNDKLENELANK-ESLHRQCEEKARHLQEllev 349
Cdd:TIGR00606  694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRdemLGLAPGRQSIIDLKEKEIPELRNKlQKVNRDIQRLKNDIEE---- 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363533  350 aEQKLQQTMRKAETLPEVeaeLAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELArVRQREKMNEDHNKRLsdtvdR 429
Cdd:TIGR00606  770 -QETLLGTIMPEEESAKV---CLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRT-VQQVNQEKQEKQHEL-----D 839

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363533  430 LLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQL 490
Cdd:TIGR00606  840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSL 900
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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