NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2017363575|ref|NP_001380879|]
View 

liprin-alpha-4 isoform 3 [Homo sapiens]

Protein Classification

liprin-alpha( domain architecture ID 13377566)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 956-1021 1.16e-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: 1.16e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363575  956 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1021
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 ...
 839-909 3.15e-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: 3.15e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363575  839 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 909
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 ...
 1041-1112 5.03e-41

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


:

Pssm-ID: 188967  Cd Length: 72  Bit Score: 145.15  E-value: 5.03e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363575 1041 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1112
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 221-481 3.36e-13

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: 74.59  E-value: 3.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  221 WKEDTGRVEELQELLEKQNFELSQARERlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITT 300
Cdd:COG1196    241 LEELEAELEELEAELEELEAELAELEAE--------------LEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  301 LEKRYLAAQREATSIHDLNDKLENELANKEslhrQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE 380
Cdd:COG1196    307 LEERRRELEERLEELEEELAELEEELEELE----EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  381 EHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLsdtvDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ 460
Cdd:COG1196    383 ELAEELLEALRAAAELAAQLEELEEAEEALLERL----ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458

                          250       260
                   ....*....|....*....|.
gi 2017363575  461 HHHKGRLSEEIEKLRQEVDQL 481
Cdd:COG1196    459 EALLELLAELLEEAALLEAAL 479
Crescentin super family cl41192
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 30-406 4.91e-04

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.


The actual alignment was detected with superfamily member pfam19220:

Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 43.90  E-value: 4.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   30 MVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS------ALPQEFATLTRELSmcreqllereeeisE 103
Cdd:pfam19220   15 MADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQeraaygKLRRELAGLTRRLS--------------A 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  104 LKAERNNTRLLLEHLECLVSRHER---SLRMTVVKRQAQSPS---GVSSEVEVLKALKslfEHHKALdekvRERLRAALE 177
Cdd:pfam19220   81 AEGELEELVARLAKLEAALREAEAakeELRIELRDKTAQAEAlerQLAAETEQNRALE---EENKAL----REEAQAAEK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  178 RVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEG--TVELGpkRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTT 255
Cdd:pfam19220  154 ALQRAEGELATARERLALLEQENRRLQALSEEQAaeLAELT--RRLAELETQLDATRARLRALEGQLAAEQAERERAEAQ 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  256 VTELEEDLGTARRDL-IKSEELSSKH---QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELAnkes 331
Cdd:pfam19220  232 LEEAVEAHRAERASLrMKLEALTARAaatEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLE---- 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  332 lHRQELLEVAEQKLQQTMRKAETLPEVeaeLAQRIAALTKAEERHGNIEEHLRQLEGQ-------LEEKNQELARVRQRE 404
Cdd:pfam19220  308 -RRTQQFQEMQRARAELEERAEMLTKA---LAAKDAALERAEERIASLSDRIAELTKRfeveraaLEQANRRLKEELQRE 383


                   ..
gi 2017363575  405 KM 406
Cdd:pfam19220  384 RA 385
 
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 ...
 956-1021 1.16e-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: 1.16e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363575  956 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1021
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 ...
 839-909 3.15e-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: 3.15e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363575  839 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 909
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 ...
 1041-1112 5.03e-41

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


Pssm-ID: 188967  Cd Length: 72  Bit Score: 145.15  E-value: 5.03e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363575 1041 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1112
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 955-1019 5.61e-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: 5.61e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363575  955 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1019
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 221-481 3.36e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.59  E-value: 3.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  221 WKEDTGRVEELQELLEKQNFELSQARERlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITT 300
Cdd:COG1196    241 LEELEAELEELEAELEELEAELAELEAE--------------LEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  301 LEKRYLAAQREATSIHDLNDKLENELANKEslhrQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE 380
Cdd:COG1196    307 LEERRRELEERLEELEEELAELEEELEELE----EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  381 EHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLsdtvDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ 460
Cdd:COG1196    383 ELAEELLEALRAAAELAAQLEELEEAEEALLERL----ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458

                          250       260
                   ....*....|....*....|.
gi 2017363575  461 HHHKGRLSEEIEKLRQEVDQL 481
Cdd:COG1196    459 EALLELLAELLEEAALLEAAL 479
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-481 4.09e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 70.86  E-value: 4.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  147 EVEVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVElgpkrlwKEDTG 226
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL-------AEAEA 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  307 AAQREATSIHDLNDKLENELANKEslhrqELLEVAEQKLQQTMrkaETLPEVEAELAQRIAALTKAEERHGNIEEHLRQL 386
Cdd:TIGR02168  863 ELEELIEELESELEALLNERASLE-----EALALLRSELEELS---EELRELESKRSELRRELEELREKLAQLELRLEGL 934

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  387 EGQLEEKNQelaRVRQREKMNEDHNKRLSDTVDRLLSESNERLQLhLKERMAALEEKN-TLIQELESSQRQIEEQHHHKG 465
Cdd:TIGR02168  935 EVRIDNLQE---RLSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNlAAIEEYEELKERYDFLTAQKE 1010

                          330
                   ....*....|....*.
gi 2017363575  466 RLSEEIEKLRQEVDQL 481
Cdd:TIGR02168 1011 DLTEAKETLEEAIEEI 1026
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
38-484 6.05e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 70.07  E-value: 6.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   38 EKLLESLRESQETLAATQSRLQDA-IHERdqlqrhLNsALPQEFATLTRElsmcreqllereeeISELKAERNNTRLLLE 116
Cdd:PRK02224   179 ERVLSDQRGSLDQLKAQIEEKEEKdLHER------LN-GLESELAELDEE--------------IERYEEQREQARETRD 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  117 HLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalERVTTLEEQLAGAHQQVSAL 196
Cdd:PRK02224   238 EADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDDL 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  197 QQGAGVRDGAAEeegTVELGPKRLWKEDtgrvEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEEL 276
Cdd:PRK02224   299 LAEAGLDDADAE---AVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  277 SSKHQRDLREALAQKEDMEERITTLEKRYLAAqreATSIHDLNDKLENELANKESLHRQEL-LEVAEQKLQQTMRKAETL 355
Cdd:PRK02224   372 LEEAREAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELREREAeLEATLRTARERVEEAEAL 448

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  356 ------PEVEAEL--AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMnEDHNKRLSD---TVDRLLSE 424
Cdd:PRK02224   449 leagkcPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEErreDLEELIAE 527

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  425 SNERLQlhlkERMAALEEKNTLIQELESSQrqiEEQHHHKGRLSEEIEKLRQEVDQLKGR 484
Cdd:PRK02224   528 RRETIE----EKRERAEELRERAAELEAEA---EEKREAAAEAEEEAEEAREEVAELNSK 580
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 21-482 1.36e-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: 62.83  E-value: 1.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   21 DADANFEQLMVNMLDErEKLLESLREsqeTLAATQSRLQDAIHERDQLQ----RHLNSALPQEFATLTRELSMCREQLLE 96
Cdd:pfam15921  167 DSNTQIEQLRKMMLSH-EGVLQEIRS---ILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   97 REEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-----RMTVVKRQAQSpsgVSSEVEVLKalkslfehhkaldE 166
Cdd:pfam15921  243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglteKASSARSQANS---IQSQLEIIQ-------------E 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  167 KVRERLRAALERVTTLEEQLAgahQQVSALQQGagvrdgaaeeegtvelgpKRLWKEdtgRVEELQELLEKQNFELSQAR 246
Cdd:pfam15921  307 QARNQNSMYMRQLSDLESTVS---QLRSELREA------------------KRMYED---KIEELEKQLVLANSELTEAR 362

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  247 ERLVTLTTTVTELEEDLGTARRDLIKSE-ELSSKHQRDLRealAQKEDMEERITT------LEKRYLAAQREATSIHDLN 319
Cdd:pfam15921  363 TERDQFSQESGNLDDQLQKLLADLHKREkELSLEKEQNKR---LWDRDTGNSITIdhlrreLDDRNMEVQRLEALLKAMK 439

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  320 DKLENELANKESL--HRQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQEL 397
Cdd:pfam15921  440 SECQGQMERQMAAiqGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI 519

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  398 ARVRQREKMNEDHNKRLSDTVDRLLSESNE--RLQLHLKERMAALEeknTLIQELEsSQRQIEEQHH--------HKGRL 467
Cdd:pfam15921  520 TKLRSRVDLKLQELQHLKNEGDHLRNVQTEceALKLQMAEKDKVIE---ILRQQIE-NMTQLVGQHGrtagamqvEKAQL 595

                          490
                   ....*....|....*
gi 2017363575  468 SEEIEKLRQEVDQLK 482
Cdd:pfam15921  596 EKEINDRRLELQEFK 610
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 839-905 4.78e-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: 50.76  E-value: 4.78e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363575   839 FAQWDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 905
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 964-1019 9.30e-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: 9.30e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363575   964 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1019
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1042-1113 7.80e-06

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 44.59  E-value: 7.80e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363575  1042 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHntlalILQIPTQNTQARQVMEREFNNLLA 1113
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEED-----LKELGITKLGHRKKILKAIQKLKE 67
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1042-1112 1.15e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 44.18  E-value: 1.15e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363575 1042 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALdeNFDHNTLAlilQIPTQNTQARQVMEREFNNLL 1112
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 30-406 4.91e-04

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: 43.90  E-value: 4.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   30 MVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS------ALPQEFATLTRELSmcreqllereeeisE 103
Cdd:pfam19220   15 MADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQeraaygKLRRELAGLTRRLS--------------A 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  104 LKAERNNTRLLLEHLECLVSRHER---SLRMTVVKRQAQSPS---GVSSEVEVLKALKslfEHHKALdekvRERLRAALE 177
Cdd:pfam19220   81 AEGELEELVARLAKLEAALREAEAakeELRIELRDKTAQAEAlerQLAAETEQNRALE---EENKAL----REEAQAAEK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  178 RVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEG--TVELGpkRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTT 255
Cdd:pfam19220  154 ALQRAEGELATARERLALLEQENRRLQALSEEQAaeLAELT--RRLAELETQLDATRARLRALEGQLAAEQAERERAEAQ 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  256 VTELEEDLGTARRDL-IKSEELSSKH---QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELAnkes 331
Cdd:pfam19220  232 LEEAVEAHRAERASLrMKLEALTARAaatEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLE---- 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  332 lHRQELLEVAEQKLQQTMRKAETLPEVeaeLAQRIAALTKAEERHGNIEEHLRQLEGQ-------LEEKNQELARVRQRE 404
Cdd:pfam19220  308 -RRTQQFQEMQRARAELEERAEMLTKA---LAAKDAALERAEERIASLSDRIAELTKRfeveraaLEQANRRLKEELQRE 383


                   ..
gi 2017363575  405 KM 406
Cdd:pfam19220  384 RA 385
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 281-484 1.51e-03

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.28  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  281 QRDLREALAQKEDMEERITTLEKRylaaqREATSIHDLNDKLEnelankeslHRQELLEVAEQKLQQTMRKAETLPEVEA 360
Cdd:cd00176      6 LRDADELEAWLSEKEELLSSTDYG-----DDLESVEALLKKHE---------ALEAELAAHEERVEALNELGEQLIEEGH 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  361 ELAQRIaaltkaEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDH---NKRLSDTVDRLLSESN-------ERLQ 430
Cdd:cd00176     72 PDAEEI------QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELL 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363575  431 LHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGR--LSEEIEKLRQEVDQLKGR 484
Cdd:cd00176    146 KKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeeIEEKLEELNERWEELLEL 201
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 841-905 1.69e-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: 1.69e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363575  841 QWDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 905
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-406 1.76e-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: 42.75  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   33 MLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLN------SALPQEFATLTRELSMCREQLLEREEEISELKA 106
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleqeeEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  107 ERNNTRLLLEHLECLVSRHERSLRMTVVKrqaqspsgvssevEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEEQL 186
Cdd:TIGR02169  766 RIEELEEDLHKLEEALNDLEARLSHSRIP-------------EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKEYL 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  187 AGAHQQvsALQQGAGVRDGAAEEEGTVElgpkrlwkEDTGRVEELQELLEKQnfelsQARERlvtltttvteleeDLGTA 266
Cdd:TIGR02169  832 EKEIQE--LQEQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEEL-----EAALR-------------DLESR 883

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  267 RRDLikseelsskhQRDLREALAQKEDMEERITTLEkryLAAQREATSIHDLNDKLEN---ELANKESLHRQELLEVAEQ 343
Cdd:TIGR02169  884 LGDL----------KKERDELEAQLRELERKIEELE---AQIEKKRKRLSELKAKLEAleeELSEIEDPKGEDEEIPEEE 950

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363575  344 KlqqtmrKAETLPEVEAELAQRIAAL----TKAEERHGNIEEHLRQLEGQL----EEKNQELARVRQREKM 406
Cdd:TIGR02169  951 L------SLEDVQAELQRVEEEIRALepvnMLAIQEYEEVLKRLDELKEKRakleEERKAILERIEEYEKK 1015
 
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 ...
 956-1021 1.16e-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: 1.16e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363575  956 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1021
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 ...
 839-909 3.15e-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: 3.15e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363575  839 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 909
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 ...
 1041-1112 5.03e-41

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


Pssm-ID: 188967  Cd Length: 72  Bit Score: 145.15  E-value: 5.03e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363575 1041 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1112
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 960-1019 8.81e-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: 8.81e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  960 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1019
Cdd:cd09495      1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 1049-1110 1.11e-26

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: 103.77  E-value: 1.11e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363575 1049 QVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNN 1110
Cdd:cd09496      1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 846-904 3.87e-25

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


Pssm-ID: 188893  Cd Length: 58  Bit Score: 99.22  E-value: 3.87e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363575  846 TVVSWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 904
Cdd:cd09494      1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 1041-1112 2.46e-19

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: 83.26  E-value: 2.46e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363575 1041 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1112
Cdd:cd09570      1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 1041-1112 2.04e-16

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 74.80  E-value: 2.04e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363575 1041 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1112
Cdd:cd09569      1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 955-1019 3.76e-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: 3.76e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363575  955 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1019
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 ...
 955-1019 4.00e-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: 4.00e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363575  955 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1019
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 ...
 840-904 1.14e-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: 1.14e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363575  840 AQWDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 904
Cdd:cd09564      2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 955-1019 5.61e-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: 5.61e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363575  955 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1019
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 221-481 3.36e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.59  E-value: 3.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  221 WKEDTGRVEELQELLEKQNFELSQARERlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITT 300
Cdd:COG1196    241 LEELEAELEELEAELEELEAELAELEAE--------------LEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  301 LEKRYLAAQREATSIHDLNDKLENELANKEslhrQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE 380
Cdd:COG1196    307 LEERRRELEERLEELEEELAELEEELEELE----EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  381 EHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLsdtvDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ 460
Cdd:COG1196    383 ELAEELLEALRAAAELAAQLEELEEAEEALLERL----ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458

                          250       260
                   ....*....|....*....|.
gi 2017363575  461 HHHKGRLSEEIEKLRQEVDQL 481
Cdd:COG1196    459 EALLELLAELLEEAALLEAAL 479
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-481 4.09e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 70.86  E-value: 4.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  147 EVEVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVElgpkrlwKEDTG 226
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL-------AEAEA 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  307 AAQREATSIHDLNDKLENELANKEslhrqELLEVAEQKLQQTMrkaETLPEVEAELAQRIAALTKAEERHGNIEEHLRQL 386
Cdd:TIGR02168  863 ELEELIEELESELEALLNERASLE-----EALALLRSELEELS---EELRELESKRSELRRELEELREKLAQLELRLEGL 934

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  387 EGQLEEKNQelaRVRQREKMNEDHNKRLSDTVDRLLSESNERLQLhLKERMAALEEKN-TLIQELESSQRQIEEQHHHKG 465
Cdd:TIGR02168  935 EVRIDNLQE---RLSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNlAAIEEYEELKERYDFLTAQKE 1010

                          330
                   ....*....|....*.
gi 2017363575  466 RLSEEIEKLRQEVDQL 481
Cdd:TIGR02168 1011 DLTEAKETLEEAIEEI 1026
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
38-484 6.05e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 70.07  E-value: 6.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   38 EKLLESLRESQETLAATQSRLQDA-IHERdqlqrhLNsALPQEFATLTRElsmcreqllereeeISELKAERNNTRLLLE 116
Cdd:PRK02224   179 ERVLSDQRGSLDQLKAQIEEKEEKdLHER------LN-GLESELAELDEE--------------IERYEEQREQARETRD 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  117 HLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalERVTTLEEQLAGAHQQVSAL 196
Cdd:PRK02224   238 EADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDDL 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  197 QQGAGVRDGAAEeegTVELGPKRLWKEDtgrvEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEEL 276
Cdd:PRK02224   299 LAEAGLDDADAE---AVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  277 SSKHQRDLREALAQKEDMEERITTLEKRYLAAqreATSIHDLNDKLENELANKESLHRQEL-LEVAEQKLQQTMRKAETL 355
Cdd:PRK02224   372 LEEAREAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELREREAeLEATLRTARERVEEAEAL 448

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  356 ------PEVEAEL--AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMnEDHNKRLSD---TVDRLLSE 424
Cdd:PRK02224   449 leagkcPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEErreDLEELIAE 527

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  425 SNERLQlhlkERMAALEEKNTLIQELESSQrqiEEQHHHKGRLSEEIEKLRQEVDQLKGR 484
Cdd:PRK02224   528 RRETIE----EKRERAEELRERAAELEAEA---EEKREAAAEAEEEAEEAREEVAELNSK 580
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 267-482 8.68e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 8.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  267 RRDLIksEELS--SKHQRDLREALAQKEDMEERIT-------TLEKRY--LAAQRE-ATSIHDLNDKLEnELANKESLHR 334
Cdd:COG1196    157 RRAII--EEAAgiSKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEkAERYRELKEELK-ELEAELLLLK 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  335 QELLEVAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKR 413
Cdd:COG1196    234 LRELEAELEELEAELEELEAeLEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363575  414 LSDTVDRL---LSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 482
Cdd:COG1196    314 LEERLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
278-485 1.38e-11

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 69.17  E-value: 1.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  278 SKHQRDLREALAQKEDMEERITTLE------KRYLAAQREATSIHDLNDKLENELANKESLHRQELLEVAEQKLQQTMRK 351
Cdd:COG4913    231 VEHFDDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  352 AETLPEVEAELAQRIAALTKAEERHGNIEehLRQLEGQLEEKNQELARVRQREkmnedhnKRLSDTVDRL---LSESNER 428
Cdd:COG4913    311 LERLEARLDALREELDELEAQIRGNGGDR--LEQLEREIERLERELEERERRR-------ARLEALLAALglpLPASAEE 381

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363575  429 LQLHLKERMAALEEKNTLIQELESSQRQIEEQHHhkgRLSEEIEKLRQEVDQLKGRG 485
Cdd:COG4913    382 FAALRAEAAALLEALEEELEALEEALAEAEAALR---DLRRELRELEAEIASLERRK 435
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 147-442 3.13e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 3.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  147 EVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEdtg 226
Cdd:COG1196    233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE--- 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1196    310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  307 AAQREATsihdlndKLENELANKESLHRQELLEVAEQKLQQTMRKAETLpEVEAELAQRIAALTKAEERHGNIEEHLRQL 386
Cdd:COG1196    390 EALRAAA-------ELAAQLEELEEAEEALLERLERLEEELEELEEALA-ELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363575  387 EGQLEEKNQELARVRQREKmnedhnkrlsdtvDRLLSESNERLQLHLKERMAALEE 442
Cdd:COG1196    462 LELLAELLEEAALLEAALA-------------ELLEELAEAAARLLLLLEAEADYE 504
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 839-903 1.26e-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: 1.26e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363575  839 FAQWDGPTVVSWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQ 903
Cdd:cd09563      1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 218-482 1.85e-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: 65.47  E-value: 1.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  218 KRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEE----LSSKHQRDLREALAQKED 293
Cdd:TIGR02169  155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEA 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQELLEVAEQKLQQTMRKAETLPEVEAELAQ---RIAA-- 368
Cdd:TIGR02169  235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlerSIAEke 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  369 --LTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSesneRLQLHLKERMAALEEKNTL 446
Cdd:TIGR02169  315 reLEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA----ELEEVDKEFAETRDELKDY 390

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2017363575  447 IQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 482
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 20-459 7.43e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 7.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   20 ADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREE 99
Cdd:COG1196    329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-EELLEALRAAAELAAQLEELEE 407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  100 EISELKAERNNTRLLLEHLEclvSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG1196    408 AEEALLERLERLEEELEELE---EALAELEEEEEEEEEALE-----EAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  180 TTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKR--------LWKEDTGRVEELQELLEKQNFELSQARERLVT 251
Cdd:COG1196    480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  252 LTTTVTELEEDLGTARR---DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQ--REATSIHDLNDKLENEL 326
Cdd:COG1196    560 AAAIEYLKAAKAGRATFlplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtlLGRTLVAARLEAALRRA 639

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  327 ANKESLHRQELLEVAEQKLQQTM----RKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ 402
Cdd:COG1196    640 VTLAGRLREVTLEGEGGSAGGSLtggsRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363575  403 REKMNEDHNKRLS--DTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEE 459
Cdd:COG1196    720 ELEEEALEEQLEAerEELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 21-482 1.36e-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: 62.83  E-value: 1.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   21 DADANFEQLMVNMLDErEKLLESLREsqeTLAATQSRLQDAIHERDQLQ----RHLNSALPQEFATLTRELSMCREQLLE 96
Cdd:pfam15921  167 DSNTQIEQLRKMMLSH-EGVLQEIRS---ILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   97 REEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-----RMTVVKRQAQSpsgVSSEVEVLKalkslfehhkaldE 166
Cdd:pfam15921  243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglteKASSARSQANS---IQSQLEIIQ-------------E 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  167 KVRERLRAALERVTTLEEQLAgahQQVSALQQGagvrdgaaeeegtvelgpKRLWKEdtgRVEELQELLEKQNFELSQAR 246
Cdd:pfam15921  307 QARNQNSMYMRQLSDLESTVS---QLRSELREA------------------KRMYED---KIEELEKQLVLANSELTEAR 362

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  247 ERLVTLTTTVTELEEDLGTARRDLIKSE-ELSSKHQRDLRealAQKEDMEERITT------LEKRYLAAQREATSIHDLN 319
Cdd:pfam15921  363 TERDQFSQESGNLDDQLQKLLADLHKREkELSLEKEQNKR---LWDRDTGNSITIdhlrreLDDRNMEVQRLEALLKAMK 439

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  320 DKLENELANKESL--HRQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQEL 397
Cdd:pfam15921  440 SECQGQMERQMAAiqGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI 519

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  398 ARVRQREKMNEDHNKRLSDTVDRLLSESNE--RLQLHLKERMAALEeknTLIQELEsSQRQIEEQHH--------HKGRL 467
Cdd:pfam15921  520 TKLRSRVDLKLQELQHLKNEGDHLRNVQTEceALKLQMAEKDKVIE---ILRQQIE-NMTQLVGQHGrtagamqvEKAQL 595

                          490
                   ....*....|....*
gi 2017363575  468 SEEIEKLRQEVDQLK 482
Cdd:pfam15921  596 EKEINDRRLELQEFK 610
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
262-484 3.22e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.23  E-value: 3.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESlhrqELLEVA 341
Cdd:PRK03918   159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEK----EVKELE 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  342 EQKlqqtmrkaETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHnKRLSDTVDRL 421
Cdd:PRK03918   235 ELK--------EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY-IKLSEFYEEY 305

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363575  422 LSESN--ERLQLHLKERMAALEEKntlIQELESSQRQIEEqhhhkgrLSEEIEKLRQEVDQLKGR 484
Cdd:PRK03918   306 LDELReiEKRLSRLEEEINGIEER---IKELEEKEERLEE-------LKKKLKELEKRLEELEER 360
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 37-432 4.55e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 4.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   37 REKLLESLRESQETLAatqsRLQDAIHERD-QLQR-HLNSALPQEFATLTRELSmcREQLLEREEEISELKAERNNTRLL 114
Cdd:TIGR02168  174 RKETERKLERTRENLD----RLEDILNELErQLKSlERQAEKAERYKELKAELR--ELELALLVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  115 LEHLECLVSRHERSLRMTvvkrqaqspsgvSSEVEVLKALKSlfEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:TIGR02168  248 LKEAEEELEELTAELQEL------------EEKLEELRLEVS--ELEEEIEE-LQKELYALANEISRLEQQKQILRERLA 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  195 ALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIkse 274
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA--- 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  275 elsskhqrdlrEALAQKEDMEERITTLEKRylaaqreatsIHDLNDKLENELANKESlHRQELLEVAEQKLQqtmrkaET 354
Cdd:TIGR02168  390 -----------QLELQIASLNNEIERLEAR----------LERLEDRRERLQQEIEE-LLKKLEEAELKELQ------AE 441

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363575  355 LPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLH 432
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 20-430 4.89e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 4.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   20 ADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSmcreqlleREE 99
Cdd:COG1196    406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL--------LEA 477

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  100 EISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHH------KALDEKVRERLR 173
Cdd:COG1196    478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAleaalaAALQNIVVEDDE 557

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  174 AALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPkRLWKEDTGRVEELQELLEKQNFELSQARERLVTLT 253
Cdd:COG1196    558 VAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV-DLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  254 TTVTELEEDLGTARRDLIKSEELSSK---HQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKE 330
Cdd:COG1196    637 RRAVTLAGRLREVTLEGEGGSAGGSLtggSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  331 SLHRQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEK---N----QELARVRQR 403
Cdd:COG1196    717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvNllaiEEYEELEER 796

                          410       420       430
                   ....*....|....*....|....*....|....
gi 2017363575  404 -EKMNEDHN------KRLSDTVDRLLSESNERLQ 430
Cdd:COG1196    797 yDFLSEQREdleearETLEEAIEEIDRETRERFL 830
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
142-483 1.46e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.31  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  142 SGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALqqgagvrdgaaeeegtvelgpkrlw 221
Cdd:PRK03918   224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL------------------------- 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  222 KEDTGRVEELQElLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKS-EELSSKHQRdLREALAQKEDMEERITT 300
Cdd:PRK03918   279 EEKVKELKELKE-KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERiKELEEKEER-LEELKKKLKELEKRLEE 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  301 LEKRYLAAQrEATSIHDLNDKLENELANKESLHRQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER----- 375
Cdd:PRK03918   357 LEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkak 435

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  376 ------HGNIEEHLRqlEGQLEEKNQELARVRQREKMNEDHNKRLSD---TVDRLLSESNERLQLH-LKERMAALEEK-- 443
Cdd:PRK03918   436 gkcpvcGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKelrELEKVLKKESELIKLKeLAEQLKELEEKlk 513

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 2017363575  444 NTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKG 483
Cdd:PRK03918   514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 34-478 1.96e-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: 59.08  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   34 LDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSmcrEQLLEREEEISELKAERNNTRl 113
Cdd:pfam12128  246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWK---EKRDELNGELSAADAAVAKDR- 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  114 llEHLECLVSRHERSLRMTVVKR---QAQSPSgVSSEVEVL-KALKSLFEHHK-------ALDEKVRERLRAALERVT-- 180
Cdd:pfam12128  322 --SELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQdvtakynRRRSKIKEQNNRDIAGIKdk 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  181 ------TLEEQLAGAHQQVSAL------QQGAGVRDGAAEEEGTVE-LGPKRLWKEDTGRVEELQELLEKQNFELSQARE 247
Cdd:pfam12128  399 lakireARDRQLAVAEDDLQALeselreQLEAGKLEFNEEEYRLKSrLGELKLRLNQATATPELLLQLENFDERIERARE 478

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  248 RLVTLTTTVTELEEDLGTARRdliKSEELSSKHQRDLREALAQKEDMEERITTLEKRylaaqrEATSIHDLNDKLEN--- 324
Cdd:pfam12128  479 EQEAANAEVERLQSELRQARK---RRDQASEALRQASRRLEERQSALDELELQLFPQ------AGTLLHFLRKEAPDweq 549

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  325 ---ELANKESLHRQELL-EVAEQKLQQTMR--------KAETLPE-------VEAELAQRIAALTKAEERHGNIEEHLRQ 385
Cdd:pfam12128  550 sigKVISPELLHRTDLDpEVWDGSVGGELNlygvkldlKRIDVPEwaaseeeLRERLDKAEEALQSAREKQAAAEEQLVQ 629

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  386 LEGQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllSESNERLQLHlKERMAALEEKNTLIQELESSQRQIEEQH---- 461
Cdd:pfam12128  630 ANGELEKASREETFARTALKNARLDLRRLFD------EKQSEKDKKN-KALAERKDSANERLNSLEAQLKQLDKKHqawl 702

                          490       500
                   ....*....|....*....|.
gi 2017363575  462 -HHKGRLSE---EIEKLRQEV 478
Cdd:pfam12128  703 eEQKEQKREartEKQAYWQVV 723
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 31-482 2.07e-08

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: 58.58  E-value: 2.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   31 VNMLDEREKLL-ESLRESQETLAATQSRLQDAiheRDQLQRHLNS--ALPQEFATLTRELSMCREQLLEREEE------- 100
Cdd:pfam05483  270 ANQLEEKTKLQdENLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKTICQLTEEKEAQMEElnkakaa 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  101 ----ISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEHHKALDEKvrER 171
Cdd:pfam05483  347 hsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  172 LRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDtgrVEELQELLEKQ---NFELSQARER 248
Cdd:pfam05483  420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE---VEDLKTELEKEklkNIELTAHCDK 496

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  249 LVTLTTTVTELEEDLgtarrdlikSEELSsKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD----------- 317
Cdd:pfam05483  497 LLLENKELTQEASDM---------TLELK-KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqkgdevkc 566

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  318 -LNDKLENELANK-ESLHRQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTK---AEERHGNIEE-HLRQLEGQLE 391
Cdd:pfam05483  567 kLDKSEENARSIEyEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKkgsAENKQLNAYEiKVNKLELELA 646

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  392 EKNQ---ELARVRQRE----KMNEDH-------NKRLSDTVDRLLSESNERLQLHLKErMAALEEK-----NTLIQELES 452
Cdd:pfam05483  647 SAKQkfeEIIDNYQKEiedkKISEEKlleevekAKAIADEAVKLQKEIDKRCQHKIAE-MVALMEKhkhqyDKIIEERDS 725

                          490       500       510
                   ....*....|....*....|....*....|....
gi 2017363575  453 S----QRQIEEQHHHKGRLSEEIEKLRQEVDQLK 482
Cdd:pfam05483  726 ElglyKNKEQEQSSAKAALEIELSNIKAELLSLK 759
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
22-484 2.20e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.54  E-value: 2.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   22 ADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQrhlnsALPQEFATLTRELSMCREQLLEREEEI 101
Cdd:PRK03918   187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-----ELKEEIEELEKELESLEGSKRKLEEKI 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  102 SELKAERNNTRLLLEHLECLVSRHE--RSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRErLRAALERV 179
Cdd:PRK03918   262 RELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERL 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  180 TTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTEL 259
Cdd:PRK03918   341 EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  260 EEDLGTARRDLIKSE--------ELSSKHQRDL-REALAQKEDMEERITTLEKRYLAAQREATsihdlndKLENELANKE 330
Cdd:PRK03918   421 IKELKKAIEELKKAKgkcpvcgrELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLRKELR-------ELEKVLKKES 493

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  331 SLHRqeLLEVAEQ--------------KLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQE 396
Cdd:PRK03918   494 ELIK--LKELAEQlkeleeklkkynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE 571

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  397 LARVRQR----------------EKMNEDHNK--RLSDTVDRL--LSESNERLQLHLKERMAALEEKNTLIQELES---- 452
Cdd:PRK03918   572 LAELLKEleelgfesveeleerlKELEPFYNEylELKDAEKELerEEKELKKLEEELDKAFEELAETEKRLEELRKelee 651

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 2017363575  453 -----SQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 484
Cdd:PRK03918   652 lekkySEEEYEELREEYLELSRELAGLRAELEELEKR 688
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
9-482 2.22e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.24  E-value: 2.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575    9 NEGDRLGPPHGADADANFEQLmvnmlDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLnSALPQEFATLTRELS 88
Cdd:COG4717     53 KEADELFKPQGRKPELNLKEL-----KELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL-EELREELEKLEKLLQ 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   89 mcreqLLEREEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVVKRQAQspsgvssEVEVLKALKSLFEHHKALDEKV 168
Cdd:COG4717    127 -----LLPLYQELEALEAELAELPERLEELE----ERLEELRELEEELEEL-------EAELAELQEELEELLEQLSLAT 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  169 RERLRAALERVTTLEEQLAGAHQQVSALQQgagvRDGAAEEEGTvELGPKRLWKEDTGRVEELQELLEKQNFELSQARER 248
Cdd:COG4717    191 EEELQDLAEELEELQQRLAELEEELEEAQE----ELEELEEELE-QLENELEAAALEERLKEARLLLLIAAALLALLGLG 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  249 LVTLTTTVTEL-----------EEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEeritTLEKRYLAAQREATSIHD 317
Cdd:COG4717    266 GSLLSLILTIAgvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEE----LLAALGLPPDLSPEELLE 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  318 LNDKLEN---ELANKESLHRQELLEVAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEErhgnIEEHLRQLEGQLEEKN 394
Cdd:COG4717    342 LLDRIEElqeLLREAEELEEELQLEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQE----LKEELEELEEQLEELL 415

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  395 QELARVRQREKmNEDHNKRLSDTVDRLLSESNERLQLHlkERMAALEEKntlIQELESSQRqIEEQHHHKGRLSEEIEKL 474
Cdd:COG4717    416 GELEELLEALD-EEELEEELEELEEELEELEEELEELR--EELAELEAE---LEQLEEDGE-LAELLQELEELKAELREL 488


                   ....*...
gi 2017363575  475 RQEVDQLK 482
Cdd:COG4717    489 AEEWAALK 496
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 335-484 3.03e-08

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 55.70  E-value: 3.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  335 QELLEVAE--QKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVrqREKMNE 408
Cdd:COG1579      7 RALLDLQEldSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY--EEQLGN 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  409 DHNKRLSDTVDR---LLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHH-KGRLSEEIEKLRQEVDQLKGR 484
Cdd:COG1579     85 VRNNKEYEALQKeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEkKAELDEELAELEAELEELEAE 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 201-482 3.39e-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: 58.14  E-value: 3.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  201 GVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLvtltttvteleedlgtarrdliksEELsskh 280
Cdd:TIGR02168  659 GVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL------------------------EEL---- 710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKEslhrqELLEVAEQKLQQTmrkAETLPEVEA 360
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE-----AEIEELEERLEEA---EEELAEAEA 782

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  361 ELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesnerlqlhlKERMAAL 440
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL------------EEQIEEL 850

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2017363575  441 EEkntliqELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 482
Cdd:TIGR02168  851 SE------DIESLAAEIEELEELIEELESELEALLNERASLE 886
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 839-905 4.78e-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: 50.76  E-value: 4.78e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363575   839 FAQWDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 905
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 964-1019 9.30e-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: 9.30e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363575   964 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1019
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 267-482 1.04e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  267 RRDLIksEELS--SKHQRDLREALAQKEDMEERITTLE---------KRYLAAQRE-ATSIHDLNDKLEN-ELA----NK 329
Cdd:TIGR02168  157 RRAIF--EEAAgiSKYKERRKETERKLERTRENLDRLEdilnelerqLKSLERQAEkAERYKELKAELRElELAllvlRL 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  330 ESLHRQ-ELLEVAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMN 407
Cdd:TIGR02168  235 EELREElEELQEELKEAEEELEELTAeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  408 EDHNKRLSDTVDRLLSESNErlqlhLKERMAALEEKNTLIQ--------ELESSQRQIEEQHHHKGRLSEEIEKLRQEVD 479
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDE-----LAEELAELEEKLEELKeelesleaELEELEAELEELESRLEELEEQLETLRSKVA 389


                   ...
gi 2017363575  480 QLK 482
Cdd:TIGR02168  390 QLE 392
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 34-482 1.05e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   34 LDEREKLLESLRESQETLAATQSRL-QDAIHERDQLQRHLNSA--LPQEFATLTRELSMCREQLLEREEEISELKAERNN 110
Cdd:COG1196    276 LEELELELEEAQAEEYELLAELARLeQDIARLEERRRELEERLeeLEEELAELEEELEELEEELEELEEELEEAEEELEE 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  111 TRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERvTTLEEQLAGAH 190
Cdd:COG1196    356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL-EELEEALAELE 434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  191 QQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARR-- 268
Cdd:COG1196    435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAal 514

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  269 DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLA--AQREATSIHDLNDKLE--------NELANKESLHRQELL 338
Cdd:COG1196    515 LLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVedDEVAAAAIEYLKAAKAgratflplDKIRARAALAAALAR 594

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  339 EVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSdtv 418
Cdd:COG1196    595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL--- 671

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017363575  419 dRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 482
Cdd:COG1196    672 -AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 264-484 1.66e-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: 1.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  264 GTARRDLIksEELS--SKHQRDLREALAQKEDMEERITTL-----EKR----YLAAQRE-ATSIHDLNDKLEnELANKES 331
Cdd:TIGR02169  152 PVERRKII--DEIAgvAEFDRKKEKALEELEEVEENIERLdliidEKRqqleRLRREREkAERYQALLKEKR-EYEGYEL 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  332 LHRqelLEVAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARvRQREKMNEDHN 411
Cdd:TIGR02169  229 LKE---KEALERQKEAIERQLASL---EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL-RVKEKIGELEA 301

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017363575  412 KRLSdtVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 484
Cdd:TIGR02169  302 EIAS--LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 232-460 1.87e-07

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: 54.77  E-value: 1.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  232 QELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQRE 311
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  312 atsIHDLNDKLENELANKESLHRQELLEV--AEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnieehLRQLEGQ 389
Cdd:COG4942     99 ---LEAQKEELAELLRALYRLGRQPPLALllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALRAE 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363575  390 LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ 460
Cdd:COG4942    169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 35-483 1.95e-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: 55.75  E-value: 1.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   35 DEREKLLeSLRESQETLAATQSRLQDAIHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLL 114
Cdd:TIGR00618  421 DLQGQLA-HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL-QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  115 LEHLECLVsrhERSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKALdEKVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:TIGR00618  499 LQEEPCPL---CGSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSE-EDVYHQLTSERKQRASLKEQMQEIQQSFS 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  195 ALQQ-----GAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQ-------------NFELSQARERLVTLTTTV 256
Cdd:TIGR00618  574 ILTQcdnrsKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQpeqdlqdvrlhlqQCSQELALKLTALHALQL 653

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  257 TELEEDLG-TARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDlNDKLENELANKESLHRQ 335
Cdd:TIGR00618  654 TLTQERVReHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE-YDREFNEIENASSSLGS 732

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  336 EL---LEVAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ---LEEKNQELArvrqrEKMNE 408
Cdd:TIGR00618  733 DLaarEDALNQSLKELMHQARTvLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFnrlREEDTHLLK-----TLEAE 807

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363575  409 DHNKRLSDTVDRLLSEsnERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKG 483
Cdd:TIGR00618  808 IGQEIPSDEDILNLQC--ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
35-482 2.07e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 2.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   35 DEREKLLESLRESQETLAATQSRLQDAIHERDQLqrhlNSALPQefatLTRELSMcreqLLEREEEISELKAERNNTRLL 114
Cdd:PRK03918   179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEI----SSELPE----LREELEK----LEKEVKELEELKEEIEELEKE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  115 LEHLECLVSRHERSLRMTV-----VKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGA 189
Cdd:PRK03918   247 LESLEGSKRKLEEKIRELEerieeLKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  190 HQQVSALQQG-----------AGVRDGAAEEEGTVELG-------------PKRLWKEDTGRVEELQELLEKQNFELSQA 245
Cdd:PRK03918   327 EERIKELEEKeerleelkkklKELEKRLEELEERHELYeeakakkeelerlKKRLTGLTPEKLEKELEELEKAKEEIEEE 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  246 RERLVTLTTTVTELEEDLGTARRDLIKSE--------ELSSKHQRDL-REALAQKEDMEERITTLEKRYLAAQREATsih 316
Cdd:PRK03918   407 ISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLRKELR--- 483

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  317 dlndKLENELANKESLHRqeLLEVAEQ--------------KLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEH 382
Cdd:PRK03918   484 ----ELEKVLKKESELIK--LKELAEQlkeleeklkkynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK 557

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  383 LRQLEGQLEEKNQELARV-RQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERmaaleEKNTLIQELESSQRQIEEQH 461
Cdd:PRK03918   558 LAELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEYLELKDAEK-----ELEREEKELKKLEEELDKAF 632

                          490       500
                   ....*....|....*....|.
gi 2017363575  462 HHKGRLSEEIEKLRQEVDQLK 482
Cdd:PRK03918   633 EELAETEKRLEELRKELEELE 653
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 229-481 2.23e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.46  E-value: 2.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  229 EELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRyLAA 308
Cdd:TIGR02169  691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR-IEE 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  309 QREAtsIHDLNDKLeNELANKESLHRQELLEVAEQKLQQTMRKAE-TLPEVEAELAQRIAALTKAEERHGNIEEHLRQLE 387
Cdd:TIGR02169  770 LEED--LHKLEEAL-NDLEARLSHSRIPEIQAELSKLEEEVSRIEaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  388 GQLEEKNQEL----ARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLhlKERMAALEEKntlIQELESsqrQIEEQHHH 463
Cdd:TIGR02169  847 EQIKSIEKEIenlnGKKEELEEELEELEAALRDLESRLGDLKKERDEL--EAQLRELERK---IEELEA---QIEKKRKR 918

                          250
                   ....*....|....*...
gi 2017363575  464 KGRLSEEIEKLRQEVDQL 481
Cdd:TIGR02169  919 LSELKAKLEALEEELSEI 936
PTZ00121 PTZ00121
MAEBL; Provisional
 159-442 2.85e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 2.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDgaAEEEGTVElgPKRLWKEDTG----RVEELQEL 234
Cdd:PTZ00121  1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK--AEEKKKAE--EAKKAEEDKNmalrKAEEAKKA 1589

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  235 LEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATS 314
Cdd:PTZ00121  1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  315 IHDlnDKLENELANKESLHRQELLEVAEQKLQQTmRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQlEGQLEEKN 394
Cdd:PTZ00121  1670 AEE--DKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK-EAEEDKKK 1745

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2017363575  395 QELARVRQREKmnedhnkrlsDTVDRLLSESNERLQLHLKERMAALEE 442
Cdd:PTZ00121  1746 AEEAKKDEEEK----------KKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
227-486 3.03e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.07  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSK---HQRDLREALAQKEDMEERITTLEK 303
Cdd:PRK03918   187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEieeLEKELESLEGSKRKLEEKIRELEE 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  304 RYlaaqreatsihdlndklenelanKESLHRQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHL 383
Cdd:PRK03918   267 RI-----------------------EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  384 RQLEGQLEEKNQELARVRQREKMNEDHNKRLSDtvdrlLSESNERLQ--LHLKERMAALEEKNTlIQELESSQRQIEEQH 461
Cdd:PRK03918   324 NGIEERIKELEEKEERLEELKKKLKELEKRLEE-----LEERHELYEeaKAKKEELERLKKRLT-GLTPEKLEKELEELE 397

                          250       260
                   ....*....|....*....|....*
gi 2017363575  462 HHKGRLSEEIEKLRQEVDQLKGRGG 486
Cdd:PRK03918   398 KAKEEIEEEISKITARIGELKKEIK 422
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
280-477 3.31e-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: 3.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  280 HQRDLREALAQK----EDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHR--QELLEVAEQKLQqTMRKAE 353
Cdd:COG4913    590 HEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEID-VASAER 668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  354 TLPEVEAELAQRIAA---LTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQ 430
Cdd:COG4913    669 EIAELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2017363575  431 LHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQE 477
Cdd:COG4913    749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 33-478 4.20e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 4.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   33 MLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREEEISELKAERNNTR 112
Cdd:COG1196    230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR-LELEELELELEEAQAEEYELLAELARLEQDIARLE 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  113 LLLEHLEclvsrherslrmtvvKRQAQspsgvssEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQ 192
Cdd:COG1196    309 ERRRELE---------------ERLEE-------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  193 VSALQQGAGVRDGAAEEEGTVELgpkrlwKEDTGRVEELQELLEKQNfELSQARERLVTLTTTVTELEEDLGTARRDLIK 272
Cdd:COG1196    367 LLEAEAELAEAEEELEELAEELL------EALRAAAELAAQLEELEE-AEEALLERLERLEEELEELEEALAELEEEEEE 439

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  273 SEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQELLEVAEQKLQQTMRKA 352
Cdd:COG1196    440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  353 ETLPEVEAELAQRIAALTKAEE-------RHGNIEEHLRQLEGQLEEKNQELARVRqREKMNEDHNKRLSDTVDRLLSES 425
Cdd:COG1196    520 RGLAGAVAVLIGVEAAYEAALEaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRAT-FLPLDKIRARAALAAALARGAIG 598

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2017363575  426 NERLQLHLKERmaALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEV 478
Cdd:COG1196    599 AAVDLVASDLR--EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 272-484 4.26e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 4.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  272 KSEELSSKhqrDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHR--QELLEVAEQKLQQTM 349
Cdd:TIGR02168  218 LKAELREL---ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSelEEEIEELQKELYALA 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  350 RKAETLPEVEAELAQRIAALTKAEERhgnIEEHLRQLEGQLEEKNQELARVRqrEKMNEDHNKRLSdtvdrlLSESNERL 429
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEE---LEAQLEELESKLDELAEELAELE--EKLEELKEELES------LEAELEEL 363

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2017363575  430 QLHLKERMAALEEKNTLIQELESSQRQIEEQhhhKGRLSEEIEKLRQEVDQLKGR 484
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDR 415
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 262-484 5.12e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.30  E-value: 5.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESlhrqELLEVA 341
Cdd:TIGR02169  689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS----ELKELE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  342 EQKLQQTMRKA---ETLPEVEAELAQRI-----AALTKAEERHGNIEEHLRQLEG----------QLEEKNQELARVRQR 403
Cdd:TIGR02169  765 ARIEELEEDLHkleEALNDLEARLSHSRipeiqAELSKLEEEVSRIEARLREIEQklnrltlekeYLEKEIQELQEQRID 844

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  404 EKMNEDHNKRLSDTVDRLLSESNERlqlhLKERMAALEEkntLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKG 483
Cdd:TIGR02169  845 LKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRD---LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917


                   .
gi 2017363575  484 R 484
Cdd:TIGR02169  918 R 918
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 265-460 5.55e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 53.30  E-value: 5.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  265 TARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENEL--ANKESLHRQELLE--- 339
Cdd:COG3883     13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaeAEAEIEERREELGera 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  340 VAEQKLQQTMRKAETLPEVE--AELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDT 417
Cdd:COG3883     93 RALYRSGGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2017363575  418 VDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ 460
Cdd:COG3883    173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 281-477 6.16e-07

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: 53.23  E-value: 6.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHR--QELLEVAEQKLQQTMRKAETLPEV 358
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRalEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  359 EAELAQRIAALTKAEERHGN----------------------IEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSD 416
Cdd:COG4942     99 LEAQKEELAELLRALYRLGRqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363575  417 TVDRlLSESNERLQLHLKERMAALEEKNtliQELESSQRQIEEQHHHKGRLSEEIEKLRQE 477
Cdd:COG4942    179 LLAE-LEEERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAE 235
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
26-484 8.34e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 8.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   26 FEQLMVNMLDER-EKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRElsmcreqllereeeISEL 104
Cdd:COG4913    285 FAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLERE--------------IERL 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  105 KAERNNTRLLLEHLECLVsrheRSLRMTVvkrqaqsPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEE 184
Cdd:COG4913    351 ERELEERERRRARLEALL----AALGLPL-------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  185 QLAGAHQQVSALQQGAGVRDGAAEEEgtvelgpKRLWKEDTG-RVEELQ---ELLE-KQNFELSQ-ARERLvtltttvte 258
Cdd:COG4913    420 ELRELEAEIASLERRKSNIPARLLAL-------RDALAEALGlDEAELPfvgELIEvRPEEERWRgAIERV--------- 483

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  259 leedLGTARRDLIkseeLSSKHQRDLREALAQkEDMEERITTLE-----KRYLAAQREATSI--------HDLNDKLENE 325
Cdd:COG4913    484 ----LGGFALTLL----VPPEHYAAALRWVNR-LHLRGRLVYERvrtglPDPERPRLDPDSLagkldfkpHPFRAWLEAE 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  326 LANK---------ESLHR------------------------------------QELLEVAEQKLQQTMRKAETLPEVEA 360
Cdd:COG4913    555 LGRRfdyvcvdspEELRRhpraitragqvkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLE 634

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  361 ELAQRIAALTKAEERHGNIEEH------LRQLEGQLEEKNQELARvrqrekmnedhnkrlsdtvdrlLSESNERLQlHLK 434
Cdd:COG4913    635 ALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELER----------------------LDASSDDLA-ALE 691

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 2017363575  435 ERMAALEEkntliqELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 484
Cdd:COG4913    692 EQLEELEA------ELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
34-481 1.38e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 52.73  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   34 LDEREKLLESLRESQE---TLAATQSRLQDAIHERDQlqrhlnsalpqEFATLTRELSMCREQLLEREEEISELKAERNN 110
Cdd:PRK02224   236 RDEADEVLEEHEERREeleTLEAEIEDLRETIAETER-----------EREELAEEVRDLRERLEELEEERDDLLAEAGL 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  111 TRL----LLEHLECLVSRHERSLRMTVVKRQAQSpsgvssevEVLKALKSLFEHHKALDEKVRErlraALERVTTLEEQL 186
Cdd:PRK02224   305 DDAdaeaVEARREELEDRDEELRDRLEECRVAAQ--------AHNEEAESLREDADDLEERAEE----LREEAAELESEL 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  187 AGAHQQVSALQ-QGAGVRDGAAEEEGTVELGPkrlwkEDTGRVEELQELLEKqnfELSQARERlvtltttVTELEEDLGT 265
Cdd:PRK02224   373 EEAREAVEDRReEIEELEEEIEELRERFGDAP-----VDLGNAEDFLEELRE---ERDELRER-------EAELEATLRT 437

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  266 ARRDLIKSEEL--------------SSKH------QRDLREAL-AQKEDMEERITTLEKRYlaaqREATSIHDLNDKLEN 324
Cdd:PRK02224   438 ARERVEEAEALleagkcpecgqpveGSPHvetieeDRERVEELeAELEDLEEEVEEVEERL----ERAEDLVEAEDRIER 513

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  325 ELANKESLhrQELLEVAEQKLQQTMRKAETL----PEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARV 400
Cdd:PRK02224   514 LEERREDL--EELIAERRETIEEKRERAEELreraAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL 591

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  401 RQ-REKMNEDHNKRlsDTVDRlLSESNERLQLHLKERMAALEEKNTLIQELESS--QRQIEEQHHHKGRLSEEIEKLRQE 477
Cdd:PRK02224   592 ERiRTLLAAIADAE--DEIER-LREKREALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEK 668


                   ....
gi 2017363575  478 VDQL 481
Cdd:PRK02224   669 LDEL 672
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 284-442 1.59e-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: 50.69  E-value: 1.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  284 LREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQelLEVAEQKLQQTMRKAETLPEVEAeLA 363
Cdd:COG1579     19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE--VEARIKKYEEQLGNVRNNKEYEA-LQ 95

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363575  364 QRIAALtkaEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEE 442
Cdd:COG1579     96 KEIESL---KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
149-403 1.60e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 1.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  149 EVLKALKSLFEHHKALDEkVRERLRAALERVTTLEeQLAGAHQQVSALQQGAGVRDGAAEeegtvelgPKRLWKEDTgRV 228
Cdd:COG4913    222 DTFEAADALVEHFDDLER-AHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRA--------ALRLWFAQR-RL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  229 EELQELLEKQNFELSQARERLVTLtttvteleedlgTARRDLIKSEELSSKHQRDlREALAQKEDMEERITTLEKRYLAA 308
Cdd:COG4913    291 ELLEAELEELRAELARLEAELERL------------EARLDALREELDELEAQIR-GNGGDRLEQLEREIERLERELEER 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  309 QREATSIHDLNDKLENELAnkesLHRQELLEVAEqklqQTMRKAETLPEVEAELAQRIAALTKAeerhgnieehLRQLEG 388
Cdd:COG4913    358 ERRRARLEALLAALGLPLP----ASAEEFAALRA----EAAALLEALEEELEALEEALAEAEAA----------LRDLRR 419

                          250
                   ....*....|....*
gi 2017363575  389 QLEEKNQELARVRQR 403
Cdd:COG4913    420 ELRELEAEIASLERR 434
mukB PRK04863
chromosome partition protein MukB;
123-484 1.68e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 52.65  E-value: 1.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  123 SRHERSLRMTVVKRqaqspsgVSSEVEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEE--QLAGAHQQ--VSAL-Q 197
Cdd:PRK04863   275 MRHANERRVHLEEA-------LELRRELYTSRRQLAAEQYRLVEMARE-LAELNEAESDLEQdyQAASDHLNlvQTALrQ 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  198 QGAGVRdgaAEEEgtvelgpkrlwkedtgrVEELQELLEKQNFELSQARERlvtltttvteleedlgtarrdLIKSEELS 277
Cdd:PRK04863   347 QEKIER---YQAD-----------------LEELEERLEEQNEVVEEADEQ---------------------QEENEARA 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  278 SKHQRDLREALAQKEDMEERITTLEKRYLAAQ------REATSIHDLND-KLEN------ELANKESLHRQELLEvAEQK 344
Cdd:PRK04863   386 EAAEEEVDELKSQLADYQQALDVQQTRAIQYQqavqalERAKQLCGLPDlTADNaedwleEFQAKEQEATEELLS-LEQK 464

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  345 LQQTmRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLE------GQLEEKNQELARVRQREkmnedhnkRLSDTV 418
Cdd:PRK04863   465 LSVA-QAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLReqrhlaEQLQQLRMRLSELEQRL--------RQQQRA 535

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363575  419 DRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 484
Cdd:PRK04863   536 ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR 601
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
34-475 2.31e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 2.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   34 LDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS---------ALPQEFATLTRELSMCREQLLEREEEISEL 104
Cdd:PRK03918   240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkelkEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  105 KAERNNTRLLLEHLECLVSR-HERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD-----EKVRERLRAALER 178
Cdd:PRK03918   320 EEEINGIEERIKELEEKEERlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKA 399

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  179 VTTLEEQLAGAHQQVSALQQGAGVRDGAAEE----EGTVELGPKRLWKEDTGRV-EELQELLEKQNFELSQARERLVTLT 253
Cdd:PRK03918   400 KEEIEEEISKITARIGELKKEIKELKKAIEElkkaKGKCPVCGRELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLR 479

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  254 TTVTELEEDLGTARR--------DLIKS--EELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK-- 321
Cdd:PRK03918   480 KELRELEKVLKKESEliklkelaEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKla 559

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  322 -LENELANKES----LHRQ---------ELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLE 387
Cdd:PRK03918   560 eLEKKLDELEEelaeLLKEleelgfesvEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETE 639

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  388 GQLEEKNQELARVRQreKMNEDHNKRLSDTVDRL------LSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQH 461
Cdd:PRK03918   640 KRLEELRKELEELEK--KYSEEEYEELREEYLELsrelagLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717

                          490
                   ....*....|....
gi 2017363575  462 HHKGRLSEEIEKLR 475
Cdd:PRK03918   718 KALERVEELREKVK 731
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
42-476 2.53e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.96  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   42 ESLRESQETLAATQSRLQDAIHE-RDQLQRHLNSA----------------LPQEFATLTRELSMCREQLLEREEEISEL 104
Cdd:PRK02224   310 EAVEARREELEDRDEELRDRLEEcRVAAQAHNEEAeslredaddleeraeeLREEAAELESELEEAREAVEDRREEIEEL 389

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  105 KAERNNTRL-----------LLEHLECLVSRHERslrmtVVKRQAQSPSGVSSEVEVLKALKSLFEHHKA-------LDE 166
Cdd:PRK02224   390 EEEIEELRErfgdapvdlgnAEDFLEELREERDE-----LREREAELEATLRTARERVEEAEALLEAGKCpecgqpvEGS 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  167 KVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvRDGAAEEEGTVELGPKRLwKEdtgRVEELQELLEKQNFELSQAR 246
Cdd:PRK02224   465 PHVETIEEDRERVEELEAELEDLEEEVEEVEE----RLERAEDLVEAEDRIERL-EE---RREDLEELIAERRETIEEKR 536

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  247 ERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKrylaaqreatsIHDLNDKLENEL 326
Cdd:PRK02224   537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-----------IRTLLAAIADAE 605

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  327 ANKESLH--RQELLEVAEQKLQQTMRKAETLPEVEAELAQriAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRE 404
Cdd:PRK02224   606 DEIERLRekREALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363575  405 KMNEDHNKRLSDtvdrllsesnerlqlhLKERMAALEEKntlIQELESSQRQIEEQHHHKGRLSEEiekLRQ 476
Cdd:PRK02224   684 GAVENELEELEE----------------LRERREALENR---VEALEALYDEAEELESMYGDLRAE---LRQ 733
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 281-482 2.88e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 2.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKEslhrqELLEVAEQKLQQTMRKAEtlpEVEA 360
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE-----QQKQILRERLANLERQLE---ELEA 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  361 ELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAAL 440
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ-----LELQIASL 398

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2017363575  441 EEKntlIQELESsqrQIEEQHHHKGRLSEEIEKLRQEVDQLK 482
Cdd:TIGR02168  399 NNE---IERLEA---RLERLEDRRERLQQEIEELLKKLEEAE 434
PTZ00121 PTZ00121
MAEBL; Provisional
 135-482 3.32e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 3.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  135 KRQAQSPSGVSSEVEVLKALKSLFEHHKALDE--KVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGT 212
Cdd:PTZ00121  1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK 1496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  213 VELGPKRLWKEDTGRVEELQELLEKQNF-ELSQARERLVTLTTTVTELEEDLGTARrdliKSEELssKHQRDLREALAQK 291
Cdd:PTZ00121  1497 KKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEEKKKADELK----KAEEL--KKAEEKKKAEEAK 1570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  292 EDMEERITTLEKRYLAAQREATSIHDLNDKLENELANK-ESLHRQELLEV-AEQ--KLQQTMRKAETLPEVEAELAQRIA 367
Cdd:PTZ00121  1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEAKIkAEElkKAEEEKKKVEQLKKKEAEEKKKAE 1650

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  368 ALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSD---TVDRLLSESNErlQLHLKERMAALEEKN 444
Cdd:PTZ00121  1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeakKAEELKKKEAE--EKKKAEELKKAEEEN 1728

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2017363575  445 TLiqELESSQRQIEEQHHHKGRLSEEiEKLRQEVDQLK 482
Cdd:PTZ00121  1729 KI--KAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLK 1763
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
367-484 4.27e-06

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 49.05  E-value: 4.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  367 AALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesNERLQLHLK---ERMA--ALE 441
Cdd:COG1842     16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreALE 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2017363575  442 EKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 484
Cdd:COG1842     92 RKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1042-1113 7.80e-06

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 44.59  E-value: 7.80e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363575  1042 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHntlalILQIPTQNTQARQVMEREFNNLLA 1113
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEED-----LKELGITKLGHRKKILKAIQKLKE 67
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 964-1015 8.62e-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: 8.62e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2017363575  964 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1015
Cdd:cd09487      4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1042-1112 1.15e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 44.18  E-value: 1.15e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363575 1042 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALdeNFDHNTLAlilQIPTQNTQARQVMEREFNNLL 1112
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 229-406 1.50e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 47.61  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  229 EELQELLEKQNF--ELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRyl 306
Cdd:COG1579      4 EDLRALLDLQELdsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  307 aaQREATSIHDLNDkLENELankESLHRQelLEVAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERhgnIEEHLRQL 386
Cdd:COG1579     82 --LGNVRNNKEYEA-LQKEI---ESLKRR--ISDLEDEILELMERIEEL---EEELAELEAELAELEAE---LEEKKAEL 147

                          170       180
                   ....*....|....*....|.
gi 2017363575  387 EGQLEEKNQELARVR-QREKM 406
Cdd:COG1579    148 DEELAELEAELEELEaEREEL 168
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
135-485 2.13e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  135 KRQAQSPSGVSSEVEVL-KALKSLFEHHKALDEKvRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTv 213
Cdd:COG4717     60 KPQGRKPELNLKELKELeEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL- 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  214 elgpKRLWKEDTGRVEELQELLEkqnfELSQARERLVTLTTTVTELEEDLGTARRDLikseelSSKHQRDLREALAQKED 293
Cdd:COG4717    138 ----EAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQL------SLATEEELQDLAEELEE 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQE------------------------------------- 336
Cdd:COG4717    204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKearlllliaaallallglggsllsliltiagvlflvl 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  337 --------LLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE-----------EHLRQLEGQLEEKNQEL 397
Cdd:COG4717    284 gllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeellelldriEELQELLREAEELEEEL 363

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  398 ARVRQREKMNEDHNKRLSDTVDRL----------------LSESNERLQLHLKERMAALE--EKNTLIQELESSQRQIEE 459
Cdd:COG4717    364 QLEELEQEIAALLAEAGVEDEEELraaleqaeeyqelkeeLEELEEQLEELLGELEELLEalDEEELEEELEELEEELEE 443

                          410       420
                   ....*....|....*....|....*.
gi 2017363575  460 QHHHKGRLSEEIEKLRQEVDQLKGRG 485
Cdd:COG4717    444 LEEELEELREELAELEAELEQLEEDG 469
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 295-482 3.75e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.09  E-value: 3.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  295 EERITTLEKRYLAAQREATSIHDLNDKLENELANKeslhrQELLEVAEQKLQQTMrkaETLPEVEAELAQRIAALTKAEE 374
Cdd:TIGR04523  210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK-----TTEISNTQTQLNQLK---DEQNKIKKQLSEKQKELEQNNK 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  375 RHGNIEEHLRQLEGQLE----EKNQELAR-----VRQREKMNEDHNKRLSDTvDRLLSESNERLQLHLKERMAALEEKNT 445
Cdd:TIGR04523  282 KIKELEKQLNQLKSEISdlnnQKEQDWNKelkseLKNQEKKLEEIQNQISQN-NKIISQLNEQISQLKKELTNSESENSE 360

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2017363575  446 LIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 482
Cdd:TIGR04523  361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 266-485 3.91e-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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 48.04  E-value: 3.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  266 ARRDLIKSEELSSKHQRDLREALAQKED-MEERITTLEKRYLAAQREATsihdlndkLENELANKESLHRQELLEVAEQK 344
Cdd:pfam02463  174 ALKKLIEETENLAELIIDLEELKLQELKlKEQAKKALEYYQLKEKLELE--------EEYLLYLDYLKLNEERIDLLQEL 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  345 L---QQTMRKAETLPEVEAELAQRIAALTKAEER-HGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDhnkrlsdtVDR 420
Cdd:pfam02463  246 LrdeQEEIESSKQEIEKEEEKLAQVLKENKEEEKeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE--------KLK 317

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363575  421 LLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGRG 485
Cdd:pfam02463  318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
PTZ00121 PTZ00121
MAEBL; Provisional
 153-484 3.93e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 3.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  153 ALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLwKEDTGRVEELQ 232
Cdd:PTZ00121  1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA-EEDKKKADELK 1411

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  233 elleKQNFELSQARErlVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREA 312
Cdd:PTZ00121  1412 ----KAAAAKKKADE--AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  313 tsiHDLNDKLENELANKESLHRQEllevAEQKLQQTMRKAETLPEVE----AELAQRIAALTKAEERHGniEEHLRQLEG 388
Cdd:PTZ00121  1486 ---DEAKKKAEEAKKKADEAKKAA----EAKKKADEAKKAEEAKKADeakkAEEAKKADEAKKAEEKKK--ADELKKAEE 1556

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  389 QleEKNQELARVRQREKMNEDHNKRLsdtvdRLLSESNERLQLHLKERMAALEEKntliQELESSQRQIEEQHHHKGRLS 468
Cdd:PTZ00121  1557 L--KKAEEKKKAEEAKKAEEDKNMAL-----RKAEEAKKAEEARIEEVMKLYEEE----KKMKAEEAKKAEEAKIKAEEL 1625

                          330
                   ....*....|....*.
gi 2017363575  469 EEIEKLRQEVDQLKGR 484
Cdd:PTZ00121  1626 KKAEEEKKKVEQLKKK 1641
PTZ00121 PTZ00121
MAEBL; Provisional
 154-413 4.24e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 4.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  154 LKSLFEHHKALDEKVRERLRAAlERVTTLEEQLAGAHQQVSALQQGAGVRDGaaeEEGTVELGPKRLWKEDTGRVEELQE 233
Cdd:PTZ00121  1539 AKKAEEKKKADELKKAEELKKA-EEKKKAEEAKKAEEDKNMALRKAEEAKKA---EEARIEEVMKLYEEEKKMKAEEAKK 1614

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  234 LLEKQNF--ELSQARERLVTLTTTVTELEEDLGTARR-------DLIKSEELSSKHQRDLREAL-AQKEDMEERitTLEK 303
Cdd:PTZ00121  1615 AEEAKIKaeELKKAEEEKKKVEQLKKKEAEEKKKAEElkkaeeeNKIKAAEEAKKAEEDKKKAEeAKKAEEDEK--KAAE 1692

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  304 RYLAAQREATSIHDLNDKLENELANKESLHRQEllEVAEQKLQQTMRKAEtlpeveaELAQRIAALTKAEERHGNIEEHL 383
Cdd:PTZ00121  1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE--EENKIKAEEAKKEAE-------EDKKKAEEAKKDEEEKKKIAHLK 1763

                          250       260       270
                   ....*....|....*....|....*....|
gi 2017363575  384 RQLEGQLEEKNQELARVRQrEKMNEDHNKR 413
Cdd:PTZ00121  1764 KEEEKKAEEIRKEKEAVIE-EELDEEDEKR 1792
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 135-475 4.79e-05

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: 47.44  E-value: 4.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  135 KRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRdgAAEEEgtV 213
Cdd:pfam09731   88 QVKIPRQSGVSSEVaEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQ--AVKAH--T 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  214 ELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSeelsSKHQRDLREALAQKED 293
Cdd:pfam09731  164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPK----LPEHLDNVEEKVEKAQ 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  294 MEERITTLEKRYLAA-----QREATSIH-DLND------KLENELANKESLHRQELLEVAEQKLQqTMRKAETLpEVEAE 361
Cdd:pfam09731  240 SLAKLVDQYKELVASerivfQQELVSIFpDIIPvlkednLLSNDDLNSLIAHAHREIDQLSKKLA-ELKKREEK-HIERA 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  362 LAQRIAALTKAEER-HGNIEEHLRQLEGQLEEKNQElARVRQREKM-----------NEDHNKRLSDTVDRLLSESNERL 429
Cdd:pfam09731  318 LEKQKEELDKLAEElSARLEEVRAADEAQLRLEFER-EREEIRESYeeklrtelerqAEAHEEHLKDVLVEQEIELQREF 396

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2017363575  430 QLHLKERMAalEEKNTL---IQELESSQRQIEEQhhHKGRLSEEIEKLR 475
Cdd:pfam09731  397 LQDIKEKVE--EERAGRllkLNELLANLKGLEKA--TSSHSEVEDENRK 441
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 32-475 6.16e-05

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: 47.27  E-value: 6.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   32 NMLDEREKLLESLRESQETLAATQsRLQDAIHERDQLQRHLNSALPQEfATLTRELSmcreqllereeEISELKAERNNT 111
Cdd:TIGR00618  223 VLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARI-EELRAQEA-----------VLEETQERINRA 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  112 RllleHLECLVsrhERSLRMTVVKRQAQspsgvssevevlkalkslfEHHKALDEKVRERLRAALERVTTLEEQLAGAHQ 191
Cdd:TIGR00618  290 R----KAAPLA---AHIKAVTQIEQQAQ-------------------RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  192 QVSA---LQQGAGVRDGAAEEEGTVELGPKRlwKEDTGRVEELQELLEKQNfELSQARERLVTLTTTVTELEEDLGTARR 268
Cdd:TIGR00618  344 RRLLqtlHSQEIHIRDAHEVATSIREISCQQ--HTLTQHIHTLQQQKTTLT-QKLQSLCKELDILQREQATIDTRTSAFR 420

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  269 DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHdlnDKLENELANKESLHRQE----------LL 338
Cdd:TIGR00618  421 DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL---KEREQQLQTKEQIHLQEtrkkavvlarLL 497

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  339 EVAEQklQQTMRKAETLPEVEAELAQRIAALT----KAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRL 414
Cdd:TIGR00618  498 ELQEE--PCPLCGSCIHPNPARQDIDNPGPLTrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL 575

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363575  415 SDTVDRLLSESNERLQLhlkermaaLEEKNTLIQELESSQRQI-EEQHHHKGRLSEEIEKLR 475
Cdd:TIGR00618  576 TQCDNRSKEDIPNLQNI--------TVRLQDLTEKLSEAEDMLaCEQHALLRKLQPEQDLQD 629
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
34-431 6.19e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 6.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   34 LDEREKLLESLRESQETLAATQSRLQDAIherDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRL 113
Cdd:COG4717    151 LEERLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  114 LLEHLECLVSRHErslrmtvvkrqaqspsgvssEVEVLKALKSLFehhkaLDEKVRERLRAALERVTTLEEQLAGAHQQV 193
Cdd:COG4717    228 ELEQLENELEAAA--------------------LEERLKEARLLL-----LIAAALLALLGLGGSLLSLILTIAGVLFLV 282

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  194 SALQQGAGVRDGAAEEEGTVELGPKRLWKEDTG-RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLik 272
Cdd:COG4717    283 LGLLALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-- 360

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  273 sEELSSKHQRDLREALAQKEDM--EERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQELLEVAEQKLQQTMR 350
Cdd:COG4717    361 -EELQLEELEQEIAALLAEAGVedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEE 439

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  351 KAETLPEVEAELAQRIAALT------KAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDT-VDRLLS 423
Cdd:COG4717    440 ELEELEEELEELREELAELEaeleqlEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREErLPPVLE 519


                   ....*...
gi 2017363575  424 ESNERLQL 431
Cdd:COG4717    520 RASEYFSR 527
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
166-480 6.82e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 6.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQgagVRDGAAEEEGTVElgpkrlwkedtGRVEELQELLEkqnfelsQA 245
Cdd:COG4913    674 EAELERLDASSDDLAALEEQLEELEAELEELEE---ELDELKGEIGRLE-----------KELEQAEEELD-------EL 732

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  246 RERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDM----EERITTLEKRYLAAQREATSIHDlndk 321
Cdd:COG4913    733 QDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARlnraEEELERAMRAFNREWPAETADLD---- 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  322 lenelANKESLHR-QELLEvaeqKLqqtmrKAETLPEVEAELAQriaALTKAEER-----HGNIEEHLRQLEGQLEEKNQ 395
Cdd:COG4913    809 -----ADLESLPEyLALLD----RL-----EEDGLPEYEERFKE---LLNENSIEfvadlLSKLRRAIREIKERIDPLND 871

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  396 ELARVRqrekMNEDHnkrlsdtvdrllsesneRLQLHLKERmaALEEKNTLIQELESSQRQI-----EEQHHHKGRLSEE 470
Cdd:COG4913    872 SLKRIP----FGPGR-----------------YLRLEARPR--PDPEVREFRQELRAVTSGAslfdeELSEARFAALKRL 928

                          330
                   ....*....|
gi 2017363575  471 IEKLRQEVDQ 480
Cdd:COG4913    929 IERLRSEEEE 938
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 232-473 7.41e-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: 47.04  E-value: 7.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  232 QELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREAlaQKEDMEERITTLEKRYLAAqrE 311
Cdd:pfam17380  298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQEEIAM--E 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  312 ATSIHDLnDKLENELANKESLHRQELLEVAEQKLQQTMRKaETLPEVEAELAQriaalTKAEERHGNiEEHLRQLEgqlE 391
Cdd:pfam17380  374 ISRMREL-ERLQMERQQKNERVRQELEAARKVKILEEERQ-RKIQQQKVEMEQ-----IRAEQEEAR-QREVRRLE---E 442

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  392 EKNQELARVRQREKMNEDHNKRLsdtvdRLLSESNERLQLHL---KERMAALEEKNTLI--QELESSQRQIEEQHHHKGR 466
Cdd:pfam17380  443 ERAREMERVRLEEQERQQQVERL-----RQQEEERKRKKLELekeKRDRKRAEEQRRKIleKELEERKQAMIEEERKRKL 517


                   ....*..
gi 2017363575  467 LSEEIEK 473
Cdd:pfam17380  518 LEKEMEE 524
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 235-477 8.45e-05

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: 46.34  E-value: 8.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  235 LEKQNFELSQARErlvtlttTVTELEEDLGTARRDLIKSEEL-SSKHQRD--LREALAQKEDMEERITTLEKRYLAAQRE 311
Cdd:pfam15905  127 LEKQLLELTRVNE-------LLKAKFSEDGTQKKMSSLSMELmKLRNKLEakMKEVMAKQEGMEGKLQVTQKNLEHSKGK 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  312 ATSIHDLNDKLENElANKESLHRQELLEvaeqklqqtmrkaetlpeveaelaqRIAALTKAEERHGNIEEHLRQLEGQLE 391
Cdd:pfam15905  200 VAQLEEKLVSTEKE-KIEEKSETEKLLE-------------------------YITELSCVSEQVEKYKLDIAQLEELLK 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  392 EKNQELARVRQREKMNEDHnkrLSDTVDRLlsesNERLQL--HLKERMAALEE--KNTLIQELESSQRQIEEQhhhkgrl 467
Cdd:pfam15905  254 EKNDEIESLKQSLEEKEQE---LSKQIKDL----NEKCKLleSEKEELLREYEekEQTLNAELEELKEKLTLE------- 319

                          250
                   ....*....|
gi 2017363575  468 SEEIEKLRQE 477
Cdd:pfam15905  320 EQEHQKLQQK 329
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 290-482 8.93e-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: 8.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  290 QKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKeslhrQELLEVAEQKLQQtmrKAETLPEVEAELA----QR 365
Cdd:TIGR04523  233 NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK-----QKELEQNNKKIKE---LEKQLNQLKSEISdlnnQK 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  366 IAALTKA-EERHGNIEEHLRQLEGQLEEKNQELARVRQ------REKMNEDHNKRlsdTVDRLLSESNERLQLHLKERMA 438
Cdd:TIGR04523  305 EQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEqisqlkKELTNSESENS---EKQRELEEKQNEIEKLKKENQS 381

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363575  439 ALEEKNTL---IQELESS-----------QRQIEEQHHHKGRLSEEIEKLRQEVDQLK 482
Cdd:TIGR04523  382 YKQEIKNLesqINDLESKiqnqeklnqqkDEQIKKLQQEKELLEKEIERLKETIIKNN 439
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 274-482 9.16e-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: 9.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  274 EELSSKHQRDLREALAQKE---DMEERITTLEKRY--LAAQREA---------TSIHDLNDKLEN---ELANKEslhrQE 336
Cdd:TIGR04523  422 ELLEKEIERLKETIIKNNSeikDLTNQDSVKELIIknLDNTRESletqlkvlsRSINKIKQNLEQkqkELKSKE----KE 497

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  337 LLEVAEQKlQQTMRKAETLPEVEAELAQRIAALTKAEERhgnIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNK--RL 414
Cdd:TIGR04523  498 LKKLNEEK-KELEEKVKDLTKKISSLKEKIEKLESEKKE---KESKISDLEDELNKDDFELKKENLEKEIDEKNKEieEL 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  415 SDTVDRLLSeSNERLQLHLKERMA-------ALEEKNTLIQELESSQRQIEEQHHhkgRLSEEI-------EKLRQEVDQ 480
Cdd:TIGR04523  574 KQTQKSLKK-KQEEKQELIDQKEKekkdlikEIEEKEKKISSLEKELEKAKKENE---KLSSIIknikskkNKLKQEVKQ 649


                   ..
gi 2017363575  481 LK 482
Cdd:TIGR04523  650 IK 651
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
318-484 1.09e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  318 LNDKLENELAN--KESLHRQELLEVAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQ 395
Cdd:COG4717     47 LLERLEKEADElfKPQGRKPELNLKELKELEEELKEAE---EKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  396 ELARVRQREKMnEDHNKRLSDTVDRLlsesnERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ--------HHHKGRL 467
Cdd:COG4717    124 LLQLLPLYQEL-EALEAELAELPERL-----EELEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQDL 197

                          170
                   ....*....|....*..
gi 2017363575  468 SEEIEKLRQEVDQLKGR 484
Cdd:COG4717    198 AEELEELQQRLAELEEE 214
PRK12704 PRK12704
phosphodiesterase; Provisional
 302-460 2.04e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  302 EKRYLAAQREATSIhdlndkLENELANKESLHRQELLEVAEQKLQQTMrkaetlpEVEAELAQRIAALTKAEERHGNIEE 381
Cdd:PRK12704    30 EAKIKEAEEEAKRI------LEEAKKEAEAIKKEALLEAKEEIHKLRN-------EFEKELRERRNELQKLEKRLLQKEE 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  382 HL-------RQLEGQLEEKNQELARvrqrekmNEDHNKRLSDTVDRLLSESNERLqlhlkERMAAL---EEKNTLIQELE 451
Cdd:PRK12704    97 NLdrklellEKREEELEKKEKELEQ-------KQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE 164

                          170
                   ....*....|....*..
gi 2017363575  452 SSQR--------QIEEQ 460
Cdd:PRK12704   165 EEARheaavlikEIEEE 181
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
169-403 2.31e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  169 RERLRAAL----ERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVElgpkrlwkedtgRVEELQELLEKQNFELSQ 244
Cdd:COG3206    170 REEARKALefleEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQ------------QLSELESQLAEARAELAE 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  245 ARERLVTLTTTVteleedlgtARRDLIKSEELSSKHQRDLREALAQkedMEERITTLEKRYLAAQREATSihdlndkLEN 324
Cdd:COG3206    238 AEARLAALRAQL---------GSGPDALPELLQSPVIQQLRAQLAE---LEAELAELSARYTPNHPDVIA-------LRA 298

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363575  325 ELANKESLHRQEllevAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR 403
Cdd:COG3206    299 QIAALRAQLQQE----AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQR 373
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 272-482 2.36e-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: 45.40  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  272 KSEELSSKhQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHrqELLEVAEQKLQQTMRK 351
Cdd:TIGR04523  361 KQRELEEK-QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK--ELLEKEIERLKETIIK 437

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  352 AETlpEVEaELAQRIAALTKAEERHGNIEEHLRQ----LEGQ-------LEEKNQELARVRQREKMNEDHNKRLSDTVDR 420
Cdd:TIGR04523  438 NNS--EIK-DLTNQDSVKELIIKNLDNTRESLETqlkvLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  421 LLSESNErlqlhLKERMAALE----EKNTLIQELES--------------------SQRQIEEQHHHKGRLSEEIEKLRQ 476
Cdd:TIGR04523  515 LTKKISS-----LKEKIEKLEsekkEKESKISDLEDelnkddfelkkenlekeideKNKEIEELKQTQKSLKKKQEEKQE 589


                   ....*.
gi 2017363575  477 EVDQLK 482
Cdd:TIGR04523  590 LIDQKE 595
PRK01156 PRK01156
chromosome segregation protein; Provisional
 283-430 3.25e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.89  E-value: 3.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQELLEVAEQKLQ-QTMR-KAETLPEVEA 360
Cdd:PRK01156   581 DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILiEKLRgKIDNYKKQIA 660

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  361 ELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVdrllSESNERLQ 430
Cdd:PRK01156   661 EIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETLE 726
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 222-481 4.29e-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: 44.56  E-value: 4.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  222 KEDTGRVEELQELLEKQNFELS-QARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRdlREALAQKEDMEERITT 300
Cdd:COG5185    274 AESSKRLNENANNLIKQFENTKeKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETE--TGIQNLTAEIEQGQES 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  301 LEKRYLAAQREATSIHDLNDKLENElANKESLHRQelLEVAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERhgNIE 380
Cdd:COG5185    352 LTENLEAIKEEIENIVGEVELSKSS-EELDSFKDT--IESTKESLDEIPQNQR---GYAQEILATLEDTLKAADR--QIE 423

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  381 EHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ 460
Cdd:COG5185    424 ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEK 503

                          250       260
                   ....*....|....*....|.
gi 2017363575  461 hhHKGRLSEEIEKLRQEVDQL 481
Cdd:COG5185    504 --LRAKLERQLEGVRSKLDQV 522
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 30-406 4.91e-04

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: 43.90  E-value: 4.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   30 MVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS------ALPQEFATLTRELSmcreqllereeeisE 103
Cdd:pfam19220   15 MADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQeraaygKLRRELAGLTRRLS--------------A 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  104 LKAERNNTRLLLEHLECLVSRHER---SLRMTVVKRQAQSPS---GVSSEVEVLKALKslfEHHKALdekvRERLRAALE 177
Cdd:pfam19220   81 AEGELEELVARLAKLEAALREAEAakeELRIELRDKTAQAEAlerQLAAETEQNRALE---EENKAL----REEAQAAEK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  178 RVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEG--TVELGpkRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTT 255
Cdd:pfam19220  154 ALQRAEGELATARERLALLEQENRRLQALSEEQAaeLAELT--RRLAELETQLDATRARLRALEGQLAAEQAERERAEAQ 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  256 VTELEEDLGTARRDL-IKSEELSSKH---QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELAnkes 331
Cdd:pfam19220  232 LEEAVEAHRAERASLrMKLEALTARAaatEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLE---- 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  332 lHRQELLEVAEQKLQQTMRKAETLPEVeaeLAQRIAALTKAEERHGNIEEHLRQLEGQ-------LEEKNQELARVRQRE 404
Cdd:pfam19220  308 -RRTQQFQEMQRARAELEERAEMLTKA---LAAKDAALERAEERIASLSDRIAELTKRfeveraaLEQANRRLKEELQRE 383


                   ..
gi 2017363575  405 KM 406
Cdd:pfam19220  384 RA 385
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
267-482 5.21e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.36  E-value: 5.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  267 RRDLI-KSEELSSKhqrdLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQ-ELLEVAEQK 344
Cdd:COG1340     45 RDELNaQVKELREE----AQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSiDKLRKEIER 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  345 LQQTMRKAETLPEVEAELAQRIAALTK-AEERhgnieEHLRQLEGQLEEKNQELARVRQREkmnEDHNKRLSDTVDRLLS 423
Cdd:COG1340    121 LEWRQQTEVLSPEEEKELVEKIKELEKeLEKA-----KKALEKNEKLKELRAELKELRKEA---EEIHKKIKELAEEAQE 192

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363575  424 ESNERLQLhLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 482
Cdd:COG1340    193 LHEEMIEL-YKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLR 250
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 286-484 6.43e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.19  E-value: 6.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  286 EALAQKEDMEERITTLEKRY----LAAQREATSIHDLNDKLENELANKESLHRQEllEVAEQKLQQTMRKAETLPEVEAE 361
Cdd:TIGR00618  184 MEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQT--QQSHAYLTQKREAQEEQLKKQQL 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  362 LAQRIAAltkaeerhgniEEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDtVDRLLSESNERLQlhlkERMAALE 441
Cdd:TIGR00618  262 LKQLRAR-----------IEELRAQEAVLEETQERINRARKAAPLAA-HIKAVTQ-IEQQAQRIHTELQ----SKMRSRA 324

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2017363575  442 EKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 484
Cdd:TIGR00618  325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 842-900 6.72e-04

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 39.24  E-value: 6.72e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363575  842 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNALHRLKLRL 900
Cdd:cd09504      5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 136-481 6.85e-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: 44.01  E-value: 6.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  136 RQAQSPSGVSSEVEVLKALKSLFEHHKAL----------DEKVRERLRAALERV----TTLEEQLAGAHQQVSALQQGAG 201
Cdd:pfam01576  160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMisdleerlkkEEKGRQELEKAKRKLegesTDLQEQIAELQAQIAELRAQLA 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  202 VRD-------GAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNfelsQARERLVTLTTTVTELEEDLGTARRDLIKS- 273
Cdd:pfam01576  240 KKEeelqaalARLEEETAQKNNALKKIRELEAQISELQEDLESER----AARNKAEKQRRDLGEELEALKTELEDTLDTt 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  274 ---EELSSKHQRDLREAlaqKEDMEERITTLEKRYLA-AQREATSIHDLNDKLENELANKESL----------------- 332
Cdd:pfam01576  316 aaqQELRSKREQEVTEL---KKALEEETRSHEAQLQEmRQKHTQALEELTEQLEQAKRNKANLekakqalesenaelqae 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  333 ------------HRQELLEVAEQKLQ--------QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQL-- 390
Cdd:pfam01576  393 lrtlqqakqdseHKRKKLEGQLQELQarlseserQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLqd 472

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  391 ------EEKNQELA---RVRQ--------REKMNEDHNKRLS-----DTVDRLLSESNERLQLHLKERMAALEEKNTLIQ 448
Cdd:pfam01576  473 tqellqEETRQKLNlstRLRQledernslQEQLEEEEEAKRNverqlSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQR 552

                          410       420       430
                   ....*....|....*....|....*....|...
gi 2017363575  449 ELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQL 481
Cdd:pfam01576  553 ELEALTQQLEEKAAAYDKLEKTKNRLQQELDDL 585
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 13-477 7.09e-04

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: 44.06  E-value: 7.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   13 RLGPPHGADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSMCRE 92
Cdd:pfam12128  445 RLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE 524

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   93 QLLEREEEISELKA-ERNNTRLLLEHLECLVSR---HERSLRMTVVKRQAQSPS---GVSSEVEVLKALKSLFeHHKALD 165
Cdd:pfam12128  525 LELQLFPQAGTLLHfLRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELnlyGVKLDLKRIDVPEWAA-SEEELR 603

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  166 E---KVRERLRAALERVTTLEEQLAGAHQQVSALQqgAGVRDGAAEEEGTvELGPKRLWKEDTGRVEELQELLEKQNFEL 242
Cdd:pfam12128  604 ErldKAEEALQSAREKQAAAEEQLVQANGELEKAS--REETFARTALKNA-RLDLRRLFDEKQSEKDKKNKALAERKDSA 680

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  243 SQARERLVTLTTTVTELEEDLGTARRDliKSEELSSKHQRDLREALAQKEDMEERI-TTLEKRYLAAQREATSIHDLND- 320
Cdd:pfam12128  681 NERLNSLEAQLKQLDKKHQAWLEEQKE--QKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWYKr 758

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  321 -------------KLENELANKE------SLHRQELLE----VAEQKLQQTMRKAETLPEVEA---ELAQRIAALTK-AE 373
Cdd:pfam12128  759 dlaslgvdpdviaKLKREIRTLErkieriAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERaisELQQQLARLIAdTK 838

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  374 ERHGNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHnkrlsdtvdrlLSESNERLQLHLKERMAALEE-KNTLIQELE 451
Cdd:pfam12128  839 LRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGERLAQLEDlKLKRDYLSE 907

                          490       500       510
                   ....*....|....*....|....*....|.
gi 2017363575  452 SSQRQIEE-----QHHHKGRLSEEIEKLRQE 477
Cdd:pfam12128  908 SVKKYVEHfknviADHSGSGLAETWESLREE 938
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 283-484 8.65e-04

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: 43.52  E-value: 8.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKES------------LHRQELLEVAEQKLQQ--T 348
Cdd:pfam05622    1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESgddsgtpggkkyLLLQKQLEQLQEENFRleT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  349 MR-----KAETLPEVEAELAQRIAALTKAeerhgniEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVD---- 419
Cdd:pfam05622   81 ARddyriKCEELEKEVLELQHRNEELTSL-------AEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDlrrq 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017363575  420 -RLLSESNerlqLHLKERMAALEEK----NTLIQELESSQRQIEEQHHhkgRLSEEI---EKLRQEVDQLKGR 484
Cdd:pfam05622  154 vKLLEERN----AEYMQRTLQLEEElkkaNALRGQLETYKRQVQELHG---KLSEESkkaDKLEFEYKKLEEK 219
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
379-482 9.17e-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: 9.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  379 IEEHLRQLEGQLEEKNQELARVRQREK-MNEDHNKRLSDTVDRLLSEsNERLQLHLKERMAALEEkntLIQELESSQRQI 457
Cdd:COG2433    382 LEELIEKELPEEEPEAEREKEHEERELtEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---LERELSEARSEE 457

                           90       100
                   ....*....|....*....|....*
gi 2017363575  458 EEQHhhkgRLSEEIEKLRQEVDQLK 482
Cdd:COG2433    458 RREI----RKDREISRLDREIERLE 478
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 104-484 9.47e-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: 43.27  E-value: 9.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  104 LKAERNNTRLLLEHLECLVSRHERSLRmtvvkRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLraaLERVTTLE 183
Cdd:pfam10174  343 LQTEVDALRLRLEEKESFLNKKTKQLQ-----DLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENL---QEQLRDKD 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  184 EQLAGAHQQVSALQQGAGVRDGA--------AEEEGTVELGPKRLWKEDTGRVEELqELLEKQNFELSQARERLVTLTTT 255
Cdd:pfam10174  415 KQLAGLKERVKSLQTDSSNTDTAlttleealSEKERIIERLKEQREREDRERLEEL-ESLKKENKDLKEKVSALQPELTE 493

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  256 VTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEdmeERITTLEKRYLAAQREAtsihdlndklENELANKESLHRQ 335
Cdd:pfam10174  494 KESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKK---EECSKLENQLKKAHNAE----------EAVRTNPEINDRI 560

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  336 ELLEvaeqklQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRls 415
Cdd:pfam10174  561 RLLE------QEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK-- 632

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363575  416 dtvdrllsESNERLQLHLKERMAALEEkntliqeleSSQRQIEEqhhhkgrLSEEIEKLRQEVDQLKGR 484
Cdd:pfam10174  633 --------KGAQLLEEARRREDNLADN---------SQQLQLEE-------LMGALEKTRQELDATKAR 677
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 165-469 1.02e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.50  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  165 DEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEgtvelgpkRLWKEDTGRVEELQELLEKQNFELSQ 244
Cdd:TIGR00606  790 DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ--------HELDTVVSKIELNRKLIQDQQEQIQH 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  245 ARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN 324
Cdd:TIGR00606  862 LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  325 ELAN-KESL-----HRQELlevaEQKLQQTmrKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQE-- 396
Cdd:TIGR00606  942 KVNDiKEKVknihgYMKDI----ENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQer 1015

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  397 -----LARVRQREKMNEdhnkrLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELES----SQRQIEEQ-HHHKGR 466
Cdd:TIGR00606 1016 wlqdnLTLRKRENELKE-----VEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVlalgRQKGYEKEiKHFKKE 1090


                   ...
gi 2017363575  467 LSE 469
Cdd:TIGR00606 1091 LRE 1093
RNase_Y_N pfam12072
RNase Y N-terminal region;
302-479 1.12e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 41.41  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  302 EKRYLAAQREATSIhdlndkLENELANKESLHRQELLEVAEQKLQQtmrKAEtlpeVEAELAQRIAALTKAEERHGNIEE 381
Cdd:pfam12072   26 EAKIGSAEELAKRI------IEEAKKEAETKKKEALLEAKEEIHKL---RAE----AERELKERRNELQRQERRLLQKEE 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  382 HLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLqlhlkERMAAL---EEKNTLIQELEssqrqiE 458
Cdd:pfam12072   93 TLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------E 161

                          170       180
                   ....*....|....*....|..
gi 2017363575  459 EQHHHKGRLSEEIE-KLRQEVD 479
Cdd:pfam12072  162 ELRHEAAVMIKEIEeEAKEEAD 183
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 353-484 1.36e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  353 ETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNE----- 427
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaei 763

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363575  428 -----RLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 484
Cdd:TIGR02168  764 eeleeRLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 281-484 1.51e-03

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.28  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  281 QRDLREALAQKEDMEERITTLEKRylaaqREATSIHDLNDKLEnelankeslHRQELLEVAEQKLQQTMRKAETLPEVEA 360
Cdd:cd00176      6 LRDADELEAWLSEKEELLSSTDYG-----DDLESVEALLKKHE---------ALEAELAAHEERVEALNELGEQLIEEGH 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  361 ELAQRIaaltkaEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDH---NKRLSDTVDRLLSESN-------ERLQ 430
Cdd:cd00176     72 PDAEEI------QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELL 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363575  431 LHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGR--LSEEIEKLRQEVDQLKGR 484
Cdd:cd00176    146 KKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeeIEEKLEELNERWEELLEL 201
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
324-482 1.58e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  324 NELANKESLHRQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELA----R 399
Cdd:COG4372      2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEqleeE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  400 VRQREKMNEDHNKRLSDTVDRLLSESNERLQLH------LKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEK 473
Cdd:COG4372     82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQeeleelQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161


                   ....*....
gi 2017363575  474 LRQEVDQLK 482
Cdd:COG4372    162 LQEELAALE 170
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 841-905 1.69e-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: 1.69e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363575  841 QWDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 905
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-406 1.76e-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: 42.75  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   33 MLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLN------SALPQEFATLTRELSMCREQLLEREEEISELKA 106
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleqeeEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  107 ERNNTRLLLEHLECLVSRHERSLRMTVVKrqaqspsgvssevEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEEQL 186
Cdd:TIGR02169  766 RIEELEEDLHKLEEALNDLEARLSHSRIP-------------EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKEYL 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  187 AGAHQQvsALQQGAGVRDGAAEEEGTVElgpkrlwkEDTGRVEELQELLEKQnfelsQARERlvtltttvteleeDLGTA 266
Cdd:TIGR02169  832 EKEIQE--LQEQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEEL-----EAALR-------------DLESR 883

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  267 RRDLikseelsskhQRDLREALAQKEDMEERITTLEkryLAAQREATSIHDLNDKLEN---ELANKESLHRQELLEVAEQ 343
Cdd:TIGR02169  884 LGDL----------KKERDELEAQLRELERKIEELE---AQIEKKRKRLSELKAKLEAleeELSEIEDPKGEDEEIPEEE 950

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363575  344 KlqqtmrKAETLPEVEAELAQRIAAL----TKAEERHGNIEEHLRQLEGQL----EEKNQELARVRQREKM 406
Cdd:TIGR02169  951 L------SLEDVQAELQRVEEEIRALepvnMLAIQEYEEVLKRLDELKEKRakleEERKAILERIEEYEKK 1015
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
964-1019 2.08e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 37.63  E-value: 2.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363575  964 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1019
Cdd:pfam07647   11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 178-478 2.15e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.19  E-value: 2.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  178 RVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKedtGRVEELQELLEKQNFELSQARERLVTLTTTVT 257
Cdd:pfam07888   28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE---RQRRELESRVAELKEELRQSREKHEELEEKYK 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  258 ELEEDLGTARRDLIKSEELSSKHQRDLREalaqkedMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQel 337
Cdd:pfam07888  105 ELSASSEELSEEKDALLAQRAAHEARIRE-------LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQ-- 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  338 levAEQKLQQTmrkaetlpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDT 417
Cdd:pfam07888  176 ---LQAKLQQT----------EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSL 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  418 VDRLlsESNERLQLHLKERMAAL---------------------------------EEKNTLIQELESSQRQIEEQHHHK 464
Cdd:pfam07888  243 QERL--NASERKVEGLGEELSSMaaqrdrtqaelhqarlqaaqltlqladaslalrEGRARWAQERETLQQSAEADKDRI 320

                          330
                   ....*....|....
gi 2017363575  465 GRLSEEIEKLRQEV 478
Cdd:pfam07888  321 EKLSAELQRLEERL 334
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 28-409 2.34e-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: 42.36  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   28 QLMVNMLDEREKLLESLRESQETLAATQSRLQDAihERDQLQRHLNSALPQEfATLTRELSMCREQLLEREEEISELKAE 107
Cdd:TIGR02169  190 DLIIDEKRQQLERLRREREKAERYQALLKEKREY--EGYELLKEKEALERQK-EAIERQLASLEEELEKLTEEISELEKR 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  108 RNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSLFEHHKALDEKVR---ERLRAALERVTTLE 183
Cdd:TIGR02169  267 LEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEKERELEDAEERLAkleAEIDKLLAEIEELE 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  184 EQLAGAHQQVSALQqgAGVRDGAAEEEGTVElgpkrlwkedtgRVEELQELLEKQNFELSQARERlvtltttVTELEEDL 263
Cdd:TIGR02169  343 REIEEERKRRDKLT--EEYAELKEELEDLRA------------ELEEVDKEFAETRDELKDYREK-------LEKLKREI 401

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  264 GTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREatsihdlndklenelankeslhrqelLEVAEQ 343
Cdd:TIGR02169  402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE--------------------------IKKQEW 455

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363575  344 KLQQTmrkaetlpeveaelaqrIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNED 409
Cdd:TIGR02169  456 KLEQL-----------------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 1042-1081 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 2017363575 1042 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHG-ALLALDEN 1081
Cdd:cd09512      4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS 44
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 227-375 2.98e-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: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEEL--SSKHQRDLREALAQKEDMEERITTLEKR 304
Cdd:COG1579     32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEALQKEIESLKRRISDLEDE 111

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017363575  305 YLAAQREAtsihdlnDKLENELANKESLH--RQELLEVAEQKLQQtmRKAETLPEVEAELAQRIAALTKAEER 375
Cdd:COG1579    112 ILELMERI-------EELEEELAELEAELaeLEAELEEKKAELDE--ELAELEAELEELEAEREELAAKIPPE 175
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 330-477 3.02e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  330 ESLHRQELLEVAEQKLQQTMRK---AETLPEVEAELaQRIAALTKAEERHGniEEHLRQLEG-QLEEKNQELARVRQREK 405
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREVERRrklEEAEKARQAEM-DRQAAIYAEQERMA--MERERELERiRQEERKRELERIRQEEI 370

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363575  406 MNEDHNKRLSDTVDRLLSESNERLQLHLKermAALEEKntlIQElESSQRQIEEQHHHKGRLSEEIEKLRQE 477
Cdd:pfam17380  371 AMEISRMRELERLQMERQQKNERVRQELE---AARKVK---ILE-EERQRKIQQQKVEMEQIRAEQEEARQR 435
PRK11281 PRK11281
mechanosensitive channel MscK;
286-457 3.07e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.82  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  286 EALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEnELANKESlHRQEL------LEVAEQKLQQTMRKAETLPEVE 359
Cdd:PRK11281    33 GDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKIDR-QKEETeqlkqqLAQAPAKLRQAQAELEALKDDN 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  360 A-ELAQRIAALTkaeerhgnieehLRQLEGQLEEKNQELARVRqrekmnedhnKRLSDTVDRLLSESN--ERLQLHLKER 436
Cdd:PRK11281   111 DeETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQAALYAN 168

                          170       180
                   ....*....|....*....|.
gi 2017363575  437 MAALEEKNTLIQELESSQRQI 457
Cdd:PRK11281   169 SQRLQQIRNLLKGGKVGGKAL 189
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 274-452 4.20e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 41.36  E-value: 4.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  274 EELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHdlndKLENELANKESLHRQELLEVAEQKLqqtmrkae 353
Cdd:PRK04778   309 EKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVR----QLEKQLESLEKQYDEITERIAEQEI-------- 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  354 TLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR--------EKMN-----EDHNKRLSDTVDR 420
Cdd:PRK04778   377 AYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKlheikrylEKSNlpglpEDYLEMFFEVSDE 456

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2017363575  421 L--LSESNERLQLHLKERMAALEEKNTLIQELES 452
Cdd:PRK04778   457 IeaLAEELEEKPINMEAVNRLLEEATEDVETLEE 490
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 222-481 4.52e-03

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: 41.36  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  222 KEDTGRVEELQELLEKQnfeLSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDM-EERITT 300
Cdd:pfam12128  610 EEALQSAREKQAAAEEQ---LVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSaNERLNS 686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  301 LEKRylaaqreatsihdlndklENELANKeslHRQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKA-------- 372
Cdd:pfam12128  687 LEAQ------------------LKQLDKK---HQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAiaarrsga 745

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  373 --------EERHGNI------EEHLRQLEGQLEEKNQELARVRQREK--------MNED---HNKRLSDTVdrllsESNE 427
Cdd:pfam12128  746 kaelkaleTWYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQevlryfdwYQETwlqRRPRLATQL-----SNIE 820

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2017363575  428 RLQLHLKERMAALEEKNTL-IQELESSQRQIEEQHHhkgRLSEEIEKLRQEVDQL 481
Cdd:pfam12128  821 RAISELQQQLARLIADTKLrRAKLEMERKASEKQQV---RLSENLRGLRCEMSKL 872
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
154-482 4.58e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvrdgaaeeegtvelgpkrlwkedtgRVEELQE 233
Cdd:COG4372     15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE----------------------------ELEQLEE 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  234 LLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALA-------QKEDMEERITTLEKRYL 306
Cdd:COG4372     67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKerqdleqQRKQLEAQIAELQSEIA 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  307 AAQREATSIHDLNDKLENELANKESLHRQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKA---EERHGNIEEHL 383
Cdd:COG4372    147 EREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLpreLAEELLEAKDS 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  384 RQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHH 463
Cdd:COG4372    227 LEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA 306

                          330
                   ....*....|....*....
gi 2017363575  464 KGRLSEEIEKLRQEVDQLK 482
Cdd:COG4372    307 LSLIGALEDALLAALLELA 325
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 281-482 5.77e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 5.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKeslhrQELLEVAEQKLQQTmrkaetlpevEA 360
Cdd:COG3883     22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-----QAEIAEAEAEIEER----------RE 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  361 ELAQRIAALTKAeerhGNIEEHLRQLegqLEEKNQE--LARVRQREKMNEDHNKRLSDTVDrlLSESNERLQLHLKERMA 438
Cdd:COG3883     87 ELGERARALYRS----GGSVSYLDVL---LGSESFSdfLDRLSALSKIADADADLLEELKA--DKAELEAKKAELEAKLA 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2017363575  439 ALEE-KNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 482
Cdd:COG3883    158 ELEAlKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 964-1008 7.00e-03

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


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 36.51  E-value: 7.00e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2017363575  964 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 1008
Cdd:cd09501     11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 169-484 7.04e-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: 7.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAG-VRD-----GAAEEEGTVELGPKRLW----------KEDTGR----V 228
Cdd:COG3096    277 ANERRELSERALELRRELFGARRQLAEEQYRLVeMAReleelSARESDLEQDYQAASDHlnlvqtalrqQEKIERyqedL 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  229 EELQELLEKQNFELSQARERLVTLTttvteleedlgtARRDLIKSEELSSKHQ-RDLREALaqkeDMEER--------IT 299
Cdd:COG3096    357 EELTERLEEQEEVVEEAAEQLAEAE------------ARLEAAEEEVDSLKSQlADYQQAL----DVQQTraiqyqqaVQ 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  300 TLEKRYLAAQREATSIHDLNDKLENELANKESLHrQELLEvAEQKLQqTMRKAETLPEVEAELAQRIAALTKAEERHGNI 379
Cdd:COG3096    421 ALEKARALCGLPDLTPENAEDYLAAFRAKEQQAT-EEVLE-LEQKLS-VADAARRQFEKAYELVCKIAGEVERSQAWQTA 497

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  380 EEHLRQ------LEGQLEEKNQELARVRQREkmNEDHNKRlsdtvdRLLSESNERLQLHLKERMAALEEKNTLIQELESS 453
Cdd:COG3096    498 RELLRRyrsqqaLAQRLQQLRAQLAELEQRL--RQQQNAE------RLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL 569

                          330       340       350
                   ....*....|....*....|....*....|.
gi 2017363575  454 QRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 484
Cdd:COG3096    570 EEQAAEAVEQRSELRQQLEQLRARIKELAAR 600
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 28-470 7.13e-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: 40.48  E-value: 7.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575   28 QLMVNMLDEREKLLESLRESQetLAATQSRLQDAIHERDQLQR--HLNSALPQEFATLTRELSMCREQLLEREEEISELK 105
Cdd:pfam05483  183 QVYMDLNNNIEKMILAFEELR--VQAENARLEMHFKLKEDHEKiqHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLT 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  106 AERNNTRLLLEHLECLVSRHERSLRMTVVKRQAqspsgVSSEVEVLK-ALKSLFEHHKALDEKvrerLRAALERVTTLEE 184
Cdd:pfam05483  261 FLLEESRDKANQLEEKTKLQDENLKELIEKKDH-----LTKELEDIKmSLQRSMSTQKALEED----LQIATKTICQLTE 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  185 QlagAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLG 264
Cdd:pfam05483  332 E---KEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE 408

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  265 TARRDLIKSEEL--SSKHQRDLREALAQKE---------------DMEERITTLEKrylAAQREATSIHDLNDKLENE-L 326
Cdd:pfam05483  409 ELKKILAEDEKLldEKKQFEKIAEELKGKEqelifllqarekeihDLEIQLTAIKT---SEEHYLKEVEDLKTELEKEkL 485

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  327 ANKESLHRQELLEVAEQKLQQtmRKAETLPEVEAElAQRIAALTKAEERHGNIEEHLRQLEGQLEEknqELARVRQREKM 406
Cdd:pfam05483  486 KNIELTAHCDKLLLENKELTQ--EASDMTLELKKH-QEDIINCKKQEERMLKQIENLEEKEMNLRD---ELESVREEFIQ 559

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363575  407 NEDHNKRLSDTVDRlLSESNERLQLHLKERMAALEEK-NTLIQELESSQRQIEEQHHHKGRLSEE 470
Cdd:pfam05483  560 KGDEVKCKLDKSEE-NARSIEYEVLKKEKQMKILENKcNNLKKQIENKNKNIEELHQENKALKKK 623
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 166-476 9.30e-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: 40.32  E-value: 9.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEeegtvelgpkrlwkedtgRVEELQELLEKQNFELSQA 245
Cdd:COG3096    378 AEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ------------------ALEKARALCGLPDLTPENA 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  246 RERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQR--DLREALA---QKEDMEERITTL-----EKRYLAAQREATSI 315
Cdd:COG3096    440 EDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayELVCKIAgevERSQAWQTARELlrryrSQQALAQRLQQLRA 519

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  316 HdLNDkLENELANKESLhrQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQ 395
Cdd:COG3096    520 Q-LAE-LEQRLRQQQNA--ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK 595

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  396 ELarvRQREKMNEDHNKRLSdtvdRLLSESNERLQlHLKERMAALEEKNTLIQELESSQRQIEEQhhhKGRLSEEIEKLR 475
Cdd:COG3096    596 EL---AARAPAWLAAQDALE----RLREQSGEALA-DSQEVTAAMQQLLEREREATVERDELAAR---KQALESQIERLS 664


                   .
gi 2017363575  476 Q 476
Cdd:COG3096    665 Q 665
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 297-482 9.44e-03

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: 39.21  E-value: 9.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  297 RITTLEKRYLAAQREATSIHDLNDKLENELANKESLHR----QELLEVAEQKLQQTMRKAETL----------------- 355
Cdd:pfam12795    1 KLDELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRaaayQKALDDAPAELRELRQELAALqakaeaapkeilaslsl 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  356 PEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTvDRLLSESnerLQLHLKE 435
Cdd:pfam12795   81 EELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPP-GEPLSEA---QRWALQA 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363575  436 RMAALEEK----------NTLIQELESSQRQIEEQHHHkgRLSEEIEKLRQEVDQLK 482
Cdd:pfam12795  157 ELAALKAQidmleqellsNNNRQDLLKARRDLLTLRIQ--RLEQQLQALQELLNEKR 211
PTZ00491 PTZ00491
major vault protein; Provisional
 272-417 9.91e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 40.00  E-value: 9.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  272 KSEELSSKHQRDLREALAQKEdmeerittlekryLAAQReatsihdLNDKLENELAnkeslhRQELLEVAEQ--KLQQTM 349
Cdd:PTZ00491   662 KSQEAAARHQAELLEQEARGR-------------LERQK-------MHDKAKAEEQ------RTKLLELQAEsaAVESSG 715

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363575  350 R-KAETLPEVEAELAQRIAALTKAEERHGNIE-EHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDT 417
Cdd:PTZ00491   716 QsRAEALAEAEARLIEAEAEVEQAELRAKALRiEAEAELEKLRKRQELELEYEQAQNELEIAKAKELADI 785
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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