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Conserved domains on  [gi|2462535324|ref|XP_054229655|]
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liprin-alpha-2 isoform X34 [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

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List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 954-1025 2.15e-44

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


:

Pssm-ID: 188967  Cd Length: 72  Bit Score: 154.40  E-value: 2.15e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  954 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1025
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 869-934 6.98e-44

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


:

Pssm-ID: 188964  Cd Length: 66  Bit Score: 153.01  E-value: 6.98e-44
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535324  869 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 934
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 ...
 745-815 7.05e-44

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


:

Pssm-ID: 188961  Cd Length: 71  Bit Score: 153.10  E-value: 7.05e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535324  745 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 815
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-388 1.11e-15

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: 82.29  E-value: 1.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemntkyqrdiREAMAQKEDMEERITTLEKRYL 195
Cdd:COG1196    247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE--------------YELLAELARLEQDIARLEERRR 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  196 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmrKAETLPEVEAELAQRIAALTKAEERHG 275
Cdd:COG1196    313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEELEELAEELL 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  276 NIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEKNVLIQESETFRKNL 355
Cdd:COG1196    390 EALRAAAELAAQLEELEEAEEALLERL---ERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEEEEEALLELL 465

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462535324  356 EESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:COG1196    466 AELLEEAALLEAALAELLEELAEAAARLLLLLE 498
DR0291 super family cl34310
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 19-200 2.29e-05

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


The actual alignment was detected with superfamily member COG1579:

Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 47.23  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   19 EVLKALKSLFEHHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKV 98
Cdd:COG1579      4 EDLRALLDLQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE-----LEIEEVEARIKK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   99 HEKRLsnGSIDSTDEtsqivelQELLEKqnyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMA 178
Cdd:COG1579     78 YEEQL--GNVRNNKE-------YEALQK---EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145

                          170       180
                   ....*....|....*....|..
gi 2462535324  179 QKEDMEERITTLEKRyLSAQRE 200
Cdd:COG1579    146 ELDEELAELEAELEE-LEAERE 166
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 954-1025 2.15e-44

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


Pssm-ID: 188967  Cd Length: 72  Bit Score: 154.40  E-value: 2.15e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  954 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1025
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 869-934 6.98e-44

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


Pssm-ID: 188964  Cd Length: 66  Bit Score: 153.01  E-value: 6.98e-44
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535324  869 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 934
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 ...
 745-815 7.05e-44

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


Pssm-ID: 188961  Cd Length: 71  Bit Score: 153.10  E-value: 7.05e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535324  745 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 815
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-388 1.11e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 82.29  E-value: 1.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemntkyqrdiREAMAQKEDMEERITTLEKRYL 195
Cdd:COG1196    247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE--------------YELLAELARLEQDIARLEERRR 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  196 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmrKAETLPEVEAELAQRIAALTKAEERHG 275
Cdd:COG1196    313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEELEELAEELL 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  276 NIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEKNVLIQESETFRKNL 355
Cdd:COG1196    390 EALRAAAELAAQLEELEEAEEALLERL---ERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEEEEEALLELL 465

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462535324  356 EESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:COG1196    466 AELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-381 1.47e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 82.03  E-value: 1.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  114 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR 193
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  194 YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 273
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  274 hgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERL-QLHLKERMAALEEKNVLIQESE 349
Cdd:TIGR02168  871 ---LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrreLEELREKLaQLELRLEGLEVRIDNLQERLSE 947

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2462535324  350 TFRKNLEESLHDKERLAEEIEKLRSELDQLKM 381
Cdd:TIGR02168  948 EYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 868-932 4.84e-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: 4.84e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  868 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 932
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
18-435 2.64e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 71.22  E-value: 2.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   18 VEVLKALKSLFEHHkaldEKVRERLRVSLERVSALEEELAAANQEIVALREQnVHIQRKMASSEGSTESEHLEGMEpgqk 97
Cdd:PRK02224   233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEE-VRDLRERLEELEEERDDLLAEAG---- 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   98 vhekrLSNGSIDSTDE-----TSQIVELQELLEKQ-------NYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEm 165
Cdd:PRK02224   304 -----LDDADAEAVEArreelEDRDEELRDRLEECrvaaqahNEEAESLREDADDLEERAEELREEAAELESELEEARE- 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  166 ntkyqrDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqq 245
Cdd:PRK02224   378 ------AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA---- 447

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  246 tMRKAETLPEVEAEL--AQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLT 321
Cdd:PRK02224   448 -LLEAGKCPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIA 526

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  322 ESNERLQlHLKERMAAL-EEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLiePTIpRTHLDTSA 400
Cdd:PRK02224   527 ERRETIE-EKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERI-RTLLAAIA 602

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2462535324  401 ELRYSVGSLVDSQSDYRTtkvIRRPRRGRMGVRRD 435
Cdd:PRK02224   603 DAEDEIERLREKREALAE---LNDERRERLAEKRE 634
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 112-377 1.03e-10

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


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 65.09  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  112 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE 191
Cdd:pfam19220   45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  192 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 271
Cdd:pfam19220  125 RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  272 ERHgniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSD-------------TVDRLLTESNERLQlHLKERMAA 337
Cdd:pfam19220  205 DAT---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASlrmklealtaraaATEQLLAEARNQLR-DRDEAIRA 280

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2462535324  338 LEEKNV-LIQESETFRKNLEESLHDKERLAE---EIEKLRSELD 377
Cdd:pfam19220  281 AERRLKeASIERDTLERRLAGLEADLERRTQqfqEMQRARAELE 324
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 745-811 3.57e-09

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 54.22  E-value: 3.57e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535324   745 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 811
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 877-932 8.17e-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: 50.37  E-value: 8.17e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535324   877 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 932
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 955-1026 4.72e-07

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.06  E-value: 4.72e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324   955 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1026
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 19-200 2.29e-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: 47.23  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   19 EVLKALKSLFEHHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKV 98
Cdd:COG1579      4 EDLRALLDLQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE-----LEIEEVEARIKK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   99 HEKRLsnGSIDSTDEtsqivelQELLEKqnyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMA 178
Cdd:COG1579     78 YEEQL--GNVRNNKE-------YEALQK---EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145

                          170       180
                   ....*....|....*....|..
gi 2462535324  179 QKEDMEERITTLEKRyLSAQRE 200
Cdd:COG1579    146 ELDEELAELEAELEE-LEAERE 166
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 747-811 9.54e-05

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 41.49  E-value: 9.54e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  747 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 811
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
955-1025 1.11e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.11e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535324  955 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1025
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 209-383 2.10e-04

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.97  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  209 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 276
Cdd:cd00176     10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  277 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 346
Cdd:cd00176     84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2462535324  347 ESETFRKNLEESLH--DKERLAEEIEKLRSELDQLKMRT 383
Cdd:cd00176    164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 954-1025 2.15e-44

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


Pssm-ID: 188967  Cd Length: 72  Bit Score: 154.40  E-value: 2.15e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  954 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1025
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 869-934 6.98e-44

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


Pssm-ID: 188964  Cd Length: 66  Bit Score: 153.01  E-value: 6.98e-44
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535324  869 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 934
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 ...
 745-815 7.05e-44

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


Pssm-ID: 188961  Cd Length: 71  Bit Score: 153.10  E-value: 7.05e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535324  745 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 815
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 873-932 1.43e-31

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


Pssm-ID: 188894  Cd Length: 60  Bit Score: 117.63  E-value: 1.43e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  873 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 932
Cdd:cd09495      1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 752-810 3.10e-27

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


Pssm-ID: 188893  Cd Length: 58  Bit Score: 105.00  E-value: 3.10e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535324  752 TVVAWLELWLGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 810
Cdd:cd09494      1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 962-1023 5.65e-25

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


Pssm-ID: 188895  Cd Length: 62  Bit Score: 98.77  E-value: 5.65e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  962 RVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNN 1023
Cdd:cd09496      1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 954-1025 1.27e-18

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


Pssm-ID: 188969  Cd Length: 72  Bit Score: 80.95  E-value: 1.27e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  954 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1025
Cdd:cd09570      1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 746-810 3.95e-17

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


Pssm-ID: 188963  Cd Length: 70  Bit Score: 76.72  E-value: 3.95e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  746 AQWDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 810
Cdd:cd09564      2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 868-932 1.25e-16

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 75.04  E-value: 1.25e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  868 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 932
Cdd:cd09566      1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 868-932 1.46e-16

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 74.75  E-value: 1.46e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  868 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 932
Cdd:cd09567      1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-388 1.11e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 82.29  E-value: 1.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemntkyqrdiREAMAQKEDMEERITTLEKRYL 195
Cdd:COG1196    247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE--------------YELLAELARLEQDIARLEERRR 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  196 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmrKAETLPEVEAELAQRIAALTKAEERHG 275
Cdd:COG1196    313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEELEELAEELL 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  276 NIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEKNVLIQESETFRKNL 355
Cdd:COG1196    390 EALRAAAELAAQLEELEEAEEALLERL---ERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEEEEEALLELL 465

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462535324  356 EESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:COG1196    466 AELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-381 1.47e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 82.03  E-value: 1.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  114 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR 193
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  194 YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 273
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  274 hgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERL-QLHLKERMAALEEKNVLIQESE 349
Cdd:TIGR02168  871 ---LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrreLEELREKLaQLELRLEGLEVRIDNLQERLSE 947

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2462535324  350 TFRKNLEESLHDKERLAEEIEKLRSELDQLKM 381
Cdd:TIGR02168  948 EYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 954-1025 1.88e-15

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 72.10  E-value: 1.88e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  954 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1025
Cdd:cd09569      1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 135-388 2.15e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.64  E-value: 2.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  135 KERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENE 214
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  215 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH-------GNIEERMRHLEGQ 287
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtllneeaANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  288 LEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKER-------MAALEEKNVLIQESETFRKNLEE 357
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERasleealALLRSELEELSEELRELESKRSE 912

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2462535324  358 SLHDKERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQE 943
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 110-382 2.88e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.26  E-value: 2.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  110 STDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITT 189
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  190 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkAETLPEVEAELAQRIAALTK 269
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL---REALDELRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  270 AEERHGNIEERMRHLEGQLEEKNQELQRAR-QREKMNEEHNKrlsdtVDRLLTESNERLQLHLKERMAALEEKNVLIQES 348
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSeDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSEL 896

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462535324  349 ETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 382
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELR 930
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 21-328 4.63e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 80.49  E-value: 4.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   21 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE 100
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  101 ---------KRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQR 171
Cdd:TIGR02168  780 aeaeieeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  172 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQT----M 247
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLevriD 939

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  248 RKAETLPEV------------------EAELAQRIAALTKAEERHGNI-----------EERMRHLEGQLEEknqeLQRA 298
Cdd:TIGR02168  940 NLQERLSEEysltleeaealenkieddEEEARRRLKRLENKIKELGPVnlaaieeyeelKERYDFLTAQKED----LTEA 1015

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2462535324  299 RQR-----EKMNEEHNKRLSDTVDRLltesNERLQ 328
Cdd:TIGR02168 1016 KETleeaiEEIDREARERFKDTFDQV----NENFQ 1046
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 868-932 4.84e-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: 4.84e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  868 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 932
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 29-388 7.40e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.51  E-value: 7.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   29 EHHKALDEKVRER-LRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrlsngs 107
Cdd:COG1196    213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE-------------------------- 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  108 idstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 187
Cdd:COG1196    267 -------AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  188 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 267
Cdd:COG1196    340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  268 TKAEERhgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNvliqe 347
Cdd:COG1196    420 EEELEE---LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA----- 491

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2462535324  348 setfRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:COG1196    492 ----RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 137-380 1.06e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.86  E-value: 1.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  137 RLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELA 216
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  217 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI----AALTKAEERHGNIEERMRHLEGQLEEKN 292
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELesleAELEELEAELEELESRLEELEEQLETLR 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  293 QELQRARQREKMNEEHNKRLSDTVDRlLTESNERLQLHLKERMAALEEKNV--LIQESETFRKNLEESLHDKERLAEEIE 370
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALE 464

                          250
                   ....*....|
gi 2462535324  371 KLRSELDQLK 380
Cdd:TIGR02168  465 ELREELEEAE 474
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 116-386 1.68e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.48  E-value: 1.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 195
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  196 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHG 275
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEELESRLEELEEQLE 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  276 NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE-EKNVLIQESETFRKN 354
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEeELEELQEELERLEEA 462

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2462535324  355 LEESLHDKERLAEEIEKLRSELDQLKMRTGSL 386
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQARLDSL 494
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 100-379 4.07e-13

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 73.95  E-value: 4.07e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  100 EKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQ 179
Cdd:TIGR02169  701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  180 KEDMEERIttlekrylsAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAE 259
Cdd:TIGR02169  781 LNDLEARL---------SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  260 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARqrekmnEEHNKRLSDTVDRL--LTESNERLQLHLKERMAA 337
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER------DELEAQLRELERKIeeLEAQIEKKRKRLSELKAK 925

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2462535324  338 LEEKNVLIQESETFRKNLEES---LHDKERLAEEIEKLRSELDQL 379
Cdd:TIGR02169  926 LEALEEELSEIEDPKGEDEEIpeeELSLEDVQAELQRVEEEIRAL 970
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-378 9.82e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 9.82e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  167 TKYQRDIREAMAQKEDMEERIT-------TLEKRY--LSAQRESTSIHdmnDKLENELANKEAILRQMEEknRQLQERLE 237
Cdd:COG1196    168 SKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEKAERY---RELKEELKELEAELLLLKL--RELEAELE 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  238 LAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVD 317
Cdd:COG1196    243 ELEAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535324  318 RLLTEsNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 378
Cdd:COG1196    320 ELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 24-330 1.12e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 72.78  E-value: 1.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   24 LKSLFEHHKALDEKVRE--RLRVSLER-VSALEEELAAANQEIVALREQNVHIQRKMASSegSTESEHLEGMEpgqKVHE 100
Cdd:TIGR02168  234 LEELREELEELQEELKEaeEELEELTAeLQELEEKLEELRLEVSELEEEIEELQKELYAL--ANEISRLEQQK---QILR 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  101 KRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLiktEEMNTKYqrdireamaqk 180
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL---EELESRL----------- 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  181 EDMEERITTLEKRYLSAQRESTSIhdmndklENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA--ETLPEVEA 258
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASL-------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEE 447

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  259 ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH 330
Cdd:TIGR02168  448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 745-809 1.21e-12

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


Pssm-ID: 188962  Cd Length: 64  Bit Score: 63.79  E-value: 1.21e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535324  745 FAQWDGPTVVAWL-ELWLGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 809
Cdd:cd09563      1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 36-380 1.37e-12

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 72.41  E-value: 1.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   36 EKVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRKMAssegstesehlegmepgqKVHEKRLSNGSIDSTDETS 115
Cdd:TIGR02169  733 EKLKERLEELEEDLSSLEQEIENVKSELKELEAR---IEELEE------------------DLHKLEEALNDLEARLSHS 791

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARkdliktEEMNTKyQRDIREAMAQKEDMEERITTLEKRYl 195
Cdd:TIGR02169  792 RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE------KEIQEL-QEQRIDLKEQIKSIEKEIENLNGKK- 863

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  196 saqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpEVEAELAQRIAALTKAeeRHG 275
Cdd:TIGR02169  864 -------------EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSELKA--KLE 927

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  276 NIEERMRHLE---GQLEEKNQELQRARQREKMNEEhnkrlsdtvdrlltesnerlqlhLKERMAALEEKNVL-IQESETF 351
Cdd:TIGR02169  928 ALEEELSEIEdpkGEDEEIPEEELSLEDVQAELQR-----------------------VEEEIRALEPVNMLaIQEYEEV 984

                          330       340       350
                   ....*....|....*....|....*....|..
gi 2462535324  352 RKNLEESLHDKERLAEE---IEKLRSELDQLK 380
Cdd:TIGR02169  985 LKRLDELKEKRAKLEEErkaILERIEEYEKKK 1016
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 102-386 2.13e-12

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 71.64  E-value: 2.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  102 RLSNGSIDSTDETSQIVELQELLEKqnyemaqMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKE 181
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  182 DMEERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERLELAEQKLQQtmrkaETLPEVEAEla 261
Cdd:TIGR02169  734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIE-------ELEEDLHKLEEALNDLEARLSH-----SRIPEIQAE-- 799

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  262 qriaaLTKAEERHGNIEERMRHLEGQLEEKNQELQRArqREKMNEEHNKRlsdtvdRLLTESNERLQLHLKERMAALEEK 341
Cdd:TIGR02169  800 -----LSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQR------IDLKEQIKSIEKEIENLNGKKEEL 866

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2462535324  342 NVLIQESETFRKNLEESLHDkerLAEEIEKLRSELDQLKMRTGSL 386
Cdd:TIGR02169  867 EEELEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEEL 908
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
18-435 2.64e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 71.22  E-value: 2.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   18 VEVLKALKSLFEHHkaldEKVRERLRVSLERVSALEEELAAANQEIVALREQnVHIQRKMASSEGSTESEHLEGMEpgqk 97
Cdd:PRK02224   233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEE-VRDLRERLEELEEERDDLLAEAG---- 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   98 vhekrLSNGSIDSTDE-----TSQIVELQELLEKQ-------NYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEm 165
Cdd:PRK02224   304 -----LDDADAEAVEArreelEDRDEELRDRLEECrvaaqahNEEAESLREDADDLEERAEELREEAAELESELEEARE- 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  166 ntkyqrDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqq 245
Cdd:PRK02224   378 ------AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA---- 447

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  246 tMRKAETLPEVEAEL--AQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLT 321
Cdd:PRK02224   448 -LLEAGKCPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIA 526

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  322 ESNERLQlHLKERMAAL-EEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLiePTIpRTHLDTSA 400
Cdd:PRK02224   527 ERRETIE-EKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERI-RTLLAAIA 602

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2462535324  401 ELRYSVGSLVDSQSDYRTtkvIRRPRRGRMGVRRD 435
Cdd:PRK02224   603 DAEDEIERLREKREALAE---LNDERRERLAEKRE 634
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-388 4.21e-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: 4.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  112 DETSQIVELQELLEKQNYEMAQMKERLA-------ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 184
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  185 ERITTLEKRYLSAQRESTSihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRI 264
Cdd:TIGR02168  337 EELAELEEKLEELKEELES-------LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLE 406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  265 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRAR--QREKMNEEHNKRLSDTVDRLLTESNERLQlhLKERMAALEEKN 342
Cdd:TIGR02168  407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEE--AEQALDAAEREL 484

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2462535324  343 VLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:TIGR02168  485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-307 5.06e-12

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 70.48  E-value: 5.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   16 SEVEVLKALKSLFEHHKALDEKVRERLrvslERVSALEEELAAANQEIVAL-REQNVHIQRKMASSEGSTES--EHLEGM 92
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELE----KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASleRSIAEK 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   93 EPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRD 172
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  173 IREAmaqKEDMEERITTLEKRYLSAQRESTSIHDMNdkleNELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkaet 252
Cdd:TIGR02169  394 LEKL---KREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL------ 460

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  253 lpeveaelaqrIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 307
Cdd:TIGR02169  461 -----------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
12-378 1.23e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 68.94  E-value: 1.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   12 SGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRKMASSEGSTESEHLEG 91
Cdd:PRK03918   224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---VKELKELKEKAEEYIKLSE 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   92 MEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNT---- 167
Cdd:PRK03918   301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkr 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  168 -------KYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLEN--------------------------E 214
Cdd:PRK03918   381 ltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeytaE 460

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  215 LANKEAILRQMEEKNRQLQERLELAEQKLQQ-----TMRK-AETLPEVEAELAQ-RIAALTKAEERHGNIEERMRHLEGQ 287
Cdd:PRK03918   461 LKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKElAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGE 540

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  288 LEEKNQELQRARQREKMNEEHNKRLsDTVDRLLTESNERLQLHLKERMAALEEKnvlIQESETFRK---NLEESLHDKER 364
Cdd:PRK03918   541 IKSLKKELEKLEELKKKLAELEKKL-DELEEELAELLKELEELGFESVEELEER---LKELEPFYNeylELKDAEKELER 616

                          410
                   ....*....|....
gi 2462535324  365 LAEEIEKLRSELDQ 378
Cdd:PRK03918   617 EEKELKKLEEELDK 630
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
135-386 9.36e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 66.24  E-value: 9.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  135 KERLAALSSRVGEVEQEAETARKDLIKTEemntkyqRDIREAMAQKEDMEERITTLEKRYlsaqRESTSIHDMNDKLENE 214
Cdd:PRK03918   178 IERLEKFIKRTENIEELIKEKEKELEEVL-------REINEISSELPELREELEKLEKEV----KELEELKEEIEELEKE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  215 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE--AELAQRIAAL-TKAEERHGNIEERMRHLEGQLEEK 291
Cdd:PRK03918   247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekAEEYIKLSEFyEEYLDELREIEKRLSRLEEEINGI 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  292 NQELQRARQREKMNEEHNKRLSDTVDRL--LTESNERLQ--LHLKERMAALEEKnVLIQESETFRKNLEESLHDKERLAE 367
Cdd:PRK03918   327 EERIKELEEKEERLEELKKKLKELEKRLeeLEERHELYEeaKAKKEELERLKKR-LTGLTPEKLEKELEELEKAKEEIEE 405

                          250
                   ....*....|....*....
gi 2462535324  368 EIEKLRSELDQLKMRTGSL 386
Cdd:PRK03918   406 EISKITARIGELKKEIKEL 424
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 112-377 1.03e-10

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


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 65.09  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  112 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE 191
Cdd:pfam19220   45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  192 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 271
Cdd:pfam19220  125 RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  272 ERHgniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSD-------------TVDRLLTESNERLQlHLKERMAA 337
Cdd:pfam19220  205 DAT---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASlrmklealtaraaATEQLLAEARNQLR-DRDEAIRA 280

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2462535324  338 LEEKNV-LIQESETFRKNLEESLHDKERLAE---EIEKLRSELD 377
Cdd:pfam19220  281 AERRLKeASIERDTLERRLAGLEADLERRTQqfqEMQRARAELE 324
mukB PRK04863
chromosome partition protein MukB;
39-386 2.29e-10

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 65.36  E-value: 2.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   39 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMA---SSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDEts 115
Cdd:PRK04863   278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAelnEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA-- 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemntkyqrdireamaqkEDMEERITTLEKR-- 193
Cdd:PRK04863   356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQL---------------------ADYQQALDVQQTRai 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  194 -YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmRKAETLPEVEAELAQRIAALTKAEE 272
Cdd:PRK04863   415 qYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRKIAGEVSRSE 493

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  273 RHgnieERMRHLEGQLEEKNQELQRARQ-REKMNE-EHNKRLSDTVDRLLTESNERLQLHLkERMAALEEknvLIQESET 350
Cdd:PRK04863   494 AW----DVARELLRRLREQRHLAEQLQQlRMRLSElEQRLRQQQRAERLLAEFCKRLGKNL-DDEDELEQ---LQEELEA 565

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2462535324  351 FRKNLEESlhdKERLAEEIEKLRSELDQLKMRTGSL 386
Cdd:PRK04863   566 RLESLSES---VSEARERRMALRQQLEQLQARIQRL 598
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 131-542 5.40e-10

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 63.98  E-value: 5.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  131 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEerITTLEKRYLSAQRESTSIHDMNDK 210
Cdd:pfam15921  226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEI 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  211 LENELANKEAI-LRQMEEknrqlqerLELAEQKLQQTMRKA-----ETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 284
Cdd:pfam15921  304 IQEQARNQNSMyMRQLSD--------LESTVSQLRSELREAkrmyeDKIEELEKQLVLANSELTEARTERDQFSQESGNL 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  285 EGQLEEKNQELQRARQREKMNEEHNKRLSD-------TVDRLLTESNER-----------------LQLHLKERMAALEE 340
Cdd:pfam15921  376 DDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRnmevqrleallkamkseCQGQMERQMAAIQG 455

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  341 KNVLIQESETFRKNLEESlhdKERLAEEIEKLRSELDQLKmrtgsliepTIPRTHLDTSAELRYSVGSLVDSQSDyrTTK 420
Cdd:pfam15921  456 KNESLEKVSSLTAQLEST---KEMLRKVVEELTAKKMTLE---------SSERTVSDLTASLQEKERAIEATNAE--ITK 521

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  421 VirrprRGRMGVRRDEPK-VKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIddddRETIFSSMDLLSPSGHSDA--QTLA 497
Cdd:pfam15921  522 L-----RSRVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL----RQQIENMTQLVGQHGRTAGamQVEK 592

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 2462535324  498 MMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNL 542
Cdd:pfam15921  593 AQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL 637
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 112-532 7.35e-10

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 63.55  E-value: 7.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  112 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEemntKYQrdirEAMAQKEDMEERITTLE 191
Cdd:TIGR02169  160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE----RYQ----ALLKEKREYEGYELLKE 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  192 KRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAelaqrIAALTKAE 271
Cdd:TIGR02169  232 KEALERQKE---------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVKEKIG 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  272 ERHGNIEErmrhLEGQLEEKNQELQRA-RQREKMNEEHNKrlsdtvdrlltesnerlqlhLKERMAALEEKnvliqeset 350
Cdd:TIGR02169  298 ELEAEIAS----LERSIAEKERELEDAeERLAKLEAEIDK--------------------LLAEIEELERE--------- 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  351 frknLEESLHDKERLAEEIEKLRSELDQLKMRTGSLieptiprthldtSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRM 430
Cdd:TIGR02169  345 ----IEEERKRRDKLTEEYAELKEELEDLRAELEEV------------DKEFAETRDELKDYREKLEKLKREINELKREL 408

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  431 GVRRDEPKVKS--LGDHEwnrtQQIGVLSSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAmmLQEQLDAIN 508
Cdd:TIGR02169  409 DRLQEELQRLSeeLADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD--LKEEYDRVE 482

                          410       420
                   ....*....|....*....|....
gi 2462535324  509 KEIRLIQEEKESTELRAEEIENRV 532
Cdd:TIGR02169  483 KELSKLQRELAEAEAQARASEERV 506
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
47-386 9.00e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.16  E-value: 9.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   47 ERVSALEEELAAANQEIVALREQnvhiQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDstdetSQIVELQELLEK 126
Cdd:PRK03918   193 ELIKEKEKELEEVLREINEISSE----LPELREELEKLEKEVKELEELKEEIEELEKELESLE-----GSKRKLEEKIRE 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  127 QNYEMAQMKERLAALSSRVGEVEqEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHD 206
Cdd:PRK03918   264 LEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  207 MNDKLEnELANKEAILRQME---EKNRQLQERLELAEQKLqqtmrKAETLPEVEAELAQRIAALTKAEERHGNIEERMRH 283
Cdd:PRK03918   343 LKKKLK-ELEKRLEELEERHelyEEAKAKKEELERLKKRL-----TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  284 LEGQLEEKNQ---ELQRARQR-----EKMNEEHNKRLSDTVDRLLTESNERLQ-LHLKERMAALEEKNV---LIQESETF 351
Cdd:PRK03918   417 LKKEIKELKKaieELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEKELKeIEEKERKLRKELRELekvLKKESELI 496

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 2462535324  352 R--------KNLEESL--HDKERL---AEEIEKLRSELDQLKMRTGSL 386
Cdd:PRK03918   497 KlkelaeqlKELEEKLkkYNLEELekkAEEYEKLKEKLIKLKGEIKSL 544
PTZ00121 PTZ00121
MAEBL; Provisional
 32-361 1.07e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   32 KALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMAssEGSTESEHLEGMEPGQKVHEKRlsngsidST 111
Cdd:PTZ00121  1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA--DEAKKAEEAKKADEAKKAEEKK-------KA 1548

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  112 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMAQKEDMEERITTLE 191
Cdd:PTZ00121  1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE----EVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  192 KRylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEEKNRQLQERLELAE-QKLQQTMRKAETLPEVEAELAQ 262
Cdd:PTZ00121  1625 LK--KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAK 1702

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  263 RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR---LSDTVDRLLTESNERLQLHLKERMAALE 339
Cdd:PTZ00121  1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782

                          330       340
                   ....*....|....*....|..
gi 2462535324  340 EKnvLIQESETFRKNLEESLHD 361
Cdd:PTZ00121  1783 EE--LDEEDEKRRMEVDKKIKD 1802
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 170-385 1.18e-09

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 61.70  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  170 QRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 249
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  250 AETLpevEAELAQRIAALTK------------------AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR 311
Cdd:COG4942     99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535324  312 LSDTVDRLLTEsNERLQLHLKERMAALEEKNvliQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGS 385
Cdd:COG4942    176 LEALLAELEEE-RAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 115-307 1.28e-09

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 61.38  E-value: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  115 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmaqKEDMEERITTLEKRY 194
Cdd:COG3883     16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  195 LSAQR------------ESTSIHDMNDKLEN----ELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAET-LPE 255
Cdd:COG3883     93 RALYRsggsvsyldvllGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAE 172

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  256 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 307
Cdd:COG3883    173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
47-386 3.06e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 61.21  E-value: 3.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   47 ERVSALEEELAAANQEIV-ALREQNVHIQRKMASSEGSTES-----EHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVEL 120
Cdd:PRK02224   310 EAVEARREELEDRDEELRdRLEECRVAAQAHNEEAESLREDaddleERAEELREEAAELESELEEAREAVEDRREEIEEL 389

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  121 QELLE--------------KQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ-----RDIREA--MAQ 179
Cdd:PRK02224   390 EEEIEelrerfgdapvdlgNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEGSphVET 469

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  180 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLEnELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PE 255
Cdd:PRK02224   470 IEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELreraAE 548

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  256 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQR-ARQREKMNEEHNKRlsDTVDRL------LTESNERLQ 328
Cdd:PRK02224   549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESlERIRTLLAAIADAE--DEIERLrekreaLAELNDERR 626

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  329 LHLKERM------------AALEEKNVLIQESETFRKNLEESLHDK--------------ERLAEEIEKLRSELDQLKMR 382
Cdd:PRK02224   627 ERLAEKRerkreleaefdeARIEEAREDKERAEEYLEQVEEKLDELreerddlqaeigavENELEELEELRERREALENR 706


                   ....
gi 2462535324  383 TGSL 386
Cdd:PRK02224   707 VEAL 710
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
13-382 3.51e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.23  E-value: 3.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   13 GVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTES-EHLEG 91
Cdd:PRK03918   290 EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKA 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   92 MEPGQKVHEKRLSNGSIDSTDETSQIV-----ELQELLEKQNYEMAQMKERLAALSSRVGEVEQE-----------AETA 155
Cdd:PRK03918   370 KKEELERLKKRLTGLTPEKLEKELEELekakeEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelTEEH 449

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  156 RKDLIK--TEEMNtKYQRDIREAMAQKEDMEERITTLEKrYLSAQRESTSIHDMNDKLEN-ELANKEAILRQMEEKNRQ- 231
Cdd:PRK03918   450 RKELLEeyTAELK-RIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEy 527

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  232 --LQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL----EGQLEEKNQELqrarqrEKMN 305
Cdd:PRK03918   528 ekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKEL------EPFY 601

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  306 EEHNkRLSDTVDRL--LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKE---------RLAEEIEKLRS 374
Cdd:PRK03918   602 NEYL-ELKDAEKELerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeylELSRELAGLRA 680


                   ....*...
gi 2462535324  375 ELDQLKMR 382
Cdd:PRK03918   681 ELEELEKR 688
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 745-811 3.57e-09

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 54.22  E-value: 3.57e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535324   745 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 811
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
171-382 4.15e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.08  E-value: 4.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  171 RDIREAMaqkEDMEERITTLE------KRYLSAQRESTSIHDMNDKLEnelankeaiLRQMEEKNRQLQERLELAEQKLQ 244
Cdd:COG4913    238 ERAHEAL---EDAREQIELLEpirelaERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELA 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  245 QTMRKAETLPEVEAELAQRIAALTKAEERHGNieERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrlLTESN 324
Cdd:COG4913    306 RLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLERELEERERRRARLEALLAALGLPLP--ASAEE 381

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535324  325 -ERLQLHLKERMAALEEknvliqESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 382
Cdd:COG4913    382 fAALRAEAAALLEALEE------ELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 122-403 4.48e-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: 4.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  122 ELLEKQnyemAQMKERLAALSSRVGEVE-----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLS 196
Cdd:TIGR02168  203 KSLERQ----AEKAERYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  197 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALtkaeerhgn 276
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL--------- 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  277 iEERMRHLEGQLEEKNQELQRARQREKMNEEHnkrlsdtvdrLLTESNERLQLhlkermaaLEEKNVLIQESETFRKNLE 356
Cdd:TIGR02168  350 -KEELESLEAELEELEAELEELESRLEELEEQ----------LETLRSKVAQL--------ELQIASLNNEIERLEARLE 410

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2462535324  357 ESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELR 403
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
PTZ00121 PTZ00121
MAEBL; Provisional
 32-388 4.77e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.93  E-value: 4.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   32 KALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDST 111
Cdd:PTZ00121  1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA 1492

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  112 DETSQIVE---LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK--------DLIKTEEMntKYQRDIREAMAQK 180
Cdd:PTZ00121  1493 EEAKKKADeakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeekkkadELKKAEEL--KKAEEKKKAEEAK 1570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  181 EDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE---------KNRQLQERLELAEQKLQQTMRKAE 251
Cdd:PTZ00121  1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKKKAE 1650

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  252 TLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesnERLQLHL 331
Cdd:PTZ00121  1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELKKAE 1725

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  332 KERMAALEEknvLIQESETFRKNLEESLHD---KERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:PTZ00121  1726 EENKIKAEE---AKKEAEEDKKKAEEAKKDeeeKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
138-386 5.70e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.46  E-value: 5.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  138 LAALSSRVGEVEQ--EAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrYLSAQREstsIHDMNDKLENEL 215
Cdd:PRK03918   127 LNAIYIRQGEIDAilESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEK-FIKRTEN---IEELIKEKEKEL 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  216 ANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ---LEEKN 292
Cdd:PRK03918   203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKV 282

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  293 QELQRARQREKMNEEHNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLE---ESLHDKER 364
Cdd:PRK03918   283 KELKELKEKAEEYIKLSEFYEEYLDELreiekRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHE 362

                          250       260
                   ....*....|....*....|..
gi 2462535324  365 LAEEIEKLRSELDQLKMRTGSL 386
Cdd:PRK03918   363 LYEEAKAKKEELERLKKRLTGL 384
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
112-357 6.31e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.08  E-value: 6.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  112 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK---DLIKTEEMNTKYQRDIREAMAQKEDMEERIT 188
Cdd:PRK03918   183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKevkELEELKEEIEELEKELESLEGSKRKLEEKIR 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  189 TLEKRylsaqrestsIHDMNDKLEnELANKEAILRQMEEKN---RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIA 265
Cdd:PRK03918   263 ELEER----------IEELKKEIE-ELEEKVKELKELKEKAeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  266 ALTKAEERHGNIEERMRHLE---GQLEEKNQELQRARQREKMNEEHNKRLS----DTVDRLLTESNERLQLHLKERMAAL 338
Cdd:PRK03918   332 ELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTgltpEKLEKELEELEKAKEEIEEEISKIT 411

                          250
                   ....*....|....*....
gi 2462535324  339 EEKNVLIQESETFRKNLEE 357
Cdd:PRK03918   412 ARIGELKKEIKELKKAIEE 430
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 61-377 8.42e-09

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 59.97  E-value: 8.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   61 QEIVALREQNVHIQRKMASSEGSTE--SEHLEGMEPGQKVHEKRLSNGSI-DSTDETSQIVELQELLEKQNYEMAQMKER 137
Cdd:COG3096    836 AELAALRQRRSELERELAQHRAQEQqlRQQLDQLKEQLQLLNKLLPQANLlADETLADRLEELREELDAAQEAQAFIQQH 915

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  138 LAALSsrvgEVEQEAETARKDLIKTEEMNTKYQRdireAMAQKEDMEERITTLEkrYLSAQRESTSIHD----------M 207
Cdd:COG3096    916 GKALA----QLEPLVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALS--EVVQRRPHFSYEDavgllgensdL 985

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  208 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL-----TKAEERhgnIEERMR 282
Cdd:COG3096    986 NEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadAEAEER---ARIRRD 1062

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  283 HLEGQL----EEKNQ-ELQRARQREKMnEEHNKRLSDtVDRLLTESNERLQLHLKERMAALEeknvLIQESetfrkNLEE 357
Cdd:COG3096   1063 ELHEELsqnrSRRSQlEKQLTRCEAEM-DSLQKRLRK-AERDYKQEREQVVQAKAGWCAVLR----LARDN-----DVER 1131

                          330       340
                   ....*....|....*....|
gi 2462535324  358 SLHDKERLAEEIEKLRSELD 377
Cdd:COG3096   1132 RLHRRELAYLSADELRSMSD 1151
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-326 1.33e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 58.24  E-value: 1.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  115 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 194
Cdd:COG4942     27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  195 ----LSAQREST--------SIHDMNDkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 262
Cdd:COG4942    107 aellRALYRLGRqpplalllSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535324  263 RIAALTKAEERHgniEERMRHLEGQLEEKNQELQRARQREkmneehnKRLSDTVDRLLTESNER 326
Cdd:COG4942    186 ERAALEALKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAA 239
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 116-280 1.71e-08

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 56.47  E-value: 1.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QIVELQELLEkqnyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR-- 193
Cdd:COG1579      8 ALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlg 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  194 -------YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAA 266
Cdd:COG1579     84 nvrnnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEE 160

                          170
                   ....*....|....*
gi 2462535324  267 LTKAEERH-GNIEER 280
Cdd:COG1579    161 LEAEREELaAKIPPE 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 171-380 3.42e-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: 3.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  171 RDIREAMAQKED----MEERITTLEKRYLSAQRestsIHDMNDKLENelANKEAILRQMEEKNRQLqERLELAEQKLQQT 246
Cdd:TIGR02168  182 ERTRENLDRLEDilneLERQLKSLERQAEKAER----YKELKAELRE--LELALLVLRLEELREEL-EELQEELKEAEEE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  247 MRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL------ 319
Cdd:TIGR02168  255 LEELTAeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELesklde 334

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  320 ----LTESNERLQLhLKERMAALEEKnvlIQESETFRKNLEESLHDKErlaEEIEKLRSELDQLK 380
Cdd:TIGR02168  335 laeeLAELEEKLEE-LKEELESLEAE---LEELEAELEELESRLEELE---EQLETLRSKVAQLE 392
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
115-405 4.80e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.45  E-value: 4.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  115 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 194
Cdd:COG4372     45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  195 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaetlpevEAELAQRIAALTKAEERH 274
Cdd:COG4372    125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKEANRN 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  275 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKN 354
Cdd:COG4372    196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462535324  355 LEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELRYS 405
Cdd:COG4372    276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 40-388 4.92e-08

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 57.29  E-value: 4.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   40 ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMepgQKVHEKRLSNgsidstdetsQIVE 119
Cdd:TIGR00618  212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQ---LRARIEELRA----------QEAV 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  120 LQELLEKQNYemAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEkrylSAQR 199
Cdd:TIGR00618  279 LEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ----TLHS 352

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  200 ESTSIHDMNDKlenELANKEAILRQMEEKN--RQLQERLELAEQKLQQTMRKAETLPE----VEAELAQRIAALTKAEER 273
Cdd:TIGR00618  353 QEIHIRDAHEV---ATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQReqatIDTRTSAFRDLQGQLAHA 429

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  274 HGNIEERMRHLEGQ----------LEEKNQELQRARQR---EKMNEEHNKRLSDTVDRLLTESNERLQLH------LKER 334
Cdd:TIGR00618  430 KKQQELQQRYAELCaaaitctaqcEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKAVVLARLLELqeepcpLCGS 509

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462535324  335 MAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:TIGR00618  510 CIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 4-386 5.26e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 57.44  E-value: 5.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324    4 VKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERL---RVSLER----VSAL-------EEELAAANQEIVALREQ 69
Cdd:pfam15921  446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTLESsertVSDLtaslqekERAIEATNAEITKLRSR 525

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   70 nvhIQRKMASSEG-STESEHLEGMEPGQKVHEKRLSngsidstdETSQIVE-LQELLEKQNYEMAQMKERLAALSSRVGE 147
Cdd:pfam15921  526 ---VDLKLQELQHlKNEGDHLRNVQTECEALKLQMA--------EKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQ 594

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  148 VEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE 227
Cdd:pfam15921  595 LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  228 KNRQLQERLELAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNE 306
Cdd:pfam15921  675 DYEVLKRNFRNKSEEMETTTNKLKMqLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLE 754

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  307 EhnkrlsdtvdrLLTESNerlqlhlKERMAALEEKNVLIQESETFRKnleeslhDKERLAEEIEKLRSELDQLKMRTGSL 386
Cdd:pfam15921  755 E-----------AMTNAN-------KEKHFLKEEKNKLSQELSTVAT-------EKNKMAGELEVLRSQERRLKEKVANM 809
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 225-380 5.29e-08

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 54.93  E-value: 5.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  225 MEEKNRQLqERLELAEQKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARq 300
Cdd:COG1579      2 MPEDLRAL-LDLQELDSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  301 rEKMNEEHNKRLSDTVDR---LLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESL-HDKERLAEEIEKLRSEL 376
Cdd:COG1579     80 -EQLGNVRNNKEYEALQKeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELeEKKAELDEELAELEAEL 158


                   ....
gi 2462535324  377 DQLK 380
Cdd:COG1579    159 EELE 162
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 16-380 5.77e-08

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: 57.06  E-value: 5.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   16 SEVEVLKALKSLFEHHKALDEKVRERL--RVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGME 93
Cdd:pfam17380  266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   94 PGQKV-----HEKRLSNGSIDSTDETSQIVELQELlEKQNYEMAQMKERlaalssrvgeVEQEAETARKDLIKTEEMntk 168
Cdd:pfam17380  346 RERELerirqEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKNER----------VRQELEAARKVKILEEER--- 411

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  169 yQRDIREAMAQKEDMeerittlekrylsaqrestsihdmndKLENELANKEAILRQMEEKNRQLqERLELAEQKLQQTMr 248
Cdd:pfam17380  412 -QRKIQQQKVEMEQI--------------------------RAEQEEARQREVRRLEEERAREM-ERVRLEEQERQQQV- 462

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  249 kaETLPEVEAELAQRIAALTKAEERHGNIEERMRH-LEGQLEEKnqelqrarqREKMNEEHNKRlsdtvdrlltesnERL 327
Cdd:pfam17380  463 --ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEER---------KQAMIEEERKR-------------KLL 518

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462535324  328 QLHLKERMAALEEKNVLIQESETFRKNLEesLHDKERLAEEIEKLRSELDQLK 380
Cdd:pfam17380  519 EKEMEERQKAIYEEERRREAEEERRKQQE--MEERRRIQEQMRKATEERSRLE 569
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 21-387 6.20e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 56.95  E-value: 6.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   21 LKALKSLFEHHKALDEKVRErlrvSLERVSALEEELAAANQEIVALRE--QNVHIQRKMASSEGSTESEHLEgmepgQKV 98
Cdd:TIGR04523  203 LSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQQEINEKTTeiSNTQTQLNQLKDEQNKIKKQLS-----EKQ 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   99 HEKRLSNGSIDSTdeTSQIVELQELLEKQNYEMAQ--MKErlaaLSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREA 176
Cdd:TIGR04523  274 KELEQNNKKIKEL--EKQLNQLKSEISDLNNQKEQdwNKE----LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  177 MAQKEDME-------ERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 249
Cdd:TIGR04523  348 KKELTNSEsensekqRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE 427

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  250 AETLPEVEAELAQRIAALTKA----EERHGNIEERMRHLEGQ--------------LEEKNQELQRARQREKMNEEHNKR 311
Cdd:TIGR04523  428 IERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQlkvlsrsinkikqnLEQKQKELKSKEKELKKLNEEKKE 507

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  312 LSDTVDRLLTESNErlqlhLKERMAALE----EKNVLIQESETFRKNLEESLhDKERLAEEIEKLRSELDQLKMRTGSLI 387
Cdd:TIGR04523  508 LEEKVKDLTKKISS-----LKEKIEKLEsekkEKESKISDLEDELNKDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLK 581
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 88-379 7.27e-08

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 56.90  E-value: 7.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   88 HLEGMEPGQKVHEKRLSNGSIdSTDETSQIVELQELLEKQNYEMAqmkERLAALSS-RVGEVEQEAETARKDLIKTEEMN 166
Cdd:TIGR00618  100 HRKTEQPEQLYLEQKKGRGRI-LAAKKSETEEVIHDLLKLDYKTF---TRVVLLPQgEFAQFLKAKSKEKKELLMNLFPL 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  167 TKYQRDIREAMAQKEDMEERITTLEKRY----LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK 242
Cdd:TIGR00618  176 DQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ 255

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  243 ------LQQTMRKAETLPEVEAELAQRIAALTKA--EERHGNIEERMRHLEGQLEEKNQELQ-RARQREKMNEEHNKRLS 313
Cdd:TIGR00618  256 lkkqqlLKQLRARIEELRAQEAVLEETQERINRArkAAPLAAHIKAVTQIEQQAQRIHTELQsKMRSRAKLLMKRAAHVK 335

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  314 DTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLH----DKERLAEEIEKLRSELDQL 379
Cdd:TIGR00618  336 QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqQKTTLTQKLQSLCKELDIL 405
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
209-375 7.67e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 7.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  209 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtLPEVEAELA---QRIAALTKAEERHGNIEERMRHLE 285
Cdd:COG4913    620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAeleAELERLDASSDDLAALEEQLEELE 698

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  286 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT-------ESNERLQLHLKERMAALEEKNVLIQESETFRKNLEES 358
Cdd:COG4913    699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDrleaaedLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778

                          170
                   ....*....|....*..
gi 2462535324  359 LHDKERLAEEIEKLRSE 375
Cdd:COG4913    779 RARLNRAEEELERAMRA 795
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 67-379 7.84e-08

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: 56.72  E-value: 7.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   67 REQNVHIQRKMASSEGSTESEHLEGMEPG-QKVH-EKRLSNGSIDSTDETSQIVELQEllEKQNYEMAQMKERLAALSSR 144
Cdd:pfam01576   90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAArQKLQlEKVTTEAKIKKLEEDILLLEDQN--SKLSKERKLLEERISEFTSN 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  145 VGEVEQEAETARKDLIKTEEMNTkyqrDIREAMAQKEDMEERittLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQ 224
Cdd:pfam01576  168 LAEEEEKAKSLSKLKNKHEAMIS----DLEERLKKEEKGRQE---LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  225 MEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK------NQE 294
Cdd:pfam01576  241 KEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldttaaQQE 320

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  295 LQRARQRE--------------------KMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKNVLI--------- 345
Cdd:pfam01576  321 LRSKREQEvtelkkaleeetrsheaqlqEMRQKHTQALEELTEQL--EQAKRNKANLEKAKQALESENAELqaelrtlqq 398

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2462535324  346 --QESETFRKNLEESLHD-----------KERLAEEIEKLRSELDQL 379
Cdd:pfam01576  399 akQDSEHKRKKLEGQLQElqarlseserqRAELAEKLSKLQSELESV 445
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 877-932 8.17e-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: 50.37  E-value: 8.17e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535324   877 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 932
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 39-374 9.08e-08

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 56.50  E-value: 9.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   39 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTE---------SEHLEGMEPGQKVHEKrlsngsID 109
Cdd:COG3096    277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESdleqdyqaaSDHLNLVQTALRQQEK------IE 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  110 STDEtsQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEERITT 189
Cdd:COG3096    351 RYQE--DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL-------ADYQQALDVQQTRAIQYQQAVQA 421

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  190 LEKrylsaQRESTSIHDMN-DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PEVEAELA-QR 263
Cdd:COG3096    422 LEK-----ARALCGLPDLTpENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVckiaGEVERSQAwQT 496

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  264 IAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKERMAALEEknv 343
Cdd:COG3096    497 ARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----AAEELEELLAELEAQLEE--- 568

                          330       340       350
                   ....*....|....*....|....*....|.
gi 2462535324  344 LIQESETFRKNLEESLHDKERLAEEIEKLRS 374
Cdd:COG3096    569 LEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
116-376 1.03e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.23  E-value: 1.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QIVELQELLEKQNYEMAQMKERLA-ALSSRVGEVEQEAETARKDLIKTEEMNTKyqrdIREAMAQKEDMEERITTLEKRY 194
Cdd:PRK03918   504 QLKELEEKLKKYNLEELEKKAEEYeKLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKEL 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  195 LSAQREStsIHDMNDKLE---------NELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpeveaELAQRIA 265
Cdd:PRK03918   580 EELGFES--VEELEERLKelepfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE-------ELRKELE 650

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  266 ALTK--AEERHGNIEERMRHLEGQLEEKNQELqrarqrekmneEHNKRLSDTVDRLLTEsnerlqlhLKERMAALEEKnv 343
Cdd:PRK03918   651 ELEKkySEEEYEELREEYLELSRELAGLRAEL-----------EELEKRREEIKKTLEK--------LKEELEEREKA-- 709

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462535324  344 lIQESEtfrkNLEESLHDKERLAEEIEKLRSEL 376
Cdd:PRK03918   710 -KKELE----KLEKALERVEELREKVKKYKALL 737
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 41-379 1.04e-07

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 56.52  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   41 RLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTE------SEHLEGMEPGQKVHEKRLSNGSIDSTDET 114
Cdd:TIGR00618  529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSiltqcdNRSKEDIPNLQNITVRLQDLTEKLSEAED 608

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  115 SQIVELQELLEKQNYEMAqmKERLAALSSRVGEVEQEAETArkdliKTEEMNTKYQRDIREAMAQKEDMEERitTLEKRY 194
Cdd:TIGR00618  609 MLACEQHALLRKLQPEQD--LQDVRLHLQQCSQELALKLTA-----LHALQLTLTQERVREHALSIRVLPKE--LLASRQ 679

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  195 LSAQRESTSIHDMNDKLEnELANKEAILRQMEE---KNRQLQERLELAEQKLQQTMR-KAETLPEVEAEL-AQRIAALTK 269
Cdd:TIGR00618  680 LALQKMQSEKEQLTYWKE-MLAQCQTLLRELEThieEYDREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKA 758

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  270 AEERHGNIEER----------MRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 339
Cdd:TIGR00618  759 RTEAHFNNNEEvtaalqtgaeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 2462535324  340 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 379
Cdd:TIGR00618  839 EKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
190-382 1.22e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 1.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  190 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 269
Cdd:COG4717     51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  270 AEERHgNIEERMRHLEGQLEE---KNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKErmaaleeknvLIQ 346
Cdd:COG4717    131 YQELE-ALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----------LAE 199

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462535324  347 ESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 382
Cdd:COG4717    200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
197-384 1.53e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.82  E-value: 1.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  197 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 276
Cdd:PRK02224   197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  277 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH-------------LKERMAALEE 340
Cdd:PRK02224   277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedrDEELRDRLEECrvaaqahneeaesLREDADDLEE 356

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462535324  341 KNVLIQE-SETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTG 384
Cdd:PRK02224   357 RAEELREeAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 52-385 1.60e-07

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: 55.60  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   52 LEEELAAANQEIVALREQNvhiqrkmaSSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEM 131
Cdd:pfam10174  441 LEEALSEKERIIERLKEQR--------EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSG 512

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  132 AQMKERLAALssrvgevEQEAETARKDLIKTEEMNTKYQrDIREAMAQKEDMEERITTLEKRYLSAQRESTsihdmndKL 211
Cdd:pfam10174  513 LKKDSKLKSL-------EIAVEQKKEECSKLENQLKKAH-NAEEAVRTNPEINDRIRLLEQEVARYKEESG-------KA 577

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  212 ENELANKEAILRQME----EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTkaEERHGNIEERMR-HLEG 286
Cdd:pfam10174  578 QAEVERLLGILREVEneknDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLL--EEARRREDNLADnSQQL 655

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  287 QLEEKNQELQRARQREkmnEEHNKRLSDTV------DRLLTESNERLQLHLKERM--------AALEEKNVLIQEsetfr 352
Cdd:pfam10174  656 QLEELMGALEKTRQEL---DATKARLSSTQqslaekDGHLTNLRAERRKQLEEILemkqeallAAISEKDANIAL----- 727

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 2462535324  353 knLEESLHDKERLAEEIEKLRSELD----QLKMRTGS 385
Cdd:pfam10174  728 --LELSSSKKKKTQEEVMALKREKDrlvhQLKQQTQN 762
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 119-373 1.67e-07

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: 55.82  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  119 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQkEDMEERITTLEKRYLSAQ 198
Cdd:TIGR00606  574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSS 652

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  199 RESTSIH---DMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELA----QRIAALTKA 270
Cdd:TIGR00606  653 KQRAMLAgatAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKkkekRRDEMLGLA 732

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  271 EERHGNIEERMRHLEgQLEEKNQELQRARQREKMNEEHNKRLSDTV-------DRLLTESN--ERLQLHLKERMAALEEK 341
Cdd:TIGR00606  733 PGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTImpeeesaKVCLTDVTimERFQMELKDVERKIAQQ 811

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462535324  342 NVLIQESE------TFRKNLEESLHDKERLAEEIEKLR 373
Cdd:TIGR00606  812 AAKLQGSDldrtvqQVNQEKQEKQHELDTVVSKIELNR 849
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
131-339 2.08e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.16  E-value: 2.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  131 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREStsihdmnDK 210
Cdd:COG4717     48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-------EK 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  211 LENELANKEAI--LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN-IEERMRHLEGQ 287
Cdd:COG4717    121 LEKLLQLLPLYqeLEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLaTEEELQDLAEE 200

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  288 LEEKNQELQRARQREKMNEEHNKRLSDTVDRLlteSNERLQLHLKERMAALE 339
Cdd:COG4717    201 LEELQQRLAELEEELEEAQEELEELEEELEQL---ENELEAAALEERLKEAR 249
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
116-300 3.19e-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: 3.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QIVELQELLEKQNyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEmnTKYQRDIREAMAQKEDMEERITTLEKRYL 195
Cdd:COG4913    250 QIELLEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLEARLDALREELD 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  196 SAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQkLQQTMRKAE-TLPEVEAELAQRI----AALTKA 270
Cdd:COG4913    327 ELEAQ---------IRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRaeaaALLEAL 396

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462535324  271 EERHGNIEERMRHLEGQLEEKNQELQRARQ 300
Cdd:COG4913    397 EEELEALEEALAEAEAALRDLRRELRELEA 426
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
115-436 3.23e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 54.66  E-value: 3.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  115 SQIVELQELLEKQNYEMAQMKERLAALSSRVGE----------VEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 184
Cdd:PRK02224   213 SELAELDEEIERYEEQREQARETRDEADEVLEEheerreeletLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  185 ERITtlekrylsaqrestsihDMNDKLENELANKEAILRQMEE---KNRQLQERLELAEQKLQQTMRKAETLPEVEAELA 261
Cdd:PRK02224   293 EERD-----------------DLLAEAGLDDADAEAVEARREEledRDEELRDRLEECRVAAQAHNEEAESLREDADDLE 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  262 QRIAAL-TKAEERHGNIE---ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrLLTESNERLQLHLKERMAA 337
Cdd:PRK02224   356 ERAEELrEEAAELESELEearEAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE-ELREERDELREREAELEAT 434

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  338 LEEKNVLIQESETFR---------KNLEESLH---------DKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTS 399
Cdd:PRK02224   435 LRTARERVEEAEALLeagkcpecgQPVEGSPHvetieedreRVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERL 514

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 2462535324  400 AELRYSVGSLVDsqsDYRTTKVIRRPRRGRMGVRRDE 436
Cdd:PRK02224   515 EERREDLEELIA---ERRETIEEKRERAEELRERAAE 548
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
91-380 3.34e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.75  E-value: 3.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   91 GMEPGQKVHEKRLSNGSIdSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ 170
Cdd:COG4372      1 GDRLGEKVGKARLSLFGL-RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  171 RDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 250
Cdd:COG4372     80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  251 ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH 330
Cdd:COG4372    160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462535324  331 LKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 380
Cdd:COG4372    240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
52-282 3.55e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 54.25  E-value: 3.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   52 LEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgQKVHEKRLSNGSIDSTDET----SQIVELQELLEKQ 127
Cdd:COG3206    166 LELRREEARKALEFLEEQLPELRKELEEAE--------------AALEEFRQKNGLVDLSEEAklllQQLSELESQLAEA 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  128 NYEMAQMKERLAALSSRVGEVEQEAETARKDlikteEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsIHDM 207
Cdd:COG3206    232 RAELAEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAAL 303

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  208 NDKLENELankEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMR 282
Cdd:COG3206    304 RAQLQQEA---QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
115-403 4.36e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 4.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  115 SQIVELQELLEKQNYEMAQMKERLAALSSRvGEVEQEAETARKDLIKTEEmntkYQRDIREAMAQKED----------ME 184
Cdd:COG4913    617 AELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVAS----AEREIAELEAELERldassddlaaLE 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  185 ERITTLEKRYlsaqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRI 264
Cdd:COG4913    692 EQLEELEAEL--------------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERF 755

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  265 AALtKAEERHGNIEERmrhLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDRLLT--ESNERLQLHLK----ERMAA 337
Cdd:COG4913    756 AAA-LGDAVERELREN---LEERIDALRARLNRAEEElERAMRAFNREWPAETADLDAdlESLPEYLALLDrleeDGLPE 831

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535324  338 LEEK--NVLIQESETFRKNLEESLHDKERLAEE-IEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELR 403
Cdd:COG4913    832 YEERfkELLNENSIEFVADLLSKLRRAIREIKErIDPLNDSLKRIPFGPGRYLRLEARPRPDPEVREFR 900
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 955-1026 4.72e-07

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.06  E-value: 4.72e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324   955 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1026
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
PTZ00121 PTZ00121
MAEBL; Provisional
 28-371 5.04e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 5.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   28 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSteseHLEGMEPGQKVHEKRLSNgS 107
Cdd:PTZ00121  1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA----HFARRQAAIKAEEARKAD-E 1282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  108 IDSTDETSQIVELQELLEKQNYE----MAQMKERLAALSSRVGEVEQEAETARKdliKTEEMNTKYQRDIREAMAQKEDM 183
Cdd:PTZ00121  1283 LKKAEEKKKADEAKKAEEKKKADeakkKAEEAKKADEAKKKAEEAKKKADAAKK---KAEEAKKAAEAAKAEAEAAADEA 1359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  184 EERITTLEKRYLSAQRESTSIHDMNDKLEnELANKEAILRQMEEKNRQLQE--RLELAEQKLQQTMRKAETLPEVEaELA 261
Cdd:PTZ00121  1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKADEAKKKAEEDKKKADElkKAAAAKKKADEAKKKAEEKKKAD-EAK 1437

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  262 QRIAALTKAEERHGNIEERMRHLEgqLEEKNQELQRARQREKMNEEhnKRLSDTVDRLLTESNERLQlhlkERMAALEEK 341
Cdd:PTZ00121  1438 KKAEEAKKADEAKKKAEEAKKAEE--AKKKAEEAKKADEAKKKAEE--AKKADEAKKKAEEAKKKAD----EAKKAAEAK 1509

                          330       340       350
                   ....*....|....*....|....*....|
gi 2462535324  342 nvliQESETFRKNLEESLHDKERLAEEIEK 371
Cdd:PTZ00121  1510 ----KKADEAKKAEEAKKADEAKKAEEAKK 1535
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
17-304 6.00e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.62  E-value: 6.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   17 EVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEgmepgQ 96
Cdd:COG4717    169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-----E 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   97 KVHEKRLS-------------NGSIDSTDETSQ---------IVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAET 154
Cdd:COG4717    244 RLKEARLLlliaaallallglGGSLLSLILTIAgvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  155 ARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKnRQLQE 234
Cdd:COG4717    324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKE 402

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535324  235 RLELAEQKLQQ------TMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE--EKNQELQRARQREKM 304
Cdd:COG4717    403 ELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEE 480
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 100-371 6.74e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 53.49  E-value: 6.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  100 EKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAEtarkdliKTEEMNTKYQRDIREAMAQ 179
Cdd:TIGR04523  348 KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-------NQEKLNQQKDEQIKKLQQE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  180 KEDMEERITTLEKRYLSAQREstsIHDmndkLENELANKEAILRQMEEKNRQLQERLEL-------AEQKLQQTMR---- 248
Cdd:TIGR04523  421 KELLEKEIERLKETIIKNNSE---IKD----LTNQDSVKELIIKNLDNTRESLETQLKVlsrsinkIKQNLEQKQKelks 493

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  249 ---KAETLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQEL-QRARQREKMNEEHNKRLSDTVDRLLTESN 324
Cdd:TIGR04523  494 kekELKKLNEEKKELEEKVKDLTK---KISSLKEKIEKLESEKKEKESKIsDLEDELNKDDFELKKENLEKEIDEKNKEI 570

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2462535324  325 ERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEK 371
Cdd:TIGR04523  571 EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 109-383 8.00e-07

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 53.64  E-value: 8.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  109 DSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIR-------EAMAQKE 181
Cdd:pfam01576  216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLEseraarnKAEKQRR 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  182 DMEERI------------TTLEKRYLSAQREsTSIHDMNDKLENELANKEAILRQMEEKNRQ----LQERLELAEQKLQQ 245
Cdd:pfam01576  296 DLGEELealkteledtldTTAAQQELRSKRE-QEVTELKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQAKRNKAN 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  246 TMRKAETLPEVEAELAQRIAALTKAEerhGNIEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNK-------------- 310
Cdd:pfam01576  375 LEKAKQALESENAELQAELRTLQQAK---QDSEHKRKKLEGQLQELQARLSESeRQRAELAEKLSKlqselesvssllne 451

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  311 ------RLSDTVDRL---LTESNERLQ------LHLKERMAALEEknvliqESETFRKNLEESLHDKERLAEEIEKLRSE 375
Cdd:pfam01576  452 aegkniKLSKDVSSLesqLQDTQELLQeetrqkLNLSTRLRQLED------ERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525


                   ....*...
gi 2462535324  376 LDQLKMRT 383
Cdd:pfam01576  526 LSDMKKKL 533
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 24-381 9.16e-07

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 53.26  E-value: 9.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   24 LKSLFEHHKALDEKVRERLRVSLERVSALEEEL------AAANQEIVALREQNVHIQRKMASSEGstesehlegmepgqK 97
Cdd:pfam01576  276 LQEDLESERAARNKAEKQRRDLGEELEALKTELedtldtTAAQQELRSKREQEVTELKKALEEET--------------R 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   98 VHEKRLSNGSIDstdETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETarkdlIKTEEMNTKYQRDIREAM 177
Cdd:pfam01576  342 SHEAQLQEMRQK---HTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRT-----LQQAKQDSEHKRKKLEGQ 413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  178 AQKedmeerittLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaETLPEve 257
Cdd:pfam01576  414 LQE---------LQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ---ELLQE-- 479

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  258 aELAQRIAALTKAEErhgnIEERMRHLEGQLEEknqELQRARQREKMNEEHNKRLSDTVDRLLTESnerlqlhlkERMAA 337
Cdd:pfam01576  480 -ETRQKLNLSTRLRQ----LEDERNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDA---------GTLEA 542

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2462535324  338 LEE-KNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKM 381
Cdd:pfam01576  543 LEEgKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLV 587
PRK12704 PRK12704
phosphodiesterase; Provisional
 214-371 9.61e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.86  E-value: 9.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  214 ELANKEAIlRQMEEKNRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 293
Cdd:PRK12704    34 KEAEEEAK-RILEEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  294 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEtfrknlEESLHDKERLAEEIE 370
Cdd:PRK12704   111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179


                   .
gi 2462535324  371 K 371
Cdd:PRK12704   180 E 180
PTZ00121 PTZ00121
MAEBL; Provisional
 87-371 1.34e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   87 EHLEGMEPGQKVHEKRLSNGSIDSTDET-----SQIVELQELL-EKQNYEMAQMKErlaalsSRVGEVEQEAETARKDLI 160
Cdd:PTZ00121  1031 ELTEYGNNDDVLKEKDIIDEDIDGNHEGkaeakAHVGQDEGLKpSYKDFDFDAKED------NRADEATEEAFGKAEEAK 1104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  161 KTEEMNTKYQRDIREAMAQKEDMeerittlekRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKnRQLQERLELAE 240
Cdd:PTZ00121  1105 KTETGKAEEARKAEEAKKKAEDA---------RKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA-RKAEEARKAED 1174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  241 QKLQQTMRKAETLPEVE----AELAQRIAALTKAEERHgNIEERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTV 316
Cdd:PTZ00121  1175 AKKAEAARKAEEVRKAEelrkAEDARKAEAARKAEEER-KAEEARKAED---AKKAEAVKKAEEAKKDAEEAKKAEEERN 1250

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535324  317 DRLLTESNERLQLHLKERMAAL--EEKnvliQESETFRKNLEESLHDKERLAEEIEK 371
Cdd:PTZ00121  1251 NEEIRKFEEARMAHFARRQAAIkaEEA----RKADELKKAEEKKKADEAKKAEEKKK 1303
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
39-418 1.45e-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: 1.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   39 RERLRVSLERVSALEEELAAANQEIVALR-EQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE------KRLSNGSIDST 111
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEaELDALQERREALQRLAEYSWDEIDVASAEREIAeleaelERLDASSDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  112 DETSQIVELQEllekqnyEMAQMKERLAALSSRVGEVEQEAETArkdlikteemntkyQRDIREAMAQKEDMEERITTLE 191
Cdd:COG4913    689 ALEEQLEELEA-------ELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLEL 747

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  192 KRYLSAQRESTSIhdmnDKLENELAnkeailRQMEEKNRQLQERLELAEQKLQQTMRKA-ETLPEVEAELAQRIAALTKA 270
Cdd:COG4913    748 RALLEERFAAALG----DAVERELR------ENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLPEY 817

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  271 EERHGNIEERmrhlegQLEEKNQELQRARQR----------EKMNEEHN---KRLsDTVDRLLTESN----ERLQLHLKE 333
Cdd:COG4913    818 LALLDRLEED------GLPEYEERFKELLNEnsiefvadllSKLRRAIReikERI-DPLNDSLKRIPfgpgRYLRLEARP 890

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  334 RmaALEEKNVLIQE-----SETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIepTIPRTHLDTSAELRYSV-G 407
Cdd:COG4913    891 R--PDPEVREFRQElravtSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRARV--LDVRNHLEFDAEEIDREdG 966

                          410
                   ....*....|.
gi 2462535324  408 SLVDSQSDYRT 418
Cdd:COG4913    967 EEVETYSSSGG 977
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
32-388 1.62e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.08  E-value: 1.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   32 KALDEKVRErLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMAS-----------SEGSTESEHLEGMEPGQKVHE 100
Cdd:COG4717     74 KELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKlekllqllplyQELEALEAELAELPERLEELE 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  101 KRLsngsidstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVG-EVEQEAETARKDLIKTEEMNTKYQRDIREAMAQ 179
Cdd:COG4717    153 ERL-----------EELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEE 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  180 KEDMEERITTLEKRYLSAQREST---------------SIHDMNDKLENELANKEAIL---------------RQMEEKN 229
Cdd:COG4717    222 LEELEEELEQLENELEAAALEERlkearlllliaaallALLGLGGSLLSLILTIAGVLflvlgllallflllaREKASLG 301

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  230 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRhlegQLEEKNQELQRARQREKMNEEHN 309
Cdd:COG4717    302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR----EAEELEEELQLEELEQEIAALLA 377

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  310 KRLSDTVDRLltesnERLQLHLKERMAALEEKNVLIQESETFRKNLEESL--HDKERLAEEIEKLRSELDQLKMRTGSLI 387
Cdd:COG4717    378 EAGVEDEEEL-----RAALEQAEEYQELKEELEELEEQLEELLGELEELLeaLDEEELEEELEELEEELEELEEELEELR 452


                   .
gi 2462535324  388 E 388
Cdd:COG4717    453 E 453
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
5-380 2.02e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.08  E-value: 2.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324    5 KRQAQSPSGVSSEVEVL-KALKSLFEHHKALDEKVRERLRVSlERVSALEEELAAANQEIVALREQnvhIQRKMASSEGS 83
Cdd:COG4717     60 KPQGRKPELNLKELKELeEELKEAEEKEEEYAELQEELEELE-EELEELEAELEELREELEKLEKL---LQLLPLYQELE 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   84 TESEHLEGMEPGQKVHEKRLSngsidstdetsQIVELQELLEKQNYEMAQMKERLAALSSRVG-EVEQEAETARKDLIKT 162
Cdd:COG4717    136 ALEAELAELPERLEELEERLE-----------ELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEEL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  163 EEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREST---------------SIHDMNDKLENELANKEAIL----- 222
Cdd:COG4717    205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallALLGLGGSLLSLILTIAGVLflvlg 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  223 ----------RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKN 292
Cdd:COG4717    285 llallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  293 QELQRARQREKMNE-------------EHNKRLSDTVDRLlTESNERLQLHLKERMAALE--EKNVLIQESETFRKNLEE 357
Cdd:COG4717    365 LEELEQEIAALLAEagvedeeelraalEQAEEYQELKEEL-EELEEQLEELLGELEELLEalDEEELEEELEELEEELEE 443

                          410       420
                   ....*....|....*....|...
gi 2462535324  358 SLHDKERLAEEIEKLRSELDQLK 380
Cdd:COG4717    444 LEEELEELREELAELEAELEQLE 466
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 35-367 2.08e-06

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 52.36  E-value: 2.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   35 DEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSteSEHLEGMEPGQKVHEKRLSNGSIdstdeT 114
Cdd:TIGR00606  770 QETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTV-----V 842

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  115 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKry 194
Cdd:TIGR00606  843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK-- 920

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  195 lSAQRESTSIHDMNDklENELANKEaiLRQMEEKNRQLQERLELAEQKLQQTmrKAETLPEVEAELAQRIAALTKAEERH 274
Cdd:TIGR00606  921 -DQQEKEELISSKET--SNKKAQDK--VNDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQ 993

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  275 GNIEERMRHLEGQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETF 351
Cdd:TIGR00606  994 EKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVL 1072

                          330       340
                   ....*....|....*....|.
gi 2462535324  352 -----RKNLEESLHDKERLAE 367
Cdd:TIGR00606 1073 algrqKGYEKEIKHFKKELRE 1093
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 111-379 2.16e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.94  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  111 TDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT-----------EEMNTKYQRDIReamaQ 179
Cdd:TIGR04523   92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFlteikkkekelEKLNNKYNDLKK----Q 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  180 KEDMEERITTLEKrylsaqrESTSIHDMNDKLENELANKE---AILRQMEEKNRQLQ-ERLELAEQKLQQTmrkaETLPE 255
Cdd:TIGR04523  168 KEELENELNLLEK-------EKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLEsQISELKKQNNQLK----DNIEK 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  256 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRArqrEKMNEEHNKRLSDTVDRLLTESNERLQLHLKERM 335
Cdd:TIGR04523  237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK 313

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2462535324  336 AALEEKNVLIQESETFRKNLEESLhdkERLAEEIEKLRSELDQL 379
Cdd:TIGR04523  314 SELKNQEKKLEEIQNQISQNNKII---SQLNEQISQLKKELTNS 354
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 36-304 2.50e-06

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


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 51.22  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   36 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGS-TESEHlegmepgqkvhekrlsngSIDSTDET 114
Cdd:pfam19220  107 EELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKAlQRAEG------------------ELATARER 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  115 SQIVE-----LQELLEKQNYEmaqmkerLAALSSRVGEVEQEAETARKDLIKTE----EMNTKYQRDIREAMAQKEDMEE 185
Cdd:pfam19220  169 LALLEqenrrLQALSEEQAAE-------LAELTRRLAELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRA 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  186 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQ-------LQERLELAEQKLQQTMRKAETLPEVEA 258
Cdd:pfam19220  242 ERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEasierdtLERRLAGLEADLERRTQQFQEMQRARA 321

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535324  259 ELAQRI-----------AALTKAEERHGNIEERMRHLEGQ-------LEEKNQELQRARQREKM 304
Cdd:pfam19220  322 ELEERAemltkalaakdAALERAEERIASLSDRIAELTKRfeveraaLEQANRRLKEELQRERA 385
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 33-318 2.57e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   33 ALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNvhiqrKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTD 112
Cdd:COG1196    543 ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD-----KIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  113 ETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEK 192
Cdd:COG1196    618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  193 RYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE 272
Cdd:COG1196    698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  273 RHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDR 318
Cdd:COG1196    778 ALGPVnllaieeyeelEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 173-340 2.64e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.92  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  173 IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAeqklqQTMRKAET 252
Cdd:COG1579     19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----RNNKEYEA 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  253 LpevEAELAQriaaltkAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLK 332
Cdd:COG1579     94 L---QKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163


                   ....*...
gi 2462535324  333 ERMAALEE 340
Cdd:COG1579    164 EREELAAK 171
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-298 3.40e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 3.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324    3 VVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEG 82
Cdd:COG1196    293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   83 STESEhlegmepgqkvhEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT 162
Cdd:COG1196    373 ELAEA------------EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  163 EEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK 242
Cdd:COG1196    441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535324  243 LQQtmRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 298
Cdd:COG1196    521 GLA--GAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 21-382 3.96e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 3.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   21 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE 100
Cdd:COG1196    402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  101 KRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGE---VEQEAETARKDLIKTEEMNTKYQRDIREAM 177
Cdd:COG1196    482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVligVEAAYEAALEAALAAALQNIVVEDDEVAAA 561

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  178 A---QKEDMEERITTLEKRyLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 254
Cdd:COG1196    562 AieyLKAAKAGRATFLPLD-KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  255 EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQRE-KMNEEHNKRLSDTVDRLLTESNERLQLHLKE 333
Cdd:COG1196    641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLaEEELELEEALLAEEEEERELAEAEEERLEEE 720

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  334 RMAALEEKNVLIQESETFRKNLEESLHDKERLAEE------IEKLRSELDQLKMR 382
Cdd:COG1196    721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEElpeppdLEELERELERLERE 775
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 112-376 4.18e-06

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 51.13  E-value: 4.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  112 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVE----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 187
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlqelKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  188 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA- 266
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKe 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  267 ----LTKAEERHGNIEERMRHLEGQLEEKN---QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 339
Cdd:pfam02463  319 sekeKKKAEKELKKEKEEIEELEKELKELEikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2462535324  340 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSEL 376
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 877-928 5.37e-06

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 44.54  E-value: 5.37e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  877 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 928
Cdd:cd09487      4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 116-388 5.52e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.40  E-value: 5.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK----------EDMEE 185
Cdd:TIGR04523  132 QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsnlKKKIQ 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  186 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAI-------LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 258
Cdd:TIGR04523  212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEisntqtqLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  259 ELAQRIAALTKAEERH---------GNIEERMRHLEGQLEEKNQELQRARQ------REKMNEEHNKRlsdTVDRLLTES 323
Cdd:TIGR04523  292 QLKSEISDLNNQKEQDwnkelkselKNQEKKLEEIQNQISQNNKIISQLNEqisqlkKELTNSESENS---EKQRELEEK 368

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535324  324 NERLQLHLKERMAALEEKNVL----------IQESETFRKNLEESLH----DKERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:TIGR04523  369 QNEIEKLKKENQSYKQEIKNLesqindleskIQNQEKLNQQKDEQIKklqqEKELLEKEIERLKETIIKNNSEIKDLTN 447
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 172-349 5.62e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 5.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  172 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA- 250
Cdd:COG3883     17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALy 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  251 ---ETLPEVEA--------ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL 319
Cdd:COG3883     97 rsgGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462535324  320 LTESNERLQLHLKERMAALEEKNVLIQESE 349
Cdd:COG3883    177 QAEQEALLAQLSAEEAAAEAQLAELEAELA 206
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 132-380 6.59e-06

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 50.12  E-value: 6.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  132 AQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRylsaqrestsihdmndkl 211
Cdd:pfam05557    2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKR------------------ 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  212 eneLANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgnieermrhlEGQLEEK 291
Cdd:pfam05557   64 ---EAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA----------ELELQST 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  292 NQELQRARQRekmNEEHNKRLSDtvdrlLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAeEIEK 371
Cdd:pfam05557  131 NSELEELQER---LDLLKAKASE-----AEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELA-RIPE 201


                   ....*....
gi 2462535324  372 LRSELDQLK 380
Cdd:pfam05557  202 LEKELERLR 210
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 37-380 6.69e-06

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 50.24  E-value: 6.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   37 KVRERLRVSLERVSALEEELAAANQEIVALREQNvhiqrkmasSEGSTESEHLEGM--EPGQKVHEKRLSNG-SIDSTDE 113
Cdd:pfam06160   83 KAKKALDEIEELLDDIEEDIKQILEELDELLESE---------EKNREEVEELKDKyrELRKTLLANRFSYGpAIDELEK 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  114 T-----SQIVELQELLEKQNYEMA-----QMKERLAALSSRVGEVEQEAETARKDLikTEEMNtkyqrDIREAMAQkedM 183
Cdd:pfam06160  154 QlaeieEEFSQFEELTESGDYLEArevleKLEEETDALEELMEDIPPLYEELKTEL--PDQLE-----ELKEGYRE---M 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  184 EERITTLEkrYLSAQRESTSIHDMNDKLENELANKEaiLRQMEEKNRQLQERLElaeqKLQQTMRKaetlpEVEAELaqr 263
Cdd:pfam06160  224 EEEGYALE--HLNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERID----QLYDLLEK-----EVDAKK--- 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  264 iaaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEH-------NKRLsDTVDRLLTESNERLQLH------ 330
Cdd:pfam06160  288 -----YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENElervrglEKQL-EELEKRYDEIVERLEEKevayse 361

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  331 LKERMAALEEKNVLIQES-ETFRKNLeESLHDKERLA-EEIEKLRSELDQLK 380
Cdd:pfam06160  362 LQEELEEILEQLEEIEEEqEEFKESL-QSLRKDELEArEKLDEFKLELREIK 412
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 23-295 7.01e-06

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 50.21  E-value: 7.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   23 ALKSLFEhhkALDEKVR--ERLRVSLERVS-ALEEELAAANQEIVALREQNVHIQRKMASSEGSTES--EHLEGMEPGQK 97
Cdd:pfam10174  437 ALTTLEE---ALSEKERiiERLKEQREREDrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDlkEHASSLASSGL 513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   98 VHEKRLSNGSIDSTDETSQIVELQELLEK-QNYEMAQMKErlAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREA 176
Cdd:pfam10174  514 KKDSKLKSLEIAVEQKKEECSKLENQLKKaHNAEEAVRTN--PEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREV 591

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  177 MAQKEDMEERITTLEKRYLSaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEV 256
Cdd:pfam10174  592 ENEKNDKDKKIAELESLTLR-QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQE 670

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2462535324  257 EAELAQRIAALTKA-EERHGNIE----ERMRHLEGQLEEKNQEL 295
Cdd:pfam10174  671 LDATKARLSSTQQSlAEKDGHLTnlraERRKQLEEILEMKQEAL 714
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 45-249 7.65e-06

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


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 47.98  E-value: 7.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   45 SLERVSALEEELAAANQEIVALREQNVHIQRKmassegstesehlegmepgQKVHEKRLSNgsIDSTDEtsqivELQELL 124
Cdd:pfam15619    9 RLHKIKELQNELAELQSKLEELRKENRLLKRL-------------------QKRQEKALGK--YEGTES-----ELPQLI 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  125 EKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREA-MAQKEDMEERITTLEKRYLSAQREsts 203
Cdd:pfam15619   63 ARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDKDEK--- 139

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462535324  204 IHDMNDKLEN-------ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 249
Cdd:pfam15619  140 IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 33-376 1.13e-05

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: 49.84  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   33 ALDEKVRERLRV-------SLERVSALEEELAAANqeiVALREQNVHIQRKMASSEGSTES-EHLEGMEPGQKVHEKRLS 104
Cdd:pfam12128  597 ASEEELRERLDKaeealqsAREKQAAAEEQLVQAN---GELEKASREETFARTALKNARLDlRRLFDEKQSEKDKKNKAL 673

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  105 NGSIDSTDETSQIVELQE--LLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK---DLIKTEEMNTKYQRDiREAMAQ 179
Cdd:pfam12128  674 AERKDSANERLNSLEAQLkqLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDaqlALLKAAIAARRSGAK-AELKAL 752

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  180 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQmeekNRQLQERLELAEQKLQQTMRKAET-LPEVEA 258
Cdd:pfam12128  753 ETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY----FDWYQETWLQRRPRLATQLSNIERaISELQQ 828

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  259 ELAQRIAaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHnkrlsdtvdrlLTESNERLQLHLKERMAA 337
Cdd:pfam12128  829 QLARLIA---DTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGERLAQ 894

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2462535324  338 LEE-KNVLIQESETFRKNLEE-----SLHDKERLAEEIEKLRSEL 376
Cdd:pfam12128  895 LEDlKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 15-341 1.30e-05

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 49.33  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   15 SSEVEVLKALKSLFEHHKALDEKvrerlrvslERVSALEEELAAANQEIVAL---REQNVH---IQ------------RK 76
Cdd:pfam05483  402 NKEVELEELKKILAEDEKLLDEK---------KQFEKIAEELKGKEQELIFLlqaREKEIHdleIQltaiktseehylKE 472

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   77 MASSEGSTESEHLEGMEPGQKVHEKRLSNGSI--DSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAET 154
Cdd:pfam05483  473 VEDLKTELEKEKLKNIELTAHCDKLLLENKELtqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELES 552

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  155 ARKDLI-----------KTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN--------------- 208
Cdd:pfam05483  553 VREEFIqkgdevkckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqln 632

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  209 ------DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL--------PEVEAELAQRIAALTKAEERH 274
Cdd:pfam05483  633 ayeikvNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIadeavklqKEIDKRCQHKIAEMVALMEKH 712

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  275 GN-----IEERMRHLeGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLL---TESNERLQLHLKERMAALEEK 341
Cdd:pfam05483  713 KHqydkiIEERDSEL-GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLeieKEEKEKLKMEAKENTAILKDK 786
PRK01156 PRK01156
chromosome segregation protein; Provisional
 37-328 1.32e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 49.51  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   37 KVRERLRVSLERVSAleeELAAANQEIVALREQNVHIQRKMASSEGSTESEhLEGMEPGQKVHEKRLSNGSIDSTDETSQ 116
Cdd:PRK01156   409 KELNEINVKLQDISS---KVSSLNQRIRALRENLDELSRNMEMLNGQSVCP-VCGTTLGEEKSNHIINHYNEKKSRLEEK 484

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  117 IVELQELLEKQNYEMAQMKERLAALSSrvGEVEQ------EAETARKDL--IKTEEMNTKYQRDIREAMAQK------ED 182
Cdd:PRK01156   485 IREIEIEVKDIDEKIVDLKKRKEYLES--EEINKsineynKIESARADLedIKIKINELKDKHDKYEEIKNRykslklED 562

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  183 MEERITTLEKryLSAQRESTSIhDMNDKLENELANK----------------------EAILRQMEEKNRQLQERLELAE 240
Cdd:PRK01156   563 LDSKRTSWLN--ALAVISLIDI-ETNRSRSNEIKKQlndlesrlqeieigfpddksyiDKSIREIENEANNLNNKYNEIQ 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  241 QK--LQQTMR-KAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVd 317
Cdd:PRK01156   640 ENkiLIEKLRgKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI- 718

                          330
                   ....*....|.
gi 2462535324  318 rllTESNERLQ 328
Cdd:PRK01156   719 ---NDINETLE 726
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 109-381 1.67e-05

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 49.05  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  109 DSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT-EEMNTKYQrdIREAMAQKEDMEERI 187
Cdd:pfam10174  158 ESIKKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLrEELHRRNQ--LQPDPAKTKALQTVI 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  188 TTLEKRYLSAQRestSIHDMNDKLENELAN-------KEAILRQME----------EKNRQLQERLELAEQKLQQTMRKA 250
Cdd:pfam10174  236 EMKDTKISSLER---NIRDLEDEVQMLKTNgllhtedREEEIKQMEvykshskfmkNKIDQLKQELSKKESELLALQTKL 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  251 ETLPEVEAELAQRI----AALTKAEERHGNIEERMRHLEGQLEEKNQEL-QRARQREKMNEE---------HNKRLSDTV 316
Cdd:pfam10174  313 ETLTNQNSDCKQHIevlkESLTAKEQRAAILQTEVDALRLRLEEKESFLnKKTKQLQDLTEEkstlageirDLKDMLDVK 392

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  317 DR---LLTESNERLQLHLKERMAALEEKNVLIQESETFRKN-------LEESLHDKERLAEEIEKLRSELDQLKM 381
Cdd:pfam10174  393 ERkinVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalttLEEALSEKERIIERLKEQREREDRERL 467
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 212-380 1.79e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  212 ENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK 291
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN---ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  292 NQELQRARQREKMNEE--HNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKnvliqesetfRKNLEESLHDKER 364
Cdd:COG3883     92 ARALYRSGGSVSYLDVllGSESFSDFLDRLsalskIADADADLLEELKADKAELEAK----------KAELEAKLAELEA 161

                          170
                   ....*....|....*.
gi 2462535324  365 LAEEIEKLRSELDQLK 380
Cdd:COG3883    162 LKAELEAAKAELEAQQ 177
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-379 1.84e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324    5 KRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGST 84
Cdd:COG1196    414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   85 ESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKqnYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEE 164
Cdd:COG1196    494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA--YEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  165 -------MNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLE 237
Cdd:COG1196    572 gratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  238 LAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnieermrhlegqLEEKNQELQRARQREKMNEEHNKRLSDTVD 317
Cdd:COG1196    652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER--------------LAEEELELEEALLAEEEEERELAEAEEERL 717

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  318 RLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 379
Cdd:COG1196    718 EEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 202-312 2.19e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 48.67  E-value: 2.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  202 TSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGN 276
Cdd:PRK00409   509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462535324  277 IEERMRHLE--GQLEEKNQELQRARQR-EKMNEEHNKRL 312
Cdd:PRK00409   589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 19-200 2.29e-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: 47.23  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   19 EVLKALKSLFEHHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKV 98
Cdd:COG1579      4 EDLRALLDLQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE-----LEIEEVEARIKK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   99 HEKRLsnGSIDSTDEtsqivelQELLEKqnyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMA 178
Cdd:COG1579     78 YEEQL--GNVRNNKE-------YEALQK---EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145

                          170       180
                   ....*....|....*....|..
gi 2462535324  179 QKEDMEERITTLEKRyLSAQRE 200
Cdd:COG1579    146 ELDEELAELEAELEE-LEAERE 166
PTZ00121 PTZ00121
MAEBL; Provisional
 28-375 2.80e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   28 FEHHKALDEKVRERLRVSLERVSALEEELAAANQeivALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGS 107
Cdd:PTZ00121  1093 TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAED---ARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA 1169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  108 iDSTDETSQIVELQELLE-KQNYEMAQMKERLAALSSRVGEVEQEAETARK--DLIKTEEMNTKYQRDIREAMAQKEDmE 184
Cdd:PTZ00121  1170 -RKAEDAKKAEAARKAEEvRKAEELRKAEDARKAEAARKAEEERKAEEARKaeDAKKAEAVKKAEEAKKDAEEAKKAE-E 1247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  185 ERITTLEKRYLSAQRESTSIHDMNDKLENelANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI 264
Cdd:PTZ00121  1248 ERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  265 AALTKAEERHGNIEERMRHLE---GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNE-RLQLHLKERMAALEE 340
Cdd:PTZ00121  1326 EAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkKKADEAKKKAEEDKK 1405

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 2462535324  341 KNVLIQESETFRKNLEESLHDKE--RLAEEIEKLRSE 375
Cdd:PTZ00121  1406 KADELKKAAAAKKKADEAKKKAEekKKADEAKKKAEE 1442
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 120-382 4.25e-05

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.58  E-value: 4.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  120 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 199
Cdd:pfam07888   32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  200 ESTSIHdmndklenelANKEAILRQMEEKNRQLQErLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE-RHGNIE 278
Cdd:pfam07888  109 SSEELS----------EEKDALLAQRAAHEARIRE-LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEaERKQLQ 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  279 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH--LKERMAALEEK-NVLIQESETFR 352
Cdd:pfam07888  178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkLTTAHRKEAENeaLLEELRSLQERlNASERKVEGLG 257

                          250       260       270
                   ....*....|....*....|....*....|
gi 2462535324  353 KNLEESLHDKERLAEEIEKLRSELDQLKMR 382
Cdd:pfam07888  258 EELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 21-380 4.61e-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: 47.66  E-value: 4.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   21 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEelaaaNQEIVALREQNVHIQRKMASSEGSTESEhLEGMEPGQKVHE 100
Cdd:TIGR00618  468 LKEREQQLQTKEQIHLQETRKKAVVLARLLELQE-----EPCPLCGSCIHPNPARQDIDNPGPLTRR-MQRGEQTYAQLE 541

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  101 KRLSNGSIDSTDETSQIVELQEllekqnyEMAQMKERLAALSSRVGEVEQEAETARK---DLIKTEEMNTKYQRDIREAM 177
Cdd:TIGR00618  542 TSEEDVYHQLTSERKQRASLKE-------QMQEIQQSFSILTQCDNRSKEDIPNLQNitvRLQDLTEKLSEAEDMLACEQ 614

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  178 -AQKEDMEERITTLEKRYLS---AQRESTSIHDMNDKLENELANKEAI-LRQMEEKNRQLQERLELAEQKLQQtmrKAET 252
Cdd:TIGR00618  615 hALLRKLQPEQDLQDVRLHLqqcSQELALKLTALHALQLTLTQERVREhALSIRVLPKELLASRQLALQKMQS---EKEQ 691

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  253 LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRarQREKMNEEHNK--RLSDTVDRLLTESNERLQLH 330
Cdd:TIGR00618  692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA--REDALNQSLKElmHQARTVLKARTEAHFNNNEE 769

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462535324  331 LKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 380
Cdd:TIGR00618  770 VTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 21-254 4.81e-05

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: 47.07  E-value: 4.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   21 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHE 100
Cdd:COG4942     29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE-----KEIAELRAELEAQK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  101 KRLSNgSIDSTDETSQIVELQELLEKQNyeMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK 180
Cdd:COG4942    104 EELAE-LLRALYRLGRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535324  181 EDMEERITTLEKryLSAQRESTSihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 254
Cdd:COG4942    181 AELEEERAALEA--LKAERQKLL-----ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
PRK12705 PRK12705
hypothetical protein; Provisional
 230-427 5.08e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.40  E-value: 5.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  230 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegqlEEKNQELQRARQREKMNEEHN 309
Cdd:PRK12705    26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  310 KRLSDTVDRLLTESN----ERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHD--KERLAEEIEKLRSELD-QLKMR 382
Cdd:PRK12705    98 EKLDNLENQLEEREKalsaRELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAelEEEKAQRVKKIEEEADlEAERK 177

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462535324  383 TGSLIEPTIPRTHLDTSAELRYSVgslVDSQSDYRTTKVIRRPRR 427
Cdd:PRK12705   178 AQNILAQAMQRIASETASDLSVSV---VPIPSDAMKGRIIGREGR 219
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 137-396 5.14e-05

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 47.16  E-value: 5.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  137 RLAALSSRVGEVEQEAET-----ARKDLIKTEEMNTKYQRDIR-------EAMAQKEDMEERITTLEKRY------LSAQ 198
Cdd:pfam06160   61 SLPDIEELLFEAEELNDKyrfkkAKKALDEIEELLDDIEEDIKqileeldELLESEEKNREEVEELKDKYrelrktLLAN 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  199 RES--TSIhdmnDKLENELANKEAILRQMEEKN--------RQLQERLELAEQKLQQTMRK--------AETLPEVEAEL 260
Cdd:pfam06160  141 RFSygPAI----DELEKQLAEIEEEFSQFEELTesgdyleaREVLEKLEEETDALEELMEDipplyeelKTELPDQLEEL 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  261 AQRIAALTKAEER--HGNIEERMRHLEGQLEE-----KNQELQRArqrEKMNEEHNKRLSDTVDRLLTESNERLQLH--- 330
Cdd:pfam06160  217 KEGYREMEEEGYAleHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVEknl 293

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535324  331 --LKERMAALEEKNVLIQE-----SETFRKNlEESLHDKERLAEEIEKLRSELDQLKMRtgsLIEPTIPRTHL 396
Cdd:pfam06160  294 peIEDYLEHAEEQNKELKEelervQQSYTLN-ENELERVRGLEKQLEELEKRYDEIVER---LEEKEVAYSEL 362
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
119-301 5.22e-05

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 47.38  E-value: 5.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  119 ELQELLEKQNyEMAQMKERL-------AALSSRVGEVEQ-EAEtaRKDLIKTEEMNTKYQRdIREAMAQKED-MEERITT 189
Cdd:COG0497    173 ELEELRADEA-ERARELDLLrfqleelEAAALQPGEEEElEEE--RRRLSNAEKLREALQE-ALEALSGGEGgALDLLGQ 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  190 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQKLQ---QTMRK----AETLPEVEAE 259
Cdd:COG0497    249 ALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdpERLEEVEERLAllrRLARKygvtVEELLAYAEE 328

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462535324  260 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 301
Cdd:COG0497    329 LRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 119-382 6.12e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.45  E-value: 6.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  119 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRE--AMAQKEDMEERITTLE--KRY 194
Cdd:pfam13868   56 ALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEedQAEAEEKLEKQRQLREeiDEF 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  195 LSAQRESTSIHDMNDKLENElANKEAILRQMEEKNRQLQERLELAEQK----------LQQTMRKAETLPEVEAELAQ-- 262
Cdd:pfam13868  136 NEEQAEWKELEKEEEREEDE-RILEYLKEKAEREEEREAEREEIEEEKereiarlraqQEKAQDEKAERDELRAKLYQee 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  263 -----RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAA 337
Cdd:pfam13868  215 qerkeRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRE 294

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2462535324  338 LEEknvLIQESE-TFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 382
Cdd:pfam13868  295 LEK---QIEEREeQRAAEREEELEEGERLREEEAERRERIEEERQK 337
PRK11281 PRK11281
mechanosensitive channel MscK;
180-379 7.59e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 47.21  E-value: 7.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  180 KEDMEERITTLEKRYLSAQRESTSIHDmndkLENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA- 258
Cdd:PRK11281    38 EADVQAQLDALNKQKLLEAEDKLVQQD----LEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  259 ELAQRIAALTkaeerhgnieerMRHLEGQLEEKNQELQRARqrekmneehnKRLSDTVDRLLTESN--ERLQlhlkermA 336
Cdd:PRK11281   113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQ-------A 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2462535324  337 ALEEKNVLIQESETFRKNLEESlhDKERLAEEIEKLRSELDQL 379
Cdd:PRK11281   164 ALYANSQRLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQALL 204
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 22-535 8.22e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 8.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   22 KALKSLFEHHKALDEKV---RERLRVSLERVSALEEELAAANQEIVALREQ----NVHIQR---KMASSEGSTESEHLEG 91
Cdd:TIGR02168  344 EKLEELKEELESLEAELeelEAELEELESRLEELEEQLETLRSKVAQLELQiaslNNEIERleaRLERLEDRRERLQQEI 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   92 MEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEM---NTK 168
Cdd:TIGR02168  424 EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqenLEG 503

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  169 YQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIH-----DMNDKL-ENELANKEAI--LRQME-----------EKN 229
Cdd:TIGR02168  504 FSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalggRLQAVVvENLNAAKKAIafLKQNElgrvtflpldsIKG 583

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  230 RQLQERLELAEQKLQQTMRKAETLPEVEAEL-------------------AQRIAALTKAEER-----------HG---- 275
Cdd:TIGR02168  584 TEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyllggvlvvddldnALELAKKLRPGYRivtldgdlvrpGGvitg 663

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  276 -----------------NIEERMRHLEGQLEEKNQELQRARQRekmNEEHNKRLSDtVDRLLTESNERLQLHLKERMAAL 338
Cdd:TIGR02168  664 gsaktnssilerrreieELEEKIEELEEKIAELEKALAELRKE---LEELEEELEQ-LRKELEELSRQISALRKDLARLE 739

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  339 EEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLiEPTIpRTHLDTSAELRYSVGSLvdsQSDYRT 418
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL-EAQI-EQLKEELKALREALDEL---RAELTL 814

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  419 TKviRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIDDDDRE---------TIFSSMDLLSPSG 489
Cdd:TIGR02168  815 LN--EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleseleallNERASLEEALALL 892

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*....
gi 2462535324  490 HSDAQTLAMMLQE---QLDAINKEIRLIQEEKESTELRAEEIENRVASV 535
Cdd:TIGR02168  893 RSELEELSEELRElesKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
mukB PRK04863
chromosome partition protein MukB;
26-312 8.54e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.87  E-value: 8.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   26 SLFEHHKALDEKVR--ERLRVSLERVSALEEELAAA---NQEIVALREQNVHIQRKMASSEGSTE--SEHLEGMEPGQKV 98
Cdd:PRK04863   797 ELAERYATLSFDVQklQRLHQAFSRFIGSHLAVAFEadpEAELRQLNRRRVELERALADHESQEQqqRSQLEQAKEGLSA 876

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   99 HEKRLsnGSIDSTDETSQIVELQELLEkQNYEMAQMKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMA 178
Cdd:PRK04863   877 LNRLL--PRLNLLADETLADRVEEIRE-QLDEAEEAKRFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQDYQQAQQ 949

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  179 QKEDMEERITTL----EKR----YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 250
Cdd:PRK04863   950 TQRDAKQQAFALtevvQRRahfsYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  251 ETLPEVEAELAQRIAALT-----KAEERhgnIEERMRHLEGQL----EEKNQ-ELQRARQREKMNEEhNKRL 312
Cdd:PRK04863  1030 DAKRQMLQELKQELQDLGvpadsGAEER---ARARRDELHARLsanrSRRNQlEKQLTFCEAEMDNL-TKKL 1097
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
265-388 8.65e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.77  E-value: 8.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  265 AALTKAEERHGNIEErmrhlegqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTEsNERLQLHLKERMAALEEknvL 344
Cdd:COG2433    380 EALEELIEKELPEEE---------PEAEREKEHEERELTEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---L 446

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462535324  345 IQESETFRKNLEESLH-DKE--RLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:COG2433    447 ERELSEARSEERREIRkDREisRLDREIERLERELEEERERIEELKR 493
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 747-811 9.54e-05

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 41.49  E-value: 9.54e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  747 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 811
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 119-347 1.02e-04

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


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 45.48  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  119 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKryLSAQ 198
Cdd:pfam06008   27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKE--INEK 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  199 RESTSIHDM---NDKLENELANKEAILRQMeeKNRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRIAALTKAeerhg 275
Cdd:pfam06008  105 VATLGENDFalpSSDLSRMLAEAQRMLGEI--RSRDFGTQLQNAEAEL----KAAQDLLSRIQTWFQSPQEENKA----- 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  276 nIEERMRHLEGQLEEKNQELQ--------RARQREKMNEEHNKRLSDTVDRLLT--ESNERLQLHLKERMAALEEKNVLI 345
Cdd:pfam06008  174 -LANALRDSLAEYEAKLSDLRellreaaaKTRDANRLNLANQANLREFQRKKEEvsEQKNQLEETLKTARDSLDAANLLL 252


                   ..
gi 2462535324  346 QE 347
Cdd:pfam06008  253 QE 254
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
173-380 1.05e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  173 IREAMAQKEDMEERITTLEKRYlsaqresTSIHDMNDKLEnELANKEAILRQMEEKNRQLQE-RLELAEQKLQQTMRKAE 251
Cdd:COG4913    213 VREYMLEEPDTFEAADALVEHF-------DDLERAHEALE-DAREQIELLEPIRELAERYAAaRERLAELEYLRAALRLW 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  252 TLPEVEAELAQRIAALtkaEERHGNIEERMRHLEGQLEEKNQELQRARQRekmneehnkRLSDTVDRL--LTESNERLQL 329
Cdd:COG4913    285 FAQRRLELLEAELEEL---RAELARLEAELERLEARLDALREELDELEAQ---------IRGNGGDRLeqLEREIERLER 352

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535324  330 HLKERMAALEEKNVLIQ--------ESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 380
Cdd:COG4913    353 ELEERERRRARLEALLAalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 36-273 1.09e-04

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: 45.91  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   36 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHEKRLSNGsidstdeTS 115
Cdd:COG4942     23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA-----RRIRALEQELAALEAELAEL-------EK 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QIVELQELLEKQNYEMAQMKeRLAALSSRVGEVEQ--EAETArKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR 193
Cdd:COG4942     91 EIAELRAELEAQKEELAELL-RALYRLGRQPPLALllSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  194 yLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 273
Cdd:COG4942    169 -LEAERA---------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
955-1025 1.11e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.11e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535324  955 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1025
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
pepcterm_ChnLen TIGR03007
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ...
 47-262 1.66e-04

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


Pssm-ID: 274386 [Multi-domain]  Cd Length: 498  Bit Score: 45.43  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   47 ERVSALEEELAAANQEIVALREQNVhiqrkmassegstesehleGMEPGQkvhekrlsngsidSTDETSQIVELQELLEK 126
Cdd:TIGR03007  168 EQIKTYEKKLEAAENRLKAFKQENG-------------------GILPDQ-------------EGDYYSEISEAQEELEA 215

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  127 QNYEMAQMKERLAALSSRVGEVEQEAETARKDLI-----KTEEMNTKYQR----------DIREAMAQKEDMEERITTLE 191
Cdd:TIGR03007  216 ARLELNEAIAQRDALKRQLGGEEPVLLAGSSVANseldgRIEALEKQLDAlrlrytdkhpDVIATKREIAQLEEQKEEEG 295

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535324  192 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqQTMRKAETLPEVEAELAQ 262
Cdd:TIGR03007  296 SAKNGGPERGEIANPVYQQLQIELAEAEAEIASLEARVAELTARIE-------RLESLLRTIPEVEAELTQ 359
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 24-380 1.75e-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: 45.98  E-value: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   24 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEH---LEGMEPGQ-KVH 99
Cdd:pfam12128  324 LEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNnrdIAGIKDKLaKIR 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  100 EKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAalsSRVGE--VEQEAETARKDLIKteemntkyqrDIREAM 177
Cdd:pfam12128  404 EARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLK---SRLGElkLRLNQATATPELLL----------QLENFD 470

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  178 AQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL---- 253
Cdd:pfam12128  471 ERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDweqs 550

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  254 ----------------PEV-----------------------------EAELAQRIAALTKA----EERHGNIEERMRHL 284
Cdd:pfam12128  551 igkvispellhrtdldPEVwdgsvggelnlygvkldlkridvpewaasEEELRERLDKAEEAlqsaREKQAAAEEQLVQA 630

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  285 EGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKERMAALE-EKNVLIQESETF-----RKNL 355
Cdd:pfam12128  631 NGELEKASREETFARTALKNARLDLRRLFDEKQSEkdkKNKALAERKDSANERLNSLEaQLKQLDKKHQAWleeqkEQKR 710

                          410       420
                   ....*....|....*....|....*
gi 2462535324  356 EESLHDKERLAEEIEKLRSELDQLK 380
Cdd:pfam12128  711 EARTEKQAYWQVVEGALDAQLALLK 735
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
24-408 1.78e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   24 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrl 103
Cdd:COG4372     15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR---------------------- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  104 sngsidstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDM 183
Cdd:COG4372     73 -----------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-------EELQKERQDLEQQRKQL 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  184 EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQME--EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELA 261
Cdd:COG4372    135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSeaEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  262 QRIAALT--KAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 339
Cdd:COG4372    215 ELAEELLeaKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535324  340 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELRYSVGS 408
Cdd:COG4372    295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 36-278 1.92e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.21  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   36 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrlsngsidstdetS 115
Cdd:COG3883     26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ---------------------------------A 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QIVELQELLEKQNyemAQMKERLAAL---SSRVGEVEQ--EAETARKDLIKTEEMNTKYQRD---IREAMAQKEDMEERI 187
Cdd:COG3883     73 EIAEAEAEIEERR---EELGERARALyrsGGSVSYLDVllGSESFSDFLDRLSALSKIADADadlLEELKADKAELEAKK 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  188 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 267
Cdd:COG3883    150 AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229

                          250
                   ....*....|.
gi 2462535324  268 TKAEERHGNIE 278
Cdd:COG3883    230 AAAAAAAAAAA 240
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 147-373 2.08e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 45.21  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  147 EVEQEAET-----ARKDLIKTEEMNTKYQRD---IREAMA----QKEDMEERITTLEKRYLSAQRE----STSIHDMNDK 210
Cdd:PRK04778    90 EAEELNDKfrfrkAKHEINEIESLLDLIEEDieqILEELQelleSEEKNREEVEQLKDLYRELRKSllanRFSFGPALDE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  211 LENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI-AALTKAEE------------ 272
Cdd:PRK04778   170 LEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKAgyrelveegyhl 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  273 RHGNIEERMRHLEGQLEEKNQELQR---ARQREKmNEEHNKRLSDTVDRLLTEsnerlqlhlkerMAAleeKNVLIQESE 349
Cdd:PRK04778   250 DHLDIEKEIQDLKEQIDENLALLEEldlDEAEEK-NEEIQERIDQLYDILERE------------VKA---RKYVEKNSD 313

                          250       260
                   ....*....|....*....|....
gi 2462535324  350 TFRKNLEESLHDKERLAEEIEKLR 373
Cdd:PRK04778   314 TLPDFLEHAKEQNKELKEEIDRVK 337
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 209-383 2.10e-04

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.97  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  209 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 276
Cdd:cd00176     10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  277 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 346
Cdd:cd00176     84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2462535324  347 ESETFRKNLEESLH--DKERLAEEIEKLRSELDQLKMRT 383
Cdd:cd00176    164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 114-379 2.69e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.83  E-value: 2.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  114 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE-- 191
Cdd:PRK04778   111 ESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVELTes 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  192 ------KRYLSAQRESTS------------IHDMNDKLENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMR 248
Cdd:PRK04778   191 gdyveaREILDQLEEELAaleqimeeipelLKELQTELPDQLQELKAGYRELVEEGyhldhLDIEKEIQDLKEQIDENLA 270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  249 KAETLpeveaelaqriaALTKAEERHGNIEERMRHLEGQLE---------EKNQElqRARQREKMNEEHNKRLSDTVDRL 319
Cdd:PRK04778   271 LLEEL------------DLDEAEEKNEEIQERIDQLYDILErevkarkyvEKNSD--TLPDFLEHAKEQNKELKEEIDRV 336

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535324  320 -----LTESNERLQLHLKERMAALEEKNVLIQE---------SETfRKNLEESLHDKERLAEEIEKLRSELDQL 379
Cdd:PRK04778   337 kqsytLNESELESVRQLEKQLESLEKQYDEITEriaeqeiaySEL-QEELEEILKQLEEIEKEQEKLSEMLQGL 409
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
127-357 3.51e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  127 QNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQR--DIREAMAQKEDMEERITTLEKRYLSAQREstsi 204
Cdd:COG3206    159 EAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAE---- 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  205 hdmndklenelankeaiLRQMEEKNRQLQERLELAEQKLQQTMRkAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 284
Cdd:COG3206    235 -----------------LAEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535324  285 EGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEE 357
Cdd:COG3206    297 RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 24-295 3.73e-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: 44.83  E-value: 3.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   24 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnVHIQRKMASSEGSTESEHLEGMEPGQKVHEKrl 103
Cdd:pfam12128  260 LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLD-- 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  104 sngsidstDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETaRKDLIKtEEMNTKYQRDIREAMAQKEDM 183
Cdd:pfam12128  337 --------ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNR-RRSKIK-EQNNRDIAGIKDKLAKIREAR 406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  184 EERITTLEKRYlsAQRESTSIHDMN-DKLENELANKEAILRQMEEKNR---------------QLQERLELAEQKLQQTM 247
Cdd:pfam12128  407 DRQLAVAEDDL--QALESELREQLEaGKLEFNEEEYRLKSRLGELKLRlnqatatpelllqleNFDERIERAREEQEAAN 484

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462535324  248 RKAETLpevEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQEL 295
Cdd:pfam12128  485 AEVERL---QSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 115-267 3.84e-04

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 42.97  E-value: 3.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  115 SQIVELQELLEKQNYEMA-------QMKERLAALSSRVGEVEQEAETARKD---LIKTEEMNTKYQRDIREAMAQKEDME 184
Cdd:pfam13851   33 EEIAELKKKEERNEKLMSeiqqenkRLTEPLQKAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEHEVLE 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  185 ERITTLEKRY--LSAQREStSIHDMNDKLENE---LANK-EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 258
Cdd:pfam13851  113 QRFEKVERERdeLYDKFEA-AIQDVQQKTGLKnllLEKKlQALGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLE 191


                   ....*....
gi 2462535324  259 ELAQRIAAL 267
Cdd:pfam13851  192 SKNQLIKDL 200
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
12-281 3.88e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   12 SGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEG--STESEHL 89
Cdd:PRK02224   509 DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSklAELKERI 588

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   90 EGMEpgqkvhekRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARkdlikteemntky 169
Cdd:PRK02224   589 ESLE--------RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR------------- 647

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  170 qrdIREAMAQKEDMEERITTLEKrYLSAQREStsihdmNDKLENELANKEAILRQMEEknrqLQERLElaeqKLQQTMRK 249
Cdd:PRK02224   648 ---IEEAREDKERAEEYLEQVEE-KLDELREE------RDDLQAEIGAVENELEELEE----LRERRE----ALENRVEA 709

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462535324  250 AETLPEvEAELAQRIAALTKAEERHGNIE--ERM 281
Cdd:PRK02224   710 LEALYD-EAEELESMYGDLRAELRQRNVEtlERM 742
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
36-237 3.90e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 3.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   36 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHEKRLSNGSIDSTDETS 115
Cdd:COG4913    674 EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE-----KELEQAEEELDELQDRLEAAEDLARLELR 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QivELQELLEKQNYEmAQMKERLAALSSRVGEVEQEAETARKDLIKT-EEMNTKYQRDIREAMAQKEDMEE---RITTLE 191
Cdd:COG4913    749 A--LLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERAmRAFNREWPAETADLDADLESLPEylaLLDRLE 825

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2462535324  192 KRYLSAQREstsihDMNDKL-ENELANKEAILRQMEEKNRQLQERLE 237
Cdd:COG4913    826 EDGLPEYEE-----RFKELLnENSIEFVADLLSKLRRAIREIKERID 867
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 116-385 3.99e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.43  E-value: 3.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QIVELQELLEKQNYEMAQMKERLAALssrvgevEQEAETARKDLIKTEEmntkyqrdireAMAQKEDMEERITtlEKRYL 195
Cdd:pfam10174  402 KIENLQEQLRDKDKQLAGLKERVKSL-------QTDSSNTDTALTTLEE-----------ALSEKERIIERLK--EQRER 461

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  196 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH- 274
Cdd:pfam10174  462 EDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLk 541

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  275 ------------GNIEERMRHLEGQLEEKNQELQRARQ---------REKMNEEHNK--RLSDTVDRLLTESNERLQLHL 331
Cdd:pfam10174  542 kahnaeeavrtnPEINDRIRLLEQEVARYKEESGKAQAeverllgilREVENEKNDKdkKIAELESLTLRQMKEQNKKVA 621

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535324  332 KERMAALEEKNVLIQESETFRKNLEESLHDK-----ERLAEEIEKLRSELDQLKMRTGS 385
Cdd:pfam10174  622 NIKHGQQEMKKKGAQLLEEARRREDNLADNSqqlqlEELMGALEKTRQELDATKARLSS 680
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
 40-467 4.07e-04

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


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 44.73  E-value: 4.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   40 ERLRVSLERVsalEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEK--RLSNGSID----STDE 113
Cdd:COG5192    363 EKMKMQLQEI---EQDPGVDGVGLQLFSNSDAIDTVDRESSEIDNVGRKTRRQPTGKAIAEEtsREDELSFDdsdvSTSD 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  114 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEvEQEAETARKDLIKTEEMNTkyQRDIREAMAQKEDMEERITTlEKR 193
Cdd:COG5192    440 ENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFD-ESEGNLRWKEGLASKLAYS--QSGKRGRNIQKIFYDESLSP-EEC 515

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  194 YLSAQRESTSIHDMNDKLENElanKEAILRQMEEKNRQLQERLE-LAEQKLQQTMRKAETLPEVEAELAQriAALTKAEE 272
Cdd:COG5192    516 IEEYKGESAKSSESDLVVQDE---PEDFFDVSKVANESISSNHEkLMESEFEELKKKWSSLAQLKSRFQK--DATLDSIE 590

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  273 RHgniEErmrhLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK---NVLIQESE 349
Cdd:COG5192    591 GE---EE----LIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEElrgNFELEERG 663

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  350 TFRKN-LEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPT------------IPRTHLDTSaELRYSV--GSLVDSQS 414
Cdd:COG5192    664 DPEKKdVDWYTEEKRKIEEQLKINRSEFETMVPESRVVIEGYragryvrivlshVPLEFVDEF-NSRYPIvlGGLLPAEK 742

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462535324  415 DYRTTKV-IRRPRRGRMGVRRDEPKVKSLGdheWNRTQQIGVLSSHPFESDTEM 467
Cdd:COG5192    743 EMGIVQGrIKRHRWHKKILKTNDPLIFSVG---WRRFQSIPVYSMKDSRTRNRM 793
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 748-806 4.62e-04

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 39.62  E-value: 4.62e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  748 WDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 806
Cdd:cd09504      5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 233-371 4.85e-04

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


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 41.52  E-value: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  233 QERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 312
Cdd:pfam12718   13 QERAEELEEKVKE-------LEQENLEKEQEIKSLTH---KNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTRKI 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535324  313 sdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEK 371
Cdd:pfam12718   83 -----QLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEE 136
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 36-334 5.15e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.96  E-value: 5.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   36 EKVRERLRVSLERVSALEEELAAANQeivALREQNVHIQRKMASSEGSTESEHlegmEPGQKVHEKRLSNGSI-DSTDET 114
Cdd:pfam05557   44 DRESDRNQELQKRIRLLEKREAEAEE---ALREQAELNRLKKKYLEALNKKLN----EKESQLADAREVISCLkNELSEL 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  115 SQIVELQEL-LEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEE-------- 185
Cdd:pfam05557  117 RRQIQRAELeLQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknsksel 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  186 -RITTLEKRyLSAQRE-----STSIHDmNDKLENELANKEAILRQME---EKNRQLQERLELAEQKLQQ----------T 246
Cdd:pfam05557  197 aRIPELEKE-LERLREhnkhlNENIEN-KLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQSwvklaqdtglN 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  247 MRKAETLPEVEAELAQRIAALTkaeERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesNER 326
Cdd:pfam05557  275 LRSPEDLSRRIEQLQQREIVLK---EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL----QRR 347


                   ....*...
gi 2462535324  327 LQLHLKER 334
Cdd:pfam05557  348 VLLLTKER 355
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
165-380 5.22e-04

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.91  E-value: 5.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  165 MNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsihdmndkLENELANKEAILRQMEEKNRQLQErleLAEQKLQ 244
Cdd:COG0497    138 LDPDAQRELLDAFAGLEELLEEYREAYRAWRALKKE----------LEELRADEAERARELDLLRFQLEE---LEAAALQ 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  245 qtmrkaetlPEVEAELAQRIAALTKAEERHGNIEERMRHLEGqlEEKN--QELQRARQR-EKMnEEHNKRLSDTVDRL-- 319
Cdd:COG0497    205 ---------PGEEEELEEERRRLSNAEKLREALQEALEALSG--GEGGalDLLGQALRAlERL-AEYDPSLAELAERLes 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  320 ----LTESNERLQLHLK------ERMAALEEK-----------NVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 378
Cdd:COG0497    273 alieLEEAASELRRYLDslefdpERLEEVEERlallrrlarkyGVTVEELLAYAEELRAELAELENSDERLEELEAELAE 352


                   ..
gi 2462535324  379 LK 380
Cdd:COG0497    353 AE 354
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 146-380 5.39e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.19  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  146 GEVEQEAETARKDLIKTEE--MNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIhDMNDKLENELANKEAILR 223
Cdd:pfam02463  142 GKIEIIAMMKPERRLEIEEeaAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL-KEQAKKALEYYQLKEKLE 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  224 QMEEKNRQLQERLELAEQK---------LQQTMRKAETLPEVEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQE 294
Cdd:pfam02463  221 LEEEYLLYLDYLKLNEERIdllqellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEK---EKKLQEEELKLLAKEEEE 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  295 LQRARQREKMNEEHNKRlsdtVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRS 374
Cdd:pfam02463  298 LKSELLKLERRKVDDEE----KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE 373


                   ....*.
gi 2462535324  375 ELDQLK 380
Cdd:pfam02463  374 ELLAKK 379
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-380 6.13e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.94  E-value: 6.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   54 EELAAANQEIvALREQNVHIQRKMASSEGSTESEHLEgMEPGQKVH--EKRLSNGSIDSTDETSQIVELQELLEKQNYEM 131
Cdd:pfam05483  193 EKMILAFEEL-RVQAENARLEMHFKLKEDHEKIQHLE-EEYKKEINdkEKQVSLLLIQITEKENKMKDLTFLLEESRDKA 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  132 AQMKERLAALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIREAMAQKEDM-----------EERITTLEK-------- 192
Cdd:pfam05483  271 NQLEEKTKLQDENLKELIEKKDHLTKEL---EDIKMSLQRSMSTQKALEEDLqiatkticqltEEKEAQMEElnkakaah 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  193 RYLSAQRESTS------IHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA 266
Cdd:pfam05483  348 SFVVTEFEATTcsleelLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF 427

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  267 LTKAEERHGNIEERMRHLEGQlEEKNQELQRARQREKMNEEH-NKRLSDTVDRLLTESNERLQLHLKERMAALEEKNvLI 345
Cdd:pfam05483  428 EKIAEELKGKEQELIFLLQAR-EKEIHDLEIQLTAIKTSEEHyLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE-LT 505

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 2462535324  346 QESETFRKNLEESLHD-------KERLAEEIEKLRSELDQLK 380
Cdd:pfam05483  506 QEASDMTLELKKHQEDiinckkqEERMLKQIENLEEKEMNLR 547
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
203-380 7.90e-04

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 42.12  E-value: 7.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  203 SIHDMND---KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK---------AETLPEVEAELAQRIAALTKA 270
Cdd:COG1842     31 AIRDMEEdlvEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlareaLERKAELEAQAEALEAQLAQL 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  271 EERHGNIEERMRHLEGQLEEKNQELQRARQREKMNeEHNKRLSDTVDRLLTESNErlqlhlkERMAALEEKnvliQESET 350
Cdd:COG1842    111 EEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDAT-------SALERMEEK----IEEME 178

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462535324  351 FRKNLEESLHDKERLAEEIEKLRS------ELDQLK 380
Cdd:COG1842    179 ARAEAAAELAAGDSLDDELAELEAdsevedELAALK 214
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 119-385 8.82e-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: 43.41  E-value: 8.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  119 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETAR-----KDLIKTEEMNTKYQRDIREA----MAQKEDMEERITT 189
Cdd:COG5185    272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETetgiQNLTAEIEQGQES 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  190 LEKRYLSAQRESTSIHDMND------KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPE-------- 255
Cdd:COG5185    352 LTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEelqrqieq 431

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  256 VEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQRE--KMNEEHNKRLSDTVDRLLT--ESNERLQLHL 331
Cdd:COG5185    432 ATSSNEEVSKLLNELISE---LNKVMREADEESQSRLEEAYDEINRSvrSKKEDLNEELTQIESRVSTlkATLEKLRAKL 508

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462535324  332 KERMAALEEKNVLIQESETFRKNLEESLHDKERlaEEIEKLRSELDQLKMRTGS 385
Cdd:COG5185    509 ERQLEGVRSKLDQVAESLKDFMRARGYAHILAL--ENLIPASELIQASNAKTDG 560
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 333-391 9.30e-04

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 42.90  E-value: 9.30e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  333 ERMAALEEKNV-LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKmrTGSLIEPTI 391
Cdd:PRK03992     1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELEKLK--SPPLIVATV 58
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 40-339 1.02e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   40 ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKR--LSNGSIDSTDETSQI 117
Cdd:pfam15921  541 DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRleLQEFKILKDKKDAKI 620

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  118 VELQELLEKQNYEMAQM----KERLAALSSRVGEVEQ---EAETARKDLIKTEEMNTKYQRDIREamaQKEDMEERITTL 190
Cdd:pfam15921  621 RELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQllnEVKTSRNELNSLSEDYEVLKRNFRN---KSEEMETTTNKL 697

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  191 EKRYLSAQRE----STSIHDMNDKLENELANKEAILRQMEEKNRQ---LQERLELAEQKLQQTMRKAETLPEVEAELAQR 263
Cdd:pfam15921  698 KMQLKSAQSEleqtRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQE 777

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535324  264 IAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMneehnkRLSDTVDRLLTESNERLQLHLKERMAALE 339
Cdd:pfam15921  778 LSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL------QFAECQDIIQRQEQESVRLKLQHTLDVKE 847
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 121-299 1.17e-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: 41.66  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  121 QELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteEMNTKYQRDIREAmaqkEDMEERITTLEKRYLSaqre 200
Cdd:cd00176     64 EQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRL----EEALDLQQFFRDA----DDLEQWLEEKEAALAS---- 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  201 stsihdmnDKLENELANKEAILRQMEEknrqLQERLELAEQKLQQTMRKAETLPEveaelAQRIAALTKAEERHGNIEER 280
Cdd:cd00176    132 --------EDLGKDLESVEELLKKHKE----LEEELEAHEPRLKSLNELAEELLE-----EGHPDADEEIEEKLEELNER 194

                          170
                   ....*....|....*....
gi 2462535324  281 MRHLEGQLEEKNQELQRAR 299
Cdd:cd00176    195 WEELLELAEERQKKLEEAL 213
COG5022 COG5022
Myosin heavy chain [General function prediction only];
156-379 1.23e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.14  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  156 RKDLIKTEEMNTKYQRDIREAMAQKEdMEERITTLEkrylsaqreSTSIHdmNDKLENELANKEAILRQMEEKNRQLQER 235
Cdd:COG5022    809 RKEYRSYLACIIKLQKTIKREKKLRE-TEEVEFSLK---------AEVLI--QKFGRSLKAKKRFSLLKKETIYLQSAQR 876

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  236 LELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE-----ERMRHLEGQLEEKNQELQRARQREKmNEE 307
Cdd:COG5022    877 VELAERQlqeLKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENlefktELIARLKKLLNNIDLEEGPSIEYVK-LPE 955

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  308 HNKRLsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 379
Cdd:COG5022    956 LNKLH--EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV 1025
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 3-538 1.24e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.11  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324    3 VVKRQAQspsgVSSEVEVLKALKSLFEHHKALDEKVRErlrvSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEG 82
Cdd:TIGR00606  226 ITSKEAQ----LESSREIVKSYENELDPLKNRLKEIEH----NLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQ 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   83 STESEHLEgmepgqkVHEKRLSNGSidstDETSQIVELQELLEKQNYEMAQMKERLAALSSRVG------EVEQEAETAR 156
Cdd:TIGR00606  298 GTDEQLND-------LYHNHQRTVR----EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrlqlqaDRHQEHIRAR 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  157 KDLIKTEEMNTKY---------QRDIREAMA-QKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQME 226
Cdd:TIGR00606  367 DSLIQSLATRLELdgfergpfsERQIKNFHTlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKK 446

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  227 EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErHGNIEERMRHLEGQLEEKNQELQRARQREKMNE 306
Cdd:TIGR00606  447 EILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLDQEME 525

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  307 EHNkRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETF--RKNLEESLH----DKERLAEEIEKLRSELDQLK 380
Cdd:TIGR00606  526 QLN-HHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWLHskskEINQTRDRLAKLNKELASLE 604

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  381 MRTGSLIEPTIPRTHLDTSAELR-YSVGSLVDSQSDY-RTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLSS 458
Cdd:TIGR00606  605 QNKNHINNELESKEEQLSSYEDKlFDVCGSQDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQ 684

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  459 HPFESDTEMSDIDDDdretiFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLE 538
Cdd:TIGR00606  685 RVFQTEAELQEFISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRD 759
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 5-228 1.37e-03

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 42.75  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324    5 KRQAQSPSGVSSEvEVLKALKSLFEHhKALDEK----VRERLRVSLERVSALE--EELAAAN-QEIVALREQNVHIQRKM 77
Cdd:pfam05622  189 KRQVQELHGKLSE-ESKKADKLEFEY-KKLEEKlealQKEKERLIIERDTLREtnEELRCAQlQQAELSQADALLSPSSD 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   78 ASSEGSTESEHLEGMEPGQKV-HE-KRLSNGSIDSTDEtsQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETA 155
Cdd:pfam05622  267 PGDNLAAEIMPAEIREKLIRLqHEnKMLRLGQEGSYRE--RLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEEL 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  156 RK----------DLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEkrylsaQRESTSIHDMNDKLENELANKEAILRQM 225
Cdd:pfam05622  345 QKalqeqgskaeDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELE------PKQDSNLAQKIDELQEALRKKDEDMKAM 418


                   ...
gi 2462535324  226 EEK 228
Cdd:pfam05622  419 EER 421
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 106-289 1.62e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.97  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  106 GSIDSTDETSQIVELQELLEKQNYEMAQM---------KERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIrea 176
Cdd:cd22656     82 AQNAGGTIDSYYAEILELIDDLADATDDEeleeakktiKALLDDLLKEAKKYQDKAAKVVDKL-------TDFENQT--- 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  177 MAQKEDMEERITTLEKRYlsaQRESTSIHDMN-DKLENELAN-KEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 254
Cdd:cd22656    152 EKDQTALETLEKALKDLL---TDEGGAIARKEiKDLQKELEKlNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2462535324  255 EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 289
Cdd:cd22656    229 AADTDLDNLLALIGPAIPALEKLQGAWQAIATDLD 263
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 209-376 1.92e-03

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


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 40.82  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  209 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 277
Cdd:pfam04012   39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  278 EERMRHLEGQLEEKNQE-------LQRARQREKMNEehnkrlsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEt 350
Cdd:pfam04012  117 RKQLAALETKIQQLKAKknllkarLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELA- 187

                          170       180
                   ....*....|....*....|....*.
gi 2462535324  351 FRKNLEESLHDKERLAEEIEKLRSEL 376
Cdd:pfam04012  188 SAVDLDAKLEQAGIQMEVSEDVLARL 213
Caldesmon pfam02029
Caldesmon;
39-375 1.96e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.16  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   39 RERLRVSLERVSAlEEELAAANQEIVALREQNVHIQRKMASSEGSTESEH----LEGMEPGQKVHEKRLSNGSIDSTDET 114
Cdd:pfam02029   12 RRRAREERRRQKE-EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafLDRTAKREERRQKRLQEALERQKEFD 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  115 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmAQKEDMEERITTLEKRY 194
Cdd:pfam02029   91 PTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQA-EEEGEEEEDKSEEAEEV 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  195 LSAQRESTSIHDMNDKLENELANKEAILRQMEEK--NRQLQERLELAEQKLQQTMRKAETLPEV---EAELAQRIAALTK 269
Cdd:pfam02029  170 PTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGhpEVKSQNGEEEVTKLKVTTKRRQGGLSQSqerEEEAEVFLEAEQK 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  270 AEErhgnieERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLsdtvdrlltesnerlqlhlKERMAALEEKNVLIQESE 349
Cdd:pfam02029  250 LEE------LRRRRQEKESEEFEKLRQKQQEAELELEELKKKR-------------------EERRKLLEEEEQRRKQEE 304

                          330       340
                   ....*....|....*....|....*.
gi 2462535324  350 TFRKNLEESlhDKERLAEEIEKLRSE 375
Cdd:pfam02029  305 AERKLREEE--EKRRMKEEIERRRAE 328
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
877-932 2.05e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 37.63  E-value: 2.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535324  877 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 932
Cdd:pfam07647   11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
PRK12704 PRK12704
phosphodiesterase; Provisional
 230-378 2.08e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  230 RQLQERLELAEQKLQQTMRKAETlpevEAELAQRIAALTKAEERHgnieERMRHLEGQLEEKNQELQRARQREKMNEEHn 309
Cdd:PRK12704    27 KIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEEN- 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535324  310 krlsdtvdrlltesnerlqlhLKERMAALEEKNvliQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 378
Cdd:PRK12704    98 ---------------------LDRKLELLEKRE---EELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 116-327 2.55e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  116 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTlekryl 195
Cdd:pfam01576  890 RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKS------ 963

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  196 saqrestsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK-AETLPEVEAElaQRIAALTKAEERH 274
Cdd:pfam01576  964 --------------KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKlKEVLLQVEDE--RRHADQYKDQAEK 1027

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462535324  275 GNIeeRMRHLEGQLEEKNQELQRAR-QREKMNEEhnkrLSDTvdrllTESNERL 327
Cdd:pfam01576 1028 GNS--RMKQLKRQLEEAEEEASRANaARRKLQRE----LDDA-----TESNESM 1070
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 222-335 2.59e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.99  E-value: 2.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  222 LRQMEEKNRQLQ-ERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 300
Cdd:COG0542    413 LDELERRLEQLEiEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535324  301 R----EKMNEEHNKRLSDTVD-----------------RLLTESNERLqLHLKERM 335
Cdd:COG0542    493 ElaelEEELAELAPLLREEVTeediaevvsrwtgipvgKLLEGEREKL-LNLEEEL 547
PRK12704 PRK12704
phosphodiesterase; Provisional
 150-307 3.01e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 3.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  150 QEAETARKDLIKTEEmntkyqrdiREAMAQKEDMEerittlekryLSAQREstsIHDMNDKLENELANKEAILRQMEEKN 229
Cdd:PRK12704    34 KEAEEEAKRILEEAK---------KEAEAIKKEAL----------LEAKEE---IHKLRNEFEKELRERRNELQKLEKRL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  230 RQLQERLElaeqklqqtmRKAETLPEVEAELAQRIAALTKAEErhgNIEERmrhlEGQLEEK----NQELQR-------- 297
Cdd:PRK12704    92 LQKEENLD----------RKLELLEKREEELEKKEKELEQKQQ---ELEKK----EEELEELieeqLQELERisgltaee 154

                          170
                   ....*....|..
gi 2462535324  298 ARQR--EKMNEE 307
Cdd:PRK12704   155 AKEIllEKVEEE 166
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 49-379 3.13e-03

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.60  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   49 VSALEEELAAANQEIVALREQnvhiqrkMASSEGSTESEHLEGMEPG--QKVHEK------RLSNGSID----STDETSQ 116
Cdd:pfam05622   23 VSLLQEEKNSLQQENKKLQER-------LDQLESGDDSGTPGGKKYLllQKQLEQlqeenfRLETARDDyrikCEELEKE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  117 IVELQ---ELLEKQNYEMAQMKERLAAL---SSRVGEVEQEAETARK------DLIKT----EEMNTKYqrdireaMAQK 180
Cdd:pfam05622   96 VLELQhrnEELTSLAEEAQALKDEMDILresSDKVKKLEATVETYKKkledlgDLRRQvkllEERNAEY-------MQRT 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  181 EDMEE---RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQKLQQTMRKAETLP 254
Cdd:pfam05622  169 LQLEEelkKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQkekERLIIERDTLRETNEELRCAQ 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  255 EVEAELAQRIAALTKAEERHGNIEERMRHLEgqLEEKNQELQRARQREKMNEEHNKRLSDT-VDRLLTESNER------- 326
Cdd:pfam05622  249 LQQAELSQADALLSPSSDPGDNLAAEIMPAE--IREKLIRLQHENKMLRLGQEGSYRERLTeLQQLLEDANRRkneletq 326

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535324  327 ----------LQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 379
Cdd:pfam05622  327 nrlanqrileLQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEEL 389
BAR_SNX7 cd07666
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ...
 124-315 3.15e-03

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


Pssm-ID: 153350  Cd Length: 243  Bit Score: 40.66  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  124 LEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQrDIREAMAQK----EDMEERITTLEKRYLSAQR 199
Cdd:cd07666     14 LTAQAWELSSHKKQGPGLLSRMGQTVKAVASSVRGVKNRPEEFTEMN-EYVEAFSQKinvlDKISQRIYKEQREYFEELK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  200 ESTSIHDMNDKLENELANK--------EAILRQMEEKNRQLQERLE-------LAEQKLQQTMRKAEtlpEVEAELAQRI 264
Cdd:cd07666     93 EYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpviheyvLYSETLMGVIKRRD---QIQAELDSKV 169

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462535324  265 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 315
Cdd:cd07666    170 EALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFT 220
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 119-371 3.20e-03

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 41.18  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  119 ELQELLEKQNYEMAQMKERLAALSSRvgEVEQEAETARKDLIKTEEmntKYQRDIRE-AMAQKEDMEERITTLEKRYLSA 197
Cdd:pfam15558   35 EELRRRDQKRQETLERERRLLLQQSQ--EQWQAEKEQRKARLGREE---RRRADRREkQVIEKESRWREQAEDQENQRQE 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  198 QRESTSIHDMNDKLENE--LANKEAILRQMEEKNR-QLQERLELAEQKLQQ--------------------TMRKAETLP 254
Cdd:pfam15558  110 KLERARQEAEQRKQCQEqrLKEKEEELQALREQNSlQLQERLEEACHKRQLkereeqkkvqennlsellnhQARKVLVDC 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  255 EVEAELAQRIAAL----TKAEERH-GNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTV---DRLLTESNE 325
Cdd:pfam15558  190 QAKAEELLRRLSLeqslQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHKEALAelaDRKIQQARQ 269

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535324  326 RLQLHLKERMAALEEKNVLIQ------------ESETFRKNLEESLHDKERLAEEIEK 371
Cdd:pfam15558  270 VAHKTVQDKAQRARELNLEREknhhilklkvekEEKCHREGIKEAIKKKEQRSEQISR 327
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 753-810 3.76e-03

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 36.45  E-value: 3.76e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535324  753 VVAWLElWLGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 810
Cdd:cd09487      2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
Caldesmon pfam02029
Caldesmon;
34-336 3.76e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.01  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   34 LDEKVRERLRVSLERVSALEEELAAANqEIVALREQNVHIQRKmassEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDE 113
Cdd:pfam02029   71 REERRQKRLQEALERQKEFDPTIADEK-ESVAERKENNEEEEN----SSWEKEEKRDSRLGRYKEEETEIREKEYQENKW 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  114 TSQIVELQELLEKQNYEMAQMKERLAAlssRVGEVEQEAETARKDLIKTEEMNTKYQRD---IREAMAQKEDMEERITTL 190
Cdd:pfam02029  146 STEVRQAEEEGEEEEDKSEEAEEVPTE---NFAKEEVKDEKIKKEKKVKYESKVFLDQKrghPEVKSQNGEEEVTKLKVT 222

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  191 EKRYLSAQRESTSIH-DMNDKLENELAnkeailrqMEEKNRQLQERLELAEQKLQQTMRKAEtlpeveAELaqriaaltk 269
Cdd:pfam02029  223 TKRRQGGLSQSQEREeEAEVFLEAEQK--------LEELRRRRQEKESEEFEKLRQKQQEAE------LEL--------- 279

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535324  270 aEERHGNIEERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMA 336
Cdd:pfam02029  280 -EELKKKREERRKLLE---EEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSS 342
RNase_Y_N pfam12072
RNase Y N-terminal region;
230-370 3.80e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.87  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  230 RQLQERLELAEQKLQQTMRKAETLP----------------EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 293
Cdd:pfam12072   27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  294 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEtfrknlEESLHDKERLAEEIE 370
Cdd:pfam12072  107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 25-314 4.73e-03

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: 40.90  E-value: 4.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   25 KSLFEHHKALDEKVRERLRvSLERVSALEEELAAANQEIVALREQNVH--IQRKMASSEGSTESEHLEGMEPGQKVHEKR 102
Cdd:pfam09731  121 KSEQEKEKALEEVLKEAIS-KAESATAVAKEAKDDAIQAVKAHTDSLKeaSDTAEISREKATDSALQKAEALAEKLKEVI 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  103 LSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAE-TARKDLIKTEEM---------------- 165
Cdd:pfam09731  200 NLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKElVASERIVFQQELvsifpdiipvlkednl 279

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  166 --NTKYQRDIREAMAQKEDMEERITTLEKR-YLSAQRESTSIHDMNDKLENELAnkEAILRQMEEKNRQLQERLELAEQK 242
Cdd:pfam09731  280 lsNDDLNSLIAHAHREIDQLSKKLAELKKReEKHIERALEKQKEELDKLAEELS--ARLEEVRAADEAQLRLEFEREREE 357

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  243 LQQTMRKaetlpEVEAELAQRIAALTKaeerhgnieermrHLEGQLEEKNQELQRARQR---EKMNEEHNKRLSD 314
Cdd:pfam09731  358 IRESYEE-----KLRTELERQAEAHEE-------------HLKDVLVEQEIELQREFLQdikEKVEEERAGRLLK 414
Kre28 pfam17097
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ...
 169-400 5.31e-03

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


Pssm-ID: 407241 [Multi-domain]  Cd Length: 360  Bit Score: 40.56  E-value: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  169 YQRDIREAMAQKEDM-EERITTLEKRYLSAQREST-SIHDMND-----KLENELANKEAILRQMEEKNRQLQERLELaeq 241
Cdd:pfam17097    9 YEAQLRELEEQTAHSsEQVLTEQDKRLLGALRELTqSVIQLIEenslvTVSGDAANLLIDPSGIEVKIRQLDQLVEL--- 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  242 kLQQTMRKAETLPEVEAELAQRIAAL---TKAEERHGNIEERMRHLE-GQLEEKNQELQRAR------------QREKMN 305
Cdd:pfam17097   86 -LKVTHLEQETLDNFLRYTISSTDLLqleSVSDPKYASLEDEVSQLEdDTLTVLNQEIDQIKgdilqvaqeiadKQDQVN 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  306 EE--HNKRLSDTVDRLLTESNE-RLQLHLKERMAALEEKNVLIQESETFR--KNLEESLHDKERLAEEIEKLRSELDQLK 380
Cdd:pfam17097  165 ELclETSNELDECWELLNELERlRDQRITVEEQTSNEKDTELDPVEETYEewKSLQESLQQLEHLKEELDQLQKQKDSLE 244

                          250       260
                   ....*....|....*....|
gi 2462535324  381 MRTGSliepTIPRTHLDTSA 400
Cdd:pfam17097  245 KVDKS----SINRTQNDEES 260
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 239-380 5.45e-03

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


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 40.35  E-value: 5.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  239 AEQKLQQTMRKAETlpeVEAELAQRIAALTKAE----ERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSD 314
Cdd:pfam02841  174 AEEVLQEFLQSKEA---VEEAILQTDQALTAKEkaieAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIE 250

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535324  315 TVdrlltESNERLQLHLKERMAALEEknvliQESETFRKnleeslhdkERLAEEIEKLRSELDQLK 380
Cdd:pfam02841  251 KM-----EAEREQLLAEQERMLEHKL-----QEQEELLK---------EGFKTEAESLQKEIQDLK 297
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
219-388 5.49e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 5.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  219 EAILRQMEEKNRQLQERLELAEQKlqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 298
Cdd:PRK03918   138 DAILESDESREKVVRQILGLDDYE-----NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  299 RQREKmneehnkRLSDTVDRLltesnERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKErlaEEIEKLRSELDQ 378
Cdd:PRK03918   213 SSELP-------ELREELEKL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE---ERIEELKKEIEE 277

                          170
                   ....*....|
gi 2462535324  379 LKMRTGSLIE 388
Cdd:PRK03918   278 LEEKVKELKE 287
46 PHA02562
endonuclease subunit; Provisional
 59-274 5.99e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324   59 ANQEIVALREQNVHIQRKMAssegsTESEHLEGMEPGQKVHEKRLSNgSIDSTDET-----SQIVELQELL-------EK 126
Cdd:PHA02562   179 LNQQIQTLDMKIDHIQQQIK-----TYNKNIEEQRKKNGENIARKQN-KYDELVEEaktikAEIEELTDELlnlvmdiED 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  127 QNYEMAQMKERLAALSSRVGEVEQEAE---------TARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSA 197
Cdd:PHA02562   253 PSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEF 332

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535324  198 QRESTSIHDMNDKLENelaNKEAILRqMEEKNRQLQERLELAEqklQQTMRKAETLPEVEAELAQRIAALTK-AEERH 274
Cdd:PHA02562   333 NEQSKKLLELKNKIST---NKQSLIT-LVDKAKKVKAAIEELQ---AEFVDNAEELAKLQDELDKIVKTKSElVKEKY 403
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 119-262 6.39e-03

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


Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 38.89  E-value: 6.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  119 ELQELLEKQNYEMAQMKER-LAALSSRVGEVEQEAETARKDLIKteEMNTKYQRDIREAMAQKEDmeERITTLEKRYLSA 197
Cdd:pfam08703   13 ELLELREEQYEQEKKRKEQhLTEQIQKLKELAREKQAAELKALK--ESSESEKKEMKKKLERKRL--ESIQEAKKRTSDK 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535324  198 QRESTSIHDMNDKLENELANkeaILRQMEEKNRQLQERLELAEQKLQQTMRkaETLPEVEAELAQ 262
Cdd:pfam08703   89 AAQERLKKEINNSHIQEVVQ---SIKQLEEKQKRRQEKLEEKQAECLQQIK--EEEPQLQAELNA 148
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 877-921 6.58e-03

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


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 36.51  E-value: 6.58e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462535324  877 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 921
Cdd:cd09501     11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
46 PHA02562
endonuclease subunit; Provisional
 141-380 6.63e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 6.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  141 LSSRVGEVEQEAET--ARKDLIKTE-EMNTKYQRDIREAMAQkedmeeRITTLEKRYLSAQRESTSIHDMNDKLENELAN 217
Cdd:PHA02562   172 NKDKIRELNQQIQTldMKIDHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLN 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  218 keaILRQMEEKNRQLQE-RLELAEQKLQ-QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQEL 295
Cdd:PHA02562   246 ---LVMDIEDPSAALNKlNTAAAKIKSKiEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  296 QRARQREKMNEEHNKRLSDTvdrlltesneRLQLHLKERMAALEEKNVLIQESETfrKNLEESLHDKErlaEEIEKLRSE 375
Cdd:PHA02562   323 DELEEIMDEFNEQSKKLLEL----------KNKISTNKQSLITLVDKAKKVKAAI--EELQAEFVDNA---EELAKLQDE 387


                   ....*
gi 2462535324  376 LDQLK 380
Cdd:PHA02562   388 LDKIV 392
PRK09039 PRK09039
peptidoglycan -binding protein;
178-299 7.91e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 7.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  178 AQKEDMEERITTLEKRYLSAQREstsihdmNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE 257
Cdd:PRK09039    74 QGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462535324  258 AELAQRIAAL--------TKAEERHGNIEERMRHLEGQLEEKNQELQRAR 299
Cdd:PRK09039   147 AALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 121-526 7.99e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.11  E-value: 7.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  121 QELLEKQNYE-MAQMKERLAALSSRVGEVEqEAETARKDLIktEEMNTKYQRDIREAMAQKEDMEeRITTLEKrylsaqr 199
Cdd:pfam17380  290 QEKFEKMEQErLRQEKEEKAREVERRRKLE-EAEKARQAEM--DRQAAIYAEQERMAMERERELE-RIRQEER------- 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  200 estsihdmndKLENELANKEAILRQMEeKNRQLqERLELAEQKLQQTMRKaetlpEVEAELAQRIaaltKAEERHGNIEE 279
Cdd:pfam17380  359 ----------KRELERIRQEEIAMEIS-RMREL-ERLQMERQQKNERVRQ-----ELEAARKVKI----LEEERQRKIQQ 417

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  280 RMRHLEGQLEEknQELQRARQREKMNEEHNKRLsdtvdrlltesnERLQLHLKERMAALEEknVLIQESETFRKNLEesL 359
Cdd:pfam17380  418 QKVEMEQIRAE--QEEARQREVRRLEEERAREM------------ERVRLEEQERQQQVER--LRQQEEERKRKKLE--L 479

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  360 HDKERLAEEIEKLRSEL--DQLKMRTGSLIEPTIPRthldtsaelrysvgSLVDSQSDYRTTKVIRRPRRgrmgvRRDEp 437
Cdd:pfam17380  480 EKEKRDRKRAEEQRRKIleKELEERKQAMIEEERKR--------------KLLEKEMEERQKAIYEEERR-----REAE- 539

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  438 kvkslgdhEWNRTQQigvlsshpfesdtEMsdiddDDRETIFSSMDLLSPSghsdaqtlammlQEQLDAINKEIRLIQEE 517
Cdd:pfam17380  540 --------EERRKQQ-------------EM-----EERRRIQEQMRKATEE------------RSRLEAMEREREMMRQI 581


                   ....*....
gi 2462535324  518 KESTELRAE 526
Cdd:pfam17380  582 VESEKARAE 590
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
204-383 9.40e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 9.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  204 IHDMndkLENELANK-EAILRQMEEKNRQLQERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKAEERHGNIEERMR 282
Cdd:COG4717     43 IRAM---LLERLEKEaDELFKPQGRKPELNLKELKELEEELKE-------AEEKEEEYAELQEELEELEEELEELEAELE 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  283 HLEGQLEEKNQELQRARQREKMnEEHNKRLSDtvdrlltesnerlqlhLKERMAALEEKnvliqesetfRKNLEESLHDK 362
Cdd:COG4717    113 ELREELEKLEKLLQLLPLYQEL-EALEAELAE----------------LPERLEELEER----------LEELRELEEEL 165

                          170       180
                   ....*....|....*....|.
gi 2462535324  363 ERLAEEIEKLRSELDQLKMRT 383
Cdd:COG4717    166 EELEAELAELQEELEELLEQL 186
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 119-380 9.55e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 9.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  119 ELQELLEKQNYEMAQM-----KERLAALSSR------VGEVEQEAETAR-------KDLIKTEEMNTKYQRDIREAMAQK 180
Cdd:pfam01576  742 EKRRQLVKQVRELEAElederKQRAQAVAAKkkleldLKELEAQIDAANkgreeavKQLKKLQAQMKDLQRELEEARASR 821

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  181 EDM-------EERITTLEKRYL-------SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQT 246
Cdd:pfam01576  822 DEIlaqskesEKKLKNLEAELLqlqedlaASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEE 901

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535324  247 MRKAETLPEVEAELAQRIAALT---KAEERHGNIEERMRHlegQLEEKNQELQ-RARQREKMNEEHNKRLSDTVDRLLTE 322
Cdd:pfam01576  902 QSNTELLNDRLRKSTLQVEQLTtelAAERSTSQKSESARQ---QLERQNKELKaKLQEMEGTVKSKFKSSIAALEAKIAQ 978

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535324  323 SNERLQLHLKERMAAleekNVLIQESETFRKNLEESLHDKERLAE----EIEKLRSELDQLK 380
Cdd:pfam01576  979 LEEQLEQESRERQAA----NKLVRRTEKKLKEVLLQVEDERRHADqykdQAEKGNSRMKQLK 1036
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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