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Conserved domains on  [gi|1720412105|ref|XP_030109966|]
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homeobox protein cut-like 1 isoform X2 [Mus musculus]

Protein Classification

CUT and homeodomain domain-containing protein( domain architecture ID 13530023)

CUT and homeodomain domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
1217-1294 5.96e-31

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


:

Pssm-ID: 460543  Cd Length: 78  Bit Score: 116.92  E-value: 5.96e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412105 1217 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1294
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
1034-1102 4.26e-28

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


:

Pssm-ID: 460543  Cd Length: 78  Bit Score: 108.83  E-value: 4.26e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412105 1034 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 1102
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
667-743 1.85e-27

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


:

Pssm-ID: 460543  Cd Length: 78  Bit Score: 106.91  E-value: 1.85e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412105  667 EGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 743
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1340-1396 2.72e-16

Homeodomain;


:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 74.46  E-value: 2.72e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412105 1340 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRR 1396
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
192-483 4.79e-14

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 77.79  E-value: 4.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  192 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQtlKSQAETIALEKEQKLQND 267
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEA--EVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  268 FAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 337
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  338 RAEVAQREAETLREQLSSANHSLqlaSQIQKAPDVLQvdgspssspraSAVSSLLcpsQEQAIEVLTRSSLEVELAAKER 417
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEI---EELEELIEELE-----------SELEALL---NERASLEEALALLRSELEELSE 901
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412105  418 EIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQLEEKL--KGQADYEEVKKELNTLKS 483
Cdd:TIGR02168  902 ELRELESKRSELRRELEELRE----KLAQLELRLEGLEVRIDNLQERLseEYSLTLEEAEALENKIED 965
PHA03247 super family cl33720
large tegument protein UL36; Provisional
845-1028 2.45e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  845 SASPMSTVSTYPPLAISLKKTPAAPETST--AALPSAPALKKEAQDVPTLDPPGSADAAQGVLRPMksELVRGSTWKDPW 922
Cdd:PHA03247   269 PETARGATGPPPPPEAAAPNGAAAPPDGVwgAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGAM--EVVSPLPRPRQH 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  923 WSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERsqlqgpsasaeywKEWPSAESPYSQSSELSLTGASRSETPQ 1002
Cdd:PHA03247   347 YPLGFPKRRRPTWTPPSSLEDLSAGRHHPKRASLPTRKR-------------RSARHAATPFARGPGGDDQTRPAAPVPA 413
                          170       180
                   ....*....|....*....|....*.
gi 1720412105 1003 NSPLPSSPIVPMAKPAKPSVPPLTPE 1028
Cdd:PHA03247   414 SVPTPAPTPVPASAPPPPATPLPSAE 439
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
103-258 1.49e-03

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKEAEAA--FLTV 177
Cdd:PRK03918   622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELsreLAGLRAELEELEKRREEIKKTleKLKE 701
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  178 YKRLID-----VPDPVPALDVGQQLEIKVQRLHDIETEN--QKLRETLEEYNKEFAEVKNQEVTIKALKEKIR------- 243
Cdd:PRK03918   702 ELEEREkakkeLEKLEKALERVEELREKVKKYKALLKERalSKVGEIASEIFEELTEGKYSGVRVKAEENKVKlfvvyqg 781
                          170
                   ....*....|....*.
gi 1720412105  244 -EYEQTLKSQAETIAL 258
Cdd:PRK03918   782 kERPLTFLSGGERIAL 797
 
Name Accession Description Interval E-value
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
1217-1294 5.96e-31

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 116.92  E-value: 5.96e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412105 1217 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1294
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
1034-1102 4.26e-28

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 108.83  E-value: 4.26e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412105 1034 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 1102
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
667-743 1.85e-27

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 106.91  E-value: 1.85e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412105  667 EGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 743
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1340-1396 2.72e-16

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 74.46  E-value: 2.72e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412105 1340 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRR 1396
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
192-483 4.79e-14

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: 77.79  E-value: 4.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  192 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQtlKSQAETIALEKEQKLQND 267
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEA--EVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  268 FAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 337
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  338 RAEVAQREAETLREQLSSANHSLqlaSQIQKAPDVLQvdgspssspraSAVSSLLcpsQEQAIEVLTRSSLEVELAAKER 417
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEI---EELEELIEELE-----------SELEALL---NERASLEEALALLRSELEELSE 901
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412105  418 EIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQLEEKL--KGQADYEEVKKELNTLKS 483
Cdd:TIGR02168  902 ELRELESKRSELRRELEELRE----KLAQLELRLEGLEVRIDNLQERLseEYSLTLEEAEALENKIED 965
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
1340-1397 9.32e-14

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


Pssm-ID: 238039 [Multi-domain]  Cd Length: 59  Bit Score: 67.27  E-value: 9.32e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412105 1340 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRE 1397
Cdd:cd00086      1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
143-478 9.52e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.90  E-value: 9.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  143 EDLRKQVAPLLKsfQGEI----DALSKRSKEAEAAFLTVYKRLIDvpdpvpaldvgQQLEIKVQRLHDIETENQKLRETL 218
Cdd:COG1196    196 GELERQLEPLER--QAEKaeryRELKEELKELEAELLLLKLRELE-----------AELEELEAELEELEAELEELEAEL 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  219 EEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKEQKlqNDFAEKERKLQETQMSTTSKLEEAEHKLQ 294
Cdd:COG1196    263 AELEAELEELRLEleelELELEEAQAEEYELLAELARLEQDIARLEERR--RELEERLEELEEELAELEEELEELEEELE 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  295 TLQTALEKTRTELFDLKTKYDEETTAKADEIEMImtdLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKApdvlq 374
Cdd:COG1196    341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL----- 412
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  375 vdgSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAK 454
Cdd:COG1196    413 ---LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
                          330       340
                   ....*....|....*....|....
gi 1720412105  455 NSTLKQLEEKLKGQADYEEVKKEL 478
Cdd:COG1196    490 AARLLLLLEAEADYEGFLEGVKAA 513
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
1340-1395 5.68e-13

Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes


Pssm-ID: 197696 [Multi-domain]  Cd Length: 57  Bit Score: 64.96  E-value: 5.68e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412105  1340 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIR 1395
Cdd:smart00389    2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
143-478 2.64e-09

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: 61.63  E-value: 2.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  143 EDLRKQVAPLL---KSFQGEIDALSKRSKEAEAafltvykrlIDVPDPVPA---LDVGQQLEIKVQRLHDIETENQKLRE 216
Cdd:pfam05622   17 HELDQQVSLLQeekNSLQQENKKLQERLDQLES---------GDDSGTPGGkkyLLLQKQLEQLQEENFRLETARDDYRI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  217 TLEEYNKEFAE--VKNQEVT-----IKALK----------EKIREYEQTLKSQaetialekEQKLQ--NDFAEKERKLQE 277
Cdd:pfam05622   88 KCEELEKEVLElqHRNEELTslaeeAQALKdemdilressDKVKKLEATVETY--------KKKLEdlGDLRRQVKLLEE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  278 TQ---MSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLEranQRAEVAQREAETL---RE 351
Cdd:pfam05622  160 RNaeyMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESK-KADKLEFEYKKLE---EKLEALQKEKERLiieRD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  352 QLSSANHSLQLAsQIQKApdvlqvdgspsssprasavssllcpSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQA 431
Cdd:pfam05622  236 TLRETNEELRCA-QLQQA-------------------------ELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQH 289
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412105  432 SLTKLRE----NSASQISQLEQQLNAKNSTLKQLEEKLKG--------QADYEEVKKEL 478
Cdd:pfam05622  290 ENKMLRLgqegSYRERLTELQQLLEDANRRKNELETQNRLanqrilelQQQVEELQKAL 348
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-485 3.62e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.62  E-value: 3.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  104 KLKRELDAtatvLANRQDESEQSRKRLIEQSREFKKNTpEDLRKQV----------------------APLLKSFQGEID 161
Cdd:PRK03918   388 KLEKELEE----LEKAKEEIEEEISKITARIGELKKEI-KELKKAIeelkkakgkcpvcgrelteehrKELLEEYTAELK 462
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  162 ALSKRSKEAEAAFLTVYKRLIDVpdpvpalDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEK 241
Cdd:PRK03918   463 RIEKELKEIEEKERKLRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEK 533
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  242 IREYEQTLKSQAETiaLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQ-TALEKTRTELFDLKTKYDE---- 316
Cdd:PRK03918   534 LIKLKGEIKSLKKE--LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEylel 607
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  317 -----ETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLqlasqiqkapdvlqvdgspsssprasavssl 391
Cdd:PRK03918   608 kdaekELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY------------------------------- 656
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  392 lcpSQEQAIEvltrssLEVELAAKEREIAQLVEDVQRLQasltKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADY 471
Cdd:PRK03918   657 ---SEEEYEE------LREEYLELSRELAGLRAELEELE----KRREEIKKTLEKLKEELEEREKAKKELEKLEKALERV 723
                          410
                   ....*....|....
gi 1720412105  472 EEVKKELNTLKSME 485
Cdd:PRK03918   724 EELREKVKKYKALL 737
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
143-335 8.13e-08

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: 55.84  E-value: 8.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  143 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRLIDvpdpvpalDVGQQLEIKVQRLHDI-ETENQKL-RETLEE 220
Cdd:cd22656    113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTE--------KDQTALETLEKALKDLlTDEGGAIaRKEIKD 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  221 YNKEFAevKNQEVTIKALKEKIREYEQTLKSQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKLQTLQTA 299
Cdd:cd22656    184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1720412105  300 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 335
Cdd:cd22656    255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
PHA03247 PHA03247
large tegument protein UL36; Provisional
845-1028 2.45e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  845 SASPMSTVSTYPPLAISLKKTPAAPETST--AALPSAPALKKEAQDVPTLDPPGSADAAQGVLRPMksELVRGSTWKDPW 922
Cdd:PHA03247   269 PETARGATGPPPPPEAAAPNGAAAPPDGVwgAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGAM--EVVSPLPRPRQH 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  923 WSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERsqlqgpsasaeywKEWPSAESPYSQSSELSLTGASRSETPQ 1002
Cdd:PHA03247   347 YPLGFPKRRRPTWTPPSSLEDLSAGRHHPKRASLPTRKR-------------RSARHAATPFARGPGGDDQTRPAAPVPA 413
                          170       180
                   ....*....|....*....|....*.
gi 1720412105 1003 NSPLPSSPIVPMAKPAKPSVPPLTPE 1028
Cdd:PHA03247   414 SVPTPAPTPVPASAPPPPATPLPSAE 439
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
203-312 1.98e-05

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 48.48  E-value: 1.98e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105   203 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDFA---EKERKLQ 276
Cdd:smart00787  138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 1720412105   277 ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKT 312
Cdd:smart00787  218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
1340-1425 3.86e-05

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 45.51  E-value: 3.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105 1340 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRelfieeiqagsQGQAGASDSPSA 1419
Cdd:COG5576     52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKK-----------KRSGKVEQRPGE 120

                   ....*.
gi 1720412105 1420 RSSRAA 1425
Cdd:COG5576    121 EEADLA 126
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
103-258 1.49e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKEAEAA--FLTV 177
Cdd:PRK03918   622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELsreLAGLRAELEELEKRREEIKKTleKLKE 701
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  178 YKRLID-----VPDPVPALDVGQQLEIKVQRLHDIETEN--QKLRETLEEYNKEFAEVKNQEVTIKALKEKIR------- 243
Cdd:PRK03918   702 ELEEREkakkeLEKLEKALERVEELREKVKKYKALLKERalSKVGEIASEIFEELTEGKYSGVRVKAEENKVKlfvvyqg 781
                          170
                   ....*....|....*.
gi 1720412105  244 -EYEQTLKSQAETIAL 258
Cdd:PRK03918   782 kERPLTFLSGGERIAL 797
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
103-277 4.14e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 4.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQvaplLKSFQGEIDALSKRSKEAEaafltvyKRLI 182
Cdd:COG1579     20 DRLEHRLKELPAELAELEDELAALEARLEAAKTEL-----EDLEKE----IKRLELEIEEVEARIKKYE-------EQLG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIAlEKEQ 262
Cdd:COG1579     84 NVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEELAELE-AELE 159
                          170
                   ....*....|....*
gi 1720412105  263 KLQNDFAEKERKLQE 277
Cdd:COG1579    160 ELEAEREELAAKIPP 174
 
Name Accession Description Interval E-value
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
1217-1294 5.96e-31

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 116.92  E-value: 5.96e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412105 1217 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1294
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
1034-1102 4.26e-28

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 108.83  E-value: 4.26e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412105 1034 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 1102
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
667-743 1.85e-27

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 106.91  E-value: 1.85e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412105  667 EGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 743
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1340-1396 2.72e-16

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 74.46  E-value: 2.72e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412105 1340 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRR 1396
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
192-483 4.79e-14

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: 77.79  E-value: 4.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  192 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQtlKSQAETIALEKEQKLQND 267
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEA--EVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  268 FAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 337
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  338 RAEVAQREAETLREQLSSANHSLqlaSQIQKAPDVLQvdgspssspraSAVSSLLcpsQEQAIEVLTRSSLEVELAAKER 417
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEI---EELEELIEELE-----------SELEALL---NERASLEEALALLRSELEELSE 901
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412105  418 EIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQLEEKL--KGQADYEEVKKELNTLKS 483
Cdd:TIGR02168  902 ELRELESKRSELRRELEELRE----KLAQLELRLEGLEVRIDNLQERLseEYSLTLEEAEALENKIED 965
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
1340-1397 9.32e-14

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


Pssm-ID: 238039 [Multi-domain]  Cd Length: 59  Bit Score: 67.27  E-value: 9.32e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412105 1340 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRE 1397
Cdd:cd00086      1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
143-478 9.52e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.90  E-value: 9.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  143 EDLRKQVAPLLKsfQGEI----DALSKRSKEAEAAFLTVYKRLIDvpdpvpaldvgQQLEIKVQRLHDIETENQKLRETL 218
Cdd:COG1196    196 GELERQLEPLER--QAEKaeryRELKEELKELEAELLLLKLRELE-----------AELEELEAELEELEAELEELEAEL 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  219 EEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKEQKlqNDFAEKERKLQETQMSTTSKLEEAEHKLQ 294
Cdd:COG1196    263 AELEAELEELRLEleelELELEEAQAEEYELLAELARLEQDIARLEERR--RELEERLEELEEELAELEEELEELEEELE 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  295 TLQTALEKTRTELFDLKTKYDEETTAKADEIEMImtdLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKApdvlq 374
Cdd:COG1196    341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL----- 412
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  375 vdgSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAK 454
Cdd:COG1196    413 ---LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
                          330       340
                   ....*....|....*....|....
gi 1720412105  455 NSTLKQLEEKLKGQADYEEVKKEL 478
Cdd:COG1196    490 AARLLLLLEAEADYEGFLEGVKAA 513
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
1340-1395 5.68e-13

Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes


Pssm-ID: 197696 [Multi-domain]  Cd Length: 57  Bit Score: 64.96  E-value: 5.68e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412105  1340 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIR 1395
Cdd:smart00389    2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
111-481 1.26e-11

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: 69.22  E-value: 1.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  111 ATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRK-----QVAPL--LKSFQGEIDA------------LSKRSKEAE 171
Cdd:COG5185    146 IADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFgltlgLLKGIseLKKAEPSGTVnsikesetgnlgSESTLLEKA 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  172 AAFLTVYKRLIDVPDPVPALdvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEKIREYE 246
Cdd:COG5185    226 KEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEKIAEYT 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  247 QTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYD-EETTAKAD-- 323
Cdd:COG5185    303 KSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSEELDsf 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  324 ---------EIEMIMTDLERANQraEVAQREAETLREQLSSANhslQLASQIQKAPDVLQVDGSPSSSPRASAV-----S 389
Cdd:COG5185    383 kdtiestkeSLDEIPQNQRGYAQ--EILATLEDTLKAADRQIE---ELQRQIEQATSSNEEVSKLLNELISELNkvmreA 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  390 SLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEeklkgQA 469
Cdd:COG5185    458 DEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFM-----RA 532
                          410
                   ....*....|..
gi 1720412105  470 DYEEVKKELNTL 481
Cdd:COG5185    533 RGYAHILALENL 544
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
195-484 7.27e-11

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 67.10  E-value: 7.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 274
Cdd:COG4717     74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  275 LQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 350
Cdd:COG4717    151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  351 EQ---LSSANHSLQLASQIQKA---------------------------PDVLQV----------DGSPSSSPRASAVSS 390
Cdd:COG4717    227 EEleqLENELEAAALEERLKEArlllliaaallallglggsllsliltiAGVLFLvlgllallflLLAREKASLGKEAEE 306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  391 LLCPSQEQAIEVL----TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLN-----AKNSTLKQ 460
Cdd:COG4717    307 LQALPALEELEEEeleeLLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEE 386
                          330       340
                   ....*....|....*....|....
gi 1720412105  461 LEEKLKGQADYEEVKKELNTLKSM 484
Cdd:COG4717    387 LRAALEQAEEYQELKEELEELEEQ 410
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
208-520 1.26e-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: 63.54  E-value: 1.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  208 ETENqKLRET---LEEYNKEFAEVKNQEVTIKALKEKIREYeQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTS 284
Cdd:TIGR02168  176 ETER-KLERTrenLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLEELREELEELQEELKEAEE 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  285 KLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETT---AKADEIEMIMTDLERANQRAEVAQREAETLREQLssanhsLQ 361
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQL------EE 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  362 LASQIQKAPDVLQvdgspsssprasavssllcpSQEQAIEVLTRSSleVELAAKEREIAQLVEDVQRLQASLTKLRENSA 441
Cdd:TIGR02168  328 LESKLDELAEELA--------------------ELEEKLEELKEEL--ESLEAELEELEAELEELESRLEELEEQLETLR 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  442 SQISQLEQQLNAKNSTLKQLEEKLKGQAD-----YEEVKKELNTLKSMEFApsEGAGTQDSTKPLEVLLLEKNRSLQSEN 516
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDrrerlQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEAL 463

                   ....
gi 1720412105  517 ATLR 520
Cdd:TIGR02168  464 EELR 467
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
143-483 1.68e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 62.78  E-value: 1.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  143 EDLRKQVAPLLK---SFQGEIDALSKRSKEAEAAFLTVYKRLidvpdpvpaLDVGQQLEIKVQRLHDIETENQKLRETLE 219
Cdd:TIGR02169  684 EGLKRELSSLQSelrRIENRLDELSQELSDASRKIGEIEKEI---------EQLEQEEEKLKERLEELEEDLSSLEQEIE 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  220 EYNKEFAEVknqEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQN--DFAEKERKLQETQmstTSKLEEAEHKLQTLQ 297
Cdd:TIGR02169  755 NVKSELKEL---EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAelSKLEEEVSRIEAR---LREIEQKLNRLTLEK 828
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  298 TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLssanhslqlaSQIQKAPDVLQVDG 377
Cdd:TIGR02169  829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----------GDLKKERDELEAQL 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  378 SPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVqrlqasltklrENSASqISQLEQQLNAKNST 457
Cdd:TIGR02169  899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-----------EEELS-LEDVQAELQRVEEE 966
                          330       340
                   ....*....|....*....|....*..
gi 1720412105  458 LKQLEE-KLKGQADYEEVKKELNTLKS 483
Cdd:TIGR02169  967 IRALEPvNMLAIQEYEEVLKRLDELKE 993
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
143-478 2.64e-09

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: 61.63  E-value: 2.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  143 EDLRKQVAPLL---KSFQGEIDALSKRSKEAEAafltvykrlIDVPDPVPA---LDVGQQLEIKVQRLHDIETENQKLRE 216
Cdd:pfam05622   17 HELDQQVSLLQeekNSLQQENKKLQERLDQLES---------GDDSGTPGGkkyLLLQKQLEQLQEENFRLETARDDYRI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  217 TLEEYNKEFAE--VKNQEVT-----IKALK----------EKIREYEQTLKSQaetialekEQKLQ--NDFAEKERKLQE 277
Cdd:pfam05622   88 KCEELEKEVLElqHRNEELTslaeeAQALKdemdilressDKVKKLEATVETY--------KKKLEdlGDLRRQVKLLEE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  278 TQ---MSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLEranQRAEVAQREAETL---RE 351
Cdd:pfam05622  160 RNaeyMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESK-KADKLEFEYKKLE---EKLEALQKEKERLiieRD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  352 QLSSANHSLQLAsQIQKApdvlqvdgspsssprasavssllcpSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQA 431
Cdd:pfam05622  236 TLRETNEELRCA-QLQQA-------------------------ELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQH 289
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412105  432 SLTKLRE----NSASQISQLEQQLNAKNSTLKQLEEKLKG--------QADYEEVKKEL 478
Cdd:pfam05622  290 ENKMLRLgqegSYRERLTELQQLLEDANRRKNELETQNRLanqrilelQQQVEELQKAL 348
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
197-483 2.67e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 62.39  E-value: 2.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  197 LEIKVQRLHDIETEnqklRETLEEYnkefaevknqevtiKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQ 276
Cdd:TIGR02169  193 IDEKRQQLERLRRE----REKAERY--------------QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELE 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  277 ETQMSTTSKLEEAEHKLQTLQTALEK----TRTELFDLKTKYdEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 352
Cdd:TIGR02169  255 KLTEEISELEKRLEEIEQLLEELNKKikdlGEEEQLRVKEKI-GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  353 LSSANHSL------------QLASQIQKAPDV---LQVDGSPSSSPRASAVSSLLcpSQEQAIEVLTR---------SSL 408
Cdd:TIGR02169  334 LLAEIEELereieeerkrrdKLTEEYAELKEEledLRAELEEVDKEFAETRDELK--DYREKLEKLKReinelkrelDRL 411
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412105  409 EVELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLNAKNSTLKQLEEKL-KGQADYEEVKKELNTLKS 483
Cdd:TIGR02169  412 QEELQRLSEELADLNAAIAGIEAKINELeeeKEDKALEIKKQEWKLEQLAADLSKYEQELyDLKEEYDRVEKELSKLQR 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
103-438 2.79e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 2.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQVAPLLKS---FQGEIDALSKRSKEAEAAFLTVYK 179
Cdd:COG1196    249 EELEAELEELEAELAELEAELEELRLELEELELEL-----EEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEE 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  180 RLidvpdpvpaLDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQTLKSQAEtiALE 259
Cdd:COG1196    324 EL---------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL---LEAEAELAEAEEELEELAE--ELL 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  260 KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtdlERANQRA 339
Cdd:COG1196    390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE------EEEALLE 463
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  340 EVAQ--REAETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKER 417
Cdd:COG1196    464 LLAEllEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
                          330       340
                   ....*....|....*....|.
gi 1720412105  418 EIAQLVEDVQRLQASLTKLRE 438
Cdd:COG1196    544 LAAALQNIVVEDDEVAAAAIE 564
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-485 3.62e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.62  E-value: 3.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  104 KLKRELDAtatvLANRQDESEQSRKRLIEQSREFKKNTpEDLRKQV----------------------APLLKSFQGEID 161
Cdd:PRK03918   388 KLEKELEE----LEKAKEEIEEEISKITARIGELKKEI-KELKKAIeelkkakgkcpvcgrelteehrKELLEEYTAELK 462
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  162 ALSKRSKEAEAAFLTVYKRLIDVpdpvpalDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEK 241
Cdd:PRK03918   463 RIEKELKEIEEKERKLRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEK 533
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  242 IREYEQTLKSQAETiaLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQ-TALEKTRTELFDLKTKYDE---- 316
Cdd:PRK03918   534 LIKLKGEIKSLKKE--LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEylel 607
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  317 -----ETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLqlasqiqkapdvlqvdgspsssprasavssl 391
Cdd:PRK03918   608 kdaekELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY------------------------------- 656
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  392 lcpSQEQAIEvltrssLEVELAAKEREIAQLVEDVQRLQasltKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADY 471
Cdd:PRK03918   657 ---SEEEYEE------LREEYLELSRELAGLRAELEELE----KRREEIKKTLEKLKEELEEREKAKKELEKLEKALERV 723
                          410
                   ....*....|....
gi 1720412105  472 EEVKKELNTLKSME 485
Cdd:PRK03918   724 EELREKVKKYKALL 737
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
251-484 6.58e-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: 59.78  E-value: 6.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  251 SQAETIA-LEKE-QKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTkydeettakadEIEMI 328
Cdd:COG4942     17 AQADAAAeAEAElEQLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALARRIRALEQ-----------ELAAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  329 MTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLcPSQEQAIEvltrssl 408
Cdd:COG4942     82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-PARREQAE------- 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412105  409 evELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKSM 484
Cdd:COG4942    154 --ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAElAAELAELQQEAEELEAL 228
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
195-479 7.00e-09

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: 60.80  E-value: 7.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  195 QQLEIKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKSQAETIALEKEQKLQNDFAE---- 270
Cdd:TIGR04523  246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSelkn 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  271 KERKLQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMI-----------------MTDLE 333
Cdd:TIGR04523  319 QEKKLEEIQ-NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLkkenqsykqeiknlesqINDLE 397
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  334 RANQRAEVAQREAETLREQLSSANHSLQ-----LASQIQKAPDVLQvDGSPSSSPRASAVSSL--LCPSQEQAIEVLTRS 406
Cdd:TIGR04523  398 SKIQNQEKLNQQKDEQIKKLQQEKELLEkeierLKETIIKNNSEIK-DLTNQDSVKELIIKNLdnTRESLETQLKVLSRS 476
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  407 ---------SLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS---QISQLEQQLNAKNSTLKQLEEKL---KGQADY 471
Cdd:TIGR04523  477 inkikqnleQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSlkeKIEKLESEKKEKESKISDLEDELnkdDFELKK 556

                   ....*...
gi 1720412105  472 EEVKKELN 479
Cdd:TIGR04523  557 ENLEKEID 564
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
103-353 7.08e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.85  E-value: 7.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNtPEDLR-KQVAPLLKSFQGE-----IDALSKRSKEAEaaflT 176
Cdd:PRK03918   455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKlKELAEQLKELEEKlkkynLEELEKKAEEYE----K 529
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  177 VYKRLIDVPDPVpaldvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlks 251
Cdd:PRK03918   530 LKEKLIKLKGEI------KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP---- 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  252 qaetiALEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEET--------TAKAD 323
Cdd:PRK03918   600 -----FYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeyLELSR 673
                          250       260       270
                   ....*....|....*....|....*....|
gi 1720412105  324 EIEMIMTDLERANQRAEVAQREAETLREQL 353
Cdd:PRK03918   674 ELAGLRAELEELEKRREEIKKTLEKLKEEL 703
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-520 1.16e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.08  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  104 KLKRELDATATVLANRQDESEQSRKRL---------IEQSREFKKNTPEDLRKQVapllksfqGEIDALSKRSKEaeaaf 174
Cdd:PRK03918   228 KEVKELEELKEEIEELEKELESLEGSKrkleekireLEERIEELKKEIEELEEKV--------KELKELKEKAEE----- 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  175 ltvYKRLIDVpdpvpaldvgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKsqae 254
Cdd:PRK03918   295 ---YIKLSEF------------YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE---- 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  255 tiALEKEQKLQNDFAEKERKLQETQMSTTSK-LEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMtDLE 333
Cdd:PRK03918   356 --ELEERHELYEEAKAKKEELERLKKRLTGLtPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE-ELK 432
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  334 RANQRAEVAQRE----------AETLREQLSSANHSLQLASQIQKAPDVL-QVDGSPSSSPRASAVSSLLcpsqEQAIEV 402
Cdd:PRK03918   433 KAKGKCPVCGRElteehrkellEEYTAELKRIEKELKEIEEKERKLRKELrELEKVLKKESELIKLKELA----EQLKEL 508
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  403 ltRSSLEV----ELAAKEREIAQLVEDVQRLQASLTKLrENSASQISQLEQQLNAKNSTLKQLEEKLK---------GQA 469
Cdd:PRK03918   509 --EEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSL-KKELEKLEELKKKLAELEKKLDELEEELAellkeleelGFE 585
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412105  470 DYEEVKKELNTLKSM--EF-----APSEGAGTQDSTKPLEVLLLEKNRSLQSENATLR 520
Cdd:PRK03918   586 SVEELEERLKELEPFynEYlelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
193-519 1.31e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.69  E-value: 1.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  193 VGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTI--------------KALKEKIREYEQTLKSQAETIAL 258
Cdd:PRK03918   198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIeelekeleslegskRKLEEKIRELEERIEELKKEIEE 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  259 EKEQ------------------KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTA---LEKTRTELFDLKTKYdEE 317
Cdd:PRK03918   278 LEEKvkelkelkekaeeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKKLKELEKRL-EE 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  318 TTAKADEIEMIMTDLERANQ-RAEVAQREAETLREQLSSA-NHSLQLASQIQKAPDVL----QVDGSPSSSPRASAVSSL 391
Cdd:PRK03918   357 LEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELeKAKEEIEEEISKITARIgelkKEIKELKKAIEELKKAKG 436
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  392 LCP------SQEQAIEVLTRSSLEV--------ELAAKEREI---AQLVEDVQRLQASLTKLREnSASQISQLEQQLNAK 454
Cdd:PRK03918   437 KCPvcgrelTEEHRKELLEEYTAELkriekelkEIEEKERKLrkeLRELEKVLKKESELIKLKE-LAEQLKELEEKLKKY 515
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720412105  455 NstLKQLEEKLKgqaDYEEVKKELNTLKsmefapSEGAGTQDSTKPLEVL------LLEKNRSLQSENATL 519
Cdd:PRK03918   516 N--LEELEKKAE---EYEKLKEKLIKLK------GEIKSLKKELEKLEELkkklaeLEKKLDELEEELAEL 575
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
143-335 8.13e-08

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: 55.84  E-value: 8.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  143 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRLIDvpdpvpalDVGQQLEIKVQRLHDI-ETENQKL-RETLEE 220
Cdd:cd22656    113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTE--------KDQTALETLEKALKDLlTDEGGAIaRKEIKD 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  221 YNKEFAevKNQEVTIKALKEKIREYEQTLKSQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKLQTLQTA 299
Cdd:cd22656    184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1720412105  300 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 335
Cdd:cd22656    255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
121-353 8.19e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 55.69  E-value: 8.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  121 DESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKE--AEAafltvyKRLIDVPDpvpalDVGQQL- 197
Cdd:COG1340     11 EELEEKIEELREEIEELKEK-----RDELNEELKELAEKRDELNAQVKElrEEA------QELREKRD-----ELNEKVk 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  198 EIKVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLksQAETIALEKEQKLQNDFAEKERKLQE 277
Cdd:COG1340     75 ELKEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEK 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  278 TQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTK----------YDEETTAKADEIEMIMTDLERANQRAEVAQREAE 347
Cdd:COG1340    152 AK-----KALEKNEKLKELRAELKELRKEAEEIHKKikelaeeaqeLHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226

                   ....*.
gi 1720412105  348 TLREQL 353
Cdd:COG1340    227 ELHEEI 232
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
103-376 1.01e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfltvykr 180
Cdd:TIGR02168  294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE------- 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  181 lidvpdpvpaldvgqqleikvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEK 260
Cdd:TIGR02168  367 -----------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRERLQ 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  261 EQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKLQTLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLERANQ 337
Cdd:TIGR02168  421 QEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLERLQE 499
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1720412105  338 RAEVAQREAETLreqlssANHSLQLASQIQKAPDVLQVD 376
Cdd:TIGR02168  500 NLEGFSEGVKAL------LKNQSGLSGILGVLSELISVD 532
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
202-344 1.12e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 54.55  E-value: 1.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  202 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KSQAETIALEKE---QKLQNDFAEK 271
Cdd:COG1579     31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEiesLKRRISDLED 110
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412105  272 E-RKLQEtqmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTdlERANQRAEVAQR 344
Cdd:COG1579    111 EiLELME-------RIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA--EREELAAKIPPE 175
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
212-459 1.42e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.46  E-value: 1.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  212 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 290
Cdd:COG4913    231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  291 HKLQTLQTALEKTRTELFDLKTKYDEettAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-----QLASQ 365
Cdd:COG4913    309 AELERLEARLDALREELDELEAQIRG---NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLpasaeEFAAL 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  366 IQKAPDVLQVdgspsssprasavssllCPSQEQAIEVlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQIS 445
Cdd:COG4913    386 RAEAAALLEA-----------------LEEELEALEE-ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
                          250
                   ....*....|....
gi 1720412105  446 QLEQQLNAKNSTLK 459
Cdd:COG4913    448 ALAEALGLDEAELP 461
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
226-443 2.04e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 55.16  E-value: 2.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  226 AEVKNQEVTIKALKEKIREYEQTLKSQAETI--ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKT 303
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALE----QELAALEAELAELEKEIAEL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  304 RTELFDLKTKYDE-----ETTAKADEIEMIM--TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQVD 376
Cdd:COG4942     96 RAELEAQKEELAEllralYRLGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412105  377 GSPSSSPRASAVSSLlcpSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 443
Cdd:COG4942    176 LEALLAELEEERAAL---EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
98-536 2.46e-07

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 55.75  E-value: 2.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105   98 LCVAGAKLKRELDATATVLANRQDE---------SEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQ---------GE 159
Cdd:TIGR00618  398 LCKELDILQREQATIDTRTSAFRDLqgqlahakkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQslkereqqlQT 477
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  160 IDALSKRSKEAEAAFLTVYKRLIDVPDPV--------PALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ 231
Cdd:TIGR00618  478 KEQIHLQETRKKAVVLARLLELQEEPCPLcgscihpnPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ 557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  232 evtIKALKEKIREYEQTLKSQAETIALEKE------------QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQT- 298
Cdd:TIGR00618  558 ---RASLKEQMQEIQQSFSILTQCDNRSKEdipnlqnitvrlQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHl 634
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  299 -------ALEKTRTELFDLKTKYDEET---------------------TAKADEIEMIMTDLERANQRAEVAQREAETL- 349
Cdd:TIGR00618  635 qqcsqelALKLTALHALQLTLTQERVRehalsirvlpkellasrqlalQKMQSEKEQLTYWKEMLAQCQTLLRELETHIe 714
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  350 -----REQLSSANHSLQ--------LASQIQK-----APDVLQVDGSPSSSPRASAVSSLLCPSQEQAIE------VLTR 405
Cdd:TIGR00618  715 eydreFNEIENASSSLGsdlaaredALNQSLKelmhqARTVLKARTEAHFNNNEEVTAALQTGAELSHLAaeiqffNRLR 794
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  406 SSLEVELAAKEREIAQLVED------------VQRLQASLTKLRENSASQIsQLEQQLNAKNSTLKQLEEKLKGQADYEE 473
Cdd:TIGR00618  795 EEDTHLLKTLEAEIGQEIPSdedilnlqcetlVQEEEQFLSRLEEKSATLG-EITHQLLKYEECSKQLAQLTQEQAKIIQ 873
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720412105  474 VKKELNTLKSMEFAPSEGAgtqdSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSARRKGRD 536
Cdd:TIGR00618  874 LSDKLNGINQIKIQFDGDA----LIKFLHEITLYANVRLANQSEGRFHGRYADSHVNARKYQG 932
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
195-355 2.59e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 2.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 274
Cdd:COG4913    274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  275 LQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 354
Cdd:COG4913    354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429

                   .
gi 1720412105  355 S 355
Cdd:COG4913    430 S 430
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
143-483 3.21e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.16  E-value: 3.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  143 EDLRKQVApLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYN 222
Cdd:COG4717     74 KELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  223 KEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEK 302
Cdd:COG4717    153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  303 TRTELFDLKtkyDEETTAKADEIEMIMT----------------------------------------------DLERAN 336
Cdd:COG4717    232 LENELEAAA---LEERLKEARLLLLIAAallallglggsllsliltiagvlflvlgllallflllarekaslgkEAEELQ 308
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  337 QRAEVAQREAETLREQLS--------SANHSLQLASQIQKAPDVL--------QVDGSPSSSPRASAVSSLLCPSQEQAI 400
Cdd:COG4717    309 ALPALEELEEEELEELLAalglppdlSPEELLELLDRIEELQELLreaeeleeELQLEELEQEIAALLAEAGVEDEEELR 388
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  401 EVLTRS----SLEVELAAKEREIAQLVEDVQRLQASLTKlrENSASQISQLEQQLNAKNSTLKQLEEK----------LK 466
Cdd:COG4717    389 AALEQAeeyqELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREElaeleaeleqLE 466
                          410
                   ....*....|....*..
gi 1720412105  467 GQADYEEVKKELNTLKS 483
Cdd:COG4717    467 EDGELAELLQELEELKA 483
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
213-540 6.21e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.69  E-value: 6.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  213 KLRETLEEYNKEFAEVKNQEVTIKALKEKIR----EYEQTLK-SQAETIALEKEQKLqndFAEKERKLQEtqmsttsKLE 287
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIEnrldELSQELSdASRKIGEIEKEIEQ---LEQEEEKLKE-------RLE 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  288 EAEHKLQTLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLER--ANQRAEVAQREAETLREQLSSANHSLQlasq 365
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR---- 815
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  366 iqkapdvlqvdgspsssprasavssllcpsqeqaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS--- 442
Cdd:TIGR02169  816 -----------------------------------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiek 854
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  443 -------QISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKsmefapsEGAGTQDSTkplevllLEKNRSLQS 514
Cdd:TIGR02169  855 eienlngKKEELEEELEELEAALRDLESRLGDlKKERDELEAQLRELE-------RKIEELEAQ-------IEKKRKRLS 920
                          330       340
                   ....*....|....*....|....*..
gi 1720412105  515 E-NATLRISNSDLSGSARRKGRDQPES 540
Cdd:TIGR02169  921 ElKAKLEALEEELSEIEDPKGEDEEIP 947
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
195-483 6.90e-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: 54.26  E-value: 6.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKeQKLQNDFAE 270
Cdd:TIGR04523  412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIK-QNLEQKQKE 490
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  271 KERKLQETQMST--TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAET 348
Cdd:TIGR04523  491 LKSKEKELKKLNeeKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI 570
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  349 lrEQLSSANHSLqLASQIQKAPDVLQvdgspsssprasavssllcpsQEQAIEVLTRsslevELAAKEREIAQLVEDVQR 428
Cdd:TIGR04523  571 --EELKQTQKSL-KKKQEEKQELIDQ---------------------KEKEKKDLIK-----EIEEKEKKISSLEKELEK 621
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412105  429 LQASLTKLrensASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKS 483
Cdd:TIGR04523  622 AKKENEKL----SSIIKNIKSKKNKLKQEVKQIKETIKEiRNKWPEIIKKIKESKT 673
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
204-482 7.21e-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: 54.06  E-value: 7.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  204 LHDIETENQKLRETLEEYNKEFAEVKN----------QEVTIKALKEKIREYEQTLKSQAETIALEKEQKlqndfaEKER 273
Cdd:pfam10174  201 LDQKEKENIHLREELHRRNQLQPDPAKtkalqtviemKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDR------EEEI 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  274 KLQETQMSTTSKLeeaEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLR 350
Cdd:pfam10174  275 KQMEVYKSHSKFM---KNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALR 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  351 EQLSSANHSLQ---------------LASQIQKAPDVLQVdgspsssprasavssllcpsQEQAIEVLTR--SSLEVELA 413
Cdd:pfam10174  352 LRLEEKESFLNkktkqlqdlteekstLAGEIRDLKDMLDV--------------------KERKINVLQKkiENLQEQLR 411
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412105  414 AKEREIAQLVEDVQRLQASLTklreNSASQISQLEQQLNAKNSTLKQLEEK--LKGQADYEEV---KKELNTLK 482
Cdd:pfam10174  412 DKDKQLAGLKERVKSLQTDSS----NTDTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
202-374 8.32e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 8.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  202 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALekeQKLQNDFAEKERKLQETQmS 281
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAE---LDALQERREALQRLAEYSWDEIDV---ASAEREIAELEAELERLD-A 682
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  282 TTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 357
Cdd:COG4913    683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
                          170
                   ....*....|....*..
gi 1720412105  358 HSLQLASQIQKAPDVLQ 374
Cdd:COG4913    763 VERELRENLEERIDALR 779
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
103-353 1.30e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTP-----EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTV 177
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  178 YKRlidvpdpvpALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFA----EVKNQEVTIKALKEKIREYEQTLKSQA 253
Cdd:TIGR02168  816 NEE---------AANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLNERASLE 886
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  254 ETIALEKE--QKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTD 331
Cdd:TIGR02168  887 EALALLRSelEELSEELRELESKRSELR----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEEAEAL 959
                          250       260
                   ....*....|....*....|..
gi 1720412105  332 LERANQRAEVAQREAETLREQL 353
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKI 981
COG5022 COG5022
Myosin heavy chain [General function prediction only];
114-374 1.49e-06

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 53.16  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  114 TVLANRQDESEQSRKRLIE---QSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKrSKEAEAAFLTVYKRLIDVPDPv 188
Cdd:COG5022    868 TIYLQSAQRVELAERQLQElkiDVKSISslKLVNLELESEIIELKKSLSSDLIENLE-FKTELIARLKKLLNNIDLEEG- 945
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  189 PALDVGQQLEikVQRLHdieTENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKS--------QAETIALEK 260
Cdd:COG5022    946 PSIEYVKLPE--LNKLH---EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAElskqygalQESTKQLKE 1020
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  261 EQK----LQND----FAEKERKLQETQMS---TTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmiM 329
Cdd:COG5022   1021 LPVevaeLQSAskiiSSESTELSILKPLQklkGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTIN--V 1098
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1720412105  330 TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQ 374
Cdd:COG5022   1099 KDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLE 1143
PHA03247 PHA03247
large tegument protein UL36; Provisional
845-1028 2.45e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  845 SASPMSTVSTYPPLAISLKKTPAAPETST--AALPSAPALKKEAQDVPTLDPPGSADAAQGVLRPMksELVRGSTWKDPW 922
Cdd:PHA03247   269 PETARGATGPPPPPEAAAPNGAAAPPDGVwgAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGAM--EVVSPLPRPRQH 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  923 WSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERsqlqgpsasaeywKEWPSAESPYSQSSELSLTGASRSETPQ 1002
Cdd:PHA03247   347 YPLGFPKRRRPTWTPPSSLEDLSAGRHHPKRASLPTRKR-------------RSARHAATPFARGPGGDDQTRPAAPVPA 413
                          170       180
                   ....*....|....*....|....*.
gi 1720412105 1003 NSPLPSSPIVPMAKPAKPSVPPLTPE 1028
Cdd:PHA03247   414 SVPTPAPTPVPASAPPPPATPLPSAE 439
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
208-528 2.71e-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: 52.28  E-value: 2.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  208 ETENQKLRETLEEYNKEFA---EVKNQEVTIKALKEKIREYEQTLKSQAETIALEKE----QKLQNDFAEKERKLQETQM 280
Cdd:pfam02463  209 ALEYYQLKEKLELEEEYLLyldYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEklaqVLKENKEEEKEKKLQEEEL 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  281 STTSKLEEAEHKlqtlQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTDLERANQRAEVAQREAETLREQLSSANHS 359
Cdd:pfam02463  289 KLLAKEEEELKS----ELLKLERRKVDDEEKLKESEKEKKKAEkELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL 364
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  360 LQLASQIQKAPDVLQVDGSPSSSPRASAvssllcpsQEQAIEVLTRSSLEVELAAKEREiaQLVEDVQRLQASLTKLREn 439
Cdd:pfam02463  365 QEKLEQLEEELLAKKKLESERLSSAAKL--------KEEELELKSEEEKEAQLLLELAR--QLEDLLKEEKKEELEILE- 433
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  440 sASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATL 519
Cdd:pfam02463  434 -EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512

                   ....*....
gi 1720412105  520 RISNSDLSG 528
Cdd:pfam02463  513 LALIKDGVG 521
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
281-652 4.37e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.98  E-value: 4.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  281 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 360
Cdd:COG3883     20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  361 QLASQIQKAPDVLqvdgspsssPRASAVSSLLcpSQEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRE 438
Cdd:COG3883     96 YRSGGSVSYLDVL---------LGSESFSDFL--DRLSALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  439 NSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKEL-NTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENA 517
Cdd:COG3883    165 ELEAAKAELEAQQAEQEALLAQLSAE---EAAAEAQLAELeAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  518 TLRISNSDLSGSARRKGRDQPESRRPGPLPASPPPQLPRNTGEQVSNTNGTHHFSPAGLSQDFFSSNLASPSLPLASTGK 597
Cdd:COG3883    242 AAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGA 321
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720412105  598 FALNSLLQRQLMQSFYSKAMQEAGSTSTIFSTGPYSTNSISSPSPLQQSPDVNGM 652
Cdd:COG3883    322 VVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGYV 376
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
197-469 4.40e-06

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 51.76  E-value: 4.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  197 LEIKVQRLH--------DIETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKSQAETIALEKEQ------ 262
Cdd:pfam12128  256 AELRLSHLHfgyksdetLIASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealed 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  263 ---KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----R 334
Cdd:pfam12128  330 qhgAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaR 406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  335 ANQRAE---VAQREAETLREQLSSANHSL-----QLASQIQKAPdvLQVDGSPsssprasaVSSLLCPSQEQAIEVLTRS 406
Cdd:pfam12128  407 DRQLAVaedDLQALESELREQLEAGKLEFneeeyRLKSRLGELK--LRLNQAT--------ATPELLLQLENFDERIERA 476
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720412105  407 SLEVELAAKEreiaqlVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQA 469
Cdd:pfam12128  477 REEQEAANAE------VERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQA 533
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
216-461 4.85e-06

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: 49.13  E-value: 4.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  216 ETLEEYNKEFAEVKN--QEVT------IKALKEKIREyeqtLKSQAEtialEKEQKLQNDFAEKERkLQEtqmsttsKLE 287
Cdd:pfam13851    1 ELMKNHEKAFNEIKNyyNDITrnnlelIKSLKEEIAE----LKKKEE----RNEKLMSEIQQENKR-LTE-------PLQ 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  288 EAEHKLQTLQTAL---EKTRTELfdlktkydEETTAKADEIEMIMTDLERAN----QRAEVAQREAETLREQLSSANHSL 360
Cdd:pfam13851   65 KAQEEVEELRKQLenyEKDKQSL--------KNLKARLKVLEKELKDLKWEHevleQRFEKVERERDELYDKFEAAIQDV 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  361 QLASQIQkapdvlqvdgspsssprasavSSLLcpsqEQAIEVLTRsslevELAAKEREIAQLvedvqrLQASltKLRENS 440
Cdd:pfam13851  137 QQKTGLK---------------------NLLL----EKKLQALGE-----TLEKKEAQLNEV------LAAA--NLDPDA 178
                          250       260
                   ....*....|....*....|..
gi 1720412105  441 ASQISQ-LEQQLNAKNSTLKQL 461
Cdd:pfam13851  179 LQAVTEkLEDVLESKNQLIKDL 200
ClyA_NheA-like cd22654
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ...
190-481 5.25e-06

Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.


Pssm-ID: 439152 [Multi-domain]  Cd Length: 333  Bit Score: 50.34  E-value: 5.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  190 ALDVGQQLEIKVQRLHDIeTENQKL-----RETLEEYNKEFAEVkNQEvtIKALKEKIREYEQTLKSQAETIALEKEQKl 264
Cdd:cd22654     18 ALVILKQPNVKIEAMPSL-TNHQQTakenvREWLDEYNPKLIDL-NQD--MINFSQRFNNYYDKLYDLAGKINEDEQAK- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  265 qNDFAEKERKLQEtqmsttskleeaehKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANqrAEVAQr 344
Cdd:cd22654     93 -EDFLNGINKLQS--------------QLQTIQNSMEQTSSNLNRFKTLLDADSKNFSTDAKKAIDSLSGSN--GEIAQ- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  345 eaetLREQLSSANHSLQlaSQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSSL----------EVELAA 414
Cdd:cd22654    155 ----LRTQIKTINDEIQ--EELTKILNRPIEVGDGSINIGKQVFTITITTATTKTVDVTSIGGLingignasddEVKEAA 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412105  415 KerEIAQLVEDVQRLQASLTKLrENSASQISQLEQQLNAKNSTLKqleeklKGQADYEEVKKELNTL 481
Cdd:cd22654    229 N--KIQQKQKELVDLIKKLSDA-EIQATQLTLVEDQVNGFTELIK------RQIATLENLVEDWEML 286
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
227-483 5.44e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 5.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  227 EVKNQEVTIKALKEKIREYEQ------TLKSQAETiaLEKEQKLQNDFAEKERKLQETQ-MSTTSKLEEAEHKLQTLQTA 299
Cdd:COG4913    219 EEPDTFEAADALVEHFDDLERahealeDAREQIEL--LEPIRELAERYAAARERLAELEyLRAALRLWFAQRRLELLEAE 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  300 LEKTRTELFDLKTKydeettakadeiemimtdLERANQRAEVAQREAETLREQLssanhslqlasqiqkapdvLQVDGsp 379
Cdd:COG4913    297 LEELRAELARLEAE------------------LERLEARLDALREELDELEAQI-------------------RGNGG-- 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  380 sssprasavssllcpsqeQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL-------RENSASQISQLEQQLN 452
Cdd:COG4913    338 ------------------DRLE-----QLEREIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLE 394
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1720412105  453 AKNSTLKQLEEKL--------KGQADYEEVKKELNTLKS 483
Cdd:COG4913    395 ALEEELEALEEALaeaeaalrDLRRELRELEAEIASLER 433
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
103-537 6.55e-06

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 50.99  E-value: 6.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEqsrkRLIEQSREFKKNTPEDlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTV---YK 179
Cdd:pfam12128  304 DELNGELSAADAAVAKDRSELE----ALEDQHGAFLDADIET-AAADQEQLPSWQSELENLEERLKALTGKHQDVtakYN 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  180 RLIdvpdpvpaLDVGQQLEIKVQRLHDiETENQKlretlEEYNKEFAEVKNQ-EVTIKALKEKIREYEQTLKSQAETIAL 258
Cdd:pfam12128  379 RRR--------SKIKEQNNRDIAGIKD-KLAKIR-----EARDRQLAVAEDDlQALESELREQLEAGKLEFNEEEYRLKS 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  259 E-KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAkadeiemimtdLERANQ 337
Cdd:pfam12128  445 RlGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEA-----------LRQASR 513
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  338 RAEVAQREAETLREQLSSANHSLqLASQIQKAPDVLQVDGSpsssprasavssLLCPsqeqaiEVLTRSSLEVEL----A 413
Cdd:pfam12128  514 RLEERQSALDELELQLFPQAGTL-LHFLRKEAPDWEQSIGK------------VISP------ELLHRTDLDPEVwdgsV 574
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  414 AKEREIAQLVEDVQRLQA-SLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLkGQAdyeevKKELNTLK-SMEFAPSEG 491
Cdd:pfam12128  575 GGELNLYGVKLDLKRIDVpEWAASEEELRERLDKAEEALQSAREKQAAAEEQL-VQA-----NGELEKASrEETFARTAL 648
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720412105  492 AGTQDSTKPL----EVLLLEKNRSLQSENATLRISNSDLSGSARRKGRDQ 537
Cdd:pfam12128  649 KNARLDLRRLfdekQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKH 698
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
210-480 8.32e-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: 50.74  E-value: 8.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  210 ENQKLRETLEeyNKEFAEVKNQEVTIKALKEKIREYEqtlksqaetiALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 289
Cdd:pfam02463  174 ALKKLIEETE--NLAELIIDLEELKLQELKLKEQAKK----------ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  290 EHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERanqRAEVAQREAETLREQLSSANHSLQLASQIQKa 369
Cdd:pfam02463  242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE---ELKLLAKEEEELKSELLKLERRKVDDEEKLK- 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  370 pdVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 449
Cdd:pfam02463  318 --ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1720412105  450 QLNAKNSTLKQLEEKLKGQADYEEVKKELNT 480
Cdd:pfam02463  396 ELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
208-473 8.62e-06

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 50.56  E-value: 8.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  208 ETENQKLRETLEEYNKEFAEV--KNQEVTikalKEKIREYEQTlksQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 285
Cdd:pfam01576   11 EEELQKVKERQQKAESELKELekKHQQLC----EEKNALQEQL---QAETELCAEAEEMRARLAARKQELEEILHELESR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  286 LEEAEHKLQTLQTALEKTRTELFDLKTKYDEE-------------TTAKADEIEMIMTDLERANQRaevAQREAETLREQ 352
Cdd:pfam01576   84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLEDQNSK---LSKERKLLEER 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  353 LSsaNHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRsSLEVELAAKEREIAQLVEDVQRLQAS 432
Cdd:pfam01576  161 IS--EFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR-KLEGESTDLQEQIAELQAQIAELRAQ 237
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1720412105  433 LTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEE 473
Cdd:pfam01576  238 LAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQE 278
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
190-443 9.02e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.76  E-value: 9.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  190 ALDVGQQLEIKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL--EKEQKLQN 266
Cdd:COG4942     18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  267 DFAEKERKLQET-----QMSTTSKLEEAEHKLQTLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 341
Cdd:COG4942     98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  342 AQREAETLREQLSSANHSLQLASQiqkapdvlqvdgspsssprasavssllcpSQEQAIEVLTR--SSLEVELAAKEREI 419
Cdd:COG4942    172 ERAELEALLAELEEERAALEALKA-----------------------------ERQKLLARLEKelAELAAELAELQQEA 222
                          250       260
                   ....*....|....*....|....
gi 1720412105  420 AQLVEDVQRLQASLTKLRENSASQ 443
Cdd:COG4942    223 EELEALIARLEAEAAAAAERTPAA 246
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
104-485 1.06e-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: 50.49  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  104 KLKRELDATATVLANRQDESEQSRKRLIEqsrefkKNTPEDLRKQVAPLLKSFQGeidalskrsKEAEAAFLtvykrlid 183
Cdd:pfam05483  388 KKSSELEEMTKFKNNKEVELEELKKILAE------DEKLLDEKKQFEKIAEELKG---------KEQELIFL-------- 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  184 vpdpvpaldvgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAE---------VKNQEVTIKALKEKIREYEQTLKSQAE 254
Cdd:pfam05483  445 -------------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlktelekekLKNIELTAHCDKLLLENKELTQEASDM 511
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  255 TIALEKEQK-LQNDFAEKERKLQEtqmsttskLEEAEHKLQTLQTALEKTRTELF----DLKTKYDE-ETTAKADEIEMI 328
Cdd:pfam05483  512 TLELKKHQEdIINCKKQEERMLKQ--------IENLEEKEMNLRDELESVREEFIqkgdEVKCKLDKsEENARSIEYEVL 583
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  329 mtdleRANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSL---LCPSQEQAIEVLTR 405
Cdd:pfam05483  584 -----KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLeleLASAKQKFEEIIDN 658
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  406 SSLEVELAAKEREiaQLVEDVQRLQASLtklrENSASQISQLEQQLNAKNSTLKQLEEKLKGQAD--YEEVKKELNTLKS 483
Cdd:pfam05483  659 YQKEIEDKKISEE--KLLEEVEKAKAIA----DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDkiIEERDSELGLYKN 732

                   ..
gi 1720412105  484 ME 485
Cdd:pfam05483  733 KE 734
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
103-464 1.15e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEQSRkrlIEQSREFKKNTPEDLRKQVAPLlKSFQGEIDALSKRSKEAEAAfLTVYKRLI 182
Cdd:COG4717    112 EELREELEKLEKLLQLLPLYQELEA---LEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEE-LEELLEQL 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNqEVTIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:COG4717    187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLGLG 265
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  263 KLQNDFAE------------------KERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTEL---FDLKTKYDEETTAK 321
Cdd:COG4717    266 GSLLSLILtiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDR 345
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  322 ADEIEMIMTDLERANQRAEVAQREAE----------TLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSL 391
Cdd:COG4717    346 IEELQELLREAEELEEELQLEELEQEiaallaeagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720412105  392 LCPSQEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAsqISQLEQQLNAKNSTLKQLEEK 464
Cdd:COG4717    426 DEEELEEELE-----ELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEE 491
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
274-479 1.15e-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: 48.38  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  274 KLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADeiemimTDLERANQRAEVAQREA--ETLRE 351
Cdd:COG1579     11 DLQELD----SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED------LEKEIKRLELEIEEVEAriKKYEE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  352 QLSSA--NHSLQ-LASQIQkapdvlqvdgspsssprasavssllcpSQEQAIEVLTRSSLEV--ELAAKEREIAQLVEDV 426
Cdd:COG1579     81 QLGNVrnNKEYEaLQKEIE---------------------------SLKRRISDLEDEILELmeRIEELEEELAELEAEL 133
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720412105  427 QRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQ--ADYEEVKKELN 479
Cdd:COG1579    134 AELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKN 188
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
181-484 1.42e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  181 LIDVPDPVPALDVGQQLEIKVQrlhDIETENQKLR---------ETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKS 251
Cdd:COG3206     60 LVEPQSSDVLLSGLSSLSASDS---PLETQIEILKsrpvlervvDKLNLDEDPLGEEASREAAIERLRKNL-----TVEP 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  252 QAETIAL---------EKEQKLQNDFAE------KERKLQETQMSTT---SKLEEAEHKLQTLQTALE--KTRTELFDLk 311
Cdd:COG3206    132 VKGSNVIeisytspdpELAAAVANALAEayleqnLELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL- 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  312 tkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSanhSLQLASQIQKAPDVLQVDGSPSSsprasavssl 391
Cdd:COG3206    211 ---SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS---GPDALPELLQSPVIQQLRAQLAE---------- 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  392 lcpsQEQAIEVLTRSSLE-----VELAAKEREI-AQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKl 465
Cdd:COG3206    275 ----LEAELAELSARYTPnhpdvIALRAQIAALrAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL- 349
                          330
                   ....*....|....*....
gi 1720412105  466 kgQADYEEVKKELNTLKSM 484
Cdd:COG3206    350 --EAELRRLEREVEVAREL 366
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
212-477 1.64e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.65  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  212 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYE----------QTLKSQAETIALEKE-------------------- 261
Cdd:PRK02224   237 DEADEVLEEHEERREELETLEAEIEDLRETIAETErereelaeevRDLRERLEELEEERDdllaeaglddadaeavearr 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  262 QKLQNDFAEKERKLQETQMSTTSKLEEAE-----------------HKLQTLQTALEKTRTELFDLKTK---YDEETTAK 321
Cdd:PRK02224   317 EELEDRDEELRDRLEECRVAAQAHNEEAEslredaddleeraeelrEEAAELESELEEAREAVEDRREEieeLEEEIEEL 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  322 ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQ-LASQIQKAPDVLQvDGSpsssprasavssllCPSQEQAI 400
Cdd:PRK02224   397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRtARERVEEAEALLE-AGK--------------CPECGQPV 461
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  401 E----VLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE--NSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEV 474
Cdd:PRK02224   462 EgsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541

                   ...
gi 1720412105  475 KKE 477
Cdd:PRK02224   542 LRE 544
46 PHA02562
endonuclease subunit; Provisional
236-464 1.68e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 49.63  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  236 KALKEKIREYEQTLKSQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKLQTLQT---------- 298
Cdd:PHA02562   170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEIEELtdellnlvmd 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  299 ------ALEKTRTELFDLKTKYdeETTAKadEIEMI---------MTDLERANQRaevaqreAETLREQLSSANHSLqla 363
Cdd:PHA02562   250 iedpsaALNKLNTAAAKIKSKI--EQFQK--VIKMYekggvcptcTQQISEGPDR-------ITKIKDKLKELQHSL--- 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  364 SQIQKAPDVLQVdgspsssprasavssLLCPSQEQAIEVLTrssLEVELAAKEREIAQLVEDVQRLQASLTKL---RENS 440
Cdd:PHA02562   316 EKLDTAIDELEE---------------IMDEFNEQSKKLLE---LKNKISTNKQSLITLVDKAKKVKAAIEELqaeFVDN 377
                          250       260
                   ....*....|....*....|....
gi 1720412105  441 ASQISQLEQQLNAKNSTLKQLEEK 464
Cdd:PHA02562   378 AEELAKLQDELDKIVKTKSELVKE 401
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
203-312 1.98e-05

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 48.48  E-value: 1.98e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105   203 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDFA---EKERKLQ 276
Cdd:smart00787  138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 1720412105   277 ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKT 312
Cdd:smart00787  218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
203-356 2.24e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 47.61  E-value: 2.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  203 RLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIAlEKEQKLQnDFAEKERKLQETQMS- 281
Cdd:COG1579     11 DLQELDSELDRLEHRLKELPAELAELEDE---LAALEARLEAAKTELEDLEKEIK-RLELEIE-EVEARIKKYEEQLGNv 85
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412105  282 TTSK-LEEAEHKLQTL---QTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSA 356
Cdd:COG1579     86 RNNKeYEALQKEIESLkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
PTZ00121 PTZ00121
MAEBL; Provisional
103-331 2.30e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 2.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaafltvykrli 182
Cdd:PTZ00121  1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----------- 1657
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  183 dvPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKsqAETIALEKEQ 262
Cdd:PTZ00121  1658 --ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAE 1733
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412105  263 KLQNDFAEKERKLQETQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 331
Cdd:PTZ00121  1734 EAKKEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
110-469 2.54e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  110 DATATVLANRQDE----SEQSRKRLIEQ--SREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRlid 183
Cdd:PRK02224   306 DADAEAVEARREEledrDEELRDRLEECrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR--- 382
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  184 vPDPVPALDvgQQLEIKVQRLHDIETEnqklRETLEEYNKEFAEVKNqevtikALKEKIREYEQTLKSQAETIAlEKEQK 263
Cdd:PRK02224   383 -REEIEELE--EEIEELRERFGDAPVD----LGNAEDFLEELREERD------ELREREAELEATLRTARERVE-EAEAL 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  264 LQ-NDFAEKERKLQETQMSTTskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAE 340
Cdd:PRK02224   449 LEaGKCPECGQPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIA 526
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  341 VAQREAETLREQLSSANHSLQ-LASQIQKAPDVLQvDGSPSSSPRASAVSSLlcpSQEQAIEVLTRSSLEvELAAKEREI 419
Cdd:PRK02224   527 ERRETIEEKRERAEELRERAAeLEAEAEEKREAAA-EAEEEAEEAREEVAEL---NSKLAELKERIESLE-RIRTLLAAI 601
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720412105  420 AQLVEDVQRLQASltklRENSASQISQLEQQLNAKNSTLKQLEEKLKGQA 469
Cdd:PRK02224   602 ADAEDEIERLREK----REALAELNDERRERLAEKRERKRELEAEFDEAR 647
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
215-519 2.89e-05

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 48.89  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  215 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETialekEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQ 294
Cdd:TIGR00606  237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-----KKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  295 TlqtalektrtelfdlktkydeETTAKADEIEMIMTDLERANQ-RAEVAQREAETLREQLSSA-------NHSLQLASQI 366
Cdd:TIGR00606  312 R---------------------TVREKERELVDCQRELEKLNKeRRLLNQEKTELLVEQGRLQlqadrhqEHIRARDSLI 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  367 QKAPDVLQVDGSPSSSPRASAVSSLLCPSQE-QAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQIS 445
Cdd:TIGR00606  371 QSLATRLELDGFERGPFSERQIKNFHTLVIErQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILE 450
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412105  446 QLEQQLNAKNSTLKQLEEKLKG--QADYEEVKKELNTLKSMEFAPSEGAGTQD-STKPLEVLLLEKNRSLQSENATL 519
Cdd:TIGR00606  451 KKQEELKFVIKELQQLEGSSDRilELDQELRKAERELSKAEKNSLTETLKKEVkSLQNEKADLDRKLRKLDQEMEQL 527
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
193-468 3.36e-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: 48.56  E-value: 3.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  193 VGQQLEIKVQRLHDIETENQKLR--------------ETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL 258
Cdd:pfam05483  132 VSLKLEEEIQENKDLIKENNATRhlcnllketcarsaEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARL 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  259 EKEQKLQNDFAEKERKLQETQMSTTSK----------LEEAEHKLQTLQTALEKTRTELFDL--KTKYDEE----TTAKA 322
Cdd:pfam05483  212 EMHFKLKEDHEKIQHLEEEYKKEINDKekqvsllliqITEKENKMKDLTFLLEESRDKANQLeeKTKLQDEnlkeLIEKK 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  323 DEIEMIMTDLERANQRAEVAQReaeTLREQLSSANHSLQLASQIQKApdvlQVDGSPSSSPRASAVSSLLcPSQEQAIEV 402
Cdd:pfam05483  292 DHLTKELEDIKMSLQRSMSTQK---ALEEDLQIATKTICQLTEEKEA----QMEELNKAKAAHSFVVTEF-EATTCSLEE 363
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720412105  403 LTRSSLEvELAAKEREIAQLVEDVQRLQASL---TKLRENSASQISQLEQQLNAKNSTL---KQLE---EKLKGQ 468
Cdd:pfam05483  364 LLRTEQQ-RLEKNEDQLKIITMELQKKSSELeemTKFKNNKEVELEELKKILAEDEKLLdekKQFEkiaEELKGK 437
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
1340-1425 3.86e-05

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 45.51  E-value: 3.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105 1340 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRelfieeiqagsQGQAGASDSPSA 1419
Cdd:COG5576     52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKK-----------KRSGKVEQRPGE 120

                   ....*.
gi 1720412105 1420 RSSRAA 1425
Cdd:COG5576    121 EEADLA 126
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
103-371 4.03e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 4.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEQSRKRLiEQSREFKKNTPEDLRkqvaplLKSFQGEIDALSKRSKEAEAAFLTVykrli 182
Cdd:COG4913    620 AELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEID------VASAEREIAELEAELERLDASSDDL----- 687
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  183 dvpdpvpaldvgQQLEikvQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:COG4913    688 ------------AALE---EQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLELRA 749
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  263 KLQNDFAEKERKLQETQMSttsklEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERANQ-RAEV 341
Cdd:COG4913    750 LLEERFAAALGDAVERELR-----ENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD---LDADLESLPEyLALL 821
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1720412105  342 AQREAETL-------REQLSSANHS--LQLASQIQKAPD 371
Cdd:COG4913    822 DRLEEDGLpeyeerfKELLNENSIEfvADLLSKLRRAIR 860
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
116-322 4.19e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.47  E-value: 4.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  116 LANRQDESEQSRKRLieqsREFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPAL 191
Cdd:COG3206    184 LPELRKELEEAEAAL----EEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  192 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDF 268
Cdd:COG3206    260 LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEAeleALQAREASLQAQL 336
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720412105  269 AEKERKLQEtqmsttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA 322
Cdd:COG3206    337 AQLEARLAE--------LPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
PTZ00121 PTZ00121
MAEBL; Provisional
103-491 6.10e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 6.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvAPLLKSFQGEIDALSKRSKEAEAAfltvyKRLI 182
Cdd:PTZ00121  1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEK-----KKAD 1434
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRET--LEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETI---- 256
Cdd:PTZ00121  1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkade 1514
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  257 ---ALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLE 333
Cdd:PTZ00121  1515 akkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKKAE 1590
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  334 --RANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASA--VSSLLCPSQEQAIEVLTRSSLE 409
Cdd:PTZ00121  1591 eaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkAEELKKAEEENKIKAAEEAKKA 1670
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  410 VELAAKEREIAQLVEDVQRLQASLTKLRENS--ASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFA 487
Cdd:PTZ00121  1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAkkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750

                   ....
gi 1720412105  488 PSEG 491
Cdd:PTZ00121  1751 KDEE 1754
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
235-486 1.05e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  235 IKALKEKIREYEqTLKSQAETIALEKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY 314
Cdd:COG4717     48 LERLEKEADELF-KPQGRKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLL 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  315 D-EETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLASQIQKApdvlqvdgspsssprasavssllc 393
Cdd:COG4717    126 QlLPLYQELEALEAELAELPERLEELEERLEELRELEEELE------ELEAELAEL------------------------ 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  394 psQEQAIEVLTRSSLevelaAKEREIAQLVEDVQRLQAsltklrensasQISQLEQQLNAKNSTLKQLEEKLKGQADYEE 473
Cdd:COG4717    176 --QEELEELLEQLSL-----ATEEELQDLAEELEELQQ-----------RLAELEEELEEAQEELEELEEELEQLENELE 237
                          250
                   ....*....|...
gi 1720412105  474 VKKELNTLKSMEF 486
Cdd:COG4717    238 AAALEERLKEARL 250
PRK10263 PRK10263
DNA translocase FtsK; Provisional
787-1052 1.27e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.00  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  787 EPVQTSSTSSSGNSDDairsILQQARREMEAQQAALDPALKPAPLSQPdltiltpkhLSASPMSTVSTYPPLAISLKKTP 866
Cdd:PRK10263   276 EEITYTARGVAADPDD----VLFSGNRATQPEYDEYDPLLNGAPITEP---------VAVAAAATTATQSWAAPVEPVTQ 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  867 AAPETSTAALPSAPALKKEAQDVPTLDPPGSADAAQGvLRPMKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTA 946
Cdd:PRK10263   343 TPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEG-YPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYY 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  947 SGKERAGSSQPRAERSQLQGPSASA-------EYWKEWPSAEsPYSQSSELSLTGASRSETPQNSPLPSSPIVPMAKPAK 1019
Cdd:PRK10263   422 APAPEQPAQQPYYAPAPEQPVAGNAwqaeeqqSTFAPQSTYQ-TEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETK 500
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1720412105 1020 PSVPPLtpeqyevYMYQEVDtiELTRQVKEKLA 1052
Cdd:PRK10263   501 PARPPL-------YYFEEVE--EKRAREREQLA 524
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
145-366 1.35e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  145 LRKQVAPLLKSFQgEIDALSKRSKEAEAAFLTVYKR--LIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLR------- 215
Cdd:COG4717    293 LAREKASLGKEAE-ELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqe 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  216 --ETLEEYN----KEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIaleKEQKLQNDFAEKERKLQETQMsttsKLEEA 289
Cdd:COG4717    372 iaALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGEL---EELLEALDEEELEEELEELEE----ELEEL 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  290 EHKLQTLQTALEKTRTELFDLKTkyDEETTAKADEIEMI---MTDLERANQRAEVAQREAETLREQLSSAN--HSLQLAS 364
Cdd:COG4717    445 EEELEELREELAELEAELEQLEE--DGELAELLQELEELkaeLRELAEEWAALKLALELLEEAREEYREERlpPVLERAS 522

                   ..
gi 1720412105  365 QI 366
Cdd:COG4717    523 EY 524
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
263-508 1.71e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  263 KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE---ETTAKADEIEMIMTDLERANQRA 339
Cdd:COG4372     17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarsELEQLEEELEELNEQLQAAQAEL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  340 EVAQREAETLREQLSSANHSLQlasQIQKAPDVLQvdgspsssprasavssllcpSQEQAIEVlTRSSLEVELAAKEREI 419
Cdd:COG4372     97 AQAQEELESLQEEAEELQEELE---ELQKERQDLE--------------------QQRKQLEA-QIAELQSEIAEREEEL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  420 AQLVEDVQRLQASLTKLRENSA--------SQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAPSEG 491
Cdd:COG4372    153 KELEEQLESLQEELAALEQELQalseaeaeQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
                          250
                   ....*....|....*..
gi 1720412105  492 AGTQDSTKPLEVLLLEK 508
Cdd:COG4372    233 LALSALLDALELEEDKE 249
PTZ00121 PTZ00121
MAEBL; Provisional
216-476 2.08e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  216 ETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKER------------KLQETQMSTT 283
Cdd:PTZ00121  1030 EELTEYGNNDDVLKEKDI-IDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDnradeateeafgKAEEAKKTET 1108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  284 SKLEEAEHKLQTLQTALEKTRTELF---DLKTKYDEETTAKADEIEMIMTDLERAnQRAEVAQREAETLREQLSSANHSL 360
Cdd:PTZ00121  1109 GKAEEARKAEEAKKKAEDARKAEEArkaEDARKAEEARKAEDAKRVEIARKAEDA-RKAEEARKAEDAKKAEAARKAEEV 1187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  361 QLASQIQKAPDVLQVDgSPSSSPRASAVSSLLCPSQEQAIEVLTRssleVELAAKEREIAQLVEDVqRLQASLTKLRENS 440
Cdd:PTZ00121  1188 RKAEELRKAEDARKAE-AARKAEEERKAEEARKAEDAKKAEAVKK----AEEAKKDAEEAKKAEEE-RNNEEIRKFEEAR 1261
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1720412105  441 ASQISQLEQQLNA----KNSTLKQLEEKLKGQA--DYEEVKK 476
Cdd:PTZ00121  1262 MAHFARRQAAIKAeearKADELKKAEEKKKADEakKAEEKKK 1303
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
259-539 2.10e-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: 45.89  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  259 EKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQR 338
Cdd:pfam05557   48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELE 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  339 AEVAQREAETLREQL----SSANHSLQLASQIQKAPDVLQVdgspssspRASAVSSLlcpsqEQAIEVLTRSSLEVElAA 414
Cdd:pfam05557  127 LQSTNSELEELQERLdllkAKASEAEQLRQNLEKQQSSLAE--------AEQRIKEL-----EFEIQSQEQDSEIVK-NS 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  415 KER--EIAQLVEDVQRLQASLTKLRENSASqISQLEQQLNAKNSTLKQLE----EKLKGQADYEEVKKELNTLKSMefap 488
Cdd:pfam05557  193 KSElaRIPELEKELERLREHNKHLNENIEN-KLLLKEEVEDLKRKLEREEkyreEAATLELEKEKLEQELQSWVKL---- 267
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720412105  489 segAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSARRKGRDQPE 539
Cdd:pfam05557  268 ---AQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRE 315
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
211-462 2.13e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 45.90  E-value: 2.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  211 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 289
Cdd:pfam07111   58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  290 EHK-LQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQlas 364
Cdd:pfam07111  138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELE--- 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  365 qiqkapdvlqvdgspsssPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAS--LTKLRENSAS 442
Cdd:pfam07111  215 ------------------AQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATveLLQVRVQSLT 276
                          250       260
                   ....*....|....*....|.
gi 1720412105  443 QISQL-EQQLNAKNSTLKQLE 462
Cdd:pfam07111  277 HMLALqEEELTRKIQPSDSLE 297
PRK11281 PRK11281
mechanosensitive channel MscK;
186-466 2.14e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.06  E-value: 2.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  186 DPVPALDVGQQLEiKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK-SQAETIALEKeqkl 264
Cdd:PRK11281    34 DLPTEADVQAQLD-ALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRqAQAELEALKD---- 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  265 QNDFAEKER--KLQETQMSttSKLEEAEHKLQTLQTALEKTRTELFDLKTKydeettakadeiemimtdLERA-NQRAEV 341
Cdd:PRK11281   109 DNDEETRETlsTLSLRQLE--SRLAQTLDQLQNAQNDLAEYNSQLVSLQTQ------------------PERAqAALYAN 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  342 AQREAEtLREQLSSanhslqlaSQIQKAPdvlqvdgspsssprasavsslLCPSQEQAievltrssLEVELAAKEREIA- 420
Cdd:PRK11281   169 SQRLQQ-IRNLLKG--------GKVGGKA---------------------LRPSQRVL--------LQAEQALLNAQNDl 210
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720412105  421 --QLVEDVQRLQASLTKLRENSASQISQLEQQL-------NAKNstLKQLEEKLK 466
Cdd:PRK11281   211 qrKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLqllqeaiNSKR--LTLSEKTVQ 263
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
195-358 2.35e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.90  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ-EVTIKALKEKIREYEQtLKSQAETIALEKE--QKLQNDFAEK 271
Cdd:COG1340     43 EKRDELNAQVKELREEAQELREKRDELNEKVKELKEErDELNEKLNELREELDE-LRKELAELNKAGGsiDKLRKEIERL 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  272 ERKLQETQMSTT------SKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTaKADEIEMIMTDL-ERANQ-RAEVAQ 343
Cdd:COG1340    122 EWRQQTEVLSPEeekelvEKIKELEKELEKAKKALEKNE-KLKELRAELKELRK-EAEEIHKKIKELaEEAQElHEEMIE 199
                          170
                   ....*....|....*..
gi 1720412105  344 --REAETLREQLSSANH 358
Cdd:COG1340    200 lyKEADELRKEADELHK 216
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
202-307 2.41e-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: 44.13  E-value: 2.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  202 QRLHDIETENQKLRETLEE--------------YNKEFAEVKNQEVTIKALKEKIR--EYEQTLKSQaetiALEKEQKLQ 265
Cdd:pfam13851   47 KLMSEIQQENKRLTEPLQKaqeeveelrkqlenYEKDKQSLKNLKARLKVLEKELKdlKWEHEVLEQ----RFEKVERER 122
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720412105  266 NDFAEK-ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTEL 307
Cdd:pfam13851  123 DELYDKfEAAIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQL 165
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
296-537 2.46e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 2.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  296 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLA-SQIQKAPDVLQ 374
Cdd:COG4372      4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQArSELEQLEEELE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  375 VdgspsssprasavssllcpSQEQAIEVLT-RSSLEVELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQ 450
Cdd:COG4372     84 E-------------------LNEQLQAAQAeLAQAQEELESLQEEAEELQEELEELQKERQDLeqqRKQLEAQIAELQSE 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  451 LNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKsmefapsegagTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGS 529
Cdd:COG4372    145 IAEREEELKELEEQLESlQEELAALEQELQALS-----------EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213

                   ....*...
gi 1720412105  530 ARRKGRDQ 537
Cdd:COG4372    214 RELAEELL 221
PRK11281 PRK11281
mechanosensitive channel MscK;
388-539 2.62e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.06  E-value: 2.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  388 VSSLLCPSQEQAIEVLTRSSLEVEL-AAKEREIAQlVED---VQRLQASLTKLrensaSQISQLEQQLNAKNSTLKQLEE 463
Cdd:PRK11281    21 CLSSAFARAASNGDLPTEADVQAQLdALNKQKLLE-AEDklvQQDLEQTLALL-----DKIDRQKEETEQLKQQLAQAPA 94
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412105  464 KLKgqadyeEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSarrkgRDQPE 539
Cdd:PRK11281    95 KLR------QAQAELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSL-----QTQPE 159
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
153-355 2.65e-04

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


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 44.25  E-value: 2.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  153 LKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDpvpALDVGQQ-LEIKVQRLHDIET---ENQKLRETLEeyNKEFAEv 228
Cdd:pfam00261   17 LKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEE---ELERTEErLAEALEKLEEAEKaadESERGRKVLE--NRALKD- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  229 knqevtikalKEKIREYEQTLKsQAETIALEKEQKLqndfAEKERKLQETQMS---TTSKLEEAEHKLQTLQTALEKTRT 305
Cdd:pfam00261   91 ----------EEKMEILEAQLK-EAKEIAEEADRKY----EEVARKLVVVEGDlerAEERAELAESKIVELEEELKVVGN 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720412105  306 ELFDLKT---KYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 355
Cdd:pfam00261  156 NLKSLEAseeKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDR 208
iSH2_PIK3R2 cd12926
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
193-333 2.96e-04

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.


Pssm-ID: 214019 [Multi-domain]  Cd Length: 161  Bit Score: 43.15  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  193 VGQQLEIKVQRLHDIETENQKLretLEEYNKEFAEVKNQEVTIKALKEKIREYEQtlksQAETialekEQKLQNDFAEKE 272
Cdd:cd12926      6 VGAQLKVYHQQYQDKSREYDQL---YEEYTRTSQELQMKRTAIEAFNETIKIFEE----QGQT-----QEKCSKEYLERF 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412105  273 RKlqetqmsttsklEEAEHKLQTLQTALEKTR---TELFDLKTKYDEETTAKAD---EIEMIMTDLE 333
Cdd:cd12926     74 RR------------EGNEKEMQRILLNSERLKsriAEIHESRTKLEQDLRAQASdnrEIDKRMNSLK 128
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
207-463 3.51e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  207 IETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYeqtlKSQAETIALEKEQKLqndFAEKERKLQETQMSTTSKL 286
Cdd:COG3206    166 LELRREEARKALEFLEEQLPELRKE---LEEAEAALEEF----RQKNGLVDLSEEAKL---LLQQLSELESQLAEARAEL 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  287 EEAEHKLQTLQTALEKTRTELFDLKTkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHslQLASQI 366
Cdd:COG3206    236 AEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA--QLQQEA 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  367 QKAPDVLQVDgspsSSPRASAVSSLlcpsqEQAIEVLTRSSLEveLAAKEREIAQLVEDVQRLQASLTKLREnsasQISQ 446
Cdd:COG3206    312 QRILASLEAE----LEALQAREASL-----QAQLAQLEARLAE--LPELEAELRRLEREVEVARELYESLLQ----RLEE 376
                          250
                   ....*....|....*..
gi 1720412105  447 LEQQLNAKNSTLKQLEE 463
Cdd:COG3206    377 ARLAEALTVGNVRVIDP 393
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
113-356 4.08e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 44.89  E-value: 4.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  113 ATVLANRQDESEQSRKRLIeQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTvykrlidvpdpvpALD 192
Cdd:pfam07888   29 AELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ-------------SRE 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  193 VGQQLEIKVQRLHDIETENQKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYEQTLKSQAETIalEKEQKLQNDFAEK 271
Cdd:pfam07888   95 KHEELEEKYKELSASSEELSEEKDALLAQRAAhEARIRELEEDIKTLTQRVLERETELERMKERA--KKAGAQRKEEEAE 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  272 ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLK----TKYDEETTA--KADEIEMIMTDLERANQRAEVAQRE 345
Cdd:pfam07888  173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtitTLTQKLTTAhrKEAENEALLEELRSLQERLNASERK 252
                          250
                   ....*....|.
gi 1720412105  346 AETLREQLSSA 356
Cdd:pfam07888  253 VEGLGEELSSM 263
PHA03247 PHA03247
large tegument protein UL36; Provisional
828-1028 5.64e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 5.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  828 PAPLSQPDLTILTPKhlSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEAQDVPTLDPPGSADAAQGVLRP 907
Cdd:PHA03247  2754 PARPARPPTTAGPPA--PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  908 MKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERSQLQGPSASAEywkewPSAESPYSQS 987
Cdd:PHA03247  2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTE-----SFALPPDQPE 2906
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1720412105  988 SELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSvPPLTPE 1028
Cdd:PHA03247  2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ-PPLAPT 2946
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
141-530 5.70e-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: 5.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  141 TPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFltvykrlidvpdpvpaldvgQQLEIKVQRLHDietENQKLRETLEE 220
Cdd:pfam12128  615 SAREKQAAAEEQLVQANGELEKASREETFARTAL--------------------KNARLDLRRLFD---EKQSEKDKKNK 671
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  221 YNKEFAEVKNQEVT-----IKALKEKIREYEQTLKSQAETIALEKEQKLQNdfAEKERKLQETQMSTTSKLEEAEHKLQt 295
Cdd:pfam12128  672 ALAERKDSANERLNsleaqLKQLDKKHQAWLEEQKEQKREARTEKQAYWQV--VEGALDAQLALLKAAIAARRSGAKAE- 748
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  296 lQTALEKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQlasqiqkapdvl 373
Cdd:pfam12128  749 -LKALETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLA------------ 813
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  374 qvdgspsssprasavssllcpsqeqaievltrssleVELAAKEREIAQLVEDVQRLQASlTKLRensasqISQLEQQLNA 453
Cdd:pfam12128  814 ------------------------------------TQLSNIERAISELQQQLARLIAD-TKLR------RAKLEMERKA 850
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  454 KNSTLKQLEEKLKGQADYEEvkkELNTLKsmEFAPSEGAGTQDSTKP--LEVLLLEKNR---SLQSENATLRISNSDLSG 528
Cdd:pfam12128  851 SEKQQVRLSENLRGLRCEMS---KLATLK--EDANSEQAQGSIGERLaqLEDLKLKRDYlseSVKKYVEHFKNVIADHSG 925

                   ..
gi 1720412105  529 SA 530
Cdd:pfam12128  926 SG 927
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
195-479 6.42e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.63  E-value: 6.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  195 QQLEIKVQRL-HDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREY---------------------------- 245
Cdd:TIGR04523   36 KQLEKKLKTIkNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLndklkknkdkinklnsdlskinseiknd 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  246 -EQTLKSQAETIALEKE----QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDeETTA 320
Cdd:TIGR04523  116 kEQKNKLEVELNKLEKQkkenKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID-KIKN 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  321 KADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQ-IQKAPDVLQvdgspSSSPRASAVSSllcpSQEQA 399
Cdd:TIGR04523  195 KLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQeINEKTTEIS-----NTQTQLNQLKD----EQNKI 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  400 IEVLTRSSLEVELAakEREIAQLVEDVQRLQASLTKLR----------------------ENSASQISQLEQQLNAKNST 457
Cdd:TIGR04523  266 KKQLSEKQKELEQN--NKKIKELEKQLNQLKSEISDLNnqkeqdwnkelkselknqekklEEIQNQISQNNKIISQLNEQ 343
                          330       340
                   ....*....|....*....|...
gi 1720412105  458 LKQLEEKLKG-QADYEEVKKELN 479
Cdd:TIGR04523  344 ISQLKKELTNsESENSEKQRELE 366
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
148-313 7.17e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.99  E-value: 7.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  148 QVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpaldvgqQLEIKvqrlhDIETENQKLRETLEEYNKEFAE 227
Cdd:COG1579     21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-----------EKEIK-----RLELEIEEVEARIKKYEEQLGN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  228 VKNQEVtIKALKEKIrEYEQTLKSQAETIALEKEQK---LQNDFAEKERKLQETQmsttsklEEAEHKLQTLQTALEKTR 304
Cdd:COG1579     85 VRNNKE-YEALQKEI-ESLKRRISDLEDEILELMERieeLEEELAELEAELAELE-------AELEEKKAELDEELAELE 155

                   ....*....
gi 1720412105  305 TELFDLKTK 313
Cdd:COG1579    156 AELEELEAE 164
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
226-496 8.42e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 8.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  226 AEVKNQEVTIKALKEKIREYEQTLKSQAETiALEKEQKLQNDFAEKERKLQETQM---STTSKLEEAEHKLQTLQTALEK 302
Cdd:COG4372      6 EKVGKARLSLFGLRPKTGILIAALSEQLRK-ALFELDKLQEELEQLREELEQAREeleQLEEELEQARSELEQLEEELEE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  303 TRTELfdlkTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLASQIQKAPDVLQvdgspsss 382
Cdd:COG4372     85 LNEQL----QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK------QLEAQIAELQSEIA-------- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  383 prasavssllcpSQEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLqaSLTKLRENSASQISQLEQQLNAKNSTLKQLE 462
Cdd:COG4372    147 ------------EREEELK-----ELEEQLESLQEELAALEQELQAL--SEAEAEQALDELLKEANRNAEKEEELAEAEK 207
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1720412105  463 EKLKGQADYEEVKKELNTLKSMEFAPSEGAGTQD 496
Cdd:COG4372    208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
212-355 9.24e-04

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.95  E-value: 9.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  212 QKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYE---QTLKSQAETIALEKEQKLQNDFAEKERK-LQETQMSTTSKL 286
Cdd:cd16269    149 EDREKLVEKYRQVpRKGVKAEEVLQEFLQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQERKlLEEQQRELEQKL 228
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720412105  287 EEAEHKLQTLQTALEKtrtelfdlktKYDEETTAKADEIEMIMTDLERANQR--AEVAQREAETLREQLSS 355
Cdd:cd16269    229 EDQERSYEEHLRQLKE----------KMEEERENLLKEQERALESKLKEQEAllEEGFKEQAELLQEEIRS 289
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
408-482 9.58e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 9.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  408 LEVELAAKEREIAQLVEDVQRLQASLTKLRENS-------------------ASQISQLEQQ---LNAKNSTLKQLEEKL 465
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvasaEREIAELEAElerLDASSDDLAALEEQL 694
                           90
                   ....*....|....*...
gi 1720412105  466 KG-QADYEEVKKELNTLK 482
Cdd:COG4913    695 EElEAELEELEEELDELK 712
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
212-302 9.63e-04

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains


Pssm-ID: 128778  Cd Length: 127  Bit Score: 40.71  E-value: 9.63e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105   212 QKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETI--ALEK-EQKLQND----FAEKERKLQETQM 280
Cdd:smart00502    3 EALEELLTKLRKKAAELEDALKQLISiiqeVEENAADVEAQIKAAFDELrnALNKrKKQLLEDleeqKENKLKVLEQQLE 82
                            90       100
                    ....*....|....*....|..
gi 1720412105   281 STTSKLEEAEHKLQTLQTALEK 302
Cdd:smart00502   83 SLTQKQEKLSHAINFTEEALNS 104
Homeobox_KN pfam05920
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ...
1359-1393 1.12e-03

Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to human and plants. They were first identified as TALE homeobox genes in eukaryotes, (including KNOX and MEIS genes). They have been recently classified.


Pssm-ID: 428673  Cd Length: 39  Bit Score: 37.88  E-value: 1.12e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720412105 1359 QQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSR 1393
Cdd:pfam05920    5 LHNPYPSEEEKAELAKETGLSRKQISNWFINARRR 39
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
103-258 1.49e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKEAEAA--FLTV 177
Cdd:PRK03918   622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELsreLAGLRAELEELEKRREEIKKTleKLKE 701
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  178 YKRLID-----VPDPVPALDVGQQLEIKVQRLHDIETEN--QKLRETLEEYNKEFAEVKNQEVTIKALKEKIR------- 243
Cdd:PRK03918   702 ELEEREkakkeLEKLEKALERVEELREKVKKYKALLKERalSKVGEIASEIFEELTEGKYSGVRVKAEENKVKlfvvyqg 781
                          170
                   ....*....|....*.
gi 1720412105  244 -EYEQTLKSQAETIAL 258
Cdd:PRK03918   782 kERPLTFLSGGERIAL 797
PRK11281 PRK11281
mechanosensitive channel MscK;
103-354 1.56e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 43.36  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDeSEQSRkRLIEQSREFKKNTpEDLRKQV--AP-LLKSFQGEIDALSKRSKEaeaafltvyk 179
Cdd:PRK11281    46 DALNKQKLLEAEDKLVQQD-LEQTL-ALLDKIDRQKEET-EQLKQQLaqAPaKLRQAQAELEALKDDNDE---------- 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  180 rliDVPDPVPALDVgQQLEikvQRLHDIETENQKLRETLEEYNKEFA---------------------EVKNQEVTIKAL 238
Cdd:PRK11281   113 ---ETRETLSTLSL-RQLE---SRLAQTLDQLQNAQNDLAEYNSQLVslqtqperaqaalyansqrlqQIRNLLKGGKVG 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  239 KEKIREYEQTLKsQAETIALEkeqkLQNDFAEKE----RKLQETQMS----TTSKLEEAEHKLQTLQTALEKTRTELFdl 310
Cdd:PRK11281   186 GKALRPSQRVLL-QAEQALLN----AQNDLQRKSlegnTQLQDLLQKqrdyLTARIQRLEHQLQLLQEAINSKRLTLS-- 258
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1720412105  311 ktkydEETTAKADEIEmimtDLERANQRAEVAQrEAETLReQLS 354
Cdd:PRK11281   259 -----EKTVQEAQSQD----EAARIQANPLVAQ-ELEINL-QLS 291
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
196-470 1.72e-03

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 42.97  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  196 QLEIKVQRLH-DIETENQKLRETLEEYNKEFA-EVKNQEVTIKALKEKIREyeqtLKSQAETIALEKeQKLQNDFAEKER 273
Cdd:pfam15964  364 ELERQKERLEkELASQQEKRAQEKEALRKEMKkEREELGATMLALSQNVAQ----LEAQVEKVTREK-NSLVSQLEEAQK 438
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  274 KLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQR-------EA 346
Cdd:pfam15964  439 QLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQdaarareEC 518
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  347 ETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQ--AIEVLTRSSLEVELAAKEREIAQLVE 424
Cdd:pfam15964  519 LKLTELLGESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQmeAQHDKTVNEQYSLLTSQNTFIAKLKE 598
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1720412105  425 DVQRLQASLTKLRENSASQISQLEQQlnakNSTLKQLEEKLKGQAD 470
Cdd:pfam15964  599 ECCTLAKKLEEITQKSRSEVEQLSQE----KEYLQDRLEKLQKRNE 640
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
127-464 1.78e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.40  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  127 RKRLIEQSREFKKntpeDLRKQVAPL------LKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVpaldvgQQLEiK 200
Cdd:COG3096    280 RRELSERALELRR----ELFGARRQLaeeqyrLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL------RQQE-K 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  201 VQRLH-DIETENQKLRE---TLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQaETIALEKEQKLQNdFAEKE 272
Cdd:COG3096    349 IERYQeDLEELTERLEEqeeVVEEAAEQLAEAEARleaaEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQAVQA-LEKAR 426
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  273 RKLQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA--DE----IEMIMTDLERAnQRAEVAQREA 346
Cdd:COG3096    427 ALCGLPDLT----PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKayelVCKIAGEVERS-QAWQTARELL 501
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  347 ETLREQLSSANHSLQLASQIQKAPDVLQvdgspsssprasavssllcpSQEQAIEVLT----RSSLEVELAAK-EREIAQ 421
Cdd:COG3096    502 RRYRSQQALAQRLQQLRAQLAELEQRLR--------------------QQQNAERLLEefcqRIGQQLDAAEElEELLAE 561
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1720412105  422 LVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQLEEK 464
Cdd:COG3096    562 LEAQLEELEEQAAEAVE----QRSELRQQLEQLRARIKELAAR 600
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
117-362 2.02e-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: 42.82  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  117 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpaldVGQQ 196
Cdd:pfam09731  231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQ--------LSKK 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  197 L-EIKVQRLHDIETENQKLRETL----EEYNKEFAEVKNQE-----VTIKALKEKIRE-YEQTLKSQAETIALEKEQKLQ 265
Cdd:pfam09731  303 LaELKKREEKHIERALEKQKEELdklaEELSARLEEVRAADeaqlrLEFEREREEIREsYEEKLRTELERQAEAHEEHLK 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  266 NDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTAlektrtelfdlktkydeETTAKADEIEMIMT---DLERANQRAEVA 342
Cdd:pfam09731  383 DVLVEQEIELQREFLQDIKEKVEEERAGRLLKLN-----------------ELLANLKGLEKATSshsEVEDENRKAQQL 445
                          250       260
                   ....*....|....*....|
gi 1720412105  343 QREAETLREQLSSANHSLQL 362
Cdd:pfam09731  446 WLAVEALRSTLEDGSADSRP 465
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
122-325 2.89e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  122 ESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQ----GEIDALSKRSKEAEAAfltvYKRLIDvpdpvpALDVGQQL 197
Cdd:PRK03918   545 KKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfESVEELEERLKELEPF----YNEYLE------LKDAEKEL 614
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  198 EIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ-----------------------EVTIKALKEKIREYEQTLKSQAE 254
Cdd:PRK03918   615 EREEKELKKLEEELDKAFEELAETEKRLEELRKEleelekkyseeeyeelreeylelSRELAGLRAELEELEKRREEIKK 694
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720412105  255 TIalekeQKLQNDFAEKERKLQETQmsttsKLEEAEHKLQTLQtalEKTRtelfDLKTKYDEETTAKADEI 325
Cdd:PRK03918   695 TL-----EKLKEELEEREKAKKELE-----KLEKALERVEELR---EKVK----KYKALLKERALSKVGEI 748
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
121-477 3.00e-03

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: 42.26  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  121 DESEQSRKRLIEQSREFK-KNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTvykrlidvpdpvPALDVGQQLEI 199
Cdd:TIGR00618  176 DQYTQLALMEFAKKKSLHgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLR------------EALQQTQQSHA 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  200 KVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKSQAETIALEKEQKLQNDFaEKERKLQETQ 279
Cdd:TIGR00618  244 YLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERI-----NRARKAAPLAAHIKAVTQIEQ-QAQRIHTELQ 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  280 mSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEEttakadeiemimtdlERANQRAEVAQREAETLREQLSSANHS 359
Cdd:TIGR00618  318 -SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE---------------IHIRDAHEVATSIREISCQQHTLTQHI 381
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  360 LQLASQIQKAPDVLQVdgspssspRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREI-AQLVEDVQRLQASLTKLRE 438
Cdd:TIGR00618  382 HTLQQQKTTLTQKLQS--------LCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQeLQQRYAELCAAAITCTAQC 453
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1720412105  439 NSASQISQLE--QQLNAKNSTLKQLEEKLKgqaDYEEVKKE 477
Cdd:TIGR00618  454 EKLEKIHLQEsaQSLKEREQQLQTKEQIHL---QETRKKAV 491
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
406-524 3.31e-03

WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.


Pssm-ID: 465345 [Multi-domain]  Cd Length: 155  Bit Score: 39.97  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  406 SSLEVELAAKEREIAQLVEDVQRLQASLTKlrENSASQISQLEQQLNAKNSTLKQLEEKLKgqADYEEVKKELNTLKsme 485
Cdd:pfam17098    7 NLLLARLAEKEQEIQELKAQLQDLKQSLQP--PSSQLRSLLLDPAVNLEFLRLKKELEEKK--KKLKEAQLELAAWK--- 79
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1720412105  486 FAPSEGAGTQdstkplevlLLEKNRSLQSENATLRISNS 524
Cdd:pfam17098   80 FTPDSTTGKR---------LMAKCRLLQQENEELGRQLS 109
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
207-338 3.91e-03

Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.


Pssm-ID: 464008 [Multi-domain]  Cd Length: 177  Bit Score: 39.90  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  207 IETENQKLRETLEEYNKEFAEVKNQEV----TIKALKEKIREYEQTLKSQAETIAlekeqKLQNDFAEKERKLQETQMsT 282
Cdd:pfam13870   47 LQIENQALNEKIEERNKELKRLKLKVTntvhALTHLKEKLHFLSAELSRLKKELR-----ERQELLAKLRKELYRVKL-E 120
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412105  283 TSKLEEAEHKLqtlqtaleKTRTELF---DLKTKYD---EETTAKADEIEMIMTDLERANQR 338
Cdd:pfam13870  121 RDKLRKQNKKL--------RQQGGLLhvpALLHDYDktkAEVEEKRKSVKKLRRKVKILEMR 174
46 PHA02562
endonuclease subunit; Provisional
199-377 4.11e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  199 IKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERK 274
Cdd:PHA02562   197 IKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNTAAAKIKSK 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  275 LQ----ETQMST--------TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEEttakadeiEMIMTDLERANQRAEVA 342
Cdd:PHA02562   271 IEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL--------EEIMDEFNEQSKKLLEL 342
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1720412105  343 QREAETLREQLSSANHSlqlASQIQKAPDVLQVDG 377
Cdd:PHA02562   343 KNKISTNKQSLITLVDK---AKKVKAAIEELQAEF 374
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
103-277 4.14e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 4.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQvaplLKSFQGEIDALSKRSKEAEaafltvyKRLI 182
Cdd:COG1579     20 DRLEHRLKELPAELAELEDELAALEARLEAAKTEL-----EDLEKE----IKRLELEIEEVEARIKKYE-------EQLG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIAlEKEQ 262
Cdd:COG1579     84 NVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEELAELE-AELE 159
                          170
                   ....*....|....*
gi 1720412105  263 KLQNDFAEKERKLQE 277
Cdd:COG1579    160 ELEAEREELAAKIPP 174
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
103-482 4.20e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 4.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRLI 182
Cdd:COG1196    421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE--EALLELLAELLEEAALLEAALAELLEELAEA-AARLLLLL 497
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYnkefaEVKNQEVTIKALKEKIREYEQTLksqAETIALEKEQ 262
Cdd:COG1196    498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY-----EAALEAALAAALQNIVVEDDEVA---AAAIEYLKAA 569
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  263 KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVA 342
Cdd:COG1196    570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  343 QREAETLREQLSSANHSLQLASQIQKAPDVLQVDGspsssprasavssllcpSQEQAIEVLTRSSLEVELAAKEREIAQL 422
Cdd:COG1196    650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL-----------------AERLAEEELELEEALLAEEEEERELAEA 712
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720412105  423 VEDVQRLQASLTKLRENSASQISQ-LEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLK 482
Cdd:COG1196    713 EEERLEEELEEEALEEQLEAEREElLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
219-306 4.44e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 39.10  E-value: 4.44e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105   219 EEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHK-----L 293
Cdd:smart00935   21 KQLEKEFKKRQAE---LEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEelqkiL 97
                            90
                    ....*....|...
gi 1720412105   294 QTLQTALEKTRTE 306
Cdd:smart00935   98 DKINKAIKEVAKK 110
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
192-483 5.38e-03

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: 41.48  E-value: 5.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  192 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEfaevKNQEVTIKALKEKIREYEQTLKSQAETIALEKE--QKLQNDFA 269
Cdd:COG5185     97 KILQEYVNSLIKLPNYEWSADILISLLYLYKSE----IVALKDELIKVEKLDEIADIEASYGEVETGIIKdiFGKLTQEL 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  270 EKERKLQETQMSTTSKL--EEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAdEIEMIMTDLERANQRAEVAQREAE 347
Cdd:COG5185    173 NQNLKKLEIFGLTLGLLkgISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKE-IINIEEALKGFQDPESELEDLAQT 251
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  348 TLR-EQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRA----------SAVSSLLCPSQEQAIEVLTRSSLEVELAAKE 416
Cdd:COG5185    252 SDKlEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQfentkekiaeYTKSIDIKKATESLEEQLAAAEAEQELEESK 331
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412105  417 REIAqlvEDVQRLQASLTKLREnsasqisQLEQQLNAKNSTLKQLEeklkGQADYEEVKKELNTLKS 483
Cdd:COG5185    332 RETE---TGIQNLTAEIEQGQE-------SLTENLEAIKEEIENIV----GEVELSKSSEELDSFKD 384
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
202-363 5.84e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.48  E-value: 5.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  202 QRLHDIETENQKLRETLE-------EYNKEFA------EVKNQevTIKALKEKIREYEQTLKSQAETIALEKEQKLQN-- 266
Cdd:COG3096    991 ARLEQAEEARREAREQLRqaqaqysQYNQVLAslkssrDAKQQ--TLQELEQELEELGVQADAEAEERARIRRDELHEel 1068
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  267 -------DFAEKERKLQETQM-STTSKLEEAEHKLQTLQTALEktrtelfdlktkydeetTAKA---DEIEMIM-TDLER 334
Cdd:COG3096   1069 sqnrsrrSQLEKQLTRCEAEMdSLQKRLRKAERDYKQEREQVV-----------------QAKAgwcAVLRLARdNDVER 1131
                          170       180
                   ....*....|....*....|....*....
gi 1720412105  335 ANQRAEVAQREAETLREQLSSANHSLQLA 363
Cdd:COG3096   1132 RLHRRELAYLSADELRSMSDKALGALRLA 1160
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
197-553 5.86e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 41.35  E-value: 5.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  197 LEIKVQRLHDIETENQKLRETLEEynKEfaevknqevtikALKEKIREYEQTLKSQAETIALEKEQkLQNDFAEKERK-- 274
Cdd:pfam10174  333 LTAKEQRAAILQTEVDALRLRLEE--KE------------SFLNKKTKQLQDLTEEKSTLAGEIRD-LKDMLDVKERKin 397
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  275 --------LQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLktkydEETTAkadEIEMIMTDLERANQRAEVAQR-E 345
Cdd:pfam10174  398 vlqkkienLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTL-----EEALS---EKERIIERLKEQREREDRERLeE 469
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  346 AETLREQLSSANHSLQlASQIQKAPDvlqvdgspsssprasavSSLLCPSQEQAiEVLTRSSLEVELAAKEREIA--QLV 423
Cdd:pfam10174  470 LESLKKENKDLKEKVS-ALQPELTEK-----------------ESSLIDLKEHA-SSLASSGLKKDSKLKSLEIAveQKK 530
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  424 EDVQRLQASLTKLRENS---------ASQISQLEQQLNAKNstlkqlEEKLKGQAdyeEVKKELNTLKSMEfapsegagT 494
Cdd:pfam10174  531 EECSKLENQLKKAHNAEeavrtnpeiNDRIRLLEQEVARYK------EESGKAQA---EVERLLGILREVE--------N 593
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  495 QDSTKPLEVLLLEKNRSLQSENATLRISN-SDLSGSARRKGRDQPESRRPGPLPASPPPQ 553
Cdd:pfam10174  594 EKNDKDKKIAELESLTLRQMKEQNKKVANiKHGQQEMKKKGAQLLEEARRREDNLADNSQ 653
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
207-485 6.25e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.26  E-value: 6.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  207 IETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK-SQAETIALEKEQKLqndfaekerKLQETQMSTTsk 285
Cdd:pfam15921  470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEaTNAEITKLRSRVDL---------KLQELQHLKN-- 538
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  286 leEAEHkLQTLQTALEKTRTELfdlkTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQ 365
Cdd:pfam15921  539 --EGDH-LRNVQTECEALKLQM----AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKI 611
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  366 IQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEV----LTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSA 441
Cdd:pfam15921  612 LKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVkdikQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEME 691
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1720412105  442 SQISQLEQQLNAKNSTLKQLEeklkgqadyeevkkelNTLKSME 485
Cdd:pfam15921  692 TTTNKLKMQLKSAQSELEQTR----------------NTLKSME 719
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
196-522 6.40e-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: 41.19  E-value: 6.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  196 QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKireyeqtlKSQAETIALEKEQKLQNDFAEKERKL 275
Cdd:TIGR00606  232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR--------KKQMEKDNSELELKMEKVFQGTDEQL 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  276 QETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADeiEMIMTDLERANQRAEVAQREAETLREQLSS 355
Cdd:TIGR00606  304 NDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGR--LQLQADRHQEHIRARDSLIQSLATRLELDG 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  356 ANHSLQLASQIQKAPDVL---QVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSS-----LEVELAAKEREIAQLVEDVQ 427
Cdd:TIGR00606  382 FERGPFSERQIKNFHTLVierQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKglgrtIELKKEILEKKQEELKFVIK 461
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  428 RLQASltklrENSASQISQLEQQLNAKNSTLKQLEEklkgQADYEEVKKELNTLKsmefapSEGAGTQDSTKPLEVLLLE 507
Cdd:TIGR00606  462 ELQQL-----EGSSDRILELDQELRKAERELSKAEK----NSLTETLKKEVKSLQ------NEKADLDRKLRKLDQEMEQ 526
                          330
                   ....*....|....*
gi 1720412105  508 KNRSLQSENATLRIS 522
Cdd:TIGR00606  527 LNHHTTTRTQMEMLT 541
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
106-450 6.81e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.26  E-value: 6.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  106 KRELDATATVLANRQDESEQSRKRLIEQSREFKK---------NTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAF-- 174
Cdd:pfam05557   50 NQELQKRIRLLEKREAEAEEALREQAELNRLKKKylealnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELqs 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  175 ----LTVYKRLIDVPDP--VPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKN--QEV----TIKALKEKI 242
Cdd:pfam05557  130 tnseLEELQERLDLLKAkaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNskSELaripELEKELERL 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  243 REYEQTLKSQAETIALEKEQK-------------------LQNDFAEKERKLQE---TQMSTTSKL---EEAEHKLQTLQ 297
Cdd:pfam05557  210 REHNKHLNENIENKLLLKEEVedlkrklereekyreeaatLELEKEKLEQELQSwvkLAQDTGLNLrspEDLSRRIEQLQ 289
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  298 T-----------------ALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS----- 355
Cdd:pfam05557  290 QreivlkeenssltssarQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESydkel 369
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  356 --ANHSLQLASQIQKAPDVLQ--------VDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVED 425
Cdd:pfam05557  370 tmSNYSPQLLERIEEAEDMTQkmqahneeMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRK 449
                          410       420
                   ....*....|....*....|....*
gi 1720412105  426 VQRLQASLTKLRENSASQISQLEQQ 450
Cdd:pfam05557  450 LETLELERQRLREQKNELEMELERR 474
mukB PRK04863
chromosome partition protein MukB;
105-467 7.44e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 7.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  105 LKRELDATATVLANRQDESEQSRKRL------------IEQSREFKKNTPEDLRKQVApLLKSFQGEIDALSKRSKEAEA 172
Cdd:PRK04863   312 MARELAELNEAESDLEQDYQAASDHLnlvqtalrqqekIERYQADLEELEERLEEQNE-VVEEADEQQEENEARAEAAEE 390
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  173 AFLTVYKRLIDVpdpVPALDVGQ----QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQT 248
Cdd:PRK04863   391 EVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE---QEATEELLSLEQK 464
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  249 LkSQAETIALEKEQKLQ---------------NDFAEKERKLQETQMSTTSkLEEAEHKLQTLQTALEKTRTeLFDLKTK 313
Cdd:PRK04863   465 L-SVAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRRLREQRHLAEQ-LQQLRMRLSELEQRLRQQQR-AERLLAE 541
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  314 YDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQK----APDVLQVDgspssspraSAV 388
Cdd:PRK04863   542 FCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLeQLQARIQRlaarAPAWLAAQ---------DAL 612
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  389 SSLlcpsQEQAIEVLTRSslevelaakeREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLN-------AKNSTLKQL 461
Cdd:PRK04863   613 ARL----REQSGEEFEDS----------QDVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggSEDPRLNAL 678

                   ....*.
gi 1720412105  462 EEKLKG 467
Cdd:PRK04863   679 AERFGG 684
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
405-482 7.91e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 7.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  405 RSSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQLEEKL---KGQADYEEVKKELNTL 481
Cdd:COG1579     26 LKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEIESL 101

                   .
gi 1720412105  482 K 482
Cdd:COG1579    102 K 102
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
196-313 8.14e-03

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 40.39  E-value: 8.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  196 QLEIKVQRLHDIETENQKLRE----------TLEEYN--------KEFAEVKNQevtIKALKEKI-REYEQTLKSQAETI 256
Cdd:pfam04849  165 QLDALQEKLRGLEEENLKLRSeashlktetdTYEEKEqqlmsdcvEQLSEANQQ---MAELSEELaRKMEENLRQQEEIT 241
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412105  257 AL-----EKEQKLQNDFAEKERKLQ------ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTK 313
Cdd:pfam04849  242 SLlaqivDLQHKCKELGIENEELQQhlqaskEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
RNase_Y_N pfam12072
RNase Y N-terminal region;
210-358 8.34e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.48  E-value: 8.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  210 ENQKLRETLEEYNKEfaevKNQEvtIKALKEKIREYEQTLKSQAETIAlEKEQKLQndfaEKERKLQETQMSTTSKLEEA 289
Cdd:pfam12072   61 EIHKLRAEAERELKE----RRNE--LQRQERRLLQKEETLDRKDESLE-KKEESLE----KKEKELEAQQQQLEEKEEEL 129
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412105  290 EHKLQTLQTALEK----TRTE----LFD-LKTKYDEETTAKADEIEmimtdlERANQRAEVAQREAETLREQLSSANH 358
Cdd:pfam12072  130 EELIEEQRQELERisglTSEEakeiLLDeVEEELRHEAAVMIKEIE------EEAKEEADKKAKEIIALAIQRCAADH 201
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
281-476 8.40e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 8.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  281 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEeTTAKADEIEMImTDLERANQRAEVAQREAETLREQLSsanhsl 360
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRL-AEYSWDEIDVASAEREIAELEAELE------ 678
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  361 qlasQIQKAPDVLQVdgspsssprasavssllcpsQEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLREns 440
Cdd:COG4913    679 ----RLDASSDDLAA--------------------LEEQLE-----ELEAELEELEEELDELKGEIGRLEKELEQAEE-- 727
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1720412105  441 asQISQLEQQLNAKNSTLKQ-----LEEKLKGQADYEEVKK 476
Cdd:COG4913    728 --ELDELQDRLEAAEDLARLelralLEERFAAALGDAVERE 766
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
203-542 8.94e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 40.80  E-value: 8.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  203 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALkEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQmST 282
Cdd:PTZ00108  1047 RFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL-GAAVSYDYLLSMPIWSLTKEKVEKLNAELEKKEKELEKLK-NT 1124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  283 TSK---LEEaehkLQTLQTALEKTRtelfdlktKYDEETTAKadEIEMIMTDLERANQRAEVAQREAETLREQLSSANHS 359
Cdd:PTZ00108  1125 TPKdmwLED----LDKFEEALEEQE--------EVEEKEIAK--EQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSK 1190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  360 LQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREN 439
Cdd:PTZ00108  1191 KASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGK 1270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  440 SASQISqleqqlnaKNSTLKQLEEKLKGQADYEEvkkelntlksmEFAPSEGAGTQDST-KPLEVLLLEKNRSLQSENAT 518
Cdd:PTZ00108  1271 PKNAPK--------RVSAVQYSPPPPSKRPDGES-----------NGGSKPSSPTKKKVkKRLEGSLAALKKKKKSEKKT 1331
                          330       340
                   ....*....|....*....|....*..
gi 1720412105  519 LRISNSD---LSGSARRKGRDQPESRR 542
Cdd:PTZ00108  1332 ARKKKSKtrvKQASASQSSRLLRRPRK 1358
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
212-326 9.66e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 38.45  E-value: 9.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412105  212 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ------KLQNDFAEKERKL---QETQMST 282
Cdd:pfam11559   20 GLLFDTAEGVEENIARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERlqskieRLKTQLEDLERELallQAKERQL 99
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1720412105  283 TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIE 326
Cdd:pfam11559  100 EKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAHEVKKRDREIE 143
 
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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