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Conserved domains on  [gi|1622917383|ref|XP_028700584|]
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protein CASP isoform X5 [Macaca mulatta]

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 ...
1147-1224 9.41e-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: 116.15  E-value: 9.41e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383 1147 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1224
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
964-1032 6.40e-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: 108.06  E-value: 6.40e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383  964 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 1032
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
572-648 1.66e-26

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: 104.21  E-value: 1.66e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383  572 EGEEMDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 648
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1270-1326 1.02e-15

Homeodomain;


:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 72.53  E-value: 1.02e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRR 1326
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
121-425 3.71e-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: 78.17  E-value: 3.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  121 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQTLKNQAETIALEkeQKLQND 196
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEAEVEQLEERIAQL--SKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  197 FAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 266
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  267 RAEVAQREAETLREQLSSANHSLqlasqiqkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLR---E 343
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEI---------------------EELEELIEELESELEALLNERASLEEALALLRselE 897
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  344 NSASQISQLEQQLSAKNSTLKQLEEKLkGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAA 423
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976

                   ..
gi 1622917383  424 LR 425
Cdd:TIGR02168  977 LE 978
PHA03247 super family cl33720
large tegument protein UL36; Provisional
772-958 1.41e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  772 STSPMPTVSSYPPLAISLKKPSAAPEAG--ASALPNPPALKKEAQDAPGLDPQGAADCAQGVLR--QVKNEVGRSGAWkd 847
Cdd:PHA03247   269 PETARGATGPPPPPEAAAPNGAAAPPDGvwGAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGamEVVSPLPRPRQH-- 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  848 hwWSAVQPERRNAASSEEAKAEETGGgkekgsggsgggsqprAERSQLQGPSSSEYWKEWPSAESPYSQSSELSLTGASR 927
Cdd:PHA03247   347 --YPLGFPKRRRPTWTPPSSLEDLSA----------------GRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTRPA 408
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1622917383  928 SETPQNSPLPSSPIVPMSKPTKPSVPPLTPE 958
Cdd:PHA03247   409 APVPASVPTPAPTPVPASAPPPPATPLPSAE 439
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
1330-1422 4.62e-04

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.89  E-value: 4.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 1330 IEEIQAGSQGQAGASDSPSARSGRAAPSSEGDSCDGVEATEGPGSADTEEP-----KSQGEAEREEAPRPAEQTEPPPSG 1404
Cdd:PRK12678    55 IKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAApaaraAAAAAAEAASAPEAAQARERRERG 134
                           90
                   ....*....|....*...
gi 1622917383 1405 TPGPDDARDDDHEGGPAE 1422
Cdd:PRK12678   135 EAARRGAARKAGEGGEQP 152
 
Name Accession Description Interval E-value
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
1147-1224 9.41e-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: 116.15  E-value: 9.41e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383 1147 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1224
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
964-1032 6.40e-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: 108.06  E-value: 6.40e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383  964 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 1032
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
572-648 1.66e-26

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: 104.21  E-value: 1.66e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383  572 EGEEMDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 648
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1270-1326 1.02e-15

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 72.53  E-value: 1.02e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRR 1326
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
121-425 3.71e-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: 78.17  E-value: 3.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  121 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQTLKNQAETIALEkeQKLQND 196
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEAEVEQLEERIAQL--SKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  197 FAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 266
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  267 RAEVAQREAETLREQLSSANHSLqlasqiqkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLR---E 343
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEI---------------------EELEELIEELESELEALLNERASLEEALALLRselE 897
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  344 NSASQISQLEQQLSAKNSTLKQLEEKLkGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAA 423
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976

                   ..
gi 1622917383  424 LR 425
Cdd:TIGR02168  977 LE 978
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
1270-1327 6.44e-13

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: 64.57  E-value: 6.44e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRRE 1327
Cdd:cd00086      1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
96-422 1.46e-12

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: 72.30  E-value: 1.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   96 SKEAEAAFLNVYKRLIDVPDPVPALdlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEK 170
Cdd:COG5185    221 LLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEK 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  171 IREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD-EETTA 249
Cdd:COG5185    298 IAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSE 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  250 KAD-----------EIEMIMTDLERANQRAE--------VAQREAETLREQLSSANHSLQLASQIQKA-----PDVEQAI 305
Cdd:COG5185    378 ELDsfkdtiestkeSLDEIPQNQRGYAQEILatledtlkAADRQIEELQRQIEQATSSNEEVSKLLNEliselNKVMREA 457
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  306 EVLTRSSLEVELAAKEREIAQ----LVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEvkk 381
Cdd:COG5185    458 DEESQSRLEEAYDEINRSVRSkkedLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG--- 534
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1622917383  382 ELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENA 422
Cdd:COG5185    535 YAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQ 575
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
1270-1325 3.70e-12

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: 62.65  E-value: 3.70e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383  1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIR 1325
Cdd:smart00389    2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
34-389 1.08e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 66.63  E-value: 1.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   34 IKRELDATATVLANRQDESEQsRKRLIEQSREFKKNTP-------EDLRKQvapLLKSFQGEIDALSKRSKEAEAAFLNV 106
Cdd:PRK03918   403 IEEEISKITARIGELKKEIKE-LKKAIEELKKAKGKCPvcgreltEEHRKE---LLEEYTAELKRIEKELKEIEEKERKL 478
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  107 YKRLIDVpdpvpalDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEKIREYEQTLKNQAETia 186
Cdd:PRK03918   479 RKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEKLIKLKGEIKSLKKE-- 547
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  187 LEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQ-TALEKTRTELFDLKTKYDEETTAKADEIEmimtdLERAN 265
Cdd:PRK03918   548 LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKE-----LEREE 618
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  266 QRAEVAQREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAsltklrens 345
Cdd:PRK03918   619 KELKKLEEELDKAFEELAETEKRLE---------ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRA--------- 680
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1622917383  346 asQISQLEQQLSAKNSTLKQLEEKLKgqaDYEEVKKELNILKSM 389
Cdd:PRK03918   681 --ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
165-438 2.60e-08

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: 58.83  E-value: 2.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  165 KALKEKIREYEQTLKNQAETIALEK-EQKLQNDFAEKERKLQETQmsttsKLEEAEhkvqsLQTALEKTRTELFDLKTKY 243
Cdd:pfam02463  173 EALKKLIEETENLAELIIDLEELKLqELKLKEQAKKALEYYQLKE-----KLELEE-----EYLLYLDYLKLNEERIDLL 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  244 DEETTAKADEIEMImtdleraNQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKERE 323
Cdd:pfam02463  243 QELLRDEQEEIESS-------KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  324 IAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSmefapSEGAGTQDAA 403
Cdd:pfam02463  316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK-----LESERLSSAA 390
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1622917383  404 KPLEVLLMEKNRSLQSENAALRISNSDLSGSARRK 438
Cdd:pfam02463  391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEK 425
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
72-264 3.55e-07

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: 53.91  E-value: 3.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   72 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLNVYKRLIDVpdpvpaldlgQQLQLK--VQRLHDI-ETENQKL-RETL 147
Cdd:cd22656    113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTEK----------DQTALEtlEKALKDLlTDEGGAIaRKEI 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  148 EEYNKEFAevKNQEVTIKALKEKIREYEQTLKNQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKVQSLQ 226
Cdd:cd22656    182 KDLQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQ 252
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1622917383  227 TALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 264
Cdd:cd22656    253 GAWQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
1270-1355 3.77e-05

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 45.51  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRRelfieeiqagsQGQAGASDSPSA 1349
Cdd:COG5576     52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKK-----------KRSGKVEQRPGE 120

                   ....*.
gi 1622917383 1350 RSGRAA 1355
Cdd:COG5576    121 EEADLA 126
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
132-241 6.08e-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: 46.93  E-value: 6.08e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   132 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAET---IALEKEQKLQNDFA---EKERKLQ 205
Cdd:smart00787  138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 1622917383   206 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKT 241
Cdd:smart00787  218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
PHA03247 PHA03247
large tegument protein UL36; Provisional
772-958 1.41e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  772 STSPMPTVSSYPPLAISLKKPSAAPEAG--ASALPNPPALKKEAQDAPGLDPQGAADCAQGVLR--QVKNEVGRSGAWkd 847
Cdd:PHA03247   269 PETARGATGPPPPPEAAAPNGAAAPPDGvwGAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGamEVVSPLPRPRQH-- 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  848 hwWSAVQPERRNAASSEEAKAEETGGgkekgsggsgggsqprAERSQLQGPSSSEYWKEWPSAESPYSQSSELSLTGASR 927
Cdd:PHA03247   347 --YPLGFPKRRRPTWTPPSSLEDLSA----------------GRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTRPA 408
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1622917383  928 SETPQNSPLPSSPIVPMSKPTKPSVPPLTPE 958
Cdd:PHA03247   409 APVPASVPTPAPTPVPASAPPPPATPLPSAE 439
PRK12678 PRK12678
transcription termination factor Rho; Provisional
1330-1422 4.62e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.89  E-value: 4.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 1330 IEEIQAGSQGQAGASDSPSARSGRAAPSSEGDSCDGVEATEGPGSADTEEP-----KSQGEAEREEAPRPAEQTEPPPSG 1404
Cdd:PRK12678    55 IKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAApaaraAAAAAAEAASAPEAAQARERRERG 134
                           90
                   ....*....|....*...
gi 1622917383 1405 TPGPDDARDDDHEGGPAE 1422
Cdd:PRK12678   135 EAARRGAARKAGEGGEQP 152
 
Name Accession Description Interval E-value
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
1147-1224 9.41e-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: 116.15  E-value: 9.41e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383 1147 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1224
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
964-1032 6.40e-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: 108.06  E-value: 6.40e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383  964 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 1032
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
572-648 1.66e-26

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: 104.21  E-value: 1.66e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383  572 EGEEMDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 648
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1270-1326 1.02e-15

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 72.53  E-value: 1.02e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRR 1326
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
121-425 3.71e-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: 78.17  E-value: 3.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  121 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQTLKNQAETIALEkeQKLQND 196
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEAEVEQLEERIAQL--SKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  197 FAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 266
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  267 RAEVAQREAETLREQLSSANHSLqlasqiqkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLR---E 343
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEI---------------------EELEELIEELESELEALLNERASLEEALALLRselE 897
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  344 NSASQISQLEQQLSAKNSTLKQLEEKLkGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAA 423
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976

                   ..
gi 1622917383  424 LR 425
Cdd:TIGR02168  977 LE 978
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
47-377 9.48e-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: 76.63  E-value: 9.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   47 NRQDESEQSRKRLIEQSREfKKNTPEDLRKQVAPL-LKSFQGEIDALSKRSKEAEaaflnvykRLIDvpdpvpalDLGQQ 125
Cdd:TIGR02168  199 ERQLKSLERQAEKAERYKE-LKAELRELELALLVLrLEELREELEELQEELKEAE--------EELE--------ELTAE 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  126 LQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKNQAETIALEKEQK--LQNDFAE 199
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEisrlEQQKQILRERLANLERQLEELEAQLEELESKLdeLAEELAE 341
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  200 KERKLQETQMSTTS---KLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQR 273
Cdd:TIGR02168  342 LEEKLEELKEELESleaELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQ 421
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  274 EAETLREQLSSAN---HSLQLASQIQKAPDVEQAIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTKLR------ 342
Cdd:TIGR02168  422 EIEELLKKLEEAElkeLQAELEELEEELEELQEELERLEEalEELREELEEAEQALDAAERELAQLQARLDSLErlqenl 501
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1622917383  343 ENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYE 377
Cdd:TIGR02168  502 EGFSEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
1270-1327 6.44e-13

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: 64.57  E-value: 6.44e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRRE 1327
Cdd:cd00086      1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
96-422 1.46e-12

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: 72.30  E-value: 1.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   96 SKEAEAAFLNVYKRLIDVPDPVPALdlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEK 170
Cdd:COG5185    221 LLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEK 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  171 IREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD-EETTA 249
Cdd:COG5185    298 IAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSE 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  250 KAD-----------EIEMIMTDLERANQRAE--------VAQREAETLREQLSSANHSLQLASQIQKA-----PDVEQAI 305
Cdd:COG5185    378 ELDsfkdtiestkeSLDEIPQNQRGYAQEILatledtlkAADRQIEELQRQIEQATSSNEEVSKLLNEliselNKVMREA 457
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  306 EVLTRSSLEVELAAKEREIAQ----LVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEvkk 381
Cdd:COG5185    458 DEESQSRLEEAYDEINRSVRSkkedLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG--- 534
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1622917383  382 ELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENA 422
Cdd:COG5185    535 YAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQ 575
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
1270-1325 3.70e-12

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: 62.65  E-value: 3.70e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383  1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIR 1325
Cdd:smart00389    2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
125-383 6.88e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.74  E-value: 6.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  125 QLQLKVQRLHDIETENQKLRETLEEYNKEFAEvknQEVTIKALKEKIREYEQTLKNQAETIalekeQKLQNDFAEKERKL 204
Cdd:COG1196    226 EAELLLLKLRELEAELEELEAELEELEAELEE---LEAELAELEAELEELRLELEELELEL-----EEAQAEEYELLAEL 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  205 QEtqmsttskLEEAEHKVQSLQTALEKTRTELfdlktkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 284
Cdd:COG1196    298 AR--------LEQDIARLEERRRELEERLEEL-------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  285 ANHSLQLASQIQKApdveqaiEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLK 364
Cdd:COG1196    363 AEEALLEAEAELAE-------AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
                          250
                   ....*....|....*....
gi 1622917383  365 QLEEKLKGQADYEEVKKEL 383
Cdd:COG1196    436 EEEEEEEALEEAAEEEAEL 454
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
47-388 1.00e-10

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: 66.58  E-value: 1.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   47 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQgEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL-----D 121
Cdd:TIGR04523  165 KKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLS-NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKqqeinE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  122 LGQQLQLKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKNQAETIALEKEQKLQNDFAE-- 199
Cdd:TIGR04523  244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSel 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  200 --KERKLQETQmsttSKLEEAEHKVQSLQ---TALEKTRTELFDLKTKYDEETTAKADEIEmimtDLERANQRaevAQRE 274
Cdd:TIGR04523  317 knQEKKLEEIQ----NQISQNNKIISQLNeqiSQLKKELTNSESENSEKQRELEEKQNEIE----KLKKENQS---YKQE 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  275 AETLREQLSSanhslqLASQIQKAPDVEQaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQ 354
Cdd:TIGR04523  386 IKNLESQIND------LESKIQNQEKLNQ--------QKDEQIKKLQQEKELLEKEIERLKETIIKN----NSEIKDLTN 447
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1622917383  355 QLSAKNSTLKQLEEKLKGQADY-EEVKKELNILKS 388
Cdd:TIGR04523  448 QDSVKELIIKNLDNTRESLETQlKVLSRSINKIKQ 482
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
34-389 1.08e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 66.63  E-value: 1.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   34 IKRELDATATVLANRQDESEQsRKRLIEQSREFKKNTP-------EDLRKQvapLLKSFQGEIDALSKRSKEAEAAFLNV 106
Cdd:PRK03918   403 IEEEISKITARIGELKKEIKE-LKKAIEELKKAKGKCPvcgreltEEHRKE---LLEEYTAELKRIEKELKEIEEKERKL 478
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  107 YKRLIDVpdpvpalDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEKIREYEQTLKNQAETia 186
Cdd:PRK03918   479 RKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEKLIKLKGEIKSLKKE-- 547
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  187 LEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQ-TALEKTRTELFDLKTKYDEETTAKADEIEmimtdLERAN 265
Cdd:PRK03918   548 LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKE-----LEREE 618
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  266 QRAEVAQREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAsltklrens 345
Cdd:PRK03918   619 KELKKLEEELDKAFEELAETEKRLE---------ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRA--------- 680
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1622917383  346 asQISQLEQQLSAKNSTLKQLEEKLKgqaDYEEVKKELNILKSM 389
Cdd:PRK03918   681 --ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
119-348 1.61e-10

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 64.79  E-value: 1.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  119 ALDLGQQLQLKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIAL--EKEQKLQN 195
Cdd:COG4942     18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  196 DFAEKERKLQET-----QMSTTSKLEEAEHKVQSLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 270
Cdd:COG4942     98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383  271 AQREAETLREQLSSANHSLQLASQIQKApdveqaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 348
Cdd:COG4942    172 ERAELEALLAELEEERAALEALKAERQK----------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
86-425 5.66e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 64.02  E-value: 5.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   86 QGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYnkefaevKNQEVTIK 165
Cdd:COG4717     94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------RELEEELE 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  166 ALKEKIREYEQTLKNQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtkyDE 245
Cdd:COG4717    167 ELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA---LE 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  246 ETTAKADEIEMIMT--------DLERANQRAEVAqrEAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLE--- 314
Cdd:COG4717    243 ERLKEARLLLLIAAallallglGGSLLSLILTIA--GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEeee 320
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  315 ---------VELAAKEREIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLS-----AKNSTLKQLEEKLKGQADYEEV 379
Cdd:COG4717    321 leellaalgLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEELRAALEQAEEYQEL 400
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1622917383  380 KKELNILKSmEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALR 425
Cdd:COG4717    401 KEELEELEE-QLEELLGELEELLEALDEEELEEELEELEEELEELE 445
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
34-386 1.08e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.16  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   34 IKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEidALSKRSKEAEaaflNVYKRLIDV 113
Cdd:PRK03918   464 IEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAEEYE----KLKEKLIKL 537
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  114 PdpvpaldlGQQLQLK--VQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlknqaetiA 186
Cdd:PRK03918   538 K--------GEIKSLKkeLEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP---------F 600
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  187 LEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERANQ 266
Cdd:PRK03918   601 YNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE---EYLELSRELA 676
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  267 RAEvaqREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQAsltKLRENS 345
Cdd:PRK03918   677 GLR---AELEELEKRREEIKKTLE---------KLKEELEEREKAKKELEKLEKALErVEELREKVKKYKA---LLKERA 741
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1622917383  346 ASQISQLEQQLSAK-------NSTLKQLEEKLKGQADYEEVKKELNIL 386
Cdd:PRK03918   742 LSKVGEIASEIFEEltegkysGVRVKAEENKVKLFVVYQGKERPLTFL 789
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
124-297 1.24e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 62.86  E-value: 1.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  124 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 203
Cdd:COG4717     74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  204 LQETQMSttskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 279
Cdd:COG4717    151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
                          170
                   ....*....|....*...
gi 1622917383  280 EQLSSANHSLQLASQIQK 297
Cdd:COG4717    227 EELEQLENELEAAALEER 244
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
50-371 5.17e-09

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 59.54  E-value: 5.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   50 DESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKEaeaaFLNVYKRLIDVPDpvpalDLGQQLQ-L 128
Cdd:COG1340     11 EELEEKIEELREEIEELKEK-----RDELNEELKELAEKRDELNAQVKE----LREEAQELREKRD-----ELNEKVKeL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  129 KVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFAEKERKLQETQ 208
Cdd:COG1340     77 KEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEKAK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  209 msttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLeranqraevaQREAETLREQLSSANHS 288
Cdd:COG1340    154 -----KALEKNEKLKELRAELKELRKEAEEIHKKI-KELAEEAQELHEEMIEL----------YKEADELRKEADELHKE 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  289 LQLASQiqkapdveqaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASqiSQLEQQLSAKNSTLKQLEE 368
Cdd:COG1340    218 IVEAQE---------------------KADELHEEIIELQKELRELRKELKKLRKKQRA--LKREKEKEELEEKAEEIFE 274

                   ...
gi 1622917383  369 KLK 371
Cdd:COG1340    275 KLK 277
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
131-388 5.63e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 61.24  E-value: 5.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  131 QRLHDIETENQKLRETLEEYNKEfaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQ----- 205
Cdd:TIGR02169  184 ENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEkltee 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  206 ---------------------------ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK---TKYDEETTAKADEIE 255
Cdd:TIGR02169  260 iselekrleeieqlleelnkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEerlAKLEAEIDKLLAEIE 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  256 MIMTDLERANQR-----AEVAQREAE--TLREQLSSANHSLQLASQIQKapDVEQAIEVLTR---------SSLEVELAA 319
Cdd:TIGR02169  340 ELEREIEEERKRrdkltEEYAELKEEleDLRAELEEVDKEFAETRDELK--DYREKLEKLKReinelkrelDRLQEELQR 417
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622917383  320 KEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQLEEKL-KGQADYEEVKKELNILKS 388
Cdd:TIGR02169  418 LSEELADLNAAIAGIEAKINELeeeKEDKALEIKKQEWKLEQLAADLSKYEQELyDLKEEYDRVEKELSKLQR 490
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
142-452 7.43e-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: 60.85  E-value: 7.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  142 KLRETLEEYNKEFAEVKNQEVTIKALKEKIR----EYEQTLKN-QAETIALEKEQKLqndFAEKERKLQEtqmsttsKLE 216
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIEnrldELSQELSDaSRKIGEIEKEIEQ---LEQEEEKLKE-------RLE 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  217 EAEHKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLER--ANQRAEVAQREAETLREQLSSANHSLQlasq 294
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR---- 815
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  295 iqkapdveqaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS----------QISQLEQQLSAKNSTLK 364
Cdd:TIGR02169  816 -----------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienlngKKEELEEELEELEAALR 878
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  365 QLEEKLKG-QADYEEVKKELNILksmefapsegagtQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSGSARRKGKDQP 443
Cdd:TIGR02169  879 DLESRLGDlKKERDELEAQLREL-------------ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945

                   ....*....
gi 1622917383  444 ESRRPGSLP 452
Cdd:TIGR02169  946 IPEEELSLE 954
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
155-396 8.18e-09

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 59.39  E-value: 8.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  155 AEVKNQEVTIKALKEKIREYEQTLKNQAETI--ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKT 232
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALE----QELAALEAELAELEKEIAEL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  233 RTELFDLKTKYDE-----ETTAKADEIEMIM--TDLERANQRAEVAQREAETLREQLSsanhslQLASQIQKAPDVEQAI 305
Cdd:COG4942     96 RAELEAQKEELAEllralYRLGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAE------ELRADLAELAALRAEL 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  306 EVlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNI 385
Cdd:COG4942    170 EA-ERAELEALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLE--AEAAAAAER 242
                          250
                   ....*....|.
gi 1622917383  386 LKSMEFAPSEG 396
Cdd:COG4942    243 TPAAGFAALKG 253
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
34-374 8.93e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 8.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   34 IKRELDATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQVAPLLKS---FQGEIDALSKRSKEAEAAFLNVYKRL 110
Cdd:COG1196    251 LEAELEELEAELAELEAELEELRLELEELELEL-----EEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEEL 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  111 idvpdpvpaLDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQTLKNQAEtiALEKE 190
Cdd:COG1196    326 ---------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL---LEAEAELAEAEEELEELAE--ELLEA 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  191 QKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtdlERANQRAEV 270
Cdd:COG1196    392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE------EEEALLELL 465
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  271 AQ--REAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS 347
Cdd:COG1196    466 AEllEEAALLEAALAELLEELaEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
                          330       340
                   ....*....|....*....|....*..
gi 1622917383  348 qiSQLEQQLSAKNSTLKQLEEKLKGQA 374
Cdd:COG1196    546 --AALQNIVVEDDEVAAAAIEYLKAAK 570
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
74-441 1.18e-08

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 59.98  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   74 LRKQVAPLLKSFQGEIDALSKRSK---EAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEY 150
Cdd:TIGR00618  554 ERKQRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  151 NKEFAEVKNQEVTIKAlkekirEYEQTLKNQAETIALE--KEQKLQNdFAEKERKLQETQ---MSTTSKLEEAEHKvqsl 225
Cdd:TIGR00618  634 LQQCSQELALKLTALH------ALQLTLTQERVREHALsiRVLPKEL-LASRQLALQKMQsekEQLTYWKEMLAQC---- 702
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  226 QTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAET-LREQ-LSSANHSLQLASQIQKAPDVEQ 303
Cdd:TIGR00618  703 QTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTvLKARtEAHFNNNEEVTAALQTGAELSH 782
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  304 AIEVLT-----RSSLEVELAAKEREIAQLVED------------VQRLQASLTKLRENSASQIsQLEQQLSAKNSTLKQL 366
Cdd:TIGR00618  783 LAAEIQffnrlREEDTHLLKTLEAEIGQEIPSdedilnlqcetlVQEEEQFLSRLEEKSATLG-EITHQLLKYEECSKQL 861
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622917383  367 EEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKplevLLMEKNRSLQSENAALRISNSDLSGSARRKGKD 441
Cdd:TIGR00618  862 AQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE----ITLYANVRLANQSEGRFHGRYADSHVNARKYQG 932
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
186-382 1.57e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 58.62  E-value: 1.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  186 ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERAN 265
Cdd:COG4942     18 QADAAAEAEAELEQLQQEIAELE----KELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  266 QRAEVAQREAETLREQLSSANHSLQLASQIQK------APDVEQAIEVLT--------RSSLEVELAAKEREIAQLVEDV 331
Cdd:COG4942     90 KEIAELRAELEAQKEELAELLRALYRLGRQPPlalllsPEDFLDAVRRLQylkylapaRREQAEELRADLAELAALRAEL 169
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622917383  332 QRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKE 382
Cdd:COG4942    170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
137-389 2.41e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 2.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  137 ETENqKLRETLEEYNKefaevknqevtIKALKEKIREYEQTLKNQAEtiALEKEQKLQNDFAEKERKLQetqmstTSKLE 216
Cdd:TIGR02168  176 ETER-KLERTRENLDR-----------LEDILNELERQLKSLERQAE--KAERYKELKAELRELELALL------VLRLE 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  217 EAEHKVQSLQTALEKTRTELFDLKTKYDEETTakadEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASqiQ 296
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEE----KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR--E 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  297 KAPDVEQAIEVLTRSSLEV---------ELAAKEREIAQLVEDVQRLQASLTKLR---ENSASQISQLEQQLSAKNSTLK 364
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELeskldelaeELAELEEKLEELKEELESLEAELEELEaelEELESRLEELEEQLETLRSKVA 389
                          250       260
                   ....*....|....*....|....*.
gi 1622917383  365 QLEEKLKG-QADYEEVKKELNILKSM 389
Cdd:TIGR02168  390 QLELQIASlNNEIERLEARLERLEDR 415
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
165-438 2.60e-08

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: 58.83  E-value: 2.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  165 KALKEKIREYEQTLKNQAETIALEK-EQKLQNDFAEKERKLQETQmsttsKLEEAEhkvqsLQTALEKTRTELFDLKTKY 243
Cdd:pfam02463  173 EALKKLIEETENLAELIIDLEELKLqELKLKEQAKKALEYYQLKE-----KLELEE-----EYLLYLDYLKLNEERIDLL 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  244 DEETTAKADEIEMImtdleraNQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKERE 323
Cdd:pfam02463  243 QELLRDEQEEIESS-------KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  324 IAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSmefapSEGAGTQDAA 403
Cdd:pfam02463  316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK-----LESERLSSAA 390
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1622917383  404 KPLEVLLMEKNRSLQSENAALRISNSDLSGSARRK 438
Cdd:pfam02463  391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEK 425
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
33-435 3.00e-08

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 58.70  E-value: 3.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   33 GIKRELDAtatVLANRQDESEQSRKRLIEQSREfKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLID 112
Cdd:pfam12128  582 GVKLDLKR---IDVPEWAASEEELRERLDKAEE-ALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRR 657
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  113 VpdpvpaLDLGQQLQLKVQRlhDIETENQKLRETLEEYNKEfaevknqevtIKALKEKIREYEQTLKNQAETIALEKEQK 192
Cdd:pfam12128  658 L------FDEKQSEKDKKNK--ALAERKDSANERLNSLEAQ----------LKQLDKKHQAWLEEQKEQKREARTEKQAY 719
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  193 LQNdfAEKERKLQETQMSTTSKLEEAEHKVQslQTALEKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERANQRAEV 270
Cdd:pfam12128  720 WQV--VEGALDAQLALLKAAIAARRSGAKAE--LKALETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERIAVRRQE 793
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  271 AQREAETLREQLSSANHSLQlasqIQKApDVEQAIEvltrsslevelaakereiaqlvedvqRLQASLTKLRENSASQIS 350
Cdd:pfam12128  794 VLRYFDWYQETWLQRRPRLA----TQLS-NIERAIS--------------------------ELQQQLARLIADTKLRRA 842
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  351 QLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSD 430
Cdd:pfam12128  843 KLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIAD 922

                   ....*
gi 1622917383  431 LSGSA 435
Cdd:pfam12128  923 HSGSG 927
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
145-366 3.39e-08

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: 55.30  E-value: 3.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  145 ETLEEYNKEFAEVKN--QEVT------IKALKEKIREyeqtLKNQAEtialEKEQKLQNDFAEKERkLQEtqmsttsKLE 216
Cdd:pfam13851    1 ELMKNHEKAFNEIKNyyNDITrnnlelIKSLKEEIAE----LKKKEE----RNEKLMSEIQQENKR-LTE-------PLQ 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  217 EAEHKVQSLQTAL---EKTRTELfdlktkydEETTAKADEIEMIMTDLERAN----QRAEVAQREAETLREQLSSANHSL 289
Cdd:pfam13851   65 KAQEEVEELRKQLenyEKDKQSL--------KNLKARLKVLEKELKDLKWEHevleQRFEKVERERDELYDKFEAAIQDV 136
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383  290 QLASQiQKAPDVEQAIEVLTRsslevELAAKEREIAQLvedvqrLQASltKLRENSASQISQ-LEQQLSAKNSTLKQL 366
Cdd:pfam13851  137 QQKTG-LKNLLLEKKLQALGE-----TLEKKEAQLNEV------LAAA--NLDPDALQAVTEkLEDVLESKNQLIKDL 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
35-313 5.21e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 5.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   35 KRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAflnvykrlid 112
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE---------- 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  113 vpdpvpaldlgqqlqlkvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALEKEQK 192
Cdd:TIGR02168  367 --------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRERLQQEI 423
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  193 LQNDFAEKERKLQETQMSTTSK---LEEAEHKVQSLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLERANQRAE 269
Cdd:TIGR02168  424 EELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLERLQENLE 502
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1622917383  270 VAQRE-AETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSL 313
Cdd:TIGR02168  503 GFSEGvKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRL 547
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
51-387 5.41e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 57.72  E-value: 5.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   51 ESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLK---SFQGEIDALsKRSKEAEAAFLNVYKRLIDVPDPvPALDLGQQLQ 127
Cdd:TIGR04523  415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdsVKELIIKNL-DNTRESLETQLKVLSRSINKIKQ-NLEQKQKELK 492
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  128 LKVQRLHDIETENQKLRETLEEYNKEFAEVKNqevTIKALKEKIREYEQTLKNQAETIaLEKEQKLQNDFAEKErkLQET 207
Cdd:TIGR04523  493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKE---KIEKLESEKKEKESKISDLEDEL-NKDDFELKKENLEKE--IDEK 566
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  208 QmsttSKLEEAEHKvqslQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ----LS 283
Cdd:TIGR04523  567 N----KEIEELKQT----QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIikniKS 638
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  284 SANHSLQLASQIQ--------KAPDVEQAIEvltrsslevELAAKEREIAQLVEDvqRLQASLTKLRENSASQIsqleqq 355
Cdd:TIGR04523  639 KKNKLKQEVKQIKetikeirnKWPEIIKKIK---------ESKTKIDDIIELMKD--WLKELSLHYKKYITRMI------ 701
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1622917383  356 lsaKNSTLKQLEEKlkgqadYEEVKKELNILK 387
Cdd:TIGR04523  702 ---RIKDLPKLEEK------YKEIEKELKKLD 724
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
164-386 5.50e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.47  E-value: 5.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  164 IKALKEKIREYE-----QTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRtelfd 238
Cdd:COG4717     48 LERLEKEADELFkpqgrKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE----- 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  239 lktkydeettaKADEIEMIMTDLERANQRAEVAQREAETLREQLssanhsLQLASQIQKAPDVEQAIEVLTRS---SLEV 315
Cdd:COG4717    123 -----------KLLQLLPLYQELEALEAELAELPERLEELEERL------EELRELEEELEELEAELAELQEEleeLLEQ 185
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622917383  316 ELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNIL 386
Cdd:COG4717    186 LSLATEEELQDLAEELEELQQRLAELEE----ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLL 252
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
131-278 5.81e-08

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 55.32  E-value: 5.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  131 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KNQAETIALEKEQklqnDFAEKERK 203
Cdd:COG1579     31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEI----ESLKRRIS 106
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383  204 LQETqmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERAN-QRAEVAQREAETL 278
Cdd:COG1579    107 DLED------EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEaEREELAAKIPPEL 176
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
39-374 5.86e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 57.74  E-value: 5.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   39 DATATVLANRQDE----SEQSRKRLIEQ--SREFKKNTPEDLRKQVAPLlksfQGEIDALSKRSKEAEAAFLNVYKRLID 112
Cdd:PRK02224   306 DADAEAVEARREEledrDEELRDRLEECrvAAQAHNEEAESLREDADDL----EERAEELREEAAELESELEEAREAVED 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  113 VPDPVPALDlgQQLQLKVQRLHDIETEnqklRETLEEYNKEFAEVKNqevtikALKEKIREYEQTLKNQAETIAlEKEQK 192
Cdd:PRK02224   382 RREEIEELE--EEIEELRERFGDAPVD----LGNAEDFLEELREERD------ELREREAELEATLRTARERVE-EAEAL 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  193 LQ-NDFAEKERKLQETQMSTTskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAE 269
Cdd:PRK02224   449 LEaGKCPECGQPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIA 526
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  270 VAQREAETLREQLSSANHSLQ-LASQIQKAPDVEQAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQ--ASLTKLRENSA 346
Cdd:PRK02224   527 ERRETIEEKRERAEELRERAAeLEAEAEEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLEriRTLLAAIADAE 605
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1622917383  347 SQISQLEQQ--------------LSAKNSTLKQLEEKLKGQA 374
Cdd:PRK02224   606 DEIERLREKrealaelnderrerLAEKRERKRELEAEFDEAR 647
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
26-370 8.26e-08

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 57.16  E-value: 8.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   26 AHWLcspgikRELDATATVLANR------QDESEQ----------------SRKRLIEQSREFKKNTPEDLRKQVAPLLK 83
Cdd:pfam12128  224 EHWI------RDIQAIAGIMKIRpeftklQQEFNTlesaelrlshlhfgykSDETLIASRQEERQETSAELNQLLRTLDD 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   84 SFQGEIDALSKRSKEAEAAFLNV----------YKRLIDVPDPVPALDLGQQLQLK-----VQRLHDIETENQklRETLE 148
Cdd:pfam12128  298 QWKEKRDELNGELSAADAAVAKDrselealedqHGAFLDADIETAAADQEQLPSWQselenLEERLKALTGKH--QDVTA 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  149 EYNKEFAEVKNQEVT----IKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQS 224
Cdd:pfam12128  376 KYNRRRSKIKEQNNRdiagIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQ 455
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  225 LQ-TALEKTRTELFD-LKTKYDEETTAKADEIEMIMTD--------------LERANQRAEVAQREAETLREQLSSANHS 288
Cdd:pfam12128  456 ATaTPELLLQLENFDeRIERAREEQEAANAEVERLQSElrqarkrrdqaseaLRQASRRLEERQSALDELELQLFPQAGT 535
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  289 LqLASQIQKAPDVEQAI------EVLTRSSLEVEL----AAKEREIAQLVEDVQRLQA-SLTKLRENSASQISQLEQQLS 357
Cdd:pfam12128  536 L-LHFLRKEAPDWEQSIgkvispELLHRTDLDPEVwdgsVGGELNLYGVKLDLKRIDVpEWAASEEELRERLDKAEEALQ 614
                          410
                   ....*....|...
gi 1622917383  358 AKNSTLKQLEEKL 370
Cdd:pfam12128  615 SAREKQAAAEEQL 627
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
133-387 1.33e-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: 56.37  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  133 LHDIETENQKLRETLEEYNK---EFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQM 209
Cdd:pfam10174  201 LDQKEKENIHLREELHRRNQlqpDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  210 STTSKLeeAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLREQLSSAN 286
Cdd:pfam10174  281 KSHSKF--MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKE 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  287 HSLQ---------------LASQIQKAPDV----EQAIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTklreNS 345
Cdd:pfam10174  359 SFLNkktkqlqdlteekstLAGEIRDLKDMldvkERKINVLQKkiENLQEQLRDKDKQLAGLKERVKSLQTDSS----NT 434
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1622917383  346 ASQISQLEQQLSAKNSTLKQLEEK--LKGQADYEEV---KKELNILK 387
Cdd:pfam10174  435 DTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
186-384 1.75e-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: 53.78  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  186 ALEKEQKLQNDFAEKERKLQETQMsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERAN 265
Cdd:COG1579      8 ALLDLQELDSELDRLEHRLKELPA----ELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKYE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  266 QRAEVA--QREAETLREQLSSanhslqLASQIQKAPDVEQAievltrssLEVELAAKEREIAQLVEDVQRLQASLTKLRE 343
Cdd:COG1579     80 EQLGNVrnNKEYEALQKEIES------LKRRISDLEDEILE--------LMERIEELEEELAELEAELAELEAELEEKKA 145
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1622917383  344 NSASQISQLEQQLSAKNSTLKQLEEKLKGQ--ADYEEVKKELN 384
Cdd:COG1579    146 ELDEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKN 188
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
110-389 1.96e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 55.79  E-value: 1.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  110 LIDVPDPVPALDLGQQLQLKVQrlhDIETENQKLR---------ETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKN 180
Cdd:COG3206     60 LVEPQSSDVLLSGLSSLSASDS---PLETQIEILKsrpvlervvDKLNLDEDPLGEEASREAAIERLRKNL-----TVEP 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  181 QAETIAL---------EKEQKLQNDFAE------KERKLQETQMSTT---SKLEEAEHKVQSLQTALE--KTRTELFDLk 240
Cdd:COG3206    132 VKGSNVIeisytspdpELAAAVANALAEayleqnLELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL- 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  241 tkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSanhSLQLASQIQKAPDVEQAIEVLtrSSLEVELA-- 318
Cdd:COG3206    211 ---SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS---GPDALPELLQSPVIQQLRAQL--AELEAELAel 282
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  319 ------------AKEREIA----QLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKE 382
Cdd:COG3206    283 sarytpnhpdviALRAQIAalraQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL---EAELRRLERE 359

                   ....*..
gi 1622917383  383 LNILKSM 389
Cdd:COG3206    360 VEVAREL 366
46 PHA02562
endonuclease subunit; Provisional
120-341 1.98e-07

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 55.79  E-value: 1.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  120 LDLGQQlQLKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKNQAETIalekeQKLQN 195
Cdd:PHA02562   190 IDHIQQ-QIKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNT 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  196 DFAEKERKLQ----ETQMST--------TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakadeiemimtdlER 263
Cdd:PHA02562   263 AAAKIKSKIEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE--------------EI 328
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383  264 ANQRAEvAQREAETLREQLSSANHSLQLAsqIQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL 341
Cdd:PHA02562   329 MDEFNE-QSKKLLELKNKISTNKQSLITL--VDKAKKVKAAIE-----ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
124-284 2.05e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.08  E-value: 2.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  124 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 203
Cdd:COG4913    274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  204 LQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 283
Cdd:COG4913    354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429

                   .
gi 1622917383  284 S 284
Cdd:COG4913    430 S 430
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
50-390 2.48e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 2.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   50 DESEQSRKRLIEQSREFKKNTPEDLRKqvapllksfqgEIDALSKRSKEAEAAFLNVYKRLIDVPDpvpaldLGQQLQLK 129
Cdd:PRK03918   365 EEAKAKKEELERLKKRLTGLTPEKLEK-----------ELEELEKAKEEIEEEISKITARIGELKK------EIKELKKA 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  130 VQRLHDIE----------TENQKLrETLEEYNKEFAEVKNQEVTIKALKEKIR----EYEQTLKNQAETIALEK------ 189
Cdd:PRK03918   428 IEELKKAKgkcpvcgrelTEEHRK-ELLEEYTAELKRIEKELKEIEEKERKLRkelrELEKVLKKESELIKLKElaeqlk 506
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  190 --EQKLQNDFAEK-ERKLQE----------------TQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK 250
Cdd:PRK03918   507 elEEKLKKYNLEElEKKAEEyeklkekliklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES 586
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  251 ADEIEMIMTDLER----------ANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIEVLTRSSLEVELAAK 320
Cdd:PRK03918   587 VEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETE--KRLEELRKELEELEKKYSEEEYEEL 664
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622917383  321 EREIAQLVEDVQRLQA---SLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSME 390
Cdd:PRK03918   665 REEYLELSRELAGLRAeleELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL 737
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
246-428 2.78e-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: 2.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  246 ETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRS----SLEVELAAKE 321
Cdd:COG4913    222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQrrleLLEAELEELR 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  322 REIAQLVEDVQRLQASLTKLRE-----------NSASQISQLEQQLSAKNSTLKQLEEKLK---------------GQAD 375
Cdd:COG4913    302 AELARLEAELERLEARLDALREeldeleaqirgNGGDRLEQLEREIERLERELEERERRRArleallaalglplpaSAEE 381
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383  376 YEEVKKELNILKsmEFAPSEGAGTQDAAKPLEVLLMEKNR---SLQSENAAL--RISN 428
Cdd:COG4913    382 FAALRAEAAALL--EALEEELEALEEALAEAEAALRDLRRelrELEAEIASLerRKSN 437
46 PHA02562
endonuclease subunit; Provisional
165-369 3.39e-07

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 55.02  E-value: 3.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  165 KALKEKIREYEQTLKNQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKVQ--SLQT-------- 227
Cdd:PHA02562   170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEieELTDellnlvmd 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  228 ------ALEKTRTELFDLKTKYdeETTAKadEIEMI---------MTDLERANQRaevaqreAETLREQLSSANHSL-QL 291
Cdd:PHA02562   250 iedpsaALNKLNTAAAKIKSKI--EQFQK--VIKMYekggvcptcTQQISEGPDR-------ITKIKDKLKELQHSLeKL 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  292 ASQIQKAPDVEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQL 366
Cdd:PHA02562   319 DTAIDELEEIMDEFNEQSKKLLELknKISTNKQSLITLVDKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSEL 398

                   ...
gi 1622917383  367 EEK 369
Cdd:PHA02562   399 VKE 401
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
72-264 3.55e-07

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: 53.91  E-value: 3.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   72 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLNVYKRLIDVpdpvpaldlgQQLQLK--VQRLHDI-ETENQKL-RETL 147
Cdd:cd22656    113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTEK----------DQTALEtlEKALKDLlTDEGGAIaRKEI 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  148 EEYNKEFAevKNQEVTIKALKEKIREYEQTLKNQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKVQSLQ 226
Cdd:cd22656    182 KDLQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQ 252
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1622917383  227 TALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 264
Cdd:cd22656    253 GAWQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
176-384 5.14e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 5.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  176 QTLKNQAETIALEKEQK-LQNDFAEKERKLQETQmSTTSKLEEAEHKVQSL----------------------------Q 226
Cdd:TIGR02168  671 SILERRREIEELEEKIEeLEEKIAELEKALAELR-KELEELEEELEQLRKEleelsrqisalrkdlarleaeveqleerI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  227 TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIE 306
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLE 827
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  307 VLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKELN 384
Cdd:TIGR02168  828 SLERriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL---RSELEELSEELR 904
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
51-388 6.46e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.30  E-value: 6.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   51 ESEQSRKRLIEQSREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEaaflNVYKRLIDVpdpvpaldlGQQLQLKV 130
Cdd:PRK03918   142 ESDESREKVVRQILGLDDY--ENAYKNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEK---------EKELEEVL 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  131 QRLHDIETENQKLRETLEEYNKEFAEV----------------------------KNQEVTIKALKEKIREYEQTLKNQA 182
Cdd:PRK03918   207 REINEISSELPELREELEKLEKEVKELeelkeeieelekeleslegskrkleekiRELEERIEELKKEIEELEEKVKELK 286
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  183 ETIALEKE----QKLQNDFAEKERKLQETQMSTT----------SKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETT 248
Cdd:PRK03918   287 ELKEKAEEyiklSEFYEEYLDELREIEKRLSRLEeeingieeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  249 AKA--------------DEIEMIMTDLERANQRAEVAQREAETLREQLSSANH---SLQLA-SQIQKAP----------D 300
Cdd:PRK03918   367 AKAkkeelerlkkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKeikELKKAiEELKKAKgkcpvcgrelT 446
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  301 VEQAIEVLTRSSLEV--------ELAAKEREI---AQLVEDVQRLQASLTKLREnSASQISQLEQQLSAKNstLKQLEEK 369
Cdd:PRK03918   447 EEHRKELLEEYTAELkriekelkEIEEKERKLrkeLRELEKVLKKESELIKLKE-LAEQLKELEEKLKKYN--LEELEKK 523
                          410
                   ....*....|....*....
gi 1622917383  370 LKgqaDYEEVKKELNILKS 388
Cdd:PRK03918   524 AE---EYEKLKEKLIKLKG 539
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
123-371 7.08e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 54.28  E-value: 7.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  123 GQQLQLKVQrlhdIE-TENQKLRETLEEYNKEFAEVKNQevtIKALKEKiREYEQTLKNQAETIALEKEQKLQ--NDFAE 199
Cdd:PRK02224   187 GSLDQLKAQ----IEeKEEKDLHERLNGLESELAELDEE---IERYEEQ-REQARETRDEADEVLEEHEERREelETLEA 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  200 KERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK-----TKYDEETTAK-----ADEIEMIMTDLERANQRAE 269
Cdd:PRK02224   259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLaeaglDDADAEAVEArreelEDRDEELRDRLEECRVAAQ 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  270 VAQREAETLRE---QLSSANHSLQlasqiQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL---RE 343
Cdd:PRK02224   339 AHNEEAESLREdadDLEERAEELR-----EEAAELESELE-----EAREAVEDRREEIEELEEEIEELRERFGDApvdLG 408
                          250       260
                   ....*....|....*....|....*...
gi 1622917383  344 NSASQISQLEQQLSAKNSTLKQLEEKLK 371
Cdd:PRK02224   409 NAEDFLEELREERDELREREAELEATLR 436
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
139-387 7.98e-07

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: 54.21  E-value: 7.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  139 ENQKLRETLE---EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKL 215
Cdd:pfam02463  174 ALKKLIEETEnlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  216 EEAEhKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA--ETLREQLSSANHSLQLAS 293
Cdd:pfam02463  254 ESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDeeKLKESEKEKKKAEKELKK 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  294 QIQKAPDVEQAIEVLTRSSLEVELA--AKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKN------STLKQ 365
Cdd:pfam02463  333 EKEEIEELEKELKELEIKREAEEEEeeELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSeeekeaQLLLE 412
                          250       260
                   ....*....|....*....|..
gi 1622917383  366 LEEKLKGQADyEEVKKELNILK 387
Cdd:pfam02463  413 LARQLEDLLK-EEKKEELEILE 433
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
185-426 8.59e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 8.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  185 IALEKEQKLQNDFAEKERKLQETQmsTTSKLEEAEHKVQSLQTALEKTRTELFDLKtkydEETTAKADEIEMIMTDLERA 264
Cdd:COG4372     26 IAALSEQLRKALFELDKLQEELEQ--LREELEQAREELEQLEEELEQARSELEQLE----EELEELNEQLQAAQAELAQA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  265 NQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLREN 344
Cdd:COG4372    100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA-------ELQSEIAEREEELKELEEQLESLQEELAALEQE 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  345 -----SASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQS 419
Cdd:COG4372    173 lqalsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252

                   ....*..
gi 1622917383  420 ENAALRI 426
Cdd:COG4372    253 EEVILKE 259
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
210-484 9.39e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.91  E-value: 9.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  210 STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 289
Cdd:COG3883     20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  290 Q-------LASQIQKAPDVE------QAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 354
Cdd:COG3883     96 YrsggsvsYLDVLLGSESFSdfldrlSALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  355 QLSAKNSTLKQLEEKlkgQADYEEVKKELNilKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSGS 434
Cdd:COG3883    176 QQAEQEALLAQLSAE---EAAAEAQLAELE--AELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622917383  435 ARRKGKDQPESRRPGSLPAPPPSQLPRNPGEQASNTNGTHQFSPAGLSQD 484
Cdd:COG3883    251 AAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAAS 300
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
137-433 1.30e-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: 53.44  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  137 ETENQKLRETLEEYNKEFAEVKNQEVTIKALK-EKIREYEQTLKNQAETIALEKEQklqNDFAEKERKLQETQMSTTSKL 215
Cdd:pfam02463  218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEqEEIESSKQEIEKEEEKLAQVLKE---NKEEEKEKKLQEEELKLLAKE 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  216 EEaehkVQSLQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTD-LERANQRAEV-AQREAETLREQLSSAN--HSLQ 290
Cdd:pfam02463  295 EE----ELKSELLKLERRKVDDEEKLKESEKEKKKAEkELKKEKEEiEELEKELKELeIKREAEEEEEEELEKLqeKLEQ 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  291 LASQIQKAPDVEQAIEVLTRSSLEVELAAKERE--IAQLVEDVQRLQASLTKLRENSAS------QISQLEQQLSAKNST 362
Cdd:pfam02463  371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEekEAQLLLELARQLEDLLKEEKKEELeileeeEESIELKQGKLTEEK 450
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622917383  363 LKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSG 433
Cdd:pfam02463  451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
141-367 2.32e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  141 QKLRETLEEYnkefaevknqevtiKALKEKIREYEQtlknQAETIALEKEQKLQNDFAEKERKLQEtqmsttsKLEEAEH 220
Cdd:COG4913    255 EPIRELAERY--------------AAARERLAELEY----LRAALRLWFAQRRLELLEAELEELRA-------ELARLEA 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  221 KVQSLQTALEKTRTELFDLKTKYDEettAKADEIEmimtDLERANQRAEVAQREAETLREQLSSANHSLQLAsqiqkAPD 300
Cdd:COG4913    310 ELERLEARLDALREELDELEAQIRG---NGGDRLE----QLEREIERLERELEERERRRARLEALLAALGLP-----LPA 377
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383  301 VEQaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLE 367
Cdd:COG4913    378 SAE------------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
133-430 2.35e-06

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 52.75  E-value: 2.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  133 LHDIETENQKLRETLEEYNKEFAevKNQEVTI--------KALKEKIREYEQTLKNqAETIALEKEQKLQNDFAEKERKL 204
Cdd:TIGR01612  988 LNDYEAKNNELIKYFNDLKANLG--KNKENMLyhqfdekeKATNDIEQKIEDANKN-IPNIEIAIHTSIYNIIDEIEKEI 1064
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  205 -QETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQls 283
Cdd:TIGR01612 1065 gKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGK--EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK-- 1140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  284 SANHSLQLASQIQKAPDVeqAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQQLSA----K 359
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDV--ADKAISNDDPE-EIEKKIENIVTKIDKKKNIYDEIKKL----LNEIAEIEKDKTSleevK 1213
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622917383  360 NSTL---KQLEEKLKGQADyEEVKKELNILKSMEfAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSD 430
Cdd:TIGR01612 1214 GINLsygKNLGKLFLEKID-EEKKKSEHMIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD 1285
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
131-333 2.40e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 2.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  131 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALekeQKLQNDFAEKERKLQETQmS 210
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAE---LDALQERREALQRLAEYSWDEIDV---ASAEREIAELEAELERLD-A 682
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  211 TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 286
Cdd:COG4913    683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622917383  287 HSLQLASQIQKApdveqaievltRSSLEVELAAKEREIAQLVEDVQR 333
Cdd:COG4913    763 VERELRENLEER-----------IDALRARLNRAEEELERAMRAFNR 798
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
37-390 2.54e-06

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: 52.42  E-value: 2.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   37 ELDATATVLANRQDESEQSRKRLIEqsrefkKNTPEDLRKQVAPLLKSFQGeidalskrsKEAEAAFLnvykrlidvpdp 116
Cdd:pfam05483  392 ELEEMTKFKNNKEVELEELKKILAE------DEKLLDEKKQFEKIAEELKG---------KEQELIFL------------ 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  117 vpaldlgqqLQLKVQRLHDIETENQKLRETLEEYNKEFAE---------VKNQEVTIKALKEKIREYEQTLKNQAETIAL 187
Cdd:pfam05483  445 ---------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlktelekekLKNIELTAHCDKLLLENKELTQEASDMTLEL 515
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  188 EKEQK-LQNDFAEKERKLQEtqmsttskLEEAEHKVQSLQTALEKTRTELF----DLKTKYDE-ETTAKADEIEMImtdl 261
Cdd:pfam05483  516 KKHQEdIINCKKQEERMLKQ--------IENLEEKEMNLRDELESVREEFIqkgdEVKCKLDKsEENARSIEYEVL---- 583
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  262 eRANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEV-------LTRSSLEVELAAKEREIAQLVEDVQRl 334
Cdd:pfam05483  584 -KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENkqlnayeIKVNKLELELASAKQKFEEIIDNYQK- 661
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622917383  335 QASLTKLRENS-----------ASQISQLEQQLSA----KNSTLKQLEEKLKGQAD--YEEVKKELNILKSME 390
Cdd:pfam05483  662 EIEDKKISEEKlleevekakaiADEAVKLQKEIDKrcqhKIAEMVALMEKHKHQYDkiIEERDSELGLYKNKE 734
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
72-388 3.36e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.69  E-value: 3.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   72 EDLRKQVApLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYN 151
Cdd:COG4717     74 KELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  152 KEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEK 231
Cdd:COG4717    153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  232 TRTELFDLK-----------------------------------------------------TKYDEETTAKADEIEMI- 257
Cdd:COG4717    232 LENELEAAAleerlkearlllliaaallallglggsllsliltiagvlflvlgllallflllAREKASLGKEAEELQALp 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  258 -MTDLERANQRAEVAQ-------------------REAETLREQLSSANHSLQLASQIQK---------APDVEQAIEVL 308
Cdd:COG4717    312 aLEELEEEELEELLAAlglppdlspeellelldriEELQELLREAEELEEELQLEELEQEiaallaeagVEDEEELRAAL 391
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  309 TRSSLEVELAAKEREI--------------------AQLVEDVQRLQASLTKLREnsasQISQLEQQLSAKNSTLKQLEE 368
Cdd:COG4717    392 EQAEEYQELKEELEELeeqleellgeleellealdeEELEEELEELEEELEELEE----ELEELREELAELEAELEQLEE 467
                          410       420
                   ....*....|....*....|
gi 1622917383  369 klkgQADYEEVKKELNILKS 388
Cdd:COG4717    468 ----DGELAELLQELEELKA 483
COG5022 COG5022
Myosin heavy chain [General function prediction only];
43-361 3.47e-06

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 52.00  E-value: 3.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   43 TVLANRQDESEQSRKRLIE---QSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKrSKEAEAAFLnvyKRLIDVPDPV 117
Cdd:COG5022    868 TIYLQSAQRVELAERQLQElkiDVKSISslKLVNLELESEIIELKKSLSSDLIENLE-FKTELIARL---KKLLNNIDLE 943
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  118 PALDLGQQLQLKVQRLHdieTENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKN--------QAETIALEK 189
Cdd:COG5022    944 EGPSIEYVKLPELNKLH---EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAElskqygalQESTKQLKE 1020
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  190 EQK----LQND----FAEKERKLQETQMS---TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEmiM 258
Cdd:COG5022   1021 LPVevaeLQSAskiiSSESTELSILKPLQklkGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTIN--V 1098
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  259 TDLERANQRAEVAQREAETLREQLSSANHSLQ----LASQIQKAPDVEQAIEV-------LTRSSLEVELAAKEREIAqL 327
Cdd:COG5022   1099 KDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEiskfLSQLVNTLEPVFQKLSVlqleldgLFWEANLEALPSPPPFAA-L 1177
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1622917383  328 VEDVQRLQASLTKLRENSASQISQLEQQLSAKNS 361
Cdd:COG5022   1178 SEKRLYQSALYDEKSKLSSSEVNDLKNELIALFS 1211
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
33-338 4.28e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 4.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   33 GIKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPED---LRKQVAPL---LKSFQGEIDALSKRSKEAEAAFLNV 106
Cdd:TIGR02169  248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrVKEKIGELeaeIASLERSIAEKERELEDAEERLAKL 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  107 YKRLIDVPDPVPALDlGQQLQLKVQRlHDIETENQKLREtleEYNKEFAEVKNQEVTIKALKEKIREYEQtlknqaetiA 186
Cdd:TIGR02169  328 EAEIDKLLAEIEELE-REIEEERKRR-DKLTEEYAELKE---ELEDLRAELEEVDKEFAETRDELKDYRE---------K 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  187 LEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALektrtelfdlkTKYDEETTAKADEIEMIMTDLERANQ 266
Cdd:TIGR02169  394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI-----------NELEEEKEDKALEIKKQEWKLEQLAA 462
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383  267 RAEVAQREAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVLTRSSLEVELAAKER------EIAQLVEDVQRLQASL 338
Cdd:TIGR02169  463 DLSKYEQELYDLKEEYDRVEKELsKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvhgTVAQLGSVGERYATAI 541
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
225-371 5.11e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.67  E-value: 5.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  225 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLA-SQIQKAPD-VE 302
Cdd:COG4372      4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQArSELEQLEEeLE 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383  303 QAIEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQLEEKLK 371
Cdd:COG4372     84 ELNEQLQAAQAELaqaqeELESLQEEAEELQEELEELQKERQDLeqqRKQLEAQIAELQSEIAEREEELKELEEQLE 160
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
60-368 6.00e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.17  E-value: 6.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   60 IEQSREFKKntpEDLRKQvaplLKSFQGEIDALSKRSKEAEAAfLNVYKRLIDVpdpvpaLDLGQQLQLKVQRLHDIETE 139
Cdd:COG3206    162 LEQNLELRR---EEARKA----LEFLEEQLPELRKELEEAEAA-LEEFRQKNGL------VDLSEEAKLLLQQLSELESQ 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  140 NQKLRETLEEynkefaevknQEVTIKALKEKIREYEQTLKNQAETIALekeQKLQNDFAEKERKLQETQmsttSKLEEAE 219
Cdd:COG3206    228 LAEARAELAE----------AEARLAALRAQLGSGPDALPELLQSPVI---QQLRAQLAELEAELAELS----ARYTPNH 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  220 HKVQSLQTALEKTRTELfdlktkydeettakADEIEMIMTDLEranQRAEVAQREAETLREQLSsanhslQLASQIQKAP 299
Cdd:COG3206    291 PDVIALRAQIAALRAQL--------------QQEAQRILASLE---AELEALQAREASLQAQLA------QLEARLAELP 347
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383  300 dveqaievltrsslevelaAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLSAKNSTLKQLEE 368
Cdd:COG3206    348 -------------------ELEAELRRLEREVEVARELYESLLQ----RLEEARLAEALTVGNVRVIDP 393
PTZ00121 PTZ00121
MAEBL; Provisional
35-382 7.91e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 7.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   35 KRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvAPLLKSFQGE---IDALSKRSKEAEAAflNVYKRLI 111
Cdd:PTZ00121  1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK--ADELKKAAAAkkkADEAKKKAEEKKKA--DEAKKKA 1440
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  112 DVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLE--EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEK 189
Cdd:PTZ00121  1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  190 EQKLQN-DFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLE--RANQ 266
Cdd:PTZ00121  1521 AKKADEaKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKKAEeaRIEE 1596
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  267 RAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSslEVELAAKEREIAQLVEDVQRLQASLTKLRENSA 346
Cdd:PTZ00121  1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK--EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1622917383  347 SQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKE 382
Cdd:PTZ00121  1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
mukB PRK04863
chromosome partition protein MukB;
119-384 1.01e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  119 ALDLGQQLQLKVQRLHDIEtenqklrETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFA 198
Cdd:PRK04863   288 ALELRRELYTSRRQLAAEQ-------YRLVEMARELAELNEAESDLEQDYQAASDHLNLV--QTALRQQEKIERYQADLE 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  199 EKERKLQETQMST---TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERANQ--------- 266
Cdd:PRK04863   359 ELEERLEEQNEVVeeaDEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-RAIQYQQAVQALERAKQlcglpdlta 437
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  267 -----RAEVAQREAETLREQLSSANHSLQLASQIQKApdVEQAIEVLTRSSLEVelaakEREIAQlvedvQRLQASLTKL 341
Cdd:PRK04863   438 dnaedWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQ--FEQAYQLVRKIAGEV-----SRSEAW-----DVARELLRRL 505
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1622917383  342 RE--NSASQISQLEQQLSAknstlkqLEEKLKGQADYEEVKKELN 384
Cdd:PRK04863   506 REqrHLAEQLQQLRMRLSE-------LEQRLRQQQRAERLLAEFC 543
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
86-382 1.01e-05

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 50.21  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   86 QGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL-----DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ 160
Cdd:pfam10174  344 QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLageirDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKER 423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  161 evtIKALKEKIREYEQTLKNQAETIAlEKE---QKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELF 237
Cdd:pfam10174  424 ---VKSLQTDSSNTDTALTTLEEALS-EKEriiERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLI 499
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  238 DLKtkydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANhslQLASQIQKAPDVEQAIevltrSSLEVEL 317
Cdd:pfam10174  500 DLK----EHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH---NAEEAVRTNPEINDRI-----RLLEQEV 567
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383  318 AAKEREIAQLVEDVQRLQASLtKLRENSAS----QISQLE---------QQLSAKNSTLKQLEEKLKGQADYEEVKKE 382
Cdd:pfam10174  568 ARYKEESGKAQAEVERLLGIL-REVENEKNdkdkKIAELEsltlrqmkeQNKKVANIKHGQQEMKKKGAQLLEEARRR 644
PRK11281 PRK11281
mechanosensitive channel MscK;
80-385 1.21e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 50.30  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   80 PLLKSFQGEIDALSKRsKEAEAAFLNVYKRLIDvpdpvpALDLGQQLQlkvqrlhDIETENQKLRETLEEYNKEFAEVKN 159
Cdd:PRK11281    36 PTEADVQAQLDALNKQ-KLLEAEDKLVQQDLEQ------TLALLDKID-------RQKEETEQLKQQLAQAPAKLRQAQA 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  160 QevtIKALKEKIreyEQTLKNQAETIALEKeqkLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFdl 239
Cdd:PRK11281   102 E---LEALKDDN---DEETRETLSTLSLRQ---LESRLAQTLDQLQNAQ----NDLAEYNSQLVSLQTQPERAQAALY-- 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  240 ktkydeettakadeiemimtdlerANQraevaQREAEtLREQLSSANHSlqlasqiQKAPDVEQaievltRSSLEVELAA 319
Cdd:PRK11281   167 ------------------------ANS-----QRLQQ-IRNLLKGGKVG-------GKALRPSQ------RVLLQAEQAL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  320 KEREIA---QLVEDVQRLQASLTKLRENSASQISQLEQQL-------SAKNstLKQLEEKLKGQADYEE---------VK 380
Cdd:PRK11281   204 LNAQNDlqrKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLqllqeaiNSKR--LTLSEKTVQEAQSQDEaariqanplVA 281

                   ....*
gi 1622917383  381 KELNI 385
Cdd:PRK11281   282 QELEI 286
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
122-459 1.27e-05

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 49.82  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  122 LGQQLQLKVQRLHDIETENQKLRETLEEynKEfaevknqevtikALKEKIREYEQTLKNQAETIALEKEQkLQNDFAEKE 201
Cdd:pfam10174  329 LKESLTAKEQRAAILQTEVDALRLRLEE--KE------------SFLNKKTKQLQDLTEEKSTLAGEIRD-LKDMLDVKE 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  202 RK----------LQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLktkydEETTAKADE-IEMIMTDLERANQ--RA 268
Cdd:pfam10174  394 RKinvlqkkienLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTL-----EEALSEKERiIERLKEQREREDRerLE 468
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  269 EVAQ--REAETLREQLSSANhsLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIA--QLVEDVQRLQASLTKLREN 344
Cdd:pfam10174  469 ELESlkKENKDLKEKVSALQ--PELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAveQKKEECSKLENQLKKAHNA 546
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  345 S---------ASQISQLEQQLSAKNstlkqlEEKLKGQAdyeEVKKELNILKSMEfapsegagTQDAAKPLEVLLMEKNR 415
Cdd:pfam10174  547 EeavrtnpeiNDRIRLLEQEVARYK------EESGKAQA---EVERLLGILREVE--------NEKNDKDKKIAELESLT 609
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1622917383  416 SLQSENAALRISN-SDLSGSARRKGKDQ-PESRRPGSLPAPPPSQL 459
Cdd:pfam10174  610 LRQMKEQNKKVANiKHGQQEMKKKGAQLlEEARRREDNLADNSQQL 655
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
67-374 1.38e-05

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 49.84  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   67 KKNTPEDLRKQVAPLLkSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQ-------LQLKVQRLH----- 134
Cdd:pfam12128  191 KEGKFRDVKSMIVAIL-EDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQefntlesAELRLSHLHfgyks 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  135 ---DIETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKNQAETIALEKEQ---------KLQNDFAEKER 202
Cdd:pfam12128  270 detLIASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealedqhgAFLDADIETAA 343
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  203 KLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----RANQRAE---VAQRE 274
Cdd:pfam12128  344 ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaRDRQLAVaedDLQAL 420
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  275 AETLREQLSSANHSL-----QLAS-------QIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQL-VEDVQRLQASLTKL 341
Cdd:pfam12128  421 ESELREQLEAGKLEFneeeyRLKSrlgelklRLNQATATPELLLQLENFDERIERAREEQEAANAeVERLQSELRQARKR 500
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1622917383  342 RENSASQISQLEQQLSAKNSTLKQLEEKLKGQA 374
Cdd:pfam12128  501 RDQASEALRQASRRLEERQSALDELELQLFPQA 533
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
47-282 1.54e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   47 NRQDESEQSRKRLIEQSREFKKNTpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPalDLGQQL 126
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEA-EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE--SLERRI 833
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  127 QLKVQRLHDIETENQKLRETLEEYNKEFAE-VKNQEVTIKALKEKIREYEQtlKNQAETIALEKEQKLQNDFAEKERKLQ 205
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLAAEIEElEELIEELESELEALLNERAS--LEEALALLRSELEELSEELRELESKRS 911
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383  206 ETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLERANQRAEVAQREAETLREQL 282
Cdd:TIGR02168  912 ELR----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
PTZ00121 PTZ00121
MAEBL; Provisional
34-423 2.03e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 2.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   34 IKRELDATATVLANRQDESEQSRKRLIEQSREFK-KNTPEDLRKQVApllksfQGEIDALSKRSKEAEAAfLNVYKRLID 112
Cdd:PTZ00121  1254 IRKFEEARMAHFARRQAAIKAEEARKADELKKAEeKKKADEAKKAEE------KKKADEAKKKAEEAKKA-DEAKKKAEE 1326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  113 VPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKA--LKEKIREYEQT---------LKNQ 181
Cdd:PTZ00121  1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAdaAKKKAEEKKKAdeakkkaeeDKKK 1406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  182 AETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTElfDLKTKYDEETtaKADEIEMIMTDL 261
Cdd:PTZ00121  1407 ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE--EAKKKAEEAK--KADEAKKKAEEA 1482
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  262 ERANQ---RAEVAQREAETLREQLSSANHSLQL--------------------ASQIQKAPDVEQAIEVltRSSLEVELA 318
Cdd:PTZ00121  1483 KKADEakkKAEEAKKKADEAKKAAEAKKKADEAkkaeeakkadeakkaeeakkADEAKKAEEKKKADEL--KKAEELKKA 1560
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  319 AKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQAD----YEEVKKELNILKSMEFAPS 394
Cdd:PTZ00121  1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikAEELKKAEEEKKKVEQLKK 1640
                          410       420
                   ....*....|....*....|....*....
gi 1622917383  395 EGAgtQDAAKPLEVLLMEKNRSLQSENAA 423
Cdd:PTZ00121  1641 KEA--EEKKKAEELKKAEEENKIKAAEEA 1667
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
45-251 2.40e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 2.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   45 LANRQDESEQSRKRLieqsREFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL 120
Cdd:COG3206    184 LPELRKELEEAEAAL----EEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  121 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAET---IALEKEQKLQNDF 197
Cdd:COG3206    260 LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEAeleALQAREASLQAQL 336
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622917383  198 AEKERKLQETQmSTTSKLEEAEHKVQSLQTALEktrtelfDLKTKYDEETTAKA 251
Cdd:COG3206    337 AQLEARLAELP-ELEAELRRLEREVEVARELYE-------SLLQRLEEARLAEA 382
PTZ00121 PTZ00121
MAEBL; Provisional
35-260 2.45e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 2.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   35 KRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaaflnvykrlidvP 114
Cdd:PTZ00121  1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-------------E 1658
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  115 DPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKnqAETIALEKEQKLQ 194
Cdd:PTZ00121  1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEEAK 1736
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383  195 NDFAEKERKLQETQmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 260
Cdd:PTZ00121  1737 KEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
35-387 2.55e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 2.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   35 KRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVP 114
Cdd:COG1196    428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  115 DPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEynkefaevknqeVTIKALKEKIREYEQTLknqAETIALEKEQKLQ 194
Cdd:COG1196    508 EGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA------------ALAAALQNIVVEDDEVA---AAAIEYLKAAKAG 572
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  195 NDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQRE 274
Cdd:COG1196    573 RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  275 AETLREQLSSANHS-------LQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS 347
Cdd:COG1196    653 GEGGSAGGSLTGGSrrellaaLLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1622917383  348 QISQ-LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILK 387
Cdd:COG1196    733 EREElLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
133-392 2.63e-05

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 49.05  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  133 LHDIETENQKLRET----LEEYNKEFAEVKNQEVTIKALKEKIREYEQTL-KNQAETIALE-KEQKLQNDFAEKERKLQE 206
Cdd:pfam10174  249 IRDLEDEVQMLKTNgllhTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELsKKESELLALQtKLETLTNQNSDCKQHIEV 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  207 TQMSTTSKLEEA---EHKVQSLQTALEKTRTeLFDLKTKY----DEETTAKADEIEMIMTDLERANQRAEVAQREAETLR 279
Cdd:pfam10174  329 LKESLTAKEQRAailQTEVDALRLRLEEKES-FLNKKTKQlqdlTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  280 EQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ-------ASLTKLRENSASQISQL 352
Cdd:pfam10174  408 EQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDrerleelESLKKENKDLKEKVSAL 487
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622917383  353 EQQLSAKNSTLKQLEEKLKGQADyEEVKKElNILKSMEFA 392
Cdd:pfam10174  488 QPELTEKESSLIDLKEHASSLAS-SGLKKD-SKLKSLEIA 525
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
124-378 2.73e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.02  E-value: 2.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  124 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVknqevtikaLKEKIREYEQTlknQAETIALEKEQKLQNDFAEKERK 203
Cdd:pfam01576    5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQL---------CEEKNALQEQL---QAETELCAEAEEMRARLAARKQE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  204 LQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEE-------------TTAKADEIEMIMTDLERANQRaev 270
Cdd:pfam01576   73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLEDQNSK--- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  271 AQREAETLREQLSsaNHSLQLASQIQKA--------------PDVEQAI--EVLTRSSLEVELAAKEREIAQLVEDVQRL 334
Cdd:pfam01576  150 LSKERKLLEERIS--EFTSNLAEEEEKAkslsklknkheamiSDLEERLkkEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622917383  335 QASLTKLR-------ENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEE 378
Cdd:pfam01576  228 QAQIAELRaqlakkeEELQAALARLEEETAQKNNALKKIRELEAQISELQE 278
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
140-367 2.97e-05

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: 48.59  E-value: 2.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  140 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 218
Cdd:pfam07111   58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  219 EHK-VQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQ--- 290
Cdd:pfam07111  138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELEaqv 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  291 -LASQIQKAPDvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAS--LTKLRENSASQISQL-EQQLSAKNSTLKQL 366
Cdd:pfam07111  218 tLVESLRKYVG-EQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATveLLQVRVQSLTHMLALqEEELTRKIQPSDSL 296

                   .
gi 1622917383  367 E 367
Cdd:pfam07111  297 E 297
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
136-444 3.17e-05

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: 48.58  E-value: 3.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  136 IETENQKLRETLEeYNKEFAEVKNQEVTIKalkekiREYEQTL-KNQAETIALEKEQKLQndfAEKERKLQETqmsttsk 214
Cdd:pfam05557   12 SQLQNEKKQMELE-HKRARIELEKKASALK------RQLDRESdRNQELQKRIRLLEKRE---AEAEEALREQ------- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  215 LEEAEHKVQSLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQL----------SS 284
Cdd:pfam05557   75 AELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLdllkakaseaEQ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  285 ANHSLQ-----LASQIQKAPDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASqISQLEQQLSA 358
Cdd:pfam05557  154 LRQNLEkqqssLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELArIPELEKELERLREHNKHLNENIEN-KLLLKEEVED 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  359 KNSTLKQlEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPleVLLMEKNRSLQSENAALRISNSDLSGSARRK 438
Cdd:pfam05557  233 LKRKLER-EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSP--EDLSRRIEQLQQREIVLKEENSSLTSSARQL 309

                   ....*.
gi 1622917383  439 GKDQPE 444
Cdd:pfam05557  310 EKARRE 315
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
1270-1355 3.77e-05

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 45.51  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRRelfieeiqagsQGQAGASDSPSA 1349
Cdd:COG5576     52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKK-----------KRSGKVEQRPGE 120

                   ....*.
gi 1622917383 1350 RSGRAA 1355
Cdd:COG5576    121 EEADLA 126
PTZ00121 PTZ00121
MAEBL; Provisional
135-447 4.02e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 4.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  135 DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQT-LKNQAETIALEKEQKLqndfAEKERKLQETQMSTTS 213
Cdd:PTZ00121  1040 DVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDaKEDNRADEATEEAFGK----AEEAKKTETGKAEEAR 1115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  214 KLEEAEHKVQSLQTALEKTRTElfDLKtKYDEETTAKADEIEMIMTDLERAnQRAEVAQReaetlreqlssanhslqlAS 293
Cdd:PTZ00121  1116 KAEEAKKKAEDARKAEEARKAE--DAR-KAEEARKAEDAKRVEIARKAEDA-RKAEEARK------------------AE 1173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  294 QIQKAPDVEQAIEVltRSSLEVELAAKEREI--AQLVEDVQRLQASLTKLRENSASQISQLEQqlsaknsTLKQLEEKLK 371
Cdd:PTZ00121  1174 DAKKAEAARKAEEV--RKAEELRKAEDARKAeaARKAEEERKAEEARKAEDAKKAEAVKKAEE-------AKKDAEEAKK 1244
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383  372 GqadyEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSGSARRKGKDQPESRR 447
Cdd:PTZ00121  1245 A----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
mukB PRK04863
chromosome partition protein MukB;
86-372 4.08e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 48.41  E-value: 4.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   86 QGEIDALSKRSKEAEAAFLNVYKRLIDVpdpVPALDLGQ----QLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQE 161
Cdd:PRK04863   375 DEQQEENEARAEAAEEEVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE 451
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  162 vtiKALKEKIREYEQTLkNQAETIALEKEQKLQ-----NDFAEKERKlQETQMSTTSKLEEAEHKVQSLQTAlektRTEL 236
Cdd:PRK04863   452 ---QEATEELLSLEQKL-SVAQAAHSQFEQAYQlvrkiAGEVSRSEA-WDVARELLRRLREQRHLAEQLQQL----RMRL 522
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  237 FDLKTKYDEETTAKA-------------DEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQK----A 298
Cdd:PRK04863   523 SELEQRLRQQQRAERllaefckrlgknlDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLeQLQARIQRlaarA 602
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  299 PDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLS-------AKNSTLKQLEEKL 370
Cdd:PRK04863   603 PAWLAAQDALARLREQSGEEFEDSQdVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggSEDPRLNALAERF 682

                   ..
gi 1622917383  371 KG 372
Cdd:PRK04863   683 GG 684
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
122-371 5.22e-05

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 47.38  E-value: 5.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  122 LGQQLQLkvqrLHDIETENQKLRETLEEYNKEfaevknqevTIKALKEKIREYEQTLKNQAETIAL------EKEQKLQN 195
Cdd:pfam04108   40 LSVQLAN----LEKVREGLEKVLNELKKDFKQ---------LLKDLDAALERLEETLDKLRNTPVEpalppgEEKQKTLL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  196 DFAEkERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEvaqrEA 275
Cdd:pfam04108  107 DFID-EDSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQ-KELESLSSPSESISLIPTLLKELESLEE----EM 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  276 ETLREQLssANHsLQLASQIQKAPDVEQA--IEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKLRENSAS- 347
Cdd:pfam04108  181 ASLLESL--TNH-YDQCVTAVKLTEGGRAemLEVLENDARELddvvpELQDRLDEMENNYERLQKLLEQKNSLIDELLSa 257
                          250       260
                   ....*....|....*....|....*.
gi 1622917383  348 --QISQLEQQLSAKNSTLKQLEEKLK 371
Cdd:pfam04108  258 lqLIAEIQSRLPEYLAALKEFEERWE 283
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
132-241 6.08e-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: 46.93  E-value: 6.08e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   132 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAET---IALEKEQKLQNDFA---EKERKLQ 205
Cdd:smart00787  138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 1622917383   206 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKT 241
Cdd:smart00787  218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
144-424 6.48e-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: 47.73  E-value: 6.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  144 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKnqaetiALEK-EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKV 222
Cdd:TIGR00606  237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK------ALKSrKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  223 QSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQ---------REAETLREQLSSANHSLQLAS 293
Cdd:TIGR00606  311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQehirardslIQSLATRLELDGFERGPFSER 390
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  294 QIQKAPDVE---QAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKL 370
Cdd:TIGR00606  391 QIKNFHTLVierQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSS 470
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383  371 KG--QADYEEVKKELNILKSMEFAPSEGAGTQDAA-KPLEVLLMEKNRSLQSENAAL 424
Cdd:TIGR00606  471 DRilELDQELRKAERELSKAEKNSLTETLKKEVKSlQNEKADLDRKLRKLDQEMEQL 527
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
124-388 7.47e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 7.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  124 QQLQLKVQRL-HDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIReyeqTLKNQaETIALEKEQKLQND--FAEK 200
Cdd:TIGR04523   36 KQLEKKLKTIkNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIK----DLNDK-LKKNKDKINKLNSDlsKINS 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  201 ERKLQETQMSTT----SKLEEAEHKVQSLQ----TALEKTRTELFDLKTKYDEETTakadEIEMIMTDLERANQRAEVAQ 272
Cdd:TIGR04523  111 EIKNDKEQKNKLevelNKLEKQKKENKKNIdkflTEIKKKEKELEKLNNKYNDLKK----QKEELENELNLLEKEKLNIQ 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  273 REAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVL--TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQI 349
Cdd:TIGR04523  187 KNIDKIKNKLLKLELLLsNLKKKIQKNKSLESQISELkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1622917383  350 SQLE---QQLSAKNSTLKQLEEKLKgqadyeEVKKELNILKS 388
Cdd:TIGR04523  267 KQLSekqKELEQNNKKIKELEKQLN------QLKSEISDLNN 302
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
123-369 8.17e-05

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 47.64  E-value: 8.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  123 GQQLQLKVQRLH-DIETENQKLRE---TLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKNQaETIALEKEQKLQ 194
Cdd:COG3096    342 ALRQQEKIERYQeDLEELTERLEEqeeVVEEAAEQLAEAEARleaaEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQAVQ 420
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  195 NdFAEKERKLQETQMSttskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKA--DE----IEMIMTDLER--ANQ 266
Cdd:COG3096    421 A-LEKARALCGLPDLT----PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKayelVCKIAGEVERsqAWQ 495
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  267 RAE-----------VAQReAETLREQLSSANhslQLASQIQKApdVEQAIEVLTRSSLEVELAAK-EREIAQLVEDVQRL 334
Cdd:COG3096    496 TARellrryrsqqaLAQR-LQQLRAQLAELE---QRLRQQQNA--ERLLEEFCQRIGQQLDAAEElEELLAELEAQLEEL 569
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1622917383  335 QASLTKLREnsasQISQLEQQLSAKNSTLKQLEEK 369
Cdd:COG3096    570 EEQAAEAVE----QRSELRQQLEQLRARIKELAAR 600
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
74-280 8.99e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 8.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   74 LRKQVAPLLKSFQgEIDALSKRSKEAEAAFLNVYKR--LIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLR------- 144
Cdd:COG4717    293 LAREKASLGKEAE-ELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqe 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  145 --ETLEEYN----KEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIaleKEQKLQNDFAEKERKLQETQMsttsKLEEA 218
Cdd:COG4717    372 iaALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGEL---EELLEALDEEELEEELEELEE----ELEEL 444
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622917383  219 EHKVQSLQTALEKTRTELFDLKTkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE 280
Cdd:COG4717    445 EEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
PRK01156 PRK01156
chromosome segregation protein; Provisional
68-387 9.05e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.20  E-value: 9.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   68 KNTPEDLRKQVAPL------LKSFQGEIDALSK--------------RSKEAEAAFLNVYKRLIDVPDPVPAL----DLG 123
Cdd:PRK01156   172 KDVIDMLRAEISNIdyleekLKSSNLELENIKKqiaddekshsitlkEIERLSIEYNNAMDDYNNLKSALNELssleDMK 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  124 QQLQLKVQ----RLHDIETENQKLRETLEEYNK--EFAEVKNQEVTIKALKEK--IREYEQTLKNQAETIA--------L 187
Cdd:PRK01156   252 NRYESEIKtaesDLSMELEKNNYYKELEERHMKiiNDPVYKNRNYINDYFKYKndIENKKQILSNIDAEINkyhaiikkL 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  188 EKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKVQSLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQR 267
Cdd:PRK01156   332 SVLQKDYNDYIKKKSRYDDLN-NQILELEGYEMDYNSYLKSIES-------LKKKIEEYSKNIERMSAFISEILKIQEID 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  268 AEVAQREAETLR---EQLSSANHSLQ--LASQIQKAPDVEQAIEVLT---------------------------RSSLEV 315
Cdd:PRK01156   404 PDAIKKELNEINvklQDISSKVSSLNqrIRALRENLDELSRNMEMLNgqsvcpvcgttlgeeksnhiinhynekKSRLEE 483
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383  316 ELAAKEREIAQLVEDVQRLQASLTKLR-------ENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKELNILK 387
Cdd:PRK01156   484 KIREIEIEVKDIDEKIVDLKKRKEYLEseeinksINEYNKIESARADLEDIKIKINELKDK---HDKYEEIKNRYKSLK 559
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
9-291 9.15e-05

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 47.06  E-value: 9.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383    9 APQTPVESPTASSKLPQAHWLCSPGIKRELDATATVLANRQDESeqsrkrLIEQSREFKKNTPEDLRKQVAPLLKSFQGE 88
Cdd:pfam09731  200 NLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAK------LVDQYKELVASERIVFQQELVSIFPDIIPV 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   89 IDALSKRSKEAEAAFLNVYKRLIDVpdpvpaldLGQQLQ-LKVQRLHDIETENQKLRETL----EEYNKEFAEVKNQE-- 161
Cdd:pfam09731  274 LKEDNLLSNDDLNSLIAHAHREIDQ--------LSKKLAeLKKREEKHIERALEKQKEELdklaEELSARLEEVRAADea 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  162 ---VTIKALKEKIRE-YEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMsttskleeaehkvQSLQTALEKTRtelf 237
Cdd:pfam09731  346 qlrLEFEREREEIREsYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-------------QDIKEKVEEER---- 408
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383  238 DLKTKYDEETTAKADEIEMIMT---DLERANQRAEVAQREAETLREQLSSANHSLQL 291
Cdd:pfam09731  409 AGRLLKLNELLANLKGLEKATSshsEVEDENRKAQQLWLAVEALRSTLEDGSADSRP 465
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
132-424 9.44e-05

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: 47.42  E-value: 9.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  132 RLHDIETENQKLRETLEEYNKEFAE--VKNQEVTIKALKEKI---REYEQTLKNQAETIalEKEQKLQND-FAEKERKLQ 205
Cdd:pfam15921  246 QLEALKSESQNKIELLLQQHQDRIEqlISEHEVEITGLTEKAssaRSQANSIQSQLEII--QEQARNQNSmYMRQLSDLE 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  206 ETQMSTTSKLEEA----EHKVQSLQTALEKTRTELFDLKTKYDE---ETTAKADEIEMIMTDLERANQRAEVAQREAETL 278
Cdd:pfam15921  324 STVSQLRSELREAkrmyEDKIEELEKQLVLANSELTEARTERDQfsqESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  279 REQlssanhslqlasqiqkapDVEQAIevlTRSSLEVELAAKEREiaqlvedVQRLQASLTKLRENSAsqiSQLEQQLSA 358
Cdd:pfam15921  404 WDR------------------DTGNSI---TIDHLRRELDDRNME-------VQRLEALLKAMKSECQ---GQMERQMAA 452
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383  359 KNSTLKQLEEKLKGQADYEEVKKEL-NILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAAL 424
Cdd:pfam15921  453 IQGKNESLEKVSSLTAQLESTKEMLrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI 519
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
29-419 1.06e-04

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 46.61  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   29 LCSPGIKRELDATatvlanRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLlksfQGEIDALSKRSKEAEAaflnvYK 108
Cdd:pfam05622   53 SGTPGGKKYLLLQ------KQLEQLQEENFRLETARDDYRIKCEELEKEVLEL----QHRNEELTSLAEEAQA-----LK 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  109 RLIDVpdpvpaldlgqqLQLKVQRLHDIETENQKLRETLEEYNkefaEVKNQevtIKALKEKIREYEQtlknqaETIALE 188
Cdd:pfam05622  118 DEMDI------------LRESSDKVKKLEATVETYKKKLEDLG----DLRRQ---VKLLEERNAEYMQ------RTLQLE 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  189 KEQK----LQNDFAEKERKLQETQ------MSTTSKLE----EAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEI 254
Cdd:pfam05622  173 EELKkanaLRGQLETYKRQVQELHgklseeSKKADKLEfeykKLEEKLEALQKEKERLIIERDTLRETNEELRCAQLQQA 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  255 EMIMTD----------------------------LERANQRAEVAQREAE-----TLREQLSSANHSL-----QLASQIQ 296
Cdd:pfam05622  253 ELSQADallspssdpgdnlaaeimpaeireklirLQHENKMLRLGQEGSYrerltELQQLLEDANRRKneletQNRLANQ 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  297 KAPDVEQAIEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKLRE-----------NSASQISQLEQQLSAKN 360
Cdd:pfam05622  333 RILELQQQVEELQKALQEQgskaeDSSLLKQKLEEHLEKLHEAQSELQKKKEqieelepkqdsNLAQKIDELQEALRKKD 412
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383  361 STLKQLEEKLKgqadyEEVKKELNILKSMEfaPSEGAGTQDAAKPLEVLLMEKNRSLQS 419
Cdd:pfam05622  413 EDMKAMEERYK-----KYVEKAKSVIKTLD--PKQNPASPPEIQALKNQLLEKDKKIEH 464
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
121-390 1.25e-04

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: 47.04  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  121 DLGQQLQ---------------------LKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK 179
Cdd:pfam15921  500 DLTASLQekeraieatnaeitklrsrvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG 579
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  180 NQAET---IALEKEQkLQNDFAEKERKLQETQM---STTSKLEEAEHKVQSLQtaLEKTR-----TELFDLKTKYDEETT 248
Cdd:pfam15921  580 QHGRTagaMQVEKAQ-LEKEINDRRLELQEFKIlkdKKDAKIRELEARVSDLE--LEKVKlvnagSERLRAVKDIKQERD 656
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  249 AKADEIEMIMTDLERANQRAEVAQR-------EAET----LREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVEL 317
Cdd:pfam15921  657 QLLNEVKTSRNELNSLSEDYEVLKRnfrnkseEMETttnkLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQI 736
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622917383  318 AAKEREIAQLVEDVQRLQASLTKLRENSASqISQLEQQLSAKNSTLKQLEEKLKGqadyeevkkELNILKSME 390
Cdd:pfam15921  737 TAKRGQIDALQSKIQFLEEAMTNANKEKHF-LKEEKNKLSQELSTVATEKNKMAG---------ELEVLRSQE 799
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
235-387 1.30e-04

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 46.39  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  235 ELFD-LKTKYDEETTAKADEIEMIMTDLERANQRAEV--AQREAETLREQLSSANHSLQlasQIQKapDVEQAIEVLTRS 311
Cdd:pfam06160   45 EKFEeWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFkkAKKALDEIEELLDDIEEDIK---QILE--ELDELLESEEKN 119
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383  312 SLEVElaakereiaQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEkLKGQADYEEVKKELNILK 387
Cdd:pfam06160  120 REEVE---------ELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEAREVLEKLE 185
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
213-483 1.36e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  213 SKLEEAEHKVQSLQTALEKTRTELFDLktkydeettakADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL--- 289
Cdd:COG3883     16 PQIQAKQKELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeer 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  290 -----QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLK 364
Cdd:COG3883     85 reelgERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  365 QLEEKLKG-QADYEEVKKELNILKsmefapSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSGSARRKGKDQP 443
Cdd:COG3883    165 ELEAAKAElEAQQAEQEALLAQLS------AEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622917383  444 ESRRPGSLPAPPPSQLPRNPGEQASNTNGTHQFSPAGLSQ 483
Cdd:COG3883    239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAA 278
PHA03247 PHA03247
large tegument protein UL36; Provisional
772-958 1.41e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  772 STSPMPTVSSYPPLAISLKKPSAAPEAG--ASALPNPPALKKEAQDAPGLDPQGAADCAQGVLR--QVKNEVGRSGAWkd 847
Cdd:PHA03247   269 PETARGATGPPPPPEAAAPNGAAAPPDGvwGAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGamEVVSPLPRPRQH-- 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  848 hwWSAVQPERRNAASSEEAKAEETGGgkekgsggsgggsqprAERSQLQGPSSSEYWKEWPSAESPYSQSSELSLTGASR 927
Cdd:PHA03247   347 --YPLGFPKRRRPTWTPPSSLEDLSA----------------GRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTRPA 408
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1622917383  928 SETPQNSPLPSSPIVPMSKPTKPSVPPLTPE 958
Cdd:PHA03247   409 APVPASVPTPAPTPVPASAPPPPATPLPSAE 439
PTZ00121 PTZ00121
MAEBL; Provisional
139-404 1.68e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  139 ENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIRE----YEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 214
Cdd:PTZ00121  1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  215 LEEAEHKVQSLQtalektrtelfdlktKYDEETTAKADEIEmimTDLERANQRAEVAQREAEtlrEQLSSANHSLQLASQ 294
Cdd:PTZ00121  1642 EAEEKKKAEELK---------------KAEEENKIKAAEEA---KKAEEDKKKAEEAKKAEE---DEKKAAEALKKEAEE 1700
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  295 IQKAPDVEQAIEVLTRSSLEVELAAKEREI----AQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTL-KQLEEK 369
Cdd:PTZ00121  1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIkaeeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIrKEKEAV 1780
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1622917383  370 LKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAK 404
Cdd:PTZ00121  1781 IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
133-390 1.84e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  133 LHDIETENQKLRETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKNQAETIALEKEQKlqndfAEKERKLQEtqmstt 212
Cdd:PRK03918   141 LESDESREKVVRQILGLDDYENAYKNLGEV-IKEIKRRIERLEKFIKRTENIEELIKEKE-----KELEEVLRE------ 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  213 skLEEAEHKVQSLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLA 292
Cdd:PRK03918   209 --INEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE------ELE 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  293 SQIQKAPDVEQ-AIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKlrensasQISQLEQQLSAKNSTLKQLEEKLK 371
Cdd:PRK03918   280 EKVKELKELKEkAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEELKKKLKELEK 352
                          250
                   ....*....|....*....
gi 1622917383  372 GQADYEEVKKELNILKSME 390
Cdd:PRK03918   353 RLEELEERHELYEEAKAKK 371
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
63-382 1.85e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 46.12  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   63 SREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDpvpALDLGQQLQLKVQRLHDIETENQK 142
Cdd:TIGR00618  183 LMEFAKK--KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE---ALQQTQQSHAYLTQKREAQEEQLK 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  143 LRETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKNQAETIALEKEQKLQNDFaEKERKLQETQmSTTSKLEEAEHKV 222
Cdd:TIGR00618  258 KQQLLKQLRARIEELRAQEAVLEETQERI-----NRARKAAPLAAHIKAVTQIEQ-QAQRIHTELQ-SKMRSRAKLLMKR 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  223 QSLQtalektrTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAE-----TLREQLSSANHSLQLASQIQK 297
Cdd:TIGR00618  331 AAHV-------KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihTLQQQKTTLTQKLQSLCKELD 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  298 APDVEQA---IEVLTRSSLEVELAAKEREI-AQLVEDVQRLQASLTKLRENSASQISQLE--QQLSAKNSTLKQLEEKLK 371
Cdd:TIGR00618  404 ILQREQAtidTRTSAFRDLQGQLAHAKKQQeLQQRYAELCAAAITCTAQCEKLEKIHLQEsaQSLKEREQQLQTKEQIHL 483
                          330
                   ....*....|.
gi 1622917383  372 gqaDYEEVKKE 382
Cdd:TIGR00618  484 ---QETRKKAV 491
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
136-390 2.25e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.88  E-value: 2.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  136 IETENQKLRETLEEYNKEFAEVKNQEVTIKAlkEKIRE-----YEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMS 210
Cdd:pfam17380  344 MERERELERIRQEERKRELERIRQEEIAMEI--SRMRElerlqMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  211 TTSKLEEAEHKVQSLQTALEKTRtelfdlktkydeettakADEIEMI-MTDLERANQRAEVAQREAETLREQLssanhsl 289
Cdd:pfam17380  422 MEQIRAEQEEARQREVRRLEEER-----------------AREMERVrLEEQERQQQVERLRQQEEERKRKKL------- 477
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  290 qlasQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQlvedVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQ--LE 367
Cdd:pfam17380  478 ----ELEKEKRDRKRAEEQRRKILEKELEERKQAMIE----EERKRKLLEKEMEERQKAIYEEERRREAEEERRKQqeME 549
                          250       260
                   ....*....|....*....|...
gi 1622917383  368 EKLKGQADYEEVKKELNILKSME 390
Cdd:pfam17380  550 ERRRIQEQMRKATEERSRLEAME 572
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
35-408 2.85e-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: 45.50  E-value: 2.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   35 KRELDATATVLANRQDESEQSRKRLIEQSREFKK---------NTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAF-- 103
Cdd:pfam05557   50 NQELQKRIRLLEKREAEAEEALREQAELNRLKKKylealnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELqs 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  104 ----LNVYKRLIDVPDP--VPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKN--QEV----TIKALKEKI 171
Cdd:pfam05557  130 tnseLEELQERLDLLKAkaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNskSELaripELEKELERL 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  172 REYEQTLKNQAETIALEKEQKlqndfAEKERKLqetqmsttSKLEEAEHKVQSLQTALEKTRTELfdlktkYDEETTAKA 251
Cdd:pfam05557  210 REHNKHLNENIENKLLLKEEV-----EDLKRKL--------EREEKYREEAATLELEKEKLEQEL------QSWVKLAQD 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  252 DEIEMIMTDLERAnqRAEVAQREAETLREQLSSANHSlqlASQIQKA-PDVEQAIEVLTRSSLEVELAAKEREiaQLVED 330
Cdd:pfam05557  271 TGLNLRSPEDLSR--RIEQLQQREIVLKEENSSLTSS---ARQLEKArRELEQELAQYLKKIEDLNKKLKRHK--ALVRR 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  331 VQRLQASLTKLRENSASQISQLEQQLSAKNSTlKQLEEKLKGQADY-EEVKKELNILK-SMEFAPSEGAGTQDAAKPLEV 408
Cdd:pfam05557  344 LQRRVLLLTKERDGYRAILESYDKELTMSNYS-PQLLERIEEAEDMtQKMQAHNEEMEaQLSVAEEELGGYKQQAQTLER 422
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
124-432 3.89e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 3.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  124 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAEtiALEKEQKLQNDFAEKERK 203
Cdd:COG4372     31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEE---LEQARSELEQLEEELEELNE--QLQAAQAELAQAQEELES 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  204 LQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 283
Cdd:COG4372    106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI-AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  284 SANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTL 363
Cdd:COG4372    185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383  364 KQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLS 432
Cdd:COG4372    265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
37-387 4.33e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 45.04  E-value: 4.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   37 ELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvaplLKSFQGEidalSKRSKEAEAA-------FLNVYKR 109
Cdd:TIGR00606  266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLND-----LYHNHQR----TVREKERELVdcqreleKLNKERR 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  110 LIDVPDPVPALDLGqQLQLKVQRLH------DIETENQKLRETLEEYNKEF---AEVKN-QEVTIKALKEKIREYEQTLK 179
Cdd:TIGR00606  337 LLNQEKTELLVEQG-RLQLQADRHQehirarDSLIQSLATRLELDGFERGPfseRQIKNfHTLVIERQEDEAKTAAQLCA 415
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  180 NQAETIALEKEQ--KLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQT-------------ALEKTRTELFDL----- 239
Cdd:TIGR00606  416 DLQSKERLKQEQadEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegssdrileldqELRKAERELSKAeknsl 495
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  240 -KTKYDEETTAKADEIEMIMTdLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPD------VEQAIEVLTRSS 312
Cdd:TIGR00606  496 tETLKKEVKSLQNEKADLDRK-LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSrhsdelTSLLGYFPNKKQ 574
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622917383  313 LEVELAAKEREIAQLVEDVQRLQASLTKLRENSasqiSQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILK 387
Cdd:TIGR00606  575 LEDWLHSKSKEINQTRDRLAKLNKELASLEQNK----NHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK 645
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
136-367 4.44e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.17  E-value: 4.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  136 IETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKNQAET-------------IALEKEQKLQNDFA 198
Cdd:pfam01576  690 LEQQVEEMKTQLEELEDELQATEDAklrlEVNMQALKAQFERDLQARDEQGEEkrrqlvkqvreleAELEDERKQRAQAV 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  199 EKERKLQ------ETQMSTTSK-LEEAEHKVQSLQTALEKTRTELFDLKTKYDE------ETTAKADEIEMIMTDLERAN 265
Cdd:pfam01576  770 AAKKKLEldlkelEAQIDAANKgREEAVKQLKKLQAQMKDLQRELEEARASRDEilaqskESEKKLKNLEAELLQLQEDL 849
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  266 QRAEVAQREAETLREQLSSanhslQLASQIQKapdveqaievltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE-- 343
Cdd:pfam01576  850 AASERARRQAQQERDELAD-----EIASGASG------------KSALQDEKRRLEARIAQLEEELEEEQSNTELLNDrl 912
                          250       260
                   ....*....|....*....|....*
gi 1622917383  344 -NSASQISQLEQQLSAKNSTLKQLE 367
Cdd:pfam01576  913 rKSTLQVEQLTTELAAERSTSQKSE 937
PRK12678 PRK12678
transcription termination factor Rho; Provisional
1330-1422 4.62e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.89  E-value: 4.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 1330 IEEIQAGSQGQAGASDSPSARSGRAAPSSEGDSCDGVEATEGPGSADTEEP-----KSQGEAEREEAPRPAEQTEPPPSG 1404
Cdd:PRK12678    55 IKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAApaaraAAAAAAEAASAPEAAQARERRERG 134
                           90
                   ....*....|....*...
gi 1622917383 1405 TPGPDDARDDDHEGGPAE 1422
Cdd:PRK12678   135 EAARRGAARKAGEGGEQP 152
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
82-284 4.92e-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: 43.48  E-value: 4.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   82 LKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAE----V 157
Cdd:pfam00261    3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALN--RRIQLLEEELERTEERLAEALEKLEEAEKAADEsergR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  158 KNQEVTIKALKEKIREYEQTLKnQAETIALEKEQKLqndfAEKERKLQETQMS---TTSKLEEAEHKVQSLQTALEKTRT 234
Cdd:pfam00261   81 KVLENRALKDEEKMEILEAQLK-EAKEIAEEADRKY----EEVARKLVVVEGDlerAEERAELAESKIVELEEELKVVGN 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622917383  235 ELFDLKT---KYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 284
Cdd:pfam00261  156 NLKSLEAseeKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDR 208
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
42-368 6.03e-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: 44.12  E-value: 6.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   42 ATVLANRQDESEQSRKRLIeQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpald 121
Cdd:pfam07888   29 AELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL-------- 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  122 lgQQLQLKVQRLHDIETENQklRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIalEKEQKLQNDFAEKE 201
Cdd:pfam07888  100 --EEKYKELSASSEELSEEK--DALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERA--KKAGAQRKEEEAER 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  202 RKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK----TKYDEETTA--KADEIEMIMTDLERANQRAEVAQREA 275
Cdd:pfam07888  174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtitTLTQKLTTAhrKEAENEALLEELRSLQERLNASERKV 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  276 ETLREQLSS-------------------ANHSLQLAsQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQA 336
Cdd:pfam07888  254 EGLGEELSSmaaqrdrtqaelhqarlqaAQLTLQLA-DASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1622917383  337 SLTKLRensaSQISQLEQQLS-AKNSTLKQLEE 368
Cdd:pfam07888  333 RLQEER----MEREKLEVELGrEKDCNRVQLSE 361
Filament pfam00038
Intermediate filament protein;
121-370 7.35e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 43.37  E-value: 7.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  121 DLGQQLQLKVQRLHDI-ETENQKLRETLEEYNKEFAevkNQEVTIKALKEKIREYEQtlKNQAEtiaLEKEQKLQNDFAE 199
Cdd:pfam00038   36 ELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERA---RLQLELDNLRLAAEDFRQ--KYEDE---LNLRTSAENDLVG 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  200 KERKLQETQMSTTskleEAEHKVQSLQTalektrtELFDLKTKYDEETTAKADEIEMIMTDLE-RANQRAEVAQREAEtL 278
Cdd:pfam00038  108 LRKDLDEATLARV----DLEAKIESLKE-------ELAFLKKNHEEEVRELQAQVSDTQVNVEmDAARKLDLTSALAE-I 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  279 REQLSS-ANHSLQLASQIQKApDVEQAIEVLTRSSLEVElAAKErEIAQLVEDVQRLQASLTKLRENSAS---QISQLEQ 354
Cdd:pfam00038  176 RAQYEEiAAKNREEAEEWYQS-KLEELQQAAARNGDALR-SAKE-EITELRRTIQSLEIELQSLKKQKASlerQLAETEE 252
                          250       260
                   ....*....|....*....|
gi 1622917383  355 QLSAK----NSTLKQLEEKL 370
Cdd:pfam00038  253 RYELQladyQELISELEAEL 272
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
77-242 7.52e-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: 7.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   77 QVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLidvpdpvpaldlgQQLQLKVQRLhdiETENQKLRETLEEYNKEFAE 156
Cdd:COG1579     21 RLEHRLKELPAELAELEDELAALEARLEAAKTEL-------------EDLEKEIKRL---ELEIEEVEARIKKYEEQLGN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  157 VKNQ-EVT-----IKALKEKIREYEQTLKNqaetiALEKEQKLQNDFAEKERKLQETQmsttsklEEAEHKVQSLQTALE 230
Cdd:COG1579     85 VRNNkEYEalqkeIESLKRRISDLEDEILE-----LMERIEELEEELAELEAELAELE-------AELEEKKAELDEELA 152
                          170
                   ....*....|..
gi 1622917383  231 KTRTELFDLKTK 242
Cdd:COG1579    153 ELEAELEELEAE 164
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
147-367 7.55e-04

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 43.59  E-value: 7.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  147 LEEYNKEFAEVKNQEVTIKALKEKIreyeqtlknqaetIALEKEQKLQNDFaekerklqETQMSTTSKLEEAEHKVQSLQ 226
Cdd:pfam09787    2 LESAKQELADYKQKAARILQSKEKL-------------IASLKEGSGVEGL--------DSSTALTLELEELRQERDLLR 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  227 TALEKTRTELFDLKTKydeettakadeiemiMTDLEranqraEVAQREAETLREQLSSANHslQLASQIQKAPDVEQAIE 306
Cdd:pfam09787   61 EEIQKLRGQIQQLRTE---------------LQELE------AQQQEEAESSREQLQELEE--QLATERSARREAEAELE 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  307 VLTR--SSLEVELaakEREIAQLVEDVQRLQASLTKLR------ENSASQISQLEQQL------------------SAKN 360
Cdd:pfam09787  118 RLQEelRYLEEEL---RRSKATLQSRIKDREAEIEKLRnqltskSQSSSSQSELENRLhqltetliqkqtmlealsTEKN 194

                   ....*..
gi 1622917383  361 STLKQLE 367
Cdd:pfam09787  195 SLVLQLE 201
PRK12704 PRK12704
phosphodiesterase; Provisional
139-236 7.63e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 7.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  139 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKNQAETiaLEKeqklqndfaeKERKLQETQMSTTSKLEEA 218
Cdd:PRK12704    65 EIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLEL--LEK----------REEELEKKEKELEQKQQEL 126
                           90
                   ....*....|....*...
gi 1622917383  219 EHKVQSLQTALEKTRTEL 236
Cdd:PRK12704   127 EKKEEELEELIEEQLQEL 144
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
141-372 8.52e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.17  E-value: 8.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  141 QKLRETLEEYnkefAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKE-QKLQNDFAEKERKLQETQMSTTSKLEEAE 219
Cdd:COG3096    495 QTARELLRRY----RSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfCQRIGQQLDAAEELEELLAELEAQLEELE 570
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  220 HKVQSLQTALEKTRTELFDLKTKYDEETtakadeiemimtdleranQRAEV---AQREAETLREQLSsanhsLQLASqiq 296
Cdd:COG3096    571 EQAAEAVEQRSELRQQLEQLRARIKELA------------------ARAPAwlaAQDALERLREQSG-----EALAD--- 624
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383  297 kAPDVEQAIEvltrsslevELAAKEREIAQLVEDVQRLQASLtklrensASQISQLEQQLSAKNSTLKQLEEKLKG 372
Cdd:COG3096    625 -SQEVTAAMQ---------QLLEREREATVERDELAARKQAL-------ESQIERLSQPGGAEDPRLLALAERLGG 683
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
133-423 8.64e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.94  E-value: 8.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  133 LHDIETENQK-LRETLEEYNKEFAEVKNQEVTIKAlkeKIREYEQTLKNQAETIALEKE--QKLQNDFAEKERKLQEtQM 209
Cdd:pfam05483   65 LKDSDFENSEgLSRLYSKLYKEAEKIKKWKVSIEA---ELKQKENKLQENRKIIEAQRKaiQELQFENEKVSLKLEE-EI 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  210 STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakaDEIEMIMTDLeraNQRAEVAQREAETLREQlsSANHSL 289
Cdd:pfam05483  141 QENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYER----EETRQVYMDL---NNNIEKMILAFEELRVQ--AENARL 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  290 QLASQIQKAPDVEQAIEvltrSSLEVELAAKEREIA----QLVEDVQRLQaSLTKLRENSASQISQLEQQLSAKNSTLKQ 365
Cdd:pfam05483  212 EMHFKLKEDHEKIQHLE----EEYKKEINDKEKQVSllliQITEKENKMK-DLTFLLEESRDKANQLEEKTKLQDENLKE 286
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383  366 LEEKLKG-QADYEEVKKELNilKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAA 423
Cdd:pfam05483  287 LIEKKDHlTKELEDIKMSLQ--RSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA 343
PTZ00121 PTZ00121
MAEBL; Provisional
57-281 9.21e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 9.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   57 KRLIEQSREFKKNTPEDLRKqvapllksfqgeidalSKRSKEAEAAFLNVYKRLIDVPDPVPALDL--GQQLQLKVQRLH 134
Cdd:PTZ00121  1563 KKKAEEAKKAEEDKNMALRK----------------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELK 1626
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  135 DIETENQK---LRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMST 211
Cdd:PTZ00121  1627 KAEEEKKKveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622917383  212 TSKLEEAE-HKVQSLQTALEKTRTELFDLKTKyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 281
Cdd:PTZ00121  1707 LKKKEAEEkKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
131-236 1.04e-03

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 42.20  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  131 QRLHDIETENQKLRETLEE--------------YNKEFAEVKNQEVTIKALKEKIREyeqtLKNQAEtIALEKEQKLQND 196
Cdd:pfam13851   47 KLMSEIQQENKRLTEPLQKaqeeveelrkqlenYEKDKQSLKNLKARLKVLEKELKD----LKWEHE-VLEQRFEKVERE 121
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1622917383  197 FAEKERK----LQETQMSTTSKLEEAEHKVQSLQTALEKTRTEL 236
Cdd:pfam13851  122 RDELYDKfeaaIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQL 165
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
54-390 1.07e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.88  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   54 QSRKRLIEQSREFKKNTPEDLRKQVAPL------LKSFQGEIDALSKRSKEAEAAFLNVYKrlidVPDPVPALDlgqqlQ 127
Cdd:TIGR00606  206 QMELKYLKQYKEKACEIRDQITSKEAQLessreiVKSYENELDPLKNRLKEIEHNLSKIMK----LDNEIKALK-----S 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  128 LKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtikalKEKIREYEQTLKN-QAETIALEKEQKLQNdfaeKERKLQE 206
Cdd:TIGR00606  277 RKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH------QRTVREKERELVDcQRELEKLNKERRLLN----QEKTELL 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  207 TQMSTTSkLEEAEHKVQSLQTALEK----TRTELFDLKTKYDEETTAK----------ADEIEMIMTDLERANQRAEVAQ 272
Cdd:TIGR00606  347 VEQGRLQ-LQADRHQEHIRARDSLIqslaTRLELDGFERGPFSERQIKnfhtlvierqEDEAKTAAQLCADLQSKERLKQ 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  273 REAETLREQLSSANHSLQLASQIqkapdVEQAIEVLTRSSLEVE-LAAKEREIAQLVEDVQRLQASLTKLRENSASQiSQ 351
Cdd:TIGR00606  426 EQADEIRDEKKGLGRTIELKKEI-----LEKKQEELKFVIKELQqLEGSSDRILELDQELRKAERELSKAEKNSLTE-TL 499
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1622917383  352 LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSME 390
Cdd:TIGR00606  500 KKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME 538
mukB PRK04863
chromosome partition protein MukB;
23-302 1.24e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.79  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   23 LPQAHWLCSPGIKRELDAtatvLANRQDESEQSRKRLIEQSREFKKntpedlRKQVAPLLKSFQGEIDALSKRSKEAEAA 102
Cdd:PRK04863   881 LPRLNLLADETLADRVEE----IREQLDEAEEAKRFVQQHGNALAQ------LEPIVSVLQSDPEQFEQLKQDYQQAQQT 950
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  103 FLNVYKRLIDVP------------DPVPALDLGQQLQLKV-QRLHDIETENQKLRETLEEYNKEFAEvKNQEVTikALKE 169
Cdd:PRK04863   951 QRDAKQQAFALTevvqrrahfsyeDAAEMLAKNSDLNEKLrQRLEQAEQERTRAREQLRQAQAQLAQ-YNQVLA--SLKS 1027
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  170 KIREYEQTLKnqaetialEKEQKLQN-----DFAEKERKlqetqMSTTSKLEEAEHKVQSLQTALEKTRTELfdlktkyd 244
Cdd:PRK04863  1028 SYDAKRQMLQ--------ELKQELQDlgvpaDSGAEERA-----RARRDELHARLSANRSRRNQLEKQLTFC-------- 1086
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383  245 eettakadEIEMimtdlERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVE 302
Cdd:PRK04863  1087 --------EAEM-----DNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVE 1131
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
155-373 1.27e-03

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


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 42.29  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  155 AEVKNQEVTIKALKEKIREYEQTLKNQAETialekeqklqNDFAEKERKLQEtqmsttsKLEEAEHKVQSLQTALEKTRT 234
Cdd:pfam12795    3 DELEKAKLDEAAKKKLLQDLQQALSLLDKI----------DASKQRAAAYQK-------ALDDAPAELRELRQELAALQA 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  235 ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA---------ETLREQLSSANHSLQ-LASQIQKAPDVEQA 304
Cdd:pfam12795   66 KAEAAPKEILASLSLEELEQRLLQTSAQLQELQNQLAQLNSqlielqtrpERAQQQLSEARQRLQqIRNRLNGPAPPGEP 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383  305 IEVLTRSSLEVELAAKEREIAQLvedvQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQ 373
Cdd:pfam12795  146 LSEAQRWALQAELAALKAQIDML----EQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEK 210
PTZ00121 PTZ00121
MAEBL; Provisional
47-390 1.32e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   47 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEA----------EAAFLNVYKRLIDVPDP 116
Cdd:PTZ00121  1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaeearkaeDAKRVEIARKAEDARKA 1166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  117 VPALDLGQQLQLKVQRLHDIETENQKLRETLE----EYNKEFAEVKNQEVTIKALKEK----IREYEQTLKNQAETIALE 188
Cdd:PTZ00121  1167 EEARKAEDAKKAEAARKAEEVRKAEELRKAEDarkaEAARKAEEERKAEEARKAEDAKkaeaVKKAEEAKKDAEEAKKAE 1246
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  189 KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELF---DLKTKYDE-----ETTAKADEI------ 254
Cdd:PTZ00121  1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkaEEKKKADEakkkaEEAKKADEAkkkaee 1326
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  255 -----EMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIEVLTRSSLEV----ELAAKEREIA 325
Cdd:PTZ00121  1327 akkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE--KKKEEAKKKADAAKKKAEEKkkadEAKKKAEEDK 1404
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622917383  326 QLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNILKSME 390
Cdd:PTZ00121  1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAE 1467
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
129-367 1.39e-03

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 43.30  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  129 KVQRLHDI-ETEnqklrETLEEYNKEFAEVKNQEvtIKALKEKIreyeqtlkNQAEtialekeqklqnDFAEKER--KLQ 205
Cdd:pfam06160   33 KVKKLNLTgETQ-----EKFEEWRKKWDDIVTKS--LPDIEELL--------FEAE------------ELNDKYRfkKAK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  206 ETQMSTTSKLEEAEHKVQSLQTAL-------EKTRTELFDLKTKYDEettakadeiemIMTDLEranqraevAQREA--- 275
Cdd:pfam06160   86 KALDEIEELLDDIEEDIKQILEELdelleseEKNREEVEELKDKYRE-----------LRKTLL--------ANRFSygp 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  276 --ETLREQLSSANHSLQLASQIQKAPDVEQAIEVLtrSSLEVELAAKER---EIAQLVEDVQ-RLQASLTKLRE------ 343
Cdd:pfam06160  147 aiDELEKQLAEIEEEFSQFEELTESGDYLEAREVL--EKLEEETDALEElmeDIPPLYEELKtELPDQLEELKEgyreme 224
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1622917383  344 ---------NSASQISQLEQQLSAKNSTLKQLE 367
Cdd:pfam06160  225 eegyalehlNVDKEIQQLEEQLEENLALLENLE 257
RNase_Y_N pfam12072
RNase Y N-terminal region;
139-287 1.60e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 41.41  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  139 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKNQAETIAlEKEQKLQndfaEKERKLQETQMSTTSKLEEA 218
Cdd:pfam12072   61 EIHKLRAEAER------ELKERRNELQRQERRLLQKEETLDRKDESLE-KKEESLE----KKEKELEAQQQQLEEKEEEL 129
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383  219 EHKVQSLQTALEK----TRTE----LFD-LKTKYDEETTAKADEIEmimtdlERANQRAEVAQREAETLREQLSSANH 287
Cdd:pfam12072  130 EELIEEQRQELERisglTSEEakeiLLDeVEEELRHEAAVMIKEIE------EEAKEEADKKAKEIIALAIQRCAADH 201
PHA03247 PHA03247
large tegument protein UL36; Provisional
712-953 1.63e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  712 TAEPAQPSSASGSGNSDDAIRSILQQA---RREMEAQQAALDPA---------LKQAPLSQSDITILTPKLlSTSPMPTv 779
Cdd:PHA03247  2833 SAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRRPPSRSPAAKPAaparppvrrLARPAVSRSTESFALPPD-QPERPPQ- 2910
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  780 ssyPPLAISLKKPSAAPEAGASALPNPPALKKEAQDAPGLDPQGAAdcaqgvlrqvknevGRSGAWKDHWWSAVQPERRN 859
Cdd:PHA03247  2911 ---PQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAG--------------EPSGAVPQPWLGALVPGRVA 2973
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  860 A--------ASSEEAKAEETGGGKEKGSGGSGGGSQPRAERSQLQGPSSSEYWKEWPSAESPYSQSSELSLTGASRSETP 931
Cdd:PHA03247  2974 VprfrvpqpAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLE 3053
                          250       260
                   ....*....|....*....|..
gi 1622917383  932 QNSPLPSSPIVPMSKPTKPSVP 953
Cdd:PHA03247  3054 ALDPLPPEPHDPFAHEPDPATP 3075
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
129-383 1.91e-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: 43.02  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  129 KVQRLH-----------------DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQ 191
Cdd:COG3096    810 KLQRLHqafsqfvgghlavafapDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE 889
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  192 KLQNDFAEKERKLQETQMSTTS------KLEEAEHKVQSLQT------ALEKTRTELFDLKTKYDEETTA---------- 249
Cdd:COG3096    890 TLADRLEELREELDAAQEAQAFiqqhgkALAQLEPLVAVLQSdpeqfeQLQADYLQAKEQQRRLKQQIFAlsevvqrrph 969
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  250 --KADEIEMIM--TDL-ERANQRAEVAQREAETLREQLSsanhslQLASQiqkapdVEQAIEVLT--RSSLEV---ELAA 319
Cdd:COG3096    970 fsYEDAVGLLGenSDLnEKLRARLEQAEEARREAREQLR------QAQAQ------YSQYNQVLAslKSSRDAkqqTLQE 1037
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383  320 KEREIAQL------------VEDVQRLQASLTKLRensaSQISQLEQQLSAKNSTLKQLEEKL-KGQADYEEVKKEL 383
Cdd:COG3096   1038 LEQELEELgvqadaeaeeraRIRRDELHEELSQNR----SRRSQLEKQLTRCEAEMDSLQKRLrKAERDYKQEREQV 1110
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
122-375 2.17e-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: 42.59  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  122 LGQQLQLKVQRLH-DIETENQKLRETLEEYNKEFA-EVKNQEVTIKALKEKIREyeqtLKNQAETIALEKeQKLQNDFAE 199
Cdd:pfam15964  361 LKSELERQKERLEkELASQQEKRAQEKEALRKEMKkEREELGATMLALSQNVAQ----LEAQVEKVTREK-NSLVSQLEE 435
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  200 KERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQR------ 273
Cdd:pfam15964  436 AQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQdaarar 515
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  274 -EAETLREQLSSANHSLQLASQ----IQKAPDVEQAIEVLTRSSLEVELAAK-----------ERE-----------IAQ 326
Cdd:pfam15964  516 eECLKLTELLGESEHQLHLTRLekesIQQSFSNEAKAQALQAQQREQELTQKmqqmeaqhdktVNEqyslltsqntfIAK 595
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1622917383  327 LVEDVQRLQASLTKLRENSASQISQLEQQlsakNSTLKQLEEKLKGQAD 375
Cdd:pfam15964  596 LKEECCTLAKKLEEITQKSRSEVEQLSQE----KEYLQDRLEKLQKRNE 640
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
54-390 2.20e-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: 42.65  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   54 QSRKRLIEQSREFKKNTPE---DLRKQVAPLLKSFQGEIdaLSKRSKEAEAAFLNVYKRLIDVPDPVPALD-----LGQQ 125
Cdd:TIGR00618  317 QSKMRSRAKLLMKRAAHVKqqsSIEEQRRLLQTLHSQEI--HIRDAHEVATSIREISCQQHTLTQHIHTLQqqkttLTQK 394
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  126 LQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQ 205
Cdd:TIGR00618  395 LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  206 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS- 284
Cdd:TIGR00618  475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSe 554
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  285 ANHSLQLASQIQKAPDVEQAIEVLTRSSLEvelaakerEIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLK 364
Cdd:TIGR00618  555 RKQRASLKEQMQEIQQSFSILTQCDNRSKE--------DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
                          330       340
                   ....*....|....*....|....*.
gi 1622917383  365 QLEEKLKGQADYEEVKKELNILKSME 390
Cdd:TIGR00618  627 LQDVRLHLQQCSQELALKLTALHALQ 652
PRK10263 PRK10263
DNA translocase FtsK; Provisional
714-982 2.23e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  714 EPAQPSSASGSGNSDDairsILQQARREMEAQQAALDPALKQAPLSQ---SDITILTPKLLSTSPMPTVSSYPPLAiSLK 790
Cdd:PRK10263   276 EEITYTARGVAADPDD----VLFSGNRATQPEYDEYDPLLNGAPITEpvaVAAAATTATQSWAAPVEPVTQTPPVA-SVD 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  791 KPSAAPEAGASALPNPPAlkKEAQDAPglDPQGAADCAQGVLRQVknevgrsgAWKDHWWSAVQPERRNAASSEEAKAEE 870
Cdd:PRK10263   351 VPPAQPTVAWQPVPGPQT--GEPVIAP--APEGYPQQSQYAQPAV--------QYNEPLQQPVQPQQPYYAPAAEQPAQQ 418
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  871 TGGGKEKGSGGSGGGSQPRAER----SQLQGPSSSEYWKEWPSAEsPYSQSSELSLTGASRSETPQNSPLPSSPIVPMSK 946
Cdd:PRK10263   419 PYYAPAPEQPAQQPYYAPAPEQpvagNAWQAEEQQSTFAPQSTYQ-TEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVE 497
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1622917383  947 PTKPSVPPLtpeqyevYMYQEVDtiELTRQVKEKLA 982
Cdd:PRK10263   498 ETKPARPPL-------YYFEEVE--EKRAREREQLA 524
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
126-305 2.25e-03

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 41.26  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  126 LQLKVQR---LHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQ---TLKNQAETIALEKEQ---KLQND 196
Cdd:pfam17078   20 LQLTVQSqnlLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDqlsELKNSYEELTESNKQlkkRLENS 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  197 FAEKERKLQETQMSTT-------SKLEEAEH---KVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQ 266
Cdd:pfam17078  100 SASETTLEAELERLQIqydalvdSQNEYKDHyqqEINTLQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFK 179
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1622917383  267 RAEVAQREAET-LREQLSSANHSLQLASQIQKAPDVEQAI 305
Cdd:pfam17078  180 NLDNIYVNKNNkLLTKLDSLAQLLDLPSWLNLYPESRNKI 219
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
141-338 2.58e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 40.96  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  141 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETiALEK-EQKLQNDFAEKERKLQETQMSTTSKLEEAE 219
Cdd:COG1842     33 RDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARL-ALEKgREDLAREALERKAELEAQAEALEAQLAQLE 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  220 HKVQSLQTALEKTRTELFDLKTKYDeetTAKAdeiemimtdleranqRAEVAQreaetLREQLSSANHSLQLAS------ 293
Cdd:COG1842    112 EQVEKLKEALRQLESKLEELKAKKD---TLKA---------------RAKAAK-----AQEKVNEALSGIDSDDatsale 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622917383  294 -----QIQKAPDVEQAIEVLTRSSLEVELAAKEREIAqlVEDV-QRLQASL 338
Cdd:COG1842    169 rmeekIEEMEARAEAAAELAAGDSLDDELAELEADSE--VEDElAALKAKM 217
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
36-383 2.73e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   36 RELDATATVLANRQDESEQSRKRLIEQSR-------EFKKNTPEDLR--KQVAPLLKSFQGEIDALSKRSKEAEAAflnv 106
Cdd:pfam01576  492 RQLEDERNSLQEQLEEEEEAKRNVERQLStlqaqlsDMKKKLEEDAGtlEALEEGKKRLQRELEALTQQLEEKAAA---- 567
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  107 YKRLidvpdpvpaldlgqqlqlkvqrlhdiETENQKLRETLEEYnkeFAEVKNQEVTIKALKEKIREYEQTLknqAETIA 186
Cdd:pfam01576  568 YDKL--------------------------EKTKNRLQQELDDL---LVDLDHQRQLVSNLEKKQKKFDQML---AEEKA 615
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  187 LEKEQKLQNDFAEKERKLQETQ-MSTTSKLEEAEHKVQSLQTALEKTRTELFDLktkydeetTAKADEIEMIMTDLERAN 265
Cdd:pfam01576  616 ISARYAEERDRAEAEAREKETRaLSLARALEEALEAKEELERTNKQLRAEMEDL--------VSSKDDVGKNVHELERSK 687
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  266 QRAEvaqREAETLREQLSsanhslQLASQIQKAPDVEQAIEVLT---RSSLEVELAAK----EREIAQLVEDVQRLQASL 338
Cdd:pfam01576  688 RALE---QQVEEMKTQLE------ELEDELQATEDAKLRLEVNMqalKAQFERDLQARdeqgEEKRRQLVKQVRELEAEL 758
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383  339 TKLRENSASQIS----------QLEQQLSAKN----STLKQLEeklKGQADYEEVKKEL 383
Cdd:pfam01576  759 EDERKQRAQAVAakkkleldlkELEAQIDAANkgreEAVKQLK---KLQAQMKDLQREL 814
iSH2_PIK3R2 cd12926
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
122-262 2.79e-03

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: 40.07  E-value: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  122 LGQQLQLKVQRLHDIETENQKLretLEEYNKEFAEVKNQEVTIKALKEKIREYEQtlknQAETialekEQKLQNDFAEKE 201
Cdd:cd12926      6 VGAQLKVYHQQYQDKSREYDQL---YEEYTRTSQELQMKRTAIEAFNETIKIFEE----QGQT-----QEKCSKEYLERF 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383  202 RKlqetqmsttsklEEAEHKVQSLQTALEKTR---TELFDLKTKYDEETTAKAD---EIEMIMTDLE 262
Cdd:cd12926     74 RR------------EGNEKEMQRILLNSERLKsriAEIHESRTKLEQDLRAQASdnrEIDKRMNSLK 128
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
126-236 2.93e-03

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 41.23  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  126 LQLKVQRLHDietENQKLRETLEEYNKEFAEVKNQEVTI-KALKEKIREYEQT---LKNQAETIALE-KEQKLQNDFAEK 200
Cdd:pfam15294  131 LHMEIERLKE---ENEKLKERLKTLESQATQALDEKSKLeKALKDLQKEQGAKkdvKSNLKEISDLEeKMAALKSDLEKT 207
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1622917383  201 ERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTEL 236
Cdd:pfam15294  208 LNASTALQKSLEEDLASTKHELLKVQEQLEMAEKEL 243
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
51-370 2.99e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.13  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   51 ESEQSRKRLIEQSREfkknTPEDLRKQVapLLKSFQ-GE-IDALSKRSKEAEAAFlNVYKRLIDVPDPV----------- 117
Cdd:PRK04778   133 ESEEKNREEVEQLKD----LYRELRKSL--LANRFSfGPaLDELEKQLENLEEEF-SQFVELTESGDYVeareildqlee 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  118 ------------PAL------DLGQQL--------QLKVQ-----------RLHDIETENQKLRETLEEYNKEFAEVKNQ 160
Cdd:PRK04778   206 elaaleqimeeiPELlkelqtELPDQLqelkagyrELVEEgyhldhldiekEIQDLKEQIDENLALLEELDLDEAEEKNE 285
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  161 EvtikaLKEKIRE-YEQtlknqaetiaLEKEQKLQNdfaekerklqetqmsttskleEAEHKVQSLQTALEKTRTELFDL 239
Cdd:PRK04778   286 E-----IQERIDQlYDI----------LEREVKARK---------------------YVEKNSDTLPDFLEHAKEQNKEL 329
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  240 KTKydeettakadeiemimtdLERANQRAEVAQREAETLR---EQLSSANHSLQlasQIQKAPDvEQAIevlTRSSLEVE 316
Cdd:PRK04778   330 KEE------------------IDRVKQSYTLNESELESVRqleKQLESLEKQYD---EITERIA-EQEI---AYSELQEE 384
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383  317 LAAKEREIAQLVEDVQRLQASLTKLR--ENSASQ-ISQLEQQLsaknSTLKQLEEKL 370
Cdd:PRK04778   385 LEEILKQLEEIEKEQEKLSEMLQGLRkdELEAREkLERYRNKL----HEIKRYLEKS 437
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
43-358 3.09e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 42.35  E-value: 3.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   43 TVLANRQDESEQSRKRLiEQSREFKknTPEDlrkqvAPLLKSFQGEIDALSKRSKEAEAAflNVYKRLIDvpdpvpaldl 122
Cdd:PRK10929    16 GAYAATAPDEKQITQEL-EQAKAAK--TPAQ-----AEIVEALQSALNWLEERKGSLERA--KQYQQVID---------- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  123 gqqlqlkvqrlhDIETENQKLRETLEEYNKEFAEVkNQEVTIKALKEKIREYEQTLKNQAETiaLEKEQKLQNDFAEKER 202
Cdd:PRK10929    76 ------------NFPKLSAELRQQLNNERDEPRSV-PPNMSTDALEQEILQVSSQLLEKSRQ--AQQEQDRAREISDSLS 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  203 KLQETQMSTTSKLEEAEHKVQSL--------QTALEKTRTELFDLKtkydeettAKADEIEMIMTDL----ERANQRAEV 270
Cdd:PRK10929   141 QLPQQQTEARRQLNEIERRLQTLgtpntplaQAQLTALQAESAALK--------ALVDELELAQLSAnnrqELARLRSEL 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  271 AQREAETLREQLSSANHslQLASQIQKapDVEQAIEvltrsslEVELAAKE---------------REIAQ-LVEDVQRL 334
Cdd:PRK10929   213 AKKRSQQLDAYLQALRN--QLNSQRQR--EAERALE-------STELLAEQsgdlpksivaqfkinRELSQaLNQQAQRM 281
                          330       340
                   ....*....|....*....|....
gi 1622917383  335 QASLTKLREnSASQISQLEQQLSA 358
Cdd:PRK10929   282 DLIASQQRQ-AASQTLQVRQALNT 304
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
266-425 3.20e-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: 42.25  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  266 QRAEVAQREAETLREQLSSANHSLQ------------LASQIQKA--PDVEQAIEVLTRSSLEVElaakeREIAQLVEDV 331
Cdd:COG3096    785 KRLEELRAERDELAEQYAKASFDVQklqrlhqafsqfVGGHLAVAfaPDPEAELAALRQRRSELE-----RELAQHRAQE 859
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  332 QRLQASLTKLRENS------------------ASQISQLEQQLSAKNS----------TLKQLEEKLKG----------- 372
Cdd:COG3096    860 QQLRQQLDQLKEQLqllnkllpqanlladetlADRLEELREELDAAQEaqafiqqhgkALAQLEPLVAVlqsdpeqfeql 939
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383  373 QADYEEVKKELNILKSMEFAPSEGA------GTQDAAKplevlLMEKNRSLqseNAALR 425
Cdd:COG3096    940 QADYLQAKEQQRRLKQQIFALSEVVqrrphfSYEDAVG-----LLGENSDL---NEKLR 990
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
121-448 3.29e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 42.34  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  121 DLGQQLQ-LKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALkEKIREYEQTLKNQAETIALEKEQKLQNDFAE 199
Cdd:PTZ00108  1035 DLVKELKkLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL-GAAVSYDYLLSMPIWSLTKEKVEKLNAELEK 1113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  200 KERKLQETQmSTTSK---LEEaehkVQSLQTALEKTRtelfdlktKYDEETTAKADEIEMIMTDLERANQR-----AEVA 271
Cdd:PTZ00108  1114 KEKELEKLK-NTTPKdmwLED----LDKFEEALEEQE--------EVEEKEIAKEQRLKSKTKGKASKLRKpklkkKEKK 1180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  272 QREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQ 351
Cdd:PTZ00108  1181 KKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEF 1260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  352 LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSmeFAPSEGAGTQDA-AKPLEVLLMEKNRSLQSENAALRISNSD 430
Cdd:PTZ00108  1261 SSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESN--GGSKPSSPTKKKvKKRLEGSLAALKKKKKSEKKTARKKKSK 1338
                          330
                   ....*....|....*...
gi 1622917383  431 lSGSARRKGKDQPESRRP 448
Cdd:PTZ00108  1339 -TRVKQASASQSSRLLRR 1355
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
225-387 3.40e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 3.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  225 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQKAPDVEQ 303
Cdd:COG4717     47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELeELREELEKLEKLLQ 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  304 AIEVL-TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAsQISQLEQQLSAK-----NSTLKQLEEKLKgqaDYE 377
Cdd:COG4717    127 LLPLYqELEALEAELAELPERLEELEERLEELRELEEELEELEA-ELAELQEELEELleqlsLATEEELQDLAE---ELE 202
                          170
                   ....*....|
gi 1622917383  378 EVKKELNILK 387
Cdd:COG4717    203 ELQQRLAELE 212
mukB PRK04863
chromosome partition protein MukB;
81-383 3.53e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.25  E-value: 3.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   81 LLKSFQGEIDALSKRSKEAEA-------------AFLNVYKRLIDVPDPVPAL-DLGQQLQLKVQRLHDIETENQKLRET 146
Cdd:PRK04863   787 RIEQLRAEREELAERYATLSFdvqklqrlhqafsRFIGSHLAVAFEADPEAELrQLNRRRVELERALADHESQEQQQRSQ 866
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  147 L----------------------EEYNKEFAEVKNQEVTIKALKEKIREYEQTLkNQAETIAlekeQKLQNDfaekerkl 204
Cdd:PRK04863   867 LeqakeglsalnrllprlnlladETLADRVEEIREQLDEAEEAKRFVQQHGNAL-AQLEPIV----SVLQSD-------- 933
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  205 qetqmstTSKLEEAEHKVQSLQTALEKTRTELFDLKT--------KYDEETTAKADEIEMImtdlERANQRAEVAQREAE 276
Cdd:PRK04863   934 -------PEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfSYEDAAEMLAKNSDLN----EKLRQRLEQAEQERT 1002
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  277 TLREQLSSANHSLQLASQIQkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRL----------QASLTK------ 340
Cdd:PRK04863  1003 RAREQLRQAQAQLAQYNQVL--------------ASLKSSYDAKRQMLQELKQELQDLgvpadsgaeeRARARRdelhar 1068
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1622917383  341 LRENSaSQISQLEQQLSAKNSTLKQLEEKL-KGQADYEEVKKEL 383
Cdd:PRK04863  1069 LSANR-SRRNQLEKQLTFCEAEMDNLTKKLrKLERDYHEMREQV 1111
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
249-375 3.92e-03

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 41.37  E-value: 3.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  249 AKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQkapdveqaievlTRSSLEVELAAKEREIAQLv 328
Cdd:COG3524    174 AREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ------------LIATLEGQLAELEAELAAL- 240
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1622917383  329 edvqrlqasLTKLRENSAsQISQLEQQLSAKNSTLKQLEEKLKGQAD 375
Cdd:COG3524    241 ---------RSYLSPNSP-QVRQLRRRIAALEKQIAAERARLTGASG 277
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
313-384 4.05e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  313 LEVELAAKEREIAQLVEDVQRLQASLTKLRENS-------------------ASQISQLEQQ---LSAKNSTLKQLEEKL 370
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvasaEREIAELEAElerLDASSDDLAALEEQL 694
                           90
                   ....*....|....*
gi 1622917383  371 KG-QADYEEVKKELN 384
Cdd:COG4913    695 EElEAELEELEEELD 709
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
141-284 4.52e-03

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: 41.02  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  141 QKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKE-----QKLQNDFAEKERK-LQETQMSTTS 213
Cdd:cd16269    149 EDREKLVEKYRQVpRKGVKAEEVLQEFLQSKEAEAEAIL--QADQALTEKEkeieaERAKAEAAEQERKlLEEQQRELEQ 226
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622917383  214 KLEEAEHkvqSLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQR--AEVAQREAETLREQLSS 284
Cdd:cd16269    227 KLEDQER---SYEEHLRQ-------LKEKMEEERENLLKEQERALESKLKEQEAllEEGFKEQAELLQEEIRS 289
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1339-1421 4.59e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 1339 GQAGASDSPSARSGRAAPSSEGD-----SCDGVEATEGPGSADTEEPKSQGEAEREEAPRPaeqtepPPSGTPGPDDARD 1413
Cdd:PHA03307   283 GPASSSSSPRERSPSPSPSSPGSgpapsSPRASSSSSSSRESSSSSTSSSSESSRGAAVSP------GPSPSRSPSPSRP 356

                   ....*...
gi 1622917383 1414 DDHEGGPA 1421
Cdd:PHA03307   357 PPPADPSS 364
COG0610 COG0610
Type I site-specific restriction-modification system, R (restriction) subunit and related ...
2-258 5.38e-03

Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];


Pssm-ID: 440375 [Multi-domain]  Cd Length: 936  Bit Score: 41.39  E-value: 5.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383    2 SAGAGKGAPQTPVEspTASSKLPQAH----WLCSPGIKRELDATATVL------ANRQDESEQSRKRLIEQSREFKKntp 71
Cdd:COG0610    664 SEEDGKEDVLTDPE--EALEELKEALdelrALFPEGVDFSAFDPTEKLealdeaVERFLGDEEARKEFKKLFKELSR--- 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   72 edLRKQVAPLLKSFQGEIDALSKRSkeaeAAFLNVYKRLIDVPDPVPAldlgQQLQLKVQRLHD--IETENQKLRETLEE 149
Cdd:COG0610    739 --LYNLLSPDDEFGDLELEKYRDDV----SFYLALRAKLRKLGEKLDL----KEYEEKIRQLLDeaIDLERKEIKPRIKQ 808
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  150 ---YNKEFAE--------VKNQEVTIKALKEKIREYEQTLKNQAETIA---LEKEQK-----LQNDFAEKERKLQETQMS 210
Cdd:COG0610    809 npvQYRKFSElleeiieeYNNGALDADEVLEELEELAKEVKEEEERAEeegLNEEELafydaLAENLGDEKLKELAKELD 888
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1622917383  211 TTSKlEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKAdeIEMIM 258
Cdd:COG0610    889 DLLK-KNVTVDWRKRESVRAKLRDAIKRLLRKYGYPKQDEA--VEEVY 933
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
291-387 5.49e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 5.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  291 LASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAsltklrensasQISQLEQQLSAKNSTLKQLEEKL 370
Cdd:COG2433    382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-----------EVEELEAELEEKDERIERLEREL 450
                           90       100
                   ....*....|....*....|.
gi 1622917383  371 K--GQADYEEVKK--ELNILK 387
Cdd:COG2433    451 SeaRSEERREIRKdrEISRLD 471
PRK12704 PRK12704
phosphodiesterase; Provisional
155-324 5.79e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 5.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  155 AEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFaEKERKLQEtqmsttSKLEEAEHKVQSLQTALEKtRT 234
Cdd:PRK12704    31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF-EKELRERR------NELQKLEKRLLQKEENLDR-KL 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  235 ELFDLKtkyDEETTAKADEIEMIMTDLEraNQRAEVAQREAETLREqlssanhsLQLASQIQKapdvEQAIEVL---TRS 311
Cdd:PRK12704   103 ELLEKR---EEELEKKEKELEQKQQELE--KKEEELEELIEEQLQE--------LERISGLTA----EEAKEILlekVEE 165
                          170
                   ....*....|...
gi 1622917383  312 SLEVELAAKEREI 324
Cdd:PRK12704   166 EARHEAAVLIKEI 178
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
42-381 6.12e-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: 6.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383   42 ATVLANRQDESEQSRKRLIEQSREFK--KNTPEDLRKQ---VAPLLKSFQ------GEIDALSKRSKEAEAAFLNVYKRL 110
Cdd:TIGR00606  736 QSIIDLKEKEIPELRNKLQKVNRDIQrlKNDIEEQETLlgtIMPEEESAKvcltdvTIMERFQMELKDVERKIAQQAAKL 815
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  111 IDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREyeqtlknqaetiALEKE 190
Cdd:TIGR00606  816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGT------------NLQRR 883
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  191 QKLQNDFAEKERKLQETqmstTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMI----------MTD 260
Cdd:TIGR00606  884 QQFEEQLVELSTEVQSL----IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIkekvknihgyMKD 959
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  261 LERANQRA---EVAQREAE--TLREQLSSA-------NHSLQLASQIQKAPDVEQAI--EVLTRSSLEVELAAKEREIAQ 326
Cdd:TIGR00606  960 IENKIQDGkddYLKQKETElnTVNAQLEECekhqekiNEDMRLMRQDIDTQKIQERWlqDNLTLRKRENELKEVEEELKQ 1039
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383  327 LvedvqrlqasLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKG-QADYEEVKK 381
Cdd:TIGR00606 1040 H----------LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGrQKGYEKEIK 1085
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
140-425 6.67e-03

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 40.36  E-value: 6.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  140 NQKLRETLEEYNKEFAEVKNQEVT--------IKALKEKIREYEQTLKNQAETIA---LEKEQKLQNDFAEKERklqetq 208
Cdd:pfam14915    1 NCMLQDEIAMLRLEIDTIKNQNQEkekkyledIEILKEKNDDLQKTLKLNEETLTktvFQYNGQLNVLKAENTM------ 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  209 msTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKadeiemimTDLERANQRaevAQREAETLREQLSSANHS 288
Cdd:pfam14915   75 --LNSKLENEKQNKERLETEVESYRSRLAAAIQDHEQSQTSK--------RDLELAFQR---ERDEWLRLQDKMNFDVSN 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  289 LQLASQI--QKAPDVEQAIevltrSSLEVEL---AAKEREIAQLVEDVQRlqasltklrensasqisqleqQLSAKNSTL 363
Cdd:pfam14915  142 LRDENEIlsQQLSKAESKA-----NSLENELhrtRDALREKTLLLESVQR---------------------DLSQAQCQK 195
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622917383  364 KQLEEKLkgQADYEEVKKELNILKSMEfapsegagtqdaakplevllmEKNRSLQSENAALR 425
Cdd:pfam14915  196 KELEHMY--QNEQDKVNKYIGKQESLE---------------------ERLAQLQSENMLLR 234
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
124-438 6.79e-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: 6.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  124 QQLQLKVQRLHDIETENQKLRETLEeyNKEFAEVKNQEVTiKALKEKIREYEQTLKNQAETIALEKEQKLQN------DF 197
Cdd:pfam15921  120 QEMQMERDAMADIRRRESQSQEDLR--NQLQNTVHELEAA-KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEirsilvDF 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  198 AEKERK--LQETQMSTT--SKLEEAEHKV-QSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD-LERANQRAEVA 271
Cdd:pfam15921  197 EEASGKkiYEHDSMSTMhfRSLGSAISKIlRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQhQDRIEQLISEH 276
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  272 QREAETLREQLSSANhslqlasqiQKAPDVEQAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQ 351
Cdd:pfam15921  277 EVEITGLTEKASSAR---------SQANSIQSQLEIIQEQARN-QNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEE 346
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  352 LEQQLSAKNSTLKQ--------------LEEKL-KGQADYEEVKKELNILKSM-EFAPSEGAGTQDAAKPLEVLLMEKNR 415
Cdd:pfam15921  347 LEKQLVLANSELTEarterdqfsqesgnLDDQLqKLLADLHKREKELSLEKEQnKRLWDRDTGNSITIDHLRRELDDRNM 426
                          330       340
                   ....*....|....*....|...
gi 1622917383  416 SLQSENAALRISNSDLSGSARRK 438
Cdd:pfam15921  427 EVQRLEALLKAMKSECQGQMERQ 449
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
129-447 6.84e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.88  E-value: 6.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  129 KVQRLHDIETENQKLRETLEEYNKEFaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQ 208
Cdd:pfam17380  235 KMERRKESFNLAEDVTTMTPEYTVRY---NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKARE 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  209 MSTTSKLEEAEHKVQSL------------QTALEKTRT-ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA 275
Cdd:pfam17380  312 VERRRKLEEAEKARQAEmdrqaaiyaeqeRMAMERERElERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  276 ETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEvelAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQ 355
Cdd:pfam17380  392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ 468
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  356 LSAKNSTLKQLEEKLKGQADYEEVKKELnILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAAlRISNSDlsgsa 435
Cdd:pfam17380  469 EEERKRKKLELEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR-REAEEE----- 541
                          330
                   ....*....|..
gi 1622917383  436 RRKGKDQPESRR 447
Cdd:pfam17380  542 RRKQQEMEERRR 553
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
139-395 7.20e-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: 7.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  139 ENQK--LRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQaetialekeqkLQNDFAEKE--RKLQETQMS-TTS 213
Cdd:pfam15921  102 EKQKfyLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQ-----------LQNTVHELEaaKCLKEDMLEdSNT 170
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  214 KLEEAEHKVQSLQTALEKTRTELFDL-----KTKYDEET----------TAKADEIEMIMTDLERANQRAEVAQREAETL 278
Cdd:pfam15921  171 QIEQLRKMMLSHEGVLQEIRSILVDFeeasgKKIYEHDSmstmhfrslgSAISKILRELDTEISYLKGRIFPVEDQLEAL 250
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  279 ReqlSSANHSLQLASQiQKAPDVEQAIevltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSA 358
Cdd:pfam15921  251 K---SESQNKIELLLQ-QHQDRIEQLI-----SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSD 321
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1622917383  359 KNSTLKQLEEKLK-GQADYEEVKKELNilKSMEFAPSE 395
Cdd:pfam15921  322 LESTVSQLRSELReAKRMYEDKIEELE--KQLVLANSE 357
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
311-429 7.87e-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: 38.82  E-value: 7.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  311 SSLEVELAAKEREIAQLVEDVQRLQASLTKlrENSASQISQLEQQLSAKNSTLKQLEEKLKgqADYEEVKKELNILKsme 390
Cdd:pfam17098    7 NLLLARLAEKEQEIQELKAQLQDLKQSLQP--PSSQLRSLLLDPAVNLEFLRLKKELEEKK--KKLKEAQLELAAWK--- 79
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622917383  391 FAPSEGAGTQdaakplevlLMEKNRSLQSENAALRISNS 429
Cdd:pfam17098   80 FTPDSTTGKR---------LMAKCRLLQQENEELGRQLS 109
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
136-267 8.20e-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: 39.13  E-value: 8.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  136 IETENQKLRETLEEYNKEFAEVKNQEV----TIKALKEKIREYEQTLKNQAETIAlekeqKLQNDFAEKERKLQETQMsT 211
Cdd:pfam13870   47 LQIENQALNEKIEERNKELKRLKLKVTntvhALTHLKEKLHFLSAELSRLKKELR-----ERQELLAKLRKELYRVKL-E 120
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622917383  212 TSKLEEAEHKVqslqtaleKTRTELF---DLKTKYD---EETTAKADEIEMIMTDLERANQR 267
Cdd:pfam13870  121 RDKLRKQNKKL--------RQQGGLLhvpALLHDYDktkAEVEEKRKSVKKLRRKVKILEMR 174
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
136-369 8.34e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.93  E-value: 8.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  136 IETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREyEQTLKNQAetiaLEKEQKLQNDFAEkerkLQETQMST 211
Cdd:pfam01576  213 LEGESTDLQEQIAELQAQIAELRAQlakkEEELQAALARLEE-ETAQKNNA----LKKIRELEAQISE----LQEDLESE 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  212 TSKLEEAEHKVQSLQTALEKTRTELFD----------LKTKYDEETT--AKADEIEMIMTDleraNQRAEVAQREA---E 276
Cdd:pfam01576  284 RAARNKAEKQRRDLGEELEALKTELEDtldttaaqqeLRSKREQEVTelKKALEEETRSHE----AQLQEMRQKHTqalE 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  277 TLREQLSSANH---SLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLE 353
Cdd:pfam01576  360 ELTEQLEQAKRnkaNLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ 439
                          250
                   ....*....|....*.
gi 1622917383  354 QQLSAKNSTLKQLEEK 369
Cdd:pfam01576  440 SELESVSSLLNEAEGK 455
Homeobox_KN pfam05920
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ...
1289-1323 8.43e-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: 35.57  E-value: 8.43e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1622917383 1289 QQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSR 1323
Cdd:pfam05920    5 LHNPYPSEEEKAELAKETGLSRKQISNWFINARRR 39
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
124-226 8.44e-03

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 37.95  E-value: 8.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  124 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREyeqtlkNQAETIALE-KEQKLQNDFAEKER 202
Cdd:pfam18595   19 RELQAKIDALQVVEKDLRSCIKLLEEIEAELAKLEEAKKKLKELRDALEE------KEIELRELErREERLQRQLENAQE 92
                           90       100
                   ....*....|....*....|....
gi 1622917383  203 KLQETQMSTTSKLEEAEHKVQSLQ 226
Cdd:pfam18595   93 KLERLREQAEEKREAAQARLEELR 116
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
121-292 9.03e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.71  E-value: 9.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  121 DLGQQLQlkvQRLHDIETENQKLRETLE-------EYNKEFA------EVKNQevTIKALKEKIREYEQTLKNQAETIAL 187
Cdd:COG3096    984 DLNEKLR---ARLEQAEEARREAREQLRqaqaqysQYNQVLAslkssrDAKQQ--TLQELEQELEELGVQADAEAEERAR 1058
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383  188 EKEQKLQNDF-AEKERKlqeTQMSTTSKLEEAEhkVQSLQTALEKTRTELFDLKTkydEETTAKA---DEIEMIM-TDLE 262
Cdd:COG3096   1059 IRRDELHEELsQNRSRR---SQLEKQLTRCEAE--MDSLQKRLRKAERDYKQERE---QVVQAKAgwcAVLRLARdNDVE 1130
                          170       180       190
                   ....*....|....*....|....*....|
gi 1622917383  263 RANQRAEVAQREAETLREQLSSANHSLQLA 292
Cdd:COG3096   1131 RRLHRRELAYLSADELRSMSDKALGALRLA 1160
 
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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